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Conserved domains on  [gi|1013071061|ref|NP_001308781|]
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tyrosine-protein kinase JAK1 isoform 1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
870-1153 0e+00

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


:

Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 626.19  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  870 FEKRFLKRIRDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGG 949
Cdd:cd05079      1 FEKRFLKRIRDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  950 NGIKLIMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIE 1029
Cdd:cd05079     81 NGIKLIMEFLPSGSLKEYLPRNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIE 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1030 TDKEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSDSSPMALFLKMIGPTHGQMTVTRLVNTLK 1109
Cdd:cd05079    161 TDKEYYTVKDDLDSPVFWYAPECLIQSKFYIASDVWSFGVTLYELLTYCDSESSPMTLFLKMIGPTHGQMTVTRLVRVLE 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1013071061 1110 EGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALL 1153
Cdd:cd05079    241 EGKRLPRPPNCPEEVYQLMRKCWEFQPSKRTTFQNLIEGFEAIL 284
PTK_Jak1_rpt1 cd05077
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely ...
583-846 0e+00

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits, common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


:

Pssm-ID: 270662 [Multi-domain]  Cd Length: 266  Bit Score: 576.12  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  583 LVQGEHLGRGTRTHIYSGTLMDYKDD--EGTSEEKKIKVILKVLDPSHRDISLAFFEAASMMRQVSHKHIVYLYGVCVRD 660
Cdd:cd05077      1 IVQGEHLGRGTRTQIYAGILNYKDDDedEGYSYEKEIKVILKVLDPSHRDISLAFFETASMMRQVSHKHIVLLYGVCVRD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  661 VENIMVEEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIDSECGPFIKLSDP 740
Cdd:cd05077     81 VENIMVEEFVEFGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNILLAREGIDGECGPFIKLSDP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  741 GIPITVLSRQECIERIPWIAPECVEDSKNLSVAADKWSFGTTLWEICYNGEIPLKDKTLIEKERFYESRCRPVTPSCKEL 820
Cdd:cd05077    161 GIPITVLSRQECVERIPWIAPECVEDSKNLSIAADKWSFGTTLWEICYNGEIPLKDKTLAEKERFYEGQCMLVTPSCKEL 240
                          250       260
                   ....*....|....*....|....*.
gi 1013071061  821 ADLMTRCMNYDPNQRPFFRAIMRDIN 846
Cdd:cd05077    241 ADLMTHCMNYDPNQRPFFRAIMRDIN 266
FERM_C_JAK1 cd13332
FERM domain C-lobe of Janus kinase 1; JAK1 is a tyrosine kinase protein essential in signaling ...
282-426 7.67e-80

FERM domain C-lobe of Janus kinase 1; JAK1 is a tyrosine kinase protein essential in signaling type I and type II cytokines. It interacts with the gamma chain of type I cytokine receptors to elicit signals from the IL-2 receptor family, the IL-4 receptor family, the gp130 receptor family, ciliary neurotrophic factor receptor (CNTF-R), neurotrophin-1 receptor (NNT-1R) and Leptin-R). It also is involved in transducing a signal by type I (IFN-alpha/beta) and type II (IFN-gamma) interferons, and members of the IL-10 family via type II cytokine receptors. JAK (also called Just Another Kinase) is a family of intracellular, non-receptor tyrosine kinases that transduce cytokine-mediated signals via the JAK-STAT pathway. The JAK family in mammals consists of 4 members: JAK1, JAK2, JAK3 and TYK2. JAKs are composed of seven JAK homology (JH) domains (JH1-JH7) . The C-terminal JH1 domain is the main catalytic domain, followed by JH2, which is often referred to as a pseudokinase domain, followed by JH3-JH4 which is homologous to the SH2 domain, and lastly JH5-JH7 which is a FERM domain. Named after Janus, the two-faced Roman god of doorways, JAKs possess two near-identical phosphate-transferring domains; one which displays the kinase activity (JH1), while the other negatively regulates the kinase activity of the first (JH2). The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


:

Pssm-ID: 275412  Cd Length: 144  Bit Score: 257.47  E-value: 7.67e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  282 GAEIFETSMLLISSENEMNWFHSNDGGNVLYYEVMVTGNLGIQWRHKPNVVSVEKEKNKLKRKKLeNKHKKDEEKNKIRE 361
Cdd:cd13332      1 GAEIFETSSLLISSESELNNFNMGDGGNYGYYEVSVTGNTGISWRRKPATTAVEKKKKGKSKKNK-LKGKKDEDKKKARE 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1013071061  362 EWNNFSYFPEITHIVIKESVVSINKQDNKKMELKLSSHEEALSFVSLVDGYFRLTADAHHYLCTD 426
Cdd:cd13332     80 GWNNFSYFPEITHIVIKESTVTINRQDNKKMELKLSSRDEALSFAALVDGYFRLTADAHHYLCTD 144
FERM_F2 pfam18377
FERM F2 acyl-CoA binding protein-like domain; This is an F2 lobe domain consisting of an ...
147-277 3.11e-73

FERM F2 acyl-CoA binding protein-like domain; This is an F2 lobe domain consisting of an acyl-CoA binding protein fold found in FERM region of Jak-family tyrosine kinases. Multidomain JAK molecules interact with receptors through their FERM and SH2-like domains, triggering a series of phosphorylation events, resulting in the activation of their kinase domains. Overall, the FERM region maintains the typical three-lobed architecture, with an F1 lobe consisting of a ubiquitin-like fold, an F2 lobe consisting of an acyl-CoA binding protein fold, and an F3 lobe consisting of a pleckstrin-homology (PH) fold. JAK1 FERM-F2 domain has been shown to act as the interaction site for the IFNLR1 box1 motif (PxxLxF) of class II cytokine receptors which is essential for kinase activation.


:

Pssm-ID: 436450  Cd Length: 131  Bit Score: 238.69  E-value: 3.11e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  147 TPLLDASSLEYLFAQGQYDLVKCLAPIRDPKTEQDGHDIENECLGMAVLAISHYAMMKKMQLPELPKDISYKRYIPETLN 226
Cdd:pfam18377    1 SPLLDAPSLEYLFAQGKYDFVNGLAPLRDSQSEQETHRIENECLGMAVLDLSHLAKEKGLSLEEIAKKVSYKRCIPESFR 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1013071061  227 KSIRQRNLLTRMRINNVFKDFLKEFNNKTICDSSVSTHDLKVKYLATLETL 277
Cdd:pfam18377   81 RQIQQRNFLTRKRIRNVFKRFLREFNQHTVGDCKLTAHDLKLKYLSTLETL 131
SH2 super family cl15255
Src homology 2 (SH2) domain; In general, SH2 domains are involved in signal transduction; they ...
426-527 3.34e-64

Src homology 2 (SH2) domain; In general, SH2 domains are involved in signal transduction; they bind pTyr-containing polypeptide ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. They are present in a wide array of proteins including: adaptor proteins (Nck1, Crk, Grb2), scaffolds (Slp76, Shc, Dapp1), kinases (Src, Syk, Fps, Tec), phosphatases (Shp-1, Shp-2), transcription factors (STAT1), Ras signaling molecules (Ras-Gap), ubiquitination factors (c-Cbl), cytoskeleton regulators (Tensin), signal regulators (SAP), and phospholipid second messengers (PLCgamma), amongst others.


The actual alignment was detected with superfamily member cd10378:

Pssm-ID: 472789  Cd Length: 102  Bit Score: 212.02  E-value: 3.34e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  426 DVAPPLIVHNIQNGCHGPICTEYAINKLRQEGSEEGMYVLRWSCTDFDNILMTVTCFEKSEQVQGAQKQFKNFQIEVQKG 505
Cdd:cd10378      1 DVAPPLIVHNIKNGCHGPICTEYAINKLRQEGNEEGMYVLRWSCTDFNNILMTVTCIELSECESRPVKQYKNFQIEVKKG 80
                           90       100
                   ....*....|....*....|..
gi 1013071061  506 RYSLHGSDRSFPSLGDLMSHLK 527
Cdd:cd10378     81 GYSLHGSDTFFPSLKELMEHLK 102
FERM_F1 super family cl39717
FERM F1 ubiquitin-like domain; This is an F1 lobe domain consisting of a ubiquitin like fold ...
36-129 4.36e-41

FERM F1 ubiquitin-like domain; This is an F1 lobe domain consisting of a ubiquitin like fold found in FERM region of Jak-family tyrosine kinases. Multidomain JAK molecules interact with receptors through their FERM and SH2-like domains, triggering a series of phosphorylation events, resulting in the activation of their kinase domains. Overall, the FERM region maintains the typical three-lobed architecture, with an F1 lobe consisting of a ubiquitin-like fold, an F2 lobe consisting of an acyl-CoA binding protein fold, and an F3 lobe consisting of a pleckstrin-homology (PH) fold.


The actual alignment was detected with superfamily member pfam18379:

Pssm-ID: 465733  Cd Length: 96  Bit Score: 146.16  E-value: 4.36e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061   36 VEVIFYLSDRE----PLRLGSGEYTAEELCIRAAQACRISPLCHNLFALYDENTKLWYAPNRTITVDDKMSLRLHYRMRF 111
Cdd:pfam18379    1 LQVHLYWSGPGdgetYLSYPPGEYTAEELCIDAAKACGITPVYHNLFALYDEDDRVWYPPNHVFHIDESTSLTLHFRIRF 80
                           90
                   ....*....|....*...
gi 1013071061  112 YFTNWHGTNDNEQsvWRH 129
Cdd:pfam18379   81 YFPNWHGLGESEP--YRY 96
 
Name Accession Description Interval E-value
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
870-1153 0e+00

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 626.19  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  870 FEKRFLKRIRDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGG 949
Cdd:cd05079      1 FEKRFLKRIRDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  950 NGIKLIMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIE 1029
Cdd:cd05079     81 NGIKLIMEFLPSGSLKEYLPRNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIE 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1030 TDKEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSDSSPMALFLKMIGPTHGQMTVTRLVNTLK 1109
Cdd:cd05079    161 TDKEYYTVKDDLDSPVFWYAPECLIQSKFYIASDVWSFGVTLYELLTYCDSESSPMTLFLKMIGPTHGQMTVTRLVRVLE 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1013071061 1110 EGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALL 1153
Cdd:cd05079    241 EGKRLPRPPNCPEEVYQLMRKCWEFQPSKRTTFQNLIEGFEAIL 284
PTK_Jak1_rpt1 cd05077
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely ...
583-846 0e+00

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits, common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270662 [Multi-domain]  Cd Length: 266  Bit Score: 576.12  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  583 LVQGEHLGRGTRTHIYSGTLMDYKDD--EGTSEEKKIKVILKVLDPSHRDISLAFFEAASMMRQVSHKHIVYLYGVCVRD 660
Cdd:cd05077      1 IVQGEHLGRGTRTQIYAGILNYKDDDedEGYSYEKEIKVILKVLDPSHRDISLAFFETASMMRQVSHKHIVLLYGVCVRD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  661 VENIMVEEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIDSECGPFIKLSDP 740
Cdd:cd05077     81 VENIMVEEFVEFGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNILLAREGIDGECGPFIKLSDP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  741 GIPITVLSRQECIERIPWIAPECVEDSKNLSVAADKWSFGTTLWEICYNGEIPLKDKTLIEKERFYESRCRPVTPSCKEL 820
Cdd:cd05077    161 GIPITVLSRQECVERIPWIAPECVEDSKNLSIAADKWSFGTTLWEICYNGEIPLKDKTLAEKERFYEGQCMLVTPSCKEL 240
                          250       260
                   ....*....|....*....|....*.
gi 1013071061  821 ADLMTRCMNYDPNQRPFFRAIMRDIN 846
Cdd:cd05077    241 ADLMTHCMNYDPNQRPFFRAIMRDIN 266
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
875-1147 2.26e-115

Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyze the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyze the reverse process. Protein kinases fall into three broad classes, characterized with respect to substrate specificity; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 358.35  E-value: 2.26e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  875 LKRIRDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGngIKL 954
Cdd:pfam07714    1 LTLGEKLGEGAFGEVYKGTLKGEGENTKIKVAVKTLKEGADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEP--LYI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIEtDKEY 1034
Cdd:pfam07714   79 VTEYMPGGDLLDFLRKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDIY-DDDY 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1035 YTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDsdsSPmalflkmigptHGQMTVTRLVNTLKEGKRL 1114
Cdd:pfam07714  158 YRKRGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLGE---QP-----------YPGMSNEEVLEFLEDGYRL 223
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1013071061 1115 PCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIE 1147
Cdd:pfam07714  224 PQPENCPDELYDLMKQCWAYDPEDRPTFSELVE 256
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
875-1149 9.00e-115

Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 356.46  E-value: 9.00e-115
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061   875 LKRIRDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGngIKL 954
Cdd:smart00219    1 LTLGKKLGEGAFGEVYKGKLKGKGGKKKVEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEP--LYI 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061   955 IMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIEtDKEY 1034
Cdd:smart00219   79 VMEYMEGGDLLSYLRKNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLY-DDDY 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  1035 YTVKDDRdSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSDsspmalflkmigptHGQMTVTRLVNTLKEGKRL 1114
Cdd:smart00219  158 YRKRGGK-LPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEQP--------------YPGMSNEEVLEYLKNGYRL 222
                           250       260       270
                    ....*....|....*....|....*....|....*
gi 1013071061  1115 PCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGF 1149
Cdd:smart00219  223 PQPPNCPPELYDLMLQCWAEDPEDRPTFSELVEIL 257
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
583-845 1.64e-86

Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyze the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyze the reverse process. Protein kinases fall into three broad classes, characterized with respect to substrate specificity; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 280.54  E-value: 1.64e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  583 LVQGEHLGRGTRTHIYSGTLMDYKddegtsEEKKIKVILKVLDPSHRDISL-AFFEAASMMRQVSHKHIVYLYGVCVRDV 661
Cdd:pfam07714    1 LTLGEKLGEGAFGEVYKGTLKGEG------ENTKIKVAVKTLKEGADEEEReDFLEEASIMKKLDHPNIVKLLGVCTQGE 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  662 ENIMVEEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLARegidsecGPFIKLSDPG 741
Cdd:pfam07714   75 PLYIVTEYMPGGDLLDFLRKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSE-------NLVVKISDFG 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  742 IPITVLS------RQECIERIPWIAPECVEDSKnLSVAADKWSFGTTLWEICYNGEIPLKDKTLIEKERFYESRCRPVTP 815
Cdd:pfam07714  148 LSRDIYDddyyrkRGGGKLPIKWMAPESLKDGK-FTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEFLEDGYRLPQP 226
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1013071061  816 --SCKELADLMTRCMNYDPNQRPFFRAIMRDI 845
Cdd:pfam07714  227 enCPDELYDLMKQCWAYDPEDRPTFSELVEDL 258
FERM_C_JAK1 cd13332
FERM domain C-lobe of Janus kinase 1; JAK1 is a tyrosine kinase protein essential in signaling ...
282-426 7.67e-80

FERM domain C-lobe of Janus kinase 1; JAK1 is a tyrosine kinase protein essential in signaling type I and type II cytokines. It interacts with the gamma chain of type I cytokine receptors to elicit signals from the IL-2 receptor family, the IL-4 receptor family, the gp130 receptor family, ciliary neurotrophic factor receptor (CNTF-R), neurotrophin-1 receptor (NNT-1R) and Leptin-R). It also is involved in transducing a signal by type I (IFN-alpha/beta) and type II (IFN-gamma) interferons, and members of the IL-10 family via type II cytokine receptors. JAK (also called Just Another Kinase) is a family of intracellular, non-receptor tyrosine kinases that transduce cytokine-mediated signals via the JAK-STAT pathway. The JAK family in mammals consists of 4 members: JAK1, JAK2, JAK3 and TYK2. JAKs are composed of seven JAK homology (JH) domains (JH1-JH7) . The C-terminal JH1 domain is the main catalytic domain, followed by JH2, which is often referred to as a pseudokinase domain, followed by JH3-JH4 which is homologous to the SH2 domain, and lastly JH5-JH7 which is a FERM domain. Named after Janus, the two-faced Roman god of doorways, JAKs possess two near-identical phosphate-transferring domains; one which displays the kinase activity (JH1), while the other negatively regulates the kinase activity of the first (JH2). The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 275412  Cd Length: 144  Bit Score: 257.47  E-value: 7.67e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  282 GAEIFETSMLLISSENEMNWFHSNDGGNVLYYEVMVTGNLGIQWRHKPNVVSVEKEKNKLKRKKLeNKHKKDEEKNKIRE 361
Cdd:cd13332      1 GAEIFETSSLLISSESELNNFNMGDGGNYGYYEVSVTGNTGISWRRKPATTAVEKKKKGKSKKNK-LKGKKDEDKKKARE 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1013071061  362 EWNNFSYFPEITHIVIKESVVSINKQDNKKMELKLSSHEEALSFVSLVDGYFRLTADAHHYLCTD 426
Cdd:cd13332     80 GWNNFSYFPEITHIVIKESTVTINRQDNKKMELKLSSRDEALSFAALVDGYFRLTADAHHYLCTD 144
FERM_F2 pfam18377
FERM F2 acyl-CoA binding protein-like domain; This is an F2 lobe domain consisting of an ...
147-277 3.11e-73

FERM F2 acyl-CoA binding protein-like domain; This is an F2 lobe domain consisting of an acyl-CoA binding protein fold found in FERM region of Jak-family tyrosine kinases. Multidomain JAK molecules interact with receptors through their FERM and SH2-like domains, triggering a series of phosphorylation events, resulting in the activation of their kinase domains. Overall, the FERM region maintains the typical three-lobed architecture, with an F1 lobe consisting of a ubiquitin-like fold, an F2 lobe consisting of an acyl-CoA binding protein fold, and an F3 lobe consisting of a pleckstrin-homology (PH) fold. JAK1 FERM-F2 domain has been shown to act as the interaction site for the IFNLR1 box1 motif (PxxLxF) of class II cytokine receptors which is essential for kinase activation.


Pssm-ID: 436450  Cd Length: 131  Bit Score: 238.69  E-value: 3.11e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  147 TPLLDASSLEYLFAQGQYDLVKCLAPIRDPKTEQDGHDIENECLGMAVLAISHYAMMKKMQLPELPKDISYKRYIPETLN 226
Cdd:pfam18377    1 SPLLDAPSLEYLFAQGKYDFVNGLAPLRDSQSEQETHRIENECLGMAVLDLSHLAKEKGLSLEEIAKKVSYKRCIPESFR 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1013071061  227 KSIRQRNLLTRMRINNVFKDFLKEFNNKTICDSSVSTHDLKVKYLATLETL 277
Cdd:pfam18377   81 RQIQQRNFLTRKRIRNVFKRFLREFNQHTVGDCKLTAHDLKLKYLSTLETL 131
Jak1_Phl pfam17887
Jak1 pleckstrin homology-like domain; This entry is for the pleckstrin homology-like (PHL) ...
284-421 2.31e-72

Jak1 pleckstrin homology-like domain; This entry is for the pleckstrin homology-like (PHL) subdomain found in Jak1 proteins. JAK1 is a member of the Janus kinase (JAK) family of non-receptor tyrosine kinases that are activated in response to cytokines and interferons. PHL (residues 283-419) together with the N-terminal ubiquitin-like subdomain (residues 36-111) and an acyl-coenzyme A binding protein-like subdomain (residues 148-282), associate into a canonical tri-lobed FERM domain.


Pssm-ID: 465552  Cd Length: 140  Bit Score: 236.45  E-value: 2.31e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  284 EIFETSMLLISSENEMNWFHSNDGGNVLYYEVMVTGNLGIQWRHKPNVVSVEKEKNKLKRKKL--ENKHKKDEEKNKIRE 361
Cdd:pfam17887    1 EAEETPCYIIDSENEPNDPNPEDADGPPTHEVLVTGTGGIQWRPKPVESSSRNPKAKLKGKKKkaESKAKKQPAKRKLEP 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  362 EWNNFSYFPEITHIVIKESVVSINKQDNKKMELKLSSHEEALSFVSLVDGYFRLTADAHH 421
Cdd:pfam17887   81 PWAYFCDFQEITHIVIKESTVSIHRQDNKCLELKLPSHAEALSFVSLVDGYFRLTADSSH 140
SH2_Jak1 cd10378
Src homology 2 (SH2) domain in the Janus kinase 1 (Jak1) proteins; Janus kinase 1 (JAK1), is a ...
426-527 3.34e-64

Src homology 2 (SH2) domain in the Janus kinase 1 (Jak1) proteins; Janus kinase 1 (JAK1), is a member of a class of protein-tyrosine kinases (PTK) characterized by the presence of a second phosphotransferase-related domain immediately N-terminal to the PTK domain. The second phosphotransferase domain bears all the hallmarks of a protein kinase, although its structure differs significantly from that of the PTK and threonine/serine kinase family members. JAK1 is a large, widely expressed membrane-associated phosphoprotein. JAK1 is involved in the interferon-alpha/beta and -gamma signal transduction pathways. The reciprocal interdependence between JAK1 and TYK2 activities in the interferon-alpha pathway, and between JAK1 and JAK2 in the interferon-gamma pathway, may reflect a requirement for these kinases in the correct assembly of interferon receptor complexes. These kinases couple cytokine ligand binding to tyrosine phosphorylation of various known signaling proteins and of a unique family of transcription factors termed the signal transducers and activators of transcription, or STATs. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198241  Cd Length: 102  Bit Score: 212.02  E-value: 3.34e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  426 DVAPPLIVHNIQNGCHGPICTEYAINKLRQEGSEEGMYVLRWSCTDFDNILMTVTCFEKSEQVQGAQKQFKNFQIEVQKG 505
Cdd:cd10378      1 DVAPPLIVHNIKNGCHGPICTEYAINKLRQEGNEEGMYVLRWSCTDFNNILMTVTCIELSECESRPVKQYKNFQIEVKKG 80
                           90       100
                   ....*....|....*....|..
gi 1013071061  506 RYSLHGSDRSFPSLGDLMSHLK 527
Cdd:cd10378     81 GYSLHGSDTFFPSLKELMEHLK 102
FERM_F1 pfam18379
FERM F1 ubiquitin-like domain; This is an F1 lobe domain consisting of a ubiquitin like fold ...
36-129 4.36e-41

FERM F1 ubiquitin-like domain; This is an F1 lobe domain consisting of a ubiquitin like fold found in FERM region of Jak-family tyrosine kinases. Multidomain JAK molecules interact with receptors through their FERM and SH2-like domains, triggering a series of phosphorylation events, resulting in the activation of their kinase domains. Overall, the FERM region maintains the typical three-lobed architecture, with an F1 lobe consisting of a ubiquitin-like fold, an F2 lobe consisting of an acyl-CoA binding protein fold, and an F3 lobe consisting of a pleckstrin-homology (PH) fold.


Pssm-ID: 465733  Cd Length: 96  Bit Score: 146.16  E-value: 4.36e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061   36 VEVIFYLSDRE----PLRLGSGEYTAEELCIRAAQACRISPLCHNLFALYDENTKLWYAPNRTITVDDKMSLRLHYRMRF 111
Cdd:pfam18379    1 LQVHLYWSGPGdgetYLSYPPGEYTAEELCIDAAKACGITPVYHNLFALYDEDDRVWYPPNHVFHIDESTSLTLHFRIRF 80
                           90
                   ....*....|....*...
gi 1013071061  112 YFTNWHGTNDNEQsvWRH 129
Cdd:pfam18379   81 YFPNWHGLGESEP--YRY 96
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
589-845 4.21e-40

Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 149.22  E-value: 4.21e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061   589 LGRGTRTHIYSGTLmdykddEGTSEEKKIKVILKVLDPSHRDISLA-FFEAASMMRQVSHKHIVYLYGVCvRDVENIM-V 666
Cdd:smart00219    7 LGEGAFGEVYKGKL------KGKGGKKKVEVAVKTLKEDASEQQIEeFLREARIMRKLDHPNVVKLLGVC-TEEEPLYiV 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061   667 EEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGipitv 746
Cdd:smart00219   80 MEYMEGGDLLSYLRKNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLV-------VKISDFG----- 147
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061   747 LSRQ--------ECIERIP--WIAPECVEDSKnLSVAADKWSFGTTLWEICYNGEIP---LKDKTLIEKERFYESRCRPv 813
Cdd:smart00219  148 LSRDlydddyyrKRGGKLPirWMAPESLKEGK-FTSKSDVWSFGVLLWEIFTLGEQPypgMSNEEVLEYLKNGYRLPQP- 225
                           250       260       270
                    ....*....|....*....|....*....|...
gi 1013071061   814 tPSC-KELADLMTRCMNYDPNQRPFFRAIMRDI 845
Cdd:smart00219  226 -PNCpPELYDLMLQCWAEDPEDRPTFSELVEIL 257
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
37-286 1.18e-33

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 128.57  E-value: 1.18e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061    37 EVIFYLSDREPLRLGSG-EYTAEELCIRAAQACRIspLCHNLFALYDENTKL----WYAPNRTITVDDKMS--LRLHYRM 109
Cdd:smart00295    1 VLKVYLLDGTTLEFEVDsSTTAEELLETVCRKLGI--RESEYFGLQFEDPDEdlrhWLDPAKTLLDQDVKSepLTLYFRV 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061   110 RFYFTNwhgtndneqsvwrhspkkqkngyekkkipDATPLLDASSLEYLFAQGQYDLVKCLAPIRdpkteqdghdiENEC 189
Cdd:smart00295   79 KFYPPD-----------------------------PNQLKEDPTRLNLLYLQVRNDILEGRLPCP-----------EEEA 118
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061   190 LGMAVLAISHYAMMKKMQLPELPKDISYKRYIPETLNKSirQRNLLTRMRINNVFKDFlkefnnkticdSSVSTHDLKVK 269
Cdd:smart00295  119 LLLAALALQAEFGDYDEELHDLRGELSLKRFLPKQLLDS--RKLKEWRERIVELHKEL-----------IGLSPEEAKLK 185
                           250
                    ....*....|....*..
gi 1013071061   270 YLATLETLTkHYGAEIF 286
Cdd:smart00295  186 YLELARKLP-TYGVELF 201
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
878-1152 4.59e-33

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 134.76  E-value: 4.59e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVELCRyDPEgdnTGEQVAVKSLKPESGGNH--IADLKKEIEILRNLYHENIVKYKGICTEDGGngIKLI 955
Cdd:COG0515     12 LRLLGRGGMGVVYLAR-DLR---LGRPVALKVLRPELAADPeaRERFRREARALARLNHPNIVRVYDVGEEDGR--PYLV 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  956 MEFLPSGSLKEYLpKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYy 1035
Cdd:COG0515     86 MEYVEGESLADLL-RRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATLT- 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1036 tvkddRDSPVFW---Y-APECLMQSKFYIASDVWSFGVTLHELLT----YcdSDSSPMALFLKMIgptHGQMTVTRLVNt 1107
Cdd:COG0515    164 -----QTGTVVGtpgYmAPEQARGEPVDPRSDVYSLGVTLYELLTgrppF--DGDSPAELLRAHL---REPPPPPSELR- 232
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1013071061 1108 lkegkrlpcpPNCPDEVYQLMRKCWEFQPSNRtsFQNLIEGFEAL 1152
Cdd:COG0515    233 ----------PDLPPALDAIVLRALAKDPEER--YQSAAELAAAL 265
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
872-1076 5.60e-21

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 95.60  E-value: 5.60e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  872 KRFLKRIRDLGEGHFGKVELCrYDpegDNTGEQVAVKSLKPESGGNHIADLK-------------KEIEILRNLYHENIV 938
Cdd:PTZ00024     8 ERYIQKGAHLGEGTYGKVEKA-YD---TLTGKIVAIKKVKIIEISNDVTKDRqlvgmcgihfttlRELKIMNEIKHENIM 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  939 KYKGICTEdgGNGIKLIMEFLpSGSLKEYLpknKNKINLKQQLKYAV--QICKGMDYLGSRQYVHRDLAARNVLVESEHQ 1016
Cdd:PTZ00024    84 GLVDVYVE--GDFINLVMDIM-ASDLKKVV---DRKIRLTESQVKCIllQILNGLNVLHKWYFMHRDLSPANIFINSKGI 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1013071061 1017 VKIGDFGLTKAI--------ETDKEYYTVKDDRDSPV--FWY-APECLMQS-KFYIASDVWSFGVTLHELLT 1076
Cdd:PTZ00024   158 CKIADFGLARRYgyppysdtLSKDETMQRREEMTSKVvtLWYrAPELLMGAeKYHFAVDMWSVGCIFAELLT 229
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
587-836 7.34e-18

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 88.15  E-value: 7.34e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  587 EHLGRGTRTHIYSGTlmdykdDEGTSEEkkikVILKVLDPSHR---DISLAFFEAASMMRQVSHKHIVYLYGVCVRDVEN 663
Cdd:COG0515     13 RLLGRGGMGVVYLAR------DLRLGRP----VALKVLRPELAadpEARERFRREARALARLNHPNIVRVYDVGEEDGRP 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  664 IMVEEFVEGGPLDLFMHRKSdVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGidsecgpFIKLSDPGIp 743
Cdd:COG0515     83 YLVMEYVEGESLADLLRRRG-PLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDG-------RVKLIDFGI- 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  744 ITVLSRQECIER------IPWIAPECVEDSKnLSVAADKWSFGTTLWEICYnGEIPLKDKTLIE-------KERFYESRC 810
Cdd:COG0515    154 ARALGGATLTQTgtvvgtPGYMAPEQARGEP-VDPRSDVYSLGVTLYELLT-GRPPFDGDSPAEllrahlrEPPPPPSEL 231
                          250       260
                   ....*....|....*....|....*.
gi 1013071061  811 RPVTPSckELADLMTRCMNYDPNQRP 836
Cdd:COG0515    232 RPDLPP--ALDAIVLRALAKDPEERY 255
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
902-1076 1.33e-09

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 62.12  E-value: 1.33e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  902 GEQVAVKSLKPESGGNHIAdlkkeieILR---------NLYHENIVK-YK-GictEDGGNGIkLIMEFLPSGSLKEYLpK 970
Cdd:NF033483    32 DRDVAVKVLRPDLARDPEF-------VARfrreaqsaaSLSHPNIVSvYDvG---EDGGIPY-IVMEYVDGRTLKDYI-R 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  971 NKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAI------ETDKEYYTVKddrdsp 1044
Cdd:NF033483   100 EHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIARALssttmtQTNSVLGTVH------ 173
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1013071061 1045 vfwY-APEclmQSKFYIA---SDVWSFGVTLHELLT 1076
Cdd:NF033483   174 ---YlSPE---QARGGTVdarSDIYSLGIVLYEMLT 203
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
586-786 4.19e-07

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 53.89  E-value: 4.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  586 GEHLGRGTRTHIYSGTLMDykddegTSEEKKIKVILKvlDPSHRDISLAffeaasMMRQVSHKHIVYL----YGVCVRDV 661
Cdd:PTZ00036    71 GNIIGNGSFGVVYEAICID------TSEKVAIKKVLQ--DPQYKNRELL------IMKNLNHINIIFLkdyyYTECFKKN 136
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  662 E-NI---MVEEFVEGGPLDLFMHRKSDVLTTPWkFKV---AKQLASALSYLEDKDLVHGNVCTKNLLlaregIDSECGPf 734
Cdd:PTZ00036   137 EkNIflnVVMEFIPQTVHKYMKHYARNNHALPL-FLVklySYQLCRALAYIHSKFICHRDLKPQNLL-----IDPNTHT- 209
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1013071061  735 IKLSDPGIPITVLSRQECIERIP---WIAPECVEDSKNLSVAADKWSFGTTLWEI 786
Cdd:PTZ00036   210 LKLCDFGSAKNLLAGQRSVSYICsrfYRAPELMLGATNYTTHIDLWSLGCIIAEM 264
 
Name Accession Description Interval E-value
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
870-1153 0e+00

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 626.19  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  870 FEKRFLKRIRDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGG 949
Cdd:cd05079      1 FEKRFLKRIRDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  950 NGIKLIMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIE 1029
Cdd:cd05079     81 NGIKLIMEFLPSGSLKEYLPRNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIE 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1030 TDKEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSDSSPMALFLKMIGPTHGQMTVTRLVNTLK 1109
Cdd:cd05079    161 TDKEYYTVKDDLDSPVFWYAPECLIQSKFYIASDVWSFGVTLYELLTYCDSESSPMTLFLKMIGPTHGQMTVTRLVRVLE 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1013071061 1110 EGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALL 1153
Cdd:cd05079    241 EGKRLPRPPNCPEEVYQLMRKCWEFQPSKRTTFQNLIEGFEAIL 284
PTK_Jak1_rpt1 cd05077
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely ...
583-846 0e+00

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits, common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270662 [Multi-domain]  Cd Length: 266  Bit Score: 576.12  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  583 LVQGEHLGRGTRTHIYSGTLMDYKDD--EGTSEEKKIKVILKVLDPSHRDISLAFFEAASMMRQVSHKHIVYLYGVCVRD 660
Cdd:cd05077      1 IVQGEHLGRGTRTQIYAGILNYKDDDedEGYSYEKEIKVILKVLDPSHRDISLAFFETASMMRQVSHKHIVLLYGVCVRD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  661 VENIMVEEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIDSECGPFIKLSDP 740
Cdd:cd05077     81 VENIMVEEFVEFGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNILLAREGIDGECGPFIKLSDP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  741 GIPITVLSRQECIERIPWIAPECVEDSKNLSVAADKWSFGTTLWEICYNGEIPLKDKTLIEKERFYESRCRPVTPSCKEL 820
Cdd:cd05077    161 GIPITVLSRQECVERIPWIAPECVEDSKNLSIAADKWSFGTTLWEICYNGEIPLKDKTLAEKERFYEGQCMLVTPSCKEL 240
                          250       260
                   ....*....|....*....|....*.
gi 1013071061  821 ADLMTRCMNYDPNQRPFFRAIMRDIN 846
Cdd:cd05077    241 ADLMTHCMNYDPNQRPFFRAIMRDIN 266
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
870-1153 2.61e-180

Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are PTKs, catalyzing the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jaks are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 528.88  E-value: 2.61e-180
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  870 FEKRFLKRIRDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGG 949
Cdd:cd05038      1 FEERHLKFIKQLGEGHFGSVELCRYDPLGDNTGEQVAVKSLQPSGEEQHMSDFKREIEILRTLDHEYIVKYKGVCESPGR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  950 NGIKLIMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIE 1029
Cdd:cd05038     81 RSLRLIMEYLPSGSLRDYLQRHRDQIDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGLAKVLP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1030 TDKEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSDSSPMALFLKMIGPTHGQMTVTRLVNTLK 1109
Cdd:cd05038    161 EDKEYYYVKEPGESPIFWYAPECLRESRFSSASDVWSFGVTLYELFTYGDPSQSPPALFLRMIGIAQGQMIVTRLLELLK 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1013071061 1110 EGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALL 1153
Cdd:cd05038    241 SGERLPRPPSCPDEVYDLMKECWEYEPQDRPSFSDLILIIDRLR 284
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
870-1152 6.00e-134

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Tyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 408.13  E-value: 6.00e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  870 FEKRFLKRIRDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGG 949
Cdd:cd05080      1 FHKRYLKKIRDLGEGHFGKVSLYCYDPTNDGTGEMVAVKALKADCGPQHRSGWKQEIDILKTLYHENIVKYKGCCSEQGG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  950 NGIKLIMEFLPSGSLKEYLPKNKnkINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIE 1029
Cdd:cd05080     81 KSLQLIMEYVPLGSLRDYLPKHS--IGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAKAVP 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1030 TDKEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSDSSPMALFLKMIGPTHGQMTVTRLVNTLK 1109
Cdd:cd05080    159 EGHEYYRVREDGDSPVFWYAPECLKEYKFYYASDVWSFGVTLYELLTHCDSSQSPPTKFLEMIGIAQGQMTVVRLIELLE 238
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1013071061 1110 EGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEAL 1152
Cdd:cd05080    239 RGERLPCPDKCPQEVYHLMKNCWETEASFRPTFENLIPILKTV 281
PTK_Tyk2_rpt1 cd05076
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; Tyk2 is ...
583-845 2.29e-126

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. The Tyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270661 [Multi-domain]  Cd Length: 273  Bit Score: 388.11  E-value: 2.29e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  583 LVQGEHLGRGTRTHIYSGTLM---------DYKDDEGTSEEKKIKVILKVLDPSHRDISLAFFEAASMMRQVSHKHIVYL 653
Cdd:cd05076      1 ITQLSHLGQGTRTNIYEGRLLvegsgepeeDKELVPGRDRGQELRVVLKVLDPSHHDIALAFFETASLMSQVSHTHLVFV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  654 YGVCVRDVENIMVEEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIDSECGP 733
Cdd:cd05076     81 HGVCVRGSENIMVEEFVEHGPLDVWLRKEKGHVPMAWKFVVARQLASALSYLENKNLVHGNVCAKNILLARLGLEEGTSP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  734 FIKLSDPGIPITVLSRQECIERIPWIAPECVEDSKNLSVAADKWSFGTTLWEICYNGEIPLKDKTLIEKERFYESRCRPV 813
Cdd:cd05076    161 FIKLSDPGVGLGVLSREERVERIPWIAPECVPGGNSLSTAADKWGFGATLLEICFNGEAPLQSRTPSEKERFYQRQHRLP 240
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1013071061  814 TPSCKELADLMTRCMNYDPNQRPFFRAIMRDI 845
Cdd:cd05076    241 EPSCPELATLISQCLTYEPTQRPSFRTILRDL 272
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
583-846 1.02e-125

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. In the case of Jak2, the presumed pseudokinase (repeat 1) domain exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270633 [Multi-domain]  Cd Length: 259  Bit Score: 385.68  E-value: 1.02e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  583 LVQGEHLGRGTRTHIYSGTLMDYKDDEGtseeKKIKVILKVLDPSHRDISLAFFEAASMMRQVSHKHIVYLYGVCVRDvE 662
Cdd:cd05037      1 ITFHEHLGQGTFTNIYDGILREVGDGRV----QEVEVLLKVLDSDHRDISESFFETASLMSQISHKHLVKLYGVCVAD-E 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  663 NIMVEEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIDSEcGPFIKLSDPGI 742
Cdd:cd05037     76 NIMVQEYVRYGPLDKYLRRMGNNVPLSWKLQVAKQLASALHYLEDKKLIHGNVRGRNILLAREGLDGY-PPFIKLSDPGV 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  743 PITVLSRQECIERIPWIAPECVE-DSKNLSVAADKWSFGTTLWEICYNGEIPLKDKTLIEKERFYESRCRPVTPSCKELA 821
Cdd:cd05037    155 PITVLSREERVDRIPWIAPECLRnLQANLTIAADKWSFGTTLWEICSGGEEPLSALSSQEKLQFYEDQHQLPAPDCAELA 234
                          250       260
                   ....*....|....*....|....*
gi 1013071061  822 DLMTRCMNYDPNQRPFFRAIMRDIN 846
Cdd:cd05037    235 ELIMQCWTYEPTKRPSFRAILRDLN 259
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
870-1152 8.77e-123

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 378.85  E-value: 8.77e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  870 FEKRFLKRIRDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKpESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGG 949
Cdd:cd05081      1 FEERHLKYISQLGKGNFGSVELCRYDPLGDNTGALVAVKQLQ-HSGPDQQRDFQREIQILKALHSDFIVKYRGVSYGPGR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  950 NGIKLIMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIE 1029
Cdd:cd05081     80 RSLRLVMEYLPSGCLRDFLQRHRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKLLP 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1030 TDKEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSDSSPMALFLKMIGPTHGQMTVTRLVNTLK 1109
Cdd:cd05081    160 LDKDYYVVREPGQSPIFWYAPESLSDNIFSRQSDVWSFGVVLYELFTYCDKSCSPSAEFLRMMGCERDVPALCRLLELLE 239
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1013071061 1110 EGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEAL 1152
Cdd:cd05081    240 EGQRLPAPPACPAEVHELMKLCWAPSPQDRPSFSALGPQLDML 282
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
870-1145 1.26e-121

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak2 is widely expressed in many tissues and is essential for the signaling of hormone-like cytokines such as growth hormone, erythropoietin, thrombopoietin, and prolactin, as well as some IFNs and cytokines that signal through the IL-3 and gp130 receptors. Disruption of Jak2 in mice results in an embryonic lethal phenotype with multiple defects including erythropoietic and cardiac abnormalities. It is the only Jak gene that results in a lethal phenotype when disrupted in mice. A mutation in the pseudokinase domain of Jak2, V617F, is present in many myeloproliferative diseases, including almost all patients with polycythemia vera, and 50% of patients with essential thrombocytosis and myelofibrosis. Jak2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 375.89  E-value: 1.26e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  870 FEKRFLKRIRDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKpESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGG 949
Cdd:cd14205      1 FEERHLKFLQQLGKGNFGSVEMCRYDPLQDNTGEVVAVKKLQ-HSTEEHLRDFEREIEILKSLQHDNIVKYKGVCYSAGR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  950 NGIKLIMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIE 1029
Cdd:cd14205     80 RNLRLIMEYLPYGSLRDYLQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLP 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1030 TDKEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSDSSPMALFLKMIG-PTHGQMTVTRLVNTL 1108
Cdd:cd14205    160 QDKEYYKVKEPGESPIFWYAPESLTESKFSVASDVWSFGVVLYELFTYIEKSKSPPAEFMRMIGnDKQGQMIVFHLIELL 239
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1013071061 1109 KEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNL 1145
Cdd:cd14205    240 KNNGRLPRPDGCPDEIYMIMTECWNNNVNQRPSFRDL 276
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
875-1147 2.26e-115

Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyze the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyze the reverse process. Protein kinases fall into three broad classes, characterized with respect to substrate specificity; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 358.35  E-value: 2.26e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  875 LKRIRDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGngIKL 954
Cdd:pfam07714    1 LTLGEKLGEGAFGEVYKGTLKGEGENTKIKVAVKTLKEGADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEP--LYI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIEtDKEY 1034
Cdd:pfam07714   79 VTEYMPGGDLLDFLRKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDIY-DDDY 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1035 YTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDsdsSPmalflkmigptHGQMTVTRLVNTLKEGKRL 1114
Cdd:pfam07714  158 YRKRGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLGE---QP-----------YPGMSNEEVLEFLEDGYRL 223
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1013071061 1115 PCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIE 1147
Cdd:pfam07714  224 PQPENCPDELYDLMKQCWAYDPEDRPTFSELVE 256
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
875-1149 9.00e-115

Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 356.46  E-value: 9.00e-115
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061   875 LKRIRDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGngIKL 954
Cdd:smart00219    1 LTLGKKLGEGAFGEVYKGKLKGKGGKKKVEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEP--LYI 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061   955 IMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIEtDKEY 1034
Cdd:smart00219   79 VMEYMEGGDLLSYLRKNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLY-DDDY 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  1035 YTVKDDRdSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSDsspmalflkmigptHGQMTVTRLVNTLKEGKRL 1114
Cdd:smart00219  158 YRKRGGK-LPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEQP--------------YPGMSNEEVLEYLKNGYRL 222
                           250       260       270
                    ....*....|....*....|....*....|....*
gi 1013071061  1115 PCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGF 1149
Cdd:smart00219  223 PQPPNCPPELYDLMLQCWAEDPEDRPTFSELVEIL 257
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
875-1149 2.67e-112

Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase.


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 349.93  E-value: 2.67e-112
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061   875 LKRIRDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGngIKL 954
Cdd:smart00221    1 LTLGKKLGEGAFGEVYKGTLKGKGDGKEVEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEP--LMI 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061   955 IMEFLPSGSLKEYLPKNKNK-INLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIEtDKE 1033
Cdd:smart00221   79 VMEYMPGGDLLDYLRKNRPKeLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLY-DDD 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  1034 YYTVKDDRdSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSDsspmalflkmigptHGQMTVTRLVNTLKEGKR 1113
Cdd:smart00221  158 YYKVKGGK-LPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEEP--------------YPGMSNAEVLEYLKKGYR 222
                           250       260       270
                    ....*....|....*....|....*....|....*.
gi 1013071061  1114 LPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGF 1149
Cdd:smart00221  223 LPKPPNCPPELYKLMLQCWAEDPEDRPTFSELVEIL 258
PTK_Jak2_rpt1 cd05078
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely ...
583-846 5.54e-97

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely expressed in many tissues. It is essential for the signaling of hormone-like cytokines such as growth hormone, erythropoietin, thrombopoietin, and prolactin, as well as some IFNs and cytokines that signal through the IL-3 and gp130 receptors. Disruption of Jak2 in mice results in an embryonic lethal phenotype with multiple defects including erythropoietic and cardiac abnormalities. It is the only Jak gene that results in a lethal phenotype when disrupted in mice. A mutation in the pseudokinase domain of Jak2, V617F, is present in many myeloproliferative diseases, including almost all patients with polycythemia vera, and 50% of patients with essential thrombocytosis and myelofibrosis. Jak2 is a cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Despite this, the presumed pseudokinase (repeat 1) domain of Jak2 exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. Inactivation of the repeat 1 domain increased Jak2 basal activity, suggesting that it modulates the kinase activity of the C-terminal catalytic (repeat 2) domain. The Jak2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270663 [Multi-domain]  Cd Length: 262  Bit Score: 309.19  E-value: 5.54e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  583 LVQGEHLGRGTRTHIYSGTLMDYKDdegTSEEKKIKVILKVLDPSHRDISLAFFEAASMMRQVSHKHIVYLYGVCVRDVE 662
Cdd:cd05078      1 LIFNESLGQGTFTKIFKGIRREVGD---YGQLHETEVLLKVLDKAHRNYSESFFEAASMMSQLSHKHLVLNYGVCVCGDE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  663 NIMVEEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGiDSECG--PFIKLSDP 740
Cdd:cd05078     78 NILVQEYVKFGSLDTYLKKNKNCINILWKLEVAKQLAWAMHFLEEKTLVHGNVCAKNILLIREE-DRKTGnpPFIKLSDP 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  741 GIPITVLSRQECIERIPWIAPECVEDSKNLSVAADKWSFGTTLWEICYNGEIPLKDKTLIEKERFYESRCRPVTPSCKEL 820
Cdd:cd05078    157 GISITVLPKDILLERIPWVPPECIENPKNLSLATDKWSFGTTLWEICSGGDKPLSALDSQRKLQFYEDRHQLPAPKWTEL 236
                          250       260
                   ....*....|....*....|....*.
gi 1013071061  821 ADLMTRCMNYDPNQRPFFRAIMRDIN 846
Cdd:cd05078    237 ANLINNCMDYEPDHRPSFRAIIRDLN 262
PTK_Jak3_rpt1 cd14208
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is ...
583-846 1.46e-93

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit, common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. Jaks are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271110 [Multi-domain]  Cd Length: 260  Bit Score: 299.90  E-value: 1.46e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  583 LVQGEHLGRGTRTHIYSGTLMDYKDDEgtseEKKIKVILKVLDPSHRDISLAFFEAASMMRQVSHKHIVYLYGVCVRDvE 662
Cdd:cd14208      1 LTFMESLGKGSFTKIYRGLRTDEEDDE----RCETEVLLKVMDPTHGNCQESFLEAASIMSQISHKHLVLLHGVCVGK-D 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  663 NIMVEEFVEGGPLDLFMHRK--SDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIDSEcGPFIKLSDP 740
Cdd:cd14208     76 SIMVQEFVCHGALDLYLKKQqqKGPVAISWKLQVVKQLAYALNYLEDKQLVHGNVSAKKVLLSREGDKGS-PPFIKLSDP 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  741 GIPITVLSRQECIERIPWIAPECVEDSKNLSVAADKWSFGTTLWEICYNGEIPLKDKTLIEKERFYESRCRPVTPSCKEL 820
Cdd:cd14208    155 GVSIKVLDEELLAERIPWVAPECLSDPQNLALEADKWGFGATLWEIFSGGHMPLSALDPSKKLQFYNDRKQLPAPHWIEL 234
                          250       260
                   ....*....|....*....|....*.
gi 1013071061  821 ADLMTRCMNYDPNQRPFFRAIMRDIN 846
Cdd:cd14208    235 ASLIQQCMSYNPLLRPSFRAIIRDLN 260
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
881-1150 5.02e-93

Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. They can be classified into receptor and non-receptor tyr kinases. PTKs play important roles in many cellular processes including, lymphocyte activation, epithelium growth and maintenance, metabolism control, organogenesis regulation, survival, proliferation, differentiation, migration, adhesion, motility, and morphogenesis. Receptor tyr kinases (RTKs) are integral membrane proteins which contain an extracellular ligand-binding region, a transmembrane segment, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain, leading to intracellular signaling. Some RTKs are orphan receptors with no known ligands. Non-receptor (or cytoplasmic) tyr kinases are distributed in different intracellular compartments and are usually multi-domain proteins containing a catalytic tyr kinase domain as well as various regulatory domains such as SH3 and SH2. PTKs are usually autoinhibited and require a mechanism for activation. In many PTKs, the phosphorylation of tyr residues in the activation loop is essential for optimal activity. Aberrant expression of PTKs is associated with many development abnormalities and cancers.The PTK family is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270623 [Multi-domain]  Cd Length: 262  Bit Score: 298.30  E-value: 5.02e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDPeGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGngIKLIMEFLP 960
Cdd:cd00192      3 LGEGAFGEVYKGKLKG-GDGKTVDVAVKTLKEDASESERKDFLKEARVMKKLGHPNVVRLLGVCTEEEP--LYLVMEYME 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  961 SGSLKEYLPKNKNK--------INLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIEtDK 1032
Cdd:cd00192     80 GGDLLDFLRKSRPVfpspepstLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLSRDIY-DD 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1033 EYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCdsdSSPmalflkmigptHGQMTVTRLVNTLKEGK 1112
Cdd:cd00192    159 DYYRKKTGGKLPIRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTLG---ATP-----------YPGLSNEEVLEYLRKGY 224
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1013071061 1113 RLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFE 1150
Cdd:cd00192    225 RLPKPENCPDELYELMLSCWQLDPEDRPTFSELVERLE 262
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
583-845 1.64e-86

Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyze the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyze the reverse process. Protein kinases fall into three broad classes, characterized with respect to substrate specificity; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 280.54  E-value: 1.64e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  583 LVQGEHLGRGTRTHIYSGTLMDYKddegtsEEKKIKVILKVLDPSHRDISL-AFFEAASMMRQVSHKHIVYLYGVCVRDV 661
Cdd:pfam07714    1 LTLGEKLGEGAFGEVYKGTLKGEG------ENTKIKVAVKTLKEGADEEEReDFLEEASIMKKLDHPNIVKLLGVCTQGE 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  662 ENIMVEEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLARegidsecGPFIKLSDPG 741
Cdd:pfam07714   75 PLYIVTEYMPGGDLLDFLRKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSE-------NLVVKISDFG 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  742 IPITVLS------RQECIERIPWIAPECVEDSKnLSVAADKWSFGTTLWEICYNGEIPLKDKTLIEKERFYESRCRPVTP 815
Cdd:pfam07714  148 LSRDIYDddyyrkRGGGKLPIKWMAPESLKDGK-FTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEFLEDGYRLPQP 226
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1013071061  816 --SCKELADLMTRCMNYDPNQRPFFRAIMRDI 845
Cdd:pfam07714  227 enCPDELYDLMKQCWAYDPEDRPTFSELVEDL 258
FERM_C_JAK1 cd13332
FERM domain C-lobe of Janus kinase 1; JAK1 is a tyrosine kinase protein essential in signaling ...
282-426 7.67e-80

FERM domain C-lobe of Janus kinase 1; JAK1 is a tyrosine kinase protein essential in signaling type I and type II cytokines. It interacts with the gamma chain of type I cytokine receptors to elicit signals from the IL-2 receptor family, the IL-4 receptor family, the gp130 receptor family, ciliary neurotrophic factor receptor (CNTF-R), neurotrophin-1 receptor (NNT-1R) and Leptin-R). It also is involved in transducing a signal by type I (IFN-alpha/beta) and type II (IFN-gamma) interferons, and members of the IL-10 family via type II cytokine receptors. JAK (also called Just Another Kinase) is a family of intracellular, non-receptor tyrosine kinases that transduce cytokine-mediated signals via the JAK-STAT pathway. The JAK family in mammals consists of 4 members: JAK1, JAK2, JAK3 and TYK2. JAKs are composed of seven JAK homology (JH) domains (JH1-JH7) . The C-terminal JH1 domain is the main catalytic domain, followed by JH2, which is often referred to as a pseudokinase domain, followed by JH3-JH4 which is homologous to the SH2 domain, and lastly JH5-JH7 which is a FERM domain. Named after Janus, the two-faced Roman god of doorways, JAKs possess two near-identical phosphate-transferring domains; one which displays the kinase activity (JH1), while the other negatively regulates the kinase activity of the first (JH2). The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 275412  Cd Length: 144  Bit Score: 257.47  E-value: 7.67e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  282 GAEIFETSMLLISSENEMNWFHSNDGGNVLYYEVMVTGNLGIQWRHKPNVVSVEKEKNKLKRKKLeNKHKKDEEKNKIRE 361
Cdd:cd13332      1 GAEIFETSSLLISSESELNNFNMGDGGNYGYYEVSVTGNTGISWRRKPATTAVEKKKKGKSKKNK-LKGKKDEDKKKARE 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1013071061  362 EWNNFSYFPEITHIVIKESVVSINKQDNKKMELKLSSHEEALSFVSLVDGYFRLTADAHHYLCTD 426
Cdd:cd13332     80 GWNNFSYFPEITHIVIKESTVTINRQDNKKMELKLSSRDEALSFAALVDGYFRLTADAHHYLCTD 144
FERM_F2 pfam18377
FERM F2 acyl-CoA binding protein-like domain; This is an F2 lobe domain consisting of an ...
147-277 3.11e-73

FERM F2 acyl-CoA binding protein-like domain; This is an F2 lobe domain consisting of an acyl-CoA binding protein fold found in FERM region of Jak-family tyrosine kinases. Multidomain JAK molecules interact with receptors through their FERM and SH2-like domains, triggering a series of phosphorylation events, resulting in the activation of their kinase domains. Overall, the FERM region maintains the typical three-lobed architecture, with an F1 lobe consisting of a ubiquitin-like fold, an F2 lobe consisting of an acyl-CoA binding protein fold, and an F3 lobe consisting of a pleckstrin-homology (PH) fold. JAK1 FERM-F2 domain has been shown to act as the interaction site for the IFNLR1 box1 motif (PxxLxF) of class II cytokine receptors which is essential for kinase activation.


Pssm-ID: 436450  Cd Length: 131  Bit Score: 238.69  E-value: 3.11e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  147 TPLLDASSLEYLFAQGQYDLVKCLAPIRDPKTEQDGHDIENECLGMAVLAISHYAMMKKMQLPELPKDISYKRYIPETLN 226
Cdd:pfam18377    1 SPLLDAPSLEYLFAQGKYDFVNGLAPLRDSQSEQETHRIENECLGMAVLDLSHLAKEKGLSLEEIAKKVSYKRCIPESFR 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1013071061  227 KSIRQRNLLTRMRINNVFKDFLKEFNNKTICDSSVSTHDLKVKYLATLETL 277
Cdd:pfam18377   81 RQIQQRNFLTRKRIRNVFKRFLREFNQHTVGDCKLTAHDLKLKYLSTLETL 131
Jak1_Phl pfam17887
Jak1 pleckstrin homology-like domain; This entry is for the pleckstrin homology-like (PHL) ...
284-421 2.31e-72

Jak1 pleckstrin homology-like domain; This entry is for the pleckstrin homology-like (PHL) subdomain found in Jak1 proteins. JAK1 is a member of the Janus kinase (JAK) family of non-receptor tyrosine kinases that are activated in response to cytokines and interferons. PHL (residues 283-419) together with the N-terminal ubiquitin-like subdomain (residues 36-111) and an acyl-coenzyme A binding protein-like subdomain (residues 148-282), associate into a canonical tri-lobed FERM domain.


Pssm-ID: 465552  Cd Length: 140  Bit Score: 236.45  E-value: 2.31e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  284 EIFETSMLLISSENEMNWFHSNDGGNVLYYEVMVTGNLGIQWRHKPNVVSVEKEKNKLKRKKL--ENKHKKDEEKNKIRE 361
Cdd:pfam17887    1 EAEETPCYIIDSENEPNDPNPEDADGPPTHEVLVTGTGGIQWRPKPVESSSRNPKAKLKGKKKkaESKAKKQPAKRKLEP 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  362 EWNNFSYFPEITHIVIKESVVSINKQDNKKMELKLSSHEEALSFVSLVDGYFRLTADAHH 421
Cdd:pfam17887   81 PWAYFCDFQEITHIVIKESTVSIHRQDNKCLELKLPSHAEALSFVSLVDGYFRLTADSSH 140
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
879-1149 1.90e-70

Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Syk-like subfamily is composed of Syk, ZAP-70, Shark, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. They are involved in the signaling downstream of activated receptors (including B-cell, T-cell, and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. Syk is important in B-cell receptor signaling, while Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor signaling. Syk also plays a central role in Fc receptor-mediated phagocytosis in the adaptive immune system. Shark is exclusively expressed in ectodermally derived epithelia, and is localized preferentially to the apical surface of the epithelial cells, it may play a role in a signaling pathway for epithelial cell polarity. The Syk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 236.09  E-value: 1.90e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGHFGKVELCRYDPEgDNTGEQVAVKSLKPEsggnHIADLKKEI----EILRNLYHENIVKYKGICTEDGgngIKL 954
Cdd:cd05060      1 KELGHGNFGSVRKGVYLMK-SGKEVEVAVKTLKQE----HEKAGKKEFlreaSVMAQLDHPCIVRLIGVCKGEP---LML 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPSGSLKEYLPKNKNkINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEY 1034
Cdd:cd05060     73 VMELAPLGPLLKYLKKRRE-IPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMSRALGAGSDY 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1035 YTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDsdsspmalflkmigPTHGQMTVTRLVNTLKEGKRL 1114
Cdd:cd05060    152 YRATTAGRWPLKWYAPECINYGKFSSKSDVWSYGVTLWEAFSYGA--------------KPYGEMKGPEVIAMLESGERL 217
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1013071061 1115 PCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGF 1149
Cdd:cd05060    218 PRPEECPQEIYSIMLSCWKYRPEDRPTFSELESTF 252
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
879-1150 1.02e-66

Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, and Yes. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, and Lyn show a limited expression pattern. The Src-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270630 [Multi-domain]  Cd Length: 248  Bit Score: 225.24  E-value: 1.02e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGHFGKVELCRYdpegdNTGEQVAVKSLKPesGGNHIADLKKEIEILRNLYHENIVKYKGICTEdgGNGIKLIMEF 958
Cdd:cd05034      1 KKLGAGQFGEVWMGVW-----NGTTKVAVKTLKP--GTMSPEAFLQEAQIMKKLRHDKLVQLYAVCSD--EEPIYIVTEL 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  959 LPSGSLKEYLPKNK-NKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKeyYTV 1037
Cdd:cd05034     72 MSKGSLLDYLRTGEgRALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNVCKVADFGLARLIEDDE--YTA 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1038 KDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYcdsdsspmalflkmiG--PTHGqMTVTRLVNTLKEGKRLP 1115
Cdd:cd05034    150 REGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLYEIVTY---------------GrvPYPG-MTNREVLEQVERGYRMP 213
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1013071061 1116 CPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFE 1150
Cdd:cd05034    214 KPPGCPDELYDIMLQCWKKEPEERPTFEYLQSFLE 248
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
881-1147 3.24e-66

Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes Ack1, thirty-eight-negative kinase 1 (Tnk1), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal catalytic domain, an SH3 domain, a Cdc42-binding CRIB domain, and a proline-rich region. They are mainly expressed in brain and skeletal tissues and are involved in the regulation of cell adhesion and growth, receptor degradation, and axonal guidance. Ack1 is also associated with androgen-independent prostate cancer progression. Tnk1 regulates TNFalpha signaling and may play an important role in cell death. The Ack-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 224.14  E-value: 3.24e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYD-PEGDNTgeQVAVKSLKPE--SGGNHIADLKKEIEILRNLYHENIVKYKGICTEdggNGIKLIME 957
Cdd:cd05040      3 LGDGSFGVVRRGEWTtPSGKVI--QVAVKCLKSDvlSQPNAMDDFLKEVNAMHSLDHPNLIRLYGVVLS---SPLMMVTE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  958 FLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYTV 1037
Cdd:cd05040     78 LAPLGSLLDRLRKDQGHFLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGDFGLMRALPQNEDHYVM 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1038 KDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCdsdsspmalFLKMIGPTHGQMtvtrLVNTLKEGKRLPCP 1117
Cdd:cd05040    158 QEHRKVPFAWCAPESLKTRKFSHASDVWMFGVTLWEMFTYG---------EEPWLGLNGSQI----LEKIDKEGERLERP 224
                          250       260       270
                   ....*....|....*....|....*....|
gi 1013071061 1118 PNCPDEVYQLMRKCWEFQPSNRTSFQNLIE 1147
Cdd:cd05040    225 DDCPQDIYNVMLQCWAHKPADRPTFVALRD 254
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
871-1145 1.40e-64

Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Frk and Srk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Frk, also known as Rak, is specifically expressed in liver, lung, kidney, intestine, mammary glands, and the islets of Langerhans. Rodent homologs were previously referred to as GTK (gastrointestinal tyr kinase), BSK (beta-cell Src-like kinase), or IYK (intestinal tyr kinase). Studies in mice reveal that Frk is not essential for viability. It plays a role in the signaling that leads to cytokine-induced beta-cell death in Type I diabetes. It also regulates beta-cell number during embryogenesis and early in life. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Frk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 219.97  E-value: 1.40e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  871 EKRFLKRIRDLGEGHFGKVElcrydpEG--DNTGEqVAVKSLKPesGGNHIADLKKEIEILRNLYHENIVKYKGICTEDg 948
Cdd:cd05068      6 DRKSLKLLRKLGSGQFGEVW------EGlwNNTTP-VAVKTLKP--GTMDPEDFLREAQIMKKLRHPKLIQLYAVCTLE- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  949 gNGIKLIMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAI 1028
Cdd:cd05068     76 -EPIYIITELMKHGSLLEYLQGKGRSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVGENNICKVADFGLARVI 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1029 ETDKEyYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCdsdsspmalflKMIGPThgqMTVTRLVNTL 1108
Cdd:cd05068    155 KVEDE-YEAREGAKFPIKWTAPEAANYNRFSIKSDVWSFGILLTEIVTYG-----------RIPYPG---MTNAEVLQQV 219
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1013071061 1109 KEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNL 1145
Cdd:cd05068    220 ERGYRMPCPPNCPPQLYDIMLECWKADPMERPTFETL 256
SH2_Jak1 cd10378
Src homology 2 (SH2) domain in the Janus kinase 1 (Jak1) proteins; Janus kinase 1 (JAK1), is a ...
426-527 3.34e-64

Src homology 2 (SH2) domain in the Janus kinase 1 (Jak1) proteins; Janus kinase 1 (JAK1), is a member of a class of protein-tyrosine kinases (PTK) characterized by the presence of a second phosphotransferase-related domain immediately N-terminal to the PTK domain. The second phosphotransferase domain bears all the hallmarks of a protein kinase, although its structure differs significantly from that of the PTK and threonine/serine kinase family members. JAK1 is a large, widely expressed membrane-associated phosphoprotein. JAK1 is involved in the interferon-alpha/beta and -gamma signal transduction pathways. The reciprocal interdependence between JAK1 and TYK2 activities in the interferon-alpha pathway, and between JAK1 and JAK2 in the interferon-gamma pathway, may reflect a requirement for these kinases in the correct assembly of interferon receptor complexes. These kinases couple cytokine ligand binding to tyrosine phosphorylation of various known signaling proteins and of a unique family of transcription factors termed the signal transducers and activators of transcription, or STATs. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198241  Cd Length: 102  Bit Score: 212.02  E-value: 3.34e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  426 DVAPPLIVHNIQNGCHGPICTEYAINKLRQEGSEEGMYVLRWSCTDFDNILMTVTCFEKSEQVQGAQKQFKNFQIEVQKG 505
Cdd:cd10378      1 DVAPPLIVHNIKNGCHGPICTEYAINKLRQEGNEEGMYVLRWSCTDFNNILMTVTCIELSECESRPVKQYKNFQIEVKKG 80
                           90       100
                   ....*....|....*....|..
gi 1013071061  506 RYSLHGSDRSFPSLGDLMSHLK 527
Cdd:cd10378     81 GYSLHGSDTFFPSLKELMEHLK 102
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
875-1145 9.24e-63

Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. FAK is a cytoplasmic (or nonreceptor) PTK that contains an autophosphorylation site and a FERM domain at the N-terminus, a central tyr kinase domain, proline-rich regions, and a C-terminal FAT (focal adhesion targeting) domain. FAK activity is dependent on integrin-mediated cell adhesion, which facilitates N-terminal autophosphorylation. Full activation is achieved by the phosphorylation of its two adjacent A-loop tyrosines. FAK is important in mediating signaling initiated at sites of cell adhesions and at growth factor receptors. Through diverse molecular interactions, FAK functions as a biosensor or integrator to control cell motility. It is a key regulator of cell survival, proliferation, migration and invasion, and thus plays an important role in the development and progression of cancer. Src binds to autophosphorylated FAK forming the FAK-Src dual kinase complex, which is activated in a wide variety of tumor cells and generates signals promoting growth and metastasis. FAK is being developed as a target for cancer therapy. The FAK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 214.59  E-value: 9.24e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  875 LKRIrdLGEGHFGKVELCRY-DPEGDNTgeQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGgngIK 953
Cdd:cd05056     10 LGRC--IGEGQFGDVYQGVYmSPENEKI--AVAVKTCKNCTSPSVREKFLQEAYIMRQFDHPHIVKLIGVITENP---VW 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  954 LIMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIEtDKE 1033
Cdd:cd05056     83 IVMELAPLGELRSYLQVNKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLSRYME-DES 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1034 YYTVKDDRdSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCdsdsspmalflkmIGPTHGqMTVTRLVNTLKEGKR 1113
Cdd:cd05056    162 YYKASKGK-LPIKWMAPESINFRRFTSASDVWMFGVCMWEILMLG-------------VKPFQG-VKNNDVIGRIENGER 226
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1013071061 1114 LPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNL 1145
Cdd:cd05056    227 LPMPPNCPPTLYSLMTKCWAYDPSKRPRFTEL 258
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
875-1154 4.71e-61

Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. Gain of function alterations, through their overexpression, deletions, or point mutations in their kinase domains, have been implicated in various cancers. These receptors are targets of many small molecule inhibitors and monoclonal antibodies used in cancer therapy. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 210.35  E-value: 4.71e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  875 LKRIRDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTedgGNGIKL 954
Cdd:cd05057      9 LEKGKVLGSGAFGTVYKGVWIPEGEKVKIPVAIKVLREETGPKANEEILDEAYVMASVDHPHLVRLLGICL---SSQVQL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEY 1034
Cdd:cd05057     86 ITQLMPLGCLLDYVRNHRDNIGSQLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFGLAKLLDVDEKE 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1035 YTVKDDRdSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSdsspmalflkmigPTHGQMTVtRLVNTLKEGKRL 1114
Cdd:cd05057    166 YHAEGGK-VPIKWMALESIQYRIYTHKSDVWSYGVTVWELMTFGAK-------------PYEGIPAV-EIPDLLEKGERL 230
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1013071061 1115 PCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALLK 1154
Cdd:cd05057    231 PQPPICTIDVYMVLVKCWMIDAESRPTFKELANEFSKMAR 270
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
879-1142 1.51e-60

Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; Fes subfamily; catalytic (c) domain. Fes subfamily members include Fes (or Fps), Fer, and similar proteins. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes subfamily proteins are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated tyr kinase activity. Fes and Fer kinases play roles in haematopoiesis, inflammation and immunity, growth factor signaling, cytoskeletal regulation, cell migration and adhesion, and the regulation of cell-cell interactions. Fes and Fer show redundancy in their biological functions.


Pssm-ID: 270637 [Multi-domain]  Cd Length: 251  Bit Score: 207.68  E-value: 1.51e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGHFGKVELCRYDPegdnTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDggNGIKLIMEF 958
Cdd:cd05041      1 EKIGRGNFGDVYRGVLKP----DNTEVAVKTCRETLPPDLKRKFLQEARILKQYDHPNIVKLIGVCVQK--QPIMIVMEL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  959 LPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKaiETDKEYYTVK 1038
Cdd:cd05041     75 VPGGSLLTFLRKKGARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSR--EEEDGEYTVS 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1039 DD-RDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSdsspmalflkmigPTHGqMTVTRLVNTLKEGKRLPCP 1117
Cdd:cd05041    153 DGlKQIPIKWTAPEALNYGRYTSESDVWSFGILLWEIFSLGAT-------------PYPG-MSNQQTREQIESGYRMPAP 218
                          250       260
                   ....*....|....*....|....*
gi 1013071061 1118 PNCPDEVYQLMRKCWEFQPSNRTSF 1142
Cdd:cd05041    219 ELCPEAVYRLMLQCWAYDPENRPSF 243
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
881-1147 1.81e-59

Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed mainly of MAP3Ks and similar proteins, including TGF-beta Activated Kinase-1 (TAK1, also called MAP3K7), MAP3K12, MAP3K13, Mixed lineage kinase (MLK), MLK-Like mitogen-activated protein Triple Kinase (MLTK), and Raf (Rapidly Accelerated Fibrosarcoma) kinases. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Also included in this subfamily is the pseudokinase Kinase Suppressor of Ras (KSR), which is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway.


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 204.31  E-value: 1.81e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDpegdntGEQVAVKSLKPESG-GNHIADLKKEIEILRNLYHENIVKYKGICTEDGGNGIklIMEFL 959
Cdd:cd13999      1 IGSGSFGEVYKGKWR------GTDVAIKKLKVEDDnDELLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCI--VTEYM 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  960 PSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKE-----Y 1034
Cdd:cd13999     73 PGGSLYDLLHKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTTEkmtgvV 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1035 YTVKddrdspvfWYAPECLMQSKFYIASDVWSFGVTLHELLTyCD---SDSSPMALFLKMIGpthgqmtvtrlvntlkEG 1111
Cdd:cd13999    153 GTPR--------WMAPEVLRGEPYTEKADVYSFGIVLWELLT-GEvpfKELSPIQIAAAVVQ----------------KG 207
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1013071061 1112 KRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIE 1147
Cdd:cd13999    208 LRPPIPPDCPPELSKLIKRCWNEDPEKRPSFSEIVK 243
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
875-1147 2.67e-59

Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The InsR subfamily is composed of InsR, Insulin-like Growth Factor-1 Receptor (IGF-1R), and similar proteins. InsR and IGF-1R are receptor PTKs (RTKs) composed of two alphabeta heterodimers. Binding of the ligand (insulin, IGF-1, or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR and IGF-1R, which share 84% sequence identity in their kinase domains, display physiologically distinct yet overlapping functions in cell growth, differentiation, and metabolism. InsR activation leads primarily to metabolic effects while IGF-1R activation stimulates mitogenic pathways. In cells expressing both receptors, InsR/IGF-1R hybrids are found together with classical receptors. Both receptors can interact with common adaptor molecules such as IRS-1 and IRS-2. The InsR-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 205.27  E-value: 2.67e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  875 LKRIRDLGEGHFGKV-ELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEdgGNGIK 953
Cdd:cd05032      8 ITLIRELGQGSFGMVyEGLAKGVVKGEPETRVAIKTVNENASMRERIEFLNEASVMKEFNCHHVVRLLGVVST--GQPTL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  954 LIMEFLPSGSLKEYL----PKNKNK-----INLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGL 1024
Cdd:cd05032     86 VVMELMAKGDLKSYLrsrrPEAENNpglgpPTLQKFIQMAAEIADGMAYLAAKKFVHRDLAARNCMVAEDLTVKIGDFGM 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1025 TKAI-ETDkeYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDsdsspmalfLKMIGPTHGQmtVTR 1103
Cdd:cd05032    166 TRDIyETD--YYRKGGKGLLPVRWMAPESLKDGVFTTKSDVWSFGVVLWEMATLAE---------QPYQGLSNEE--VLK 232
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1013071061 1104 LVntlKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIE 1147
Cdd:cd05032    233 FV---IDGGHLDLPENCPDKLLELMRMCWQYNPKMRPTFLEIVS 273
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
869-1145 3.32e-59

Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Trk subfamily consists of TrkA, TrkB, TrkC, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, the nerve growth factor (NGF) family of neutrotrophins, leads to Trk receptor oligomerization and activation of the catalytic domain. Trk receptors are mainly expressed in the peripheral and central nervous systems. They play important roles in cell fate determination, neuronal survival and differentiation, as well as in the regulation of synaptic plasticity. Altered expression of Trk receptors is associated with many human diseases. The Trk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 205.01  E-value: 3.32e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  869 HFEKRFLKRIRDLGEGHFGKV---ELCRYDPEGDNTgeQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICT 945
Cdd:cd05049      1 HIKRDTIVLKRELGEGAFGKVflgECYNLEPEQDKM--LVAVKTLKDASSPDARKDFEREAELLTNLQHENIVKFYGVCT 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  946 EdgGNGIKLIMEFLPSGSLKEYL-------------PKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVE 1012
Cdd:cd05049     79 E--GDPLLMVFEYMEHGDLNKFLrshgpdaaflaseDSAPGELTLSQLLHIAVQIASGMVYLASQHFVHRDLATRNCLVG 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1013 SEHQVKIGDFGLTKAIETDkEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYcdsDSSPMAlflkmi 1092
Cdd:cd05049    157 TNLVVKIGDFGMSRDIYST-DYYRVGGHTMLPIRWMPPESILYRKFTTESDVWSFGVVLWEIFTY---GKQPWF------ 226
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1013071061 1093 gpthgQMTVTRLVNTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNL 1145
Cdd:cd05049    227 -----QLSNTEVIECITQGRLLQRPRTCPSEVYAVMLGCWKREPQQRLNIKDI 274
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
876-1147 1.36e-58

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 202.37  E-value: 1.36e-58
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061   876 KRIRDLGEGHFGKVELCRYDpegdNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDggNGIKLI 955
Cdd:smart00220    2 EILEKLGEGSFGKVYLARDK----KTGKLVAIKVIKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDE--DKLYLV 75
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061   956 MEFLPSGSLKEYLpKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYY 1035
Cdd:smart00220   76 MEYCEGGDLFDLL-KKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKLT 154
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  1036 TVkddrDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLT----YCDsDSSPMALFLKMIGPTHGQMtvtrlvntlkeg 1111
Cdd:smart00220  155 TF----VGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTgkppFPG-DDQLLELFKKIGKPKPPFP------------ 217
                           250       260       270
                    ....*....|....*....|....*....|....*.
gi 1013071061  1112 krlPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIE 1147
Cdd:smart00220  218 ---PPEWDISPEAKDLIRKLLVKDPEKRLTAEEALQ 250
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
881-1151 1.38e-58

Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily contains c-ros, Sevenless, and similar proteins. The proto-oncogene c-ros encodes an orphan receptor PTK (RTK) with an unknown ligand. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. C-ros is expressed in embryonic cells of the kidney, intestine and lung, but disappears soon after birth. It persists only in the adult epididymis. Male mice bearing inactive mutations of c-ros lack the initial segment of the epididymis and are infertile. The Drosophila protein, Sevenless, is required for the specification of the R7 photoreceptor cell during eye development. The c-ros subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 202.65  E-value: 1.38e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKV-ELCRYDPEGDNTGEQ-VAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGNGIklIMEF 958
Cdd:cd05044      3 LGSGAFGEVfEGTAKDILGDGSGETkVAVKTLRKGATDQEKAEFLKEAHLMSNFKHPNILKLLGVCLDNDPQYI--ILEL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  959 LPSGSLKEYLPKNK------NKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVES----EHQVKIGDFGLTKAI 1028
Cdd:cd05044     81 MEGGDLLSYLRAARptaftpPLLTLKDLLSICVDVAKGCVYLEDMHFVHRDLAARNCLVSSkdyrERVVKIGDFGLARDI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1029 ETDkEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYcdsDSSPMalflkmigPTHGQMTVTRLVntl 1108
Cdd:cd05044    161 YKN-DYYRKEGEGLLPVRWMAPESLVDGVFTTQSDVWAFGVLMWEILTL---GQQPY--------PARNNLEVLHFV--- 225
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1013071061 1109 KEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEA 1151
Cdd:cd05044    226 RAGGRLDQPDNCPDDLYELMLRCWSTDPEERPSFARILEQLQN 268
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
881-1153 1.43e-57

Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The FGFR subfamily consists of FGFR1, FGFR2, FGFR3, FGFR4, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, and to heparin/heparan sulfate (HS) results in the formation of a ternary complex, which leads to receptor dimerization and activation, and intracellular signaling. There are at least 23 FGFs and four types of FGFRs. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. FGF/FGFR signaling is important in the regulation of embryonic development, homeostasis, and regenerative processes. Depending on the cell type and stage, FGFR signaling produces diverse cellular responses including proliferation, growth arrest, differentiation, and apoptosis. Aberrant signaling leads to many human diseases such as skeletal, olfactory, and metabolic disorders, as well as cancer. The FGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 200.72  E-value: 1.43e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKV---ELCRYDPEGDNTgEQVAVKSLKPESGGNHIADLKKEIEILRNL-YHENIVKYKGICTEDGGngIKLIM 956
Cdd:cd05053     20 LGEGAFGQVvkaEAVGLDNKPNEV-VTVAVKMLKDDATEKDLSDLVSEMEMMKMIgKHKNIINLLGACTQDGP--LYVVV 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  957 EFLPSGSLKEYLPKNK---------------NKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGD 1021
Cdd:cd05053     97 EYASKGNLREFLRARRppgeeaspddprvpeEQLTQKDLVSFAYQVARGMEYLASKKCIHRDLAARNVLVTEDNVMKIAD 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1022 FGLTKAIEtDKEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSdsspmalflkmigPTHGqMTV 1101
Cdd:cd05053    177 FGLARDIH-HIDYYRKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGS-------------PYPG-IPV 241
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1013071061 1102 TRLVNTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALL 1153
Cdd:cd05053    242 EELFKLLKEGHRMEKPQNCTQELYMLMRDCWHEVPSQRPTFKQLVEDLDRIL 293
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
872-1152 1.46e-57

Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of Csk, Chk, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. They negatively regulate the activity of Src kinases that are anchored to the plasma membrane. To inhibit Src kinases, Csk and Chk are translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Chk inhibit Src kinases using a noncatalytic mechanism by simply binding to them. As negative regulators of Src kinases, Csk and Chk play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. The Csk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 199.50  E-value: 1.46e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  872 KRFLKRIRDLGEGHFGKVELcrydpeGDNTGEQVAVKSLKPEsgGNHIADLKKEIEILRNLYHENIVKYKGICTEdgGNG 951
Cdd:cd05039      5 KKDLKLGELIGKGEFGDVML------GDYRGQKVAVKCLKDD--STAAQAFLAEASVMTTLRHPNLVQLLGVVLE--GNG 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  952 IKLIMEFLPSGSLKEYL-PKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAiet 1030
Cdd:cd05039     75 LYIVTEYMAKGSLVDYLrSRGRAVITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAKE--- 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1031 dkeyytVKDDRDS---PVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYcdsDSSPmalflkmigptHGQMTVTRLVNT 1107
Cdd:cd05039    152 ------ASSNQDGgklPIKWTAPEALREKKFSTKSDVWSFGILLWEIYSF---GRVP-----------YPRIPLKDVVPH 211
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1013071061 1108 LKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEAL 1152
Cdd:cd05039    212 VEKGYRMEAPEGCPPEVYKVMKNCWELDPAKRPTFKQLREKLEHI 256
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
879-1153 1.08e-56

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Unlike other FGFRs, there is only one splice form of FGFR4. It binds FGF1, FGF2, FGF6, FGF19, and FGF23. FGF19 is a selective ligand for FGFR4. Although disruption of FGFR4 in mice causes no obvious phenotype, in vivo inhibition of FGFR4 in cultured skeletal muscle cells resulted in an arrest of muscle progenitor differentiation. FGF6 and FGFR4 are uniquely expressed in myofibers and satellite cells. FGF6/FGFR4 signaling appears to play a key role in the regulation of muscle regeneration. A polymorphism in FGFR4 is found in head and neck squamous cell carcinoma. FGFR4 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 199.04  E-value: 1.08e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGHFGKV---ELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNL-YHENIVKYKGICTEDGGngIKL 954
Cdd:cd05099     18 KPLGEGCFGQVvraEAYGIDKSRPDQTVTVAVKMLKDNATDKDLADLISEMELMKLIgKHKNIINLLGVCTQEGP--LYV 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPSGSLKEYL--------------PK-NKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKI 1019
Cdd:cd05099     96 IVEYAAKGNLREFLrarrppgpdytfdiTKvPEEQLSFKDLVSCAYQVARGMEYLESRRCIHRDLAARNVLVTEDNVMKI 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1020 GDFGLTKAIEtDKEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTycdsdsspmalflkMIGPTHGQM 1099
Cdd:cd05099    176 ADFGLARGVH-DIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILMWEIFT--------------LGGSPYPGI 240
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1013071061 1100 TVTRLVNTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALL 1153
Cdd:cd05099    241 PVEELFKLLREGHRMDKPSNCTHELYMLMRECWHAVPTQRPTFKQLVEALDKVL 294
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
873-1145 1.68e-56

Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Ror subfamily consists of Ror1, Ror2, and similar proteins. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. Ror kinases are expressed in many tissues during development. They play important roles in bone and heart formation. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Drosophila Ror is expressed only in the developing nervous system during neurite outgrowth and neuronal differentiation, suggesting a role for Drosophila Ror in neural development. More recently, mouse Ror1 and Ror2 have also been found to play an important role in regulating neurite growth in central neurons. Ror1 and Ror2 are believed to have some overlapping and redundant functions. The Ror subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 197.21  E-value: 1.68e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  873 RFLKrirDLGEGHFGKV---ELcrYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGG 949
Cdd:cd05048      8 RFLE---ELGEGAFGKVykgEL--LGPSSEESAISVAIKTLKENASPKTQQDFRREAELMSDLQHPNIVCLLGVCTKEQP 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  950 NGikLIMEFLPSGSLKEYLPKN-------------KNKINLKQ--QLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESE 1014
Cdd:cd05048     83 QC--MLFEYMAHGDLHEFLVRHsphsdvgvssdddGTASSLDQsdFLHIAIQIAAGMEYLSSHHYVHRDLAARNCLVGDG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1015 HQVKIGDFGLTKAIETdKEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCdsdsspmalflkmIGP 1094
Cdd:cd05048    161 LTVKISDFGLSRDIYS-SDYYRVQSKSLLPVRWMPPEAILYGKFTTESDVWSFGVVLWEIFSYG-------------LQP 226
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1013071061 1095 THGqMTVTRLVNTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNL 1145
Cdd:cd05048    227 YYG-YSNQEVIEMIRSRQLLPCPEDCPARVYSLMVECWHEIPSRRPRFKEI 276
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
875-1145 7.81e-56

Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The DDR subfamily consists of homologs of mammalian DDR1, DDR2, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270644 [Multi-domain]  Cd Length: 297  Bit Score: 196.02  E-value: 7.81e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  875 LKRIRDLGEGHFGKVELCRYD----------PEGDNTGEQ--VAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKG 942
Cdd:cd05051      7 LEFVEKLGEGQFGEVHLCEANglsdltsddfIGNDNKDEPvlVAVKMLRPDASKNAREDFLKEVKIMSQLKDPNIVRLLG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  943 ICTEDggNGIKLIMEFLPSGSLKEYLPK-----NKNKINLKQQLKY------AVQICKGMDYLGSRQYVHRDLAARNVLV 1011
Cdd:cd05051     87 VCTRD--EPLCMIVEYMENGDLNQFLQKheaetQGASATNSKTLSYgtllymATQIASGMKYLESLNFVHRDLATRNCLV 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1012 ESEHQVKIGDFGLTKAIETdKEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCdsDSSPmalflkm 1091
Cdd:cd05051    165 GPNYTIKIADFGMSRNLYS-GDYYRIEGRAVLPIRWMAWESILLGKFTTKSDVWAFGVTLWEILTLC--KEQP------- 234
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1013071061 1092 igptHGQMTVTRLVNTLKEGKR-------LPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNL 1145
Cdd:cd05051    235 ----YEHLTDEQVIENAGEFFRddgmevyLSRPPNCPKEIYELMLECWRRDEEDRPTFREI 291
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
879-1147 1.15e-55

Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristylation sites (Srm) and Breast tumor kinase (Brk); PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Srm and Brk (also called protein tyrosine kinase 6) are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Brk has been found to be overexpressed in a majority of breast tumors. Src kinases in general contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr; they are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Srm and Brk however, lack the N-terminal myristylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. The Srm/Brk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133248 [Multi-domain]  Cd Length: 261  Bit Score: 194.19  E-value: 1.15e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGHFGKVELCRYdpegdNTGEQVAVKSLKPESGGNHiADLKKEIEILRNLYHENIVKYKGICTEdgGNGIKLIMEF 958
Cdd:cd05148     12 RKLGSGYFGEVWEGLW-----KNRVRVAIKILKSDDLLKQ-QDFQKEVQALKRLRHKHLISLFAVCSV--GEPVYIITEL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  959 LPSGSLKEYL--PKNKNkINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIetdKEYYT 1036
Cdd:cd05148     84 MEKGSLLAFLrsPEGQV-LPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLARLI---KEDVY 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1037 VKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSdsspmalflkmigPTHGqMTVTRLVNTLKEGKRLPC 1116
Cdd:cd05148    160 LSSDKKIPYKWTAPEAASHGTFSTKSDVWSFGILLYEMFTYGQV-------------PYPG-MNNHEVYDQITAGYRMPC 225
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1013071061 1117 PPNCPDEVYQLMRKCWEFQPSNRTSFQNLIE 1147
Cdd:cd05148    226 PAKCPQEIYKIMLECWAAEPEDRPSFKALRE 256
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
880-1142 1.61e-55

Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Syk is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Syk was first cloned from the spleen, and its function in hematopoietic cells is well-established. It is involved in the signaling downstream of activated receptors (including B-cell and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. More recently, Syk expression has been detected in other cell types (including epithelial cells, vascular endothelial cells, neurons, hepatocytes, and melanocytes), suggesting a variety of biological functions in non-immune cells. Syk plays a critical role in maintaining vascular integrity and in wound healing during embryogenesis. It also regulates Vav3, which is important in osteoclast function including bone development. In breast epithelial cells, where Syk acts as a negative regulator for EGFR signaling, loss of Syk expression is associated with abnormal proliferation during cancer development suggesting a potential role as a tumor suppressor. In mice, Syk has been shown to inhibit malignant transformation of mammary epithelial cells induced with murine mammary tumor virus (MMTV). The Syk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 193.64  E-value: 1.61e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  880 DLGEGHFGKVELCRYdpEGDNTGEQVAVKSLKPESGGNHIAD-LKKEIEILRNLYHENIVKYKGICTedgGNGIKLIMEF 958
Cdd:cd05116      2 ELGSGNFGTVKKGYY--QMKKVVKTVAVKILKNEANDPALKDeLLREANVMQQLDNPYIVRMIGICE---AESWMLVMEM 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  959 LPSGSLKEYLPKNKNkINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYTVK 1038
Cdd:cd05116     77 AELGPLNKFLQKNRH-VTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKALRADENYYKAQ 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1039 DDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYcdsDSSPmalFLKMIGPTHGQMtvtrlvntLKEGKRLPCPP 1118
Cdd:cd05116    156 THGKWPVKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSY---GQKP---YKGMKGNEVTQM--------IEKGERMECPA 221
                          250       260
                   ....*....|....*....|....
gi 1013071061 1119 NCPDEVYQLMRKCWEFQPSNRTSF 1142
Cdd:cd05116    222 GCPPEMYDLMKLCWTYDVDERPGF 245
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
880-1145 1.71e-54

Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Zap-70 is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor (TCR) signaling. Zap-70 binds the phosphorylated ITAM (immunoreceptor tyr activation motif) sequences of the activated TCR zeta-chain through its SH2 domains, leading to its phosphorylation and activation. It then phosphorylates target proteins, which propagate the signals to downstream pathways. Zap-70 is hardly detected in normal peripheral B-cells, but is present in some B-cell malignancies. It is used as a diagnostic marker for chronic lymphocytic leukemia (CLL) as it is associated with the more aggressive subtype of the disease. The Zap-70 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 191.31  E-value: 1.71e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  880 DLGEGHFGKVELCRYDPEGDNTgeQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGgngIKLIMEFL 959
Cdd:cd05115     11 ELGSGNFGCVKKGVYKMRKKQI--DVAIKVLKQGNEKAVRDEMMREAQIMHQLDNPYIVRMIGVCEAEA---LMLVMEMA 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  960 PSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYTVKD 1039
Cdd:cd05115     86 SGGPLNKFLSGKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFGLSKALGADDSYYKARS 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1040 DRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYcdsDSSPmalFLKMIGPthgqmtvtRLVNTLKEGKRLPCPPN 1119
Cdd:cd05115    166 AGKWPLKWYAPECINFRKFSSRSDVWSYGVTMWEAFSY---GQKP---YKKMKGP--------EVMSFIEQGKRMDCPAE 231
                          250       260
                   ....*....|....*....|....*.
gi 1013071061 1120 CPDEVYQLMRKCWEFQPSNRTSFQNL 1145
Cdd:cd05115    232 CPPEMYALMSDCWIYKWEDRPNFLTV 257
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
879-1153 1.42e-53

Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Met and Ron are receptor PTKs (RTKs) composed of an alpha-beta heterodimer. The extracellular alpha chain is disulfide linked to the beta chain, which contains an extracellular ligand-binding region with a sema domain, a PSI domain and four IPT repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. Met binds to the ligand, hepatocyte growth factor/scatter factor (HGF/SF), and is also called the HGF receptor. HGF/Met signaling plays a role in growth, transformation, cell motility, invasion, metastasis, angiogenesis, wound healing, and tissue regeneration. Aberrant expression of Met through mutations or gene amplification is associated with many human cancers including hereditary papillary renal and gastric carcinomas. The ligand for Ron is macrophage stimulating protein (MSP). Ron signaling is important in regulating cell motility, adhesion, proliferation, and apoptosis. Aberrant Ron expression is implicated in tumorigenesis and metastasis. The Met/Ron subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270649 [Multi-domain]  Cd Length: 262  Bit Score: 188.07  E-value: 1.42e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGHFGKVELCRY-DPEGDNTgeQVAVKSLkpesggNHIADLK------KEIEILRNLYHENIVKYKGICTEDGGNG 951
Cdd:cd05058      1 EVIGKGHFGCVYHGTLiDSDGQKI--HCAVKSL------NRITDIEeveqflKEGIIMKDFSHPNVLSLLGICLPSEGSP 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  952 IkLIMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIeTD 1031
Cdd:cd05058     73 L-VVLPYMKHGDLRNFIRSETHNPTVKDLIGFGLQVAKGMEYLASKKFVHRDLAARNCMLDESFTVKVADFGLARDI-YD 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1032 KEYYTVKDDRDS--PVFWYAPECLMQSKFYIASDVWSFGVTLHELLT-----YCDSDSspmalflkmigpthgqmtvTRL 1104
Cdd:cd05058    151 KEYYSVHNHTGAklPVKWMALESLQTQKFTTKSDVWSFGVLLWELMTrgappYPDVDS-------------------FDI 211
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1013071061 1105 VNTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALL 1153
Cdd:cd05058    212 TVYLLQGRRLLQPEYCPDPLYEVMLSCWHPKPEMRPTFSELVSRISQIF 260
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
869-1146 1.62e-53

Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also called protein tyrosine kinase 7 (PTK7), is an orphan receptor PTK (RTK) containing an extracellular region with seven immunoglobulin domains, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Studies in mice reveal that CCK4 is essential for neural development. Mouse embryos containing a truncated CCK4 die perinatally and display craniorachischisis, a severe form of neural tube defect. The mechanism of action of the CCK4 pseudokinase is still unknown. Other pseudokinases such as HER3 rely on the activity of partner RTKs. The CCK4 subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133178 [Multi-domain]  Cd Length: 275  Bit Score: 188.44  E-value: 1.62e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  869 HFEKRFLKRIRDLGEGHFGKVELCRYDPEGDNTGEQ-VAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTED 947
Cdd:cd05046      1 AFPRSNLQEITTLGRGEFGEVFLAKAKGIEEEGGETlVLVKALQKTKDENLQSEFRRELDMFRKLSHKNVVRLLGLCREA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  948 GGNGIklIMEFLPSGSLKEYLPKNKNKINL--------KQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKI 1019
Cdd:cd05046     81 EPHYM--ILEYTDLGDLKQFLRATKSKDEKlkppplstKQKVALCTQIALGMDHLSNARFVHRDLAARNCLVSSQREVKV 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1020 GDFGLTKAIETDkEYYTVKDDRdSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSdsspmalflkmigpTHGQM 1099
Cdd:cd05046    159 SLLSLSKDVYNS-EYYKLRNAL-IPLRWLAPEAVQEDDFSTKSDVWSFGVLMWEVFTQGEL--------------PFYGL 222
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1013071061 1100 TVTRLVNTLKEGK-RLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLI 1146
Cdd:cd05046    223 SDEEVLNRLQAGKlELPVPEGCPSRLYKLMTRCWAVNPKDRPSFSELV 270
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
875-1154 1.91e-53

Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER1, ErbB1) is a receptor PTK (RTK) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands for EGFR include EGF, heparin binding EGF-like growth factor (HBEGF), epiregulin, amphiregulin, TGFalpha, and betacellulin. Upon ligand binding, EGFR can form homo- or heterodimers with other EGFR subfamily members. The EGFR signaling pathway is one of the most important pathways regulating cell proliferation, differentiation, survival, and growth. Overexpression and mutation in the kinase domain of EGFR have been implicated in the development and progression of a variety of cancers. A number of monoclonal antibodies and small molecule inhibitors have been developed that target EGFR, including the antibodies Cetuximab and Panitumumab, which are used in combination with other therapies for the treatment of colorectal cancer and non-small cell lung carcinoma (NSCLC). The small molecule inhibitors Gefitinib (Iressa) and Erlotinib (Tarceva), already used for NSCLC, are undergoing clinical trials for other types of cancer including gastrointestinal, breast, head and neck, and bladder. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 189.85  E-value: 1.91e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  875 LKRIRDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEdggNGIKL 954
Cdd:cd05108      9 FKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLT---STVQL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETD-KE 1033
Cdd:cd05108     86 ITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEeKE 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1034 YYTvkDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYcdsDSSPmalflkmigptHGQMTVTRLVNTLKEGKR 1113
Cdd:cd05108    166 YHA--EGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTF---GSKP-----------YDGIPASEISSILEKGER 229
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1013071061 1114 LPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALLK 1154
Cdd:cd05108    230 LPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMAR 270
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
869-1145 2.59e-53

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkA is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkA to its ligand, nerve growth factor (NGF), results in receptor oligomerization and activation of the catalytic domain. TrkA is expressed mainly in neural-crest-derived sensory and sympathetic neurons of the peripheral nervous system, and in basal forebrain cholinergic neurons of the central nervous system. It is critical for neuronal growth, differentiation and survival. Alternative TrkA splicing has been implicated as a pivotal regulator of neuroblastoma (NB) behavior. Normal TrkA expression is associated with better NB prognosis, while the hypoxia-regulated TrkAIII splice variant promotes NB pathogenesis and progression. Aberrant TrkA expression has also been demonstrated in non-neural tumors including prostate, breast, lung, and pancreatic cancers. The TrkA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 188.25  E-value: 2.59e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  869 HFEKRFLKRIRDLGEGHFGKV---ELCRYDPEGDNTgeQVAVKSLKpESGGNHIADLKKEIEILRNLYHENIVKYKGICT 945
Cdd:cd05092      1 HIKRRDIVLKWELGEGAFGKVflaECHNLLPEQDKM--LVAVKALK-EATESARQDFQREAELLTVLQHQHIVRFYGVCT 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  946 EdgGNGIKLIMEFLPSGSLKEYL----PKNK----------NKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLV 1011
Cdd:cd05092     78 E--GEPLIMVFEYMRHGDLNRFLrshgPDAKildggegqapGQLTLGQMLQIASQIASGMVYLASLHFVHRDLATRNCLV 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1012 ESEHQVKIGDFGLTKAIETdKEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSdsspmalflkm 1091
Cdd:cd05092    156 GQGLVVKIGDFGMSRDIYS-TDYYRVGGRTMLPIRWMPPESILYRKFTTESDIWSFGVVLWEIFTYGKQ----------- 223
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1013071061 1092 igPTHgQMTVTRLVNTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNL 1145
Cdd:cd05092    224 --PWY-QLSNTEAIECITQGRELERPRTCPPEVYAIMQGCWQREPQQRHSIKDI 274
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
881-1153 7.11e-53

Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They can be classified into two classes (EphA and EphB), according to their extracellular sequences, which largely correspond to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.The EphR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 186.42  E-value: 7.11e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDPEGDNTgEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEdgGNGIKLIMEFLP 960
Cdd:cd05033     12 IGGGEFGEVCSGSLKLPGKKE-IDVAIKTLKSGYSDKQRLDFLTEASIMGQFDHPNVIRLEGVVTK--SRPVMIVTEYME 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  961 SGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYTVKDD 1040
Cdd:cd05033     89 NGSLDKFLRENDGKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDFGLSRRLEDSEATYTTKGG 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1041 RdSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSdsspmalflkmigpTHGQMTVTRLVNTLKEGKRLPCPPNC 1120
Cdd:cd05033    169 K-IPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSYGER--------------PYWDMSNQDVIKAVEDGYRLPPPMDC 233
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1013071061 1121 PDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALL 1153
Cdd:cd05033    234 PSALYQLMLDCWQKDRNERPTFSQIVSTLDKMI 266
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
875-1149 7.90e-53

Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lck and Blk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lck is expressed in T-cells and natural killer cells. It plays a critical role in T-cell maturation, activation, and T-cell receptor (TCR) signaling. Lck phosphorylates ITAM (immunoreceptor tyr activation motif) sequences on several subunits of TCRs, leading to the activation of different second messenger cascades. Phosphorylated ITAMs serve as binding sites for other signaling factor such as Syk and ZAP-70, leading to their activation and propagation of downstream events. In addition, Lck regulates drug-induced apoptosis by interfering with the mitochondrial death pathway. The apototic role of Lck is independent of its primary function in T-cell signaling. Blk is expressed specifically in B-cells. It is involved in pre-BCR (B-cell receptor) signaling. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lck/Blk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 186.25  E-value: 7.90e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  875 LKRIRDLGEGHFGKVELCRYdpegdNTGEQVAVKSLKPesGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGgngIKL 954
Cdd:cd05067      9 LKLVERLGAGQFGEVWMGYY-----NGHTKVAIKSLKQ--GSMSPDAFLAEANLMKQLQHQRLVRLYAVVTQEP---IYI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPSGSLKEYLPKNKN-KINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKe 1033
Cdd:cd05067     79 ITEYMENGSLVDFLKTPSGiKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARLIEDNE- 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1034 yYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSdsspmalflkmigPTHGqMTVTRLVNTLKEGKR 1113
Cdd:cd05067    158 -YTAREGAKFPIKWTAPEAINYGTFTIKSDVWSFGILLTEIVTHGRI-------------PYPG-MTNPEVIQNLERGYR 222
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1013071061 1114 LPCPPNCPDEVYQLMRKCWEFQPSNRTSF---QNLIEGF 1149
Cdd:cd05067    223 MPRPDNCPEELYQLMRLCWKERPEDRPTFeylRSVLEDF 261
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
881-1152 2.38e-52

Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Abl (or c-Abl) is a ubiquitously-expressed cytoplasmic (or nonreceptor) PTK that contains SH3, SH2, and tyr kinase domains in its N-terminal region, as well as nuclear localization motifs, a putative DNA-binding domain, and F- and G-actin binding domains in its C-terminal tail. It also contains a short autoinhibitory cap region in its N-terminus. Abl function depends on its subcellular localization. In the cytoplasm, Abl plays a role in cell proliferation and survival. In response to DNA damage or oxidative stress, Abl is transported to the nucleus where it induces apoptosis. In chronic myelogenous leukemia (CML) patients, an aberrant translocation results in the replacement of the first exon of Abl with the BCR (breakpoint cluster region) gene. The resulting BCR-Abl fusion protein is constitutively active and associates into tetramers, resulting in a hyperactive kinase sending a continuous signal. This leads to uncontrolled proliferation, morphological transformation and anti-apoptotic effects. BCR-Abl is the target of selective inhibitors, such as imatinib (Gleevec), used in the treatment of CML. Abl2, also known as ARG (Abelson-related gene), is thought to play a cooperative role with Abl in the proper development of the nervous system. The Tel-ARG fusion protein, resulting from reciprocal translocation between chromosomes 1 and 12, is associated with acute myeloid leukemia (AML). The TEL gene is a frequent fusion partner of other tyr kinase oncogenes, including Tel/Abl, Tel/PDGFRbeta, and Tel/Jak2, found in patients with leukemia and myeloproliferative disorders. The Abl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 184.55  E-value: 2.38e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVelcrYDPEGDNTGEQVAVKSLKPESggNHIADLKKEIEILRNLYHENIVKYKGICTEDGGngIKLIMEFLP 960
Cdd:cd05052     14 LGGGQYGEV----YEGVWKKYNLTVAVKTLKEDT--MEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPP--FYIITEFMP 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  961 SGSLKEYLPK-NKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKeyYTVKD 1039
Cdd:cd05052     86 YGNLLDYLREcNREELNAVVLLYMATQIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDT--YTAHA 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1040 DRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSdsspmalflkmigPTHGqMTVTRLVNTLKEGKRLPCPPN 1119
Cdd:cd05052    164 GAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMS-------------PYPG-IDLSQVYELLEKGYRMERPEG 229
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1013071061 1120 CPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEAL 1152
Cdd:cd05052    230 CPPKVYELMRACWQWNPSDRPSFAEIHQALETM 262
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
875-1149 4.09e-52

Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lyn is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lyn is expressed in B lymphocytes and myeloid cells. It exhibits both positive and negative regulatory roles in B cell receptor (BCR) signaling. Lyn, as well as Fyn and Blk, promotes B cell activation by phosphorylating ITAMs (immunoreceptor tyr activation motifs) in CD19 and in Ig components of BCR. It negatively regulates signaling by its unique ability to phosphorylate ITIMs (immunoreceptor tyr inhibition motifs) in cell surface receptors like CD22 and CD5. Lyn also plays an important role in G-CSF receptor signaling by phosphorylating a variety of adaptor molecules. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lyn subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 184.47  E-value: 4.09e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  875 LKRIRDLGEGHFGKVELCRYdpegdNTGEQVAVKSLKPesGGNHIADLKKEIEILRNLYHENIVKYKGICTEDggNGIKL 954
Cdd:cd05072      9 IKLVKKLGAGQFGEVWMGYY-----NNSTKVAVKTLKP--GTMSVQAFLEEANLMKTLQHDKLVRLYAVVTKE--EPIYI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPSGSLKEYLPKNK-NKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKe 1033
Cdd:cd05072     80 ITEYMAKGSLLDFLKSDEgGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIEDNE- 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1034 yYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSdsspmalflkmigPTHGqMTVTRLVNTLKEGKR 1113
Cdd:cd05072    159 -YTAREGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLYEIVTYGKI-------------PYPG-MSNSDVMSALQRGYR 223
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1013071061 1114 LPCPPNCPDEVYQLMRKCWEFQPSNRTSF---QNLIEGF 1149
Cdd:cd05072    224 MPRMENCPDELYDIMKTCWKEKAEERPTFdylQSVLDDF 262
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
875-1147 4.27e-52

Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Tec-like subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases form the second largest subfamily of nonreceptor PTKs and are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. Tec kinases play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. Mutations in Btk cause the severe B-cell immunodeficiency, X-linked agammaglobulinaemia (XLA). The Tec-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 183.80  E-value: 4.27e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  875 LKRIRDLGEGHFGKVELCRYDPEGDntgeqVAVKSLKpeSGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGngIKL 954
Cdd:cd05059      6 LTFLKELGSGQFGVVHLGKWRGKID-----VAIKMIK--EGSMSEDDFIEEAKVMMKLSHPKLVQLYGVCTKQRP--IFI 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKey 1034
Cdd:cd05059     77 VTEYMANGCLLNYLRERRGKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLARYVLDDE-- 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1035 YTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCdsdsspmalflKMigpTHGQMTVTRLVNTLKEGKRL 1114
Cdd:cd05059    155 YTSSVGTKFPVKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSEG-----------KM---PYERFSNSEVVEHISQGYRL 220
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1013071061 1115 PCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIE 1147
Cdd:cd05059    221 YRPHLAPTEVYTIMYSCWHEKPEERPTFKILLS 253
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
881-1153 3.67e-51

Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. RET is a receptor PTK (RTK) containing an extracellular region with four cadherin-like repeats, a calcium-binding site, and a cysteine-rich domain, a transmembrane segment, and an intracellular catalytic domain. It is part of a multisubunit complex that binds glial-derived neurotropic factor (GDNF) family ligands (GFLs) including GDNF, neurturin, artemin, and persephin. GFLs bind RET along with four GPI-anchored coreceptors, bringing two RET molecules together, leading to autophosphorylation, activation, and intracellular signaling. RET is essential for the development of the sympathetic, parasympathetic and enteric nervous systems, and the kidney. RET disruption by germline mutations causes diseases in humans including congenital aganglionosis of the gastrointestinal tract (Hirschsprung's disease) and three related inherited cancers: multiple endocrine neoplasia type 2A (MEN2A), MEN2B, and familial medullary thyroid carcinoma. The RET subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 182.47  E-value: 3.67e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKV-ELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGngIKLIMEFL 959
Cdd:cd05045      8 LGEGEFGKVvKATAFRLKGRAGYTTVAVKMLKENASSSELRDLLSEFNLLKQVNHPHVIKLYGACSQDGP--LLLIVEYA 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  960 PSGSLKEYLPKNKN-----------------------KINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQ 1016
Cdd:cd05045     86 KYGSLRSFLRESRKvgpsylgsdgnrnssyldnpderALTMGDLISFAWQISRGMQYLAEMKLVHRDLAARNVLVAEGRK 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1017 VKIGDFGLTKAIETDKEYytVKDDRDS-PVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYcdsDSSPMAlflkMIGPt 1095
Cdd:cd05045    166 MKISDFGLSRDVYEEDSY--VKRSKGRiPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTL---GGNPYP----GIAP- 235
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1013071061 1096 hgqmtvTRLVNTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALL 1153
Cdd:cd05045    236 ------ERLFNLLKTGYRMERPENCSEEMYNLMLTCWKQEPDKRPTFADISKELEKMM 287
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
879-1153 4.52e-51

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Alternative splicing of FGFR1 transcripts produces a variety of isoforms, which are differentially expressed in cells. FGFR1 binds the ligands, FGF1 and FGF2, with high affinity and has also been reported to bind FGF4, FGF6, and FGF9. FGFR1 signaling is critical in the control of cell migration during embryo development. It promotes cell proliferation in fibroblasts. Nuclear FGFR1 plays a role in the regulation of transcription. Mutations, insertions or deletions of FGFR1 have been identified in patients with Kallman's syndrome (KS), an inherited disorder characterized by hypogonadotropic hypogonadism and loss of olfaction. Aberrant FGFR1 expression has been found in some human cancers including 8P11 myeloproliferative syndrome (EMS), breast cancer, and pancreatic adenocarcinoma. FGFR1 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 182.52  E-value: 4.52e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGHFGKV---ELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNL-YHENIVKYKGICTEDGGngIKL 954
Cdd:cd05098     19 KPLGEGCFGQVvlaEAIGLDKDKPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIgKHKNIINLLGACTQDGP--LYV 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPSGSLKEYLPKNK---------------NKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKI 1019
Cdd:cd05098     97 IVEYASKGNLREYLQARRppgmeycynpshnpeEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDNVMKI 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1020 GDFGLTKAIEtDKEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTycdsdsspmalflkMIGPTHGQM 1099
Cdd:cd05098    177 ADFGLARDIH-HIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFT--------------LGGSPYPGV 241
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1013071061 1100 TVTRLVNTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALL 1153
Cdd:cd05098    242 PVEELFKLLKEGHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIV 295
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
875-1154 4.70e-51

Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER2 (ErbB2, HER2/neu) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER2 does not bind to any known EGFR subfamily ligands, but contributes to the kinase activity of all possible heterodimers. It acts as the preferred partner of other ligand-bound EGFR proteins and functions as a signal amplifier, with the HER2-HER3 heterodimer being the most potent pair in mitogenic signaling. HER2 plays an important role in cell development, proliferation, survival and motility. Overexpression of HER2 results in its activation and downstream signaling, even in the absence of ligand. HER2 overexpression, mainly due to gene amplification, has been shown in a variety of human cancers. Its role in breast cancer is especially well-documented. HER2 is up-regulated in about 25% of breast tumors and is associated with increases in tumor aggressiveness, recurrence and mortality. HER2 is a target for monoclonal antibodies and small molecule inhibitors, which are being developed as treatments for cancer. The first humanized antibody approved for clinical use is Trastuzumab (Herceptin), which is being used in combination with other therapies to improve the survival rates of patients with HER2-overexpressing breast cancer. The HER2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270684 [Multi-domain]  Cd Length: 279  Bit Score: 181.76  E-value: 4.70e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  875 LKRIRDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEdggNGIKL 954
Cdd:cd05109      9 LKKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVCRLLGICLT---STVQL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETD-KE 1033
Cdd:cd05109     86 VTQLMPYGCLLDYVRENKDRIGSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDeTE 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1034 YYTvkDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCdsdsspmalflkmIGPTHGqMTVTRLVNTLKEGKR 1113
Cdd:cd05109    166 YHA--DGGKVPIKWMALESILHRRFTHQSDVWSYGVTVWELMTFG-------------AKPYDG-IPAREIPDLLEKGER 229
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1013071061 1114 LPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALLK 1154
Cdd:cd05109    230 LPQPPICTIDVYMIMVKCWMIDSECRPRFRELVDEFSRMAR 270
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
875-1150 1.04e-50

Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Csk is expressed in a wide variety of tissues. As a negative regulator of Src, Csk plays a role in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Csk is a cytoplasmic (or nonreceptor) PTK containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases, Csk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. In addition, Csk also shows Src-independent functions. It is a critical component in G-protein signaling, and plays a role in cytoskeletal reorganization and cell migration. The Csk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 179.79  E-value: 1.04e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  875 LKRIRDLGEGHFGKVELcrydpeGDNTGEQVAVKSLKPESGGNHIAdlkKEIEILRNLYHENIVKYKGICTEDGGnGIKL 954
Cdd:cd05082      8 LKLLQTIGKGEFGDVML------GDYRGNKVAVKCIKNDATAQAFL---AEASVMTQLRHSNLVQLLGVIVEEKG-GLYI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPSGSLKEYL-PKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTkaietdKE 1033
Cdd:cd05082     78 VTEYMAKGSLVDYLrSRGRSVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLT------KE 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1034 YYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTycdsdsspmalFLKMIGPthgQMTVTRLVNTLKEGKR 1113
Cdd:cd05082    152 ASSTQDTGKLPVKWTAPEALREKKFSTKSDVWSFGILLWEIYS-----------FGRVPYP---RIPLKDVVPRVEKGYK 217
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1013071061 1114 LPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFE 1150
Cdd:cd05082    218 MDAPDGCPPAVYDVMKNCWHLDAAMRPSFLQLREQLE 254
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
878-1142 1.17e-50

Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Musk is a receptor PTK (RTK) containing an extracellular region with four immunoglobulin-like domains and a cysteine-rich cluster, a transmembrane segment, and an intracellular catalytic domain. Musk is expressed and concentrated in the postsynaptic membrane in skeletal muscle. It is essential for the establishment of the neuromuscular junction (NMJ), a peripheral synapse that conveys signals from motor neurons to muscle cells. Agrin, a large proteoglycan released from motor neurons, stimulates Musk autophosphorylation and activation, leading to the clustering of acetylcholine receptors (AChRs). To date, there is no evidence to suggest that agrin binds directly to Musk. Mutations in AChR, Musk and other partners are responsible for diseases of the NMJ, such as the autoimmune syndrome myasthenia gravis. The Musk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 180.80  E-value: 1.17e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVELCRYD---PEGDNTgeQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEdgGNGIKL 954
Cdd:cd05050     10 VRDIGQGAFGRVFQARAPgllPYEPFT--MVAVKMLKEEASADMQADFQREAALMAEFDHPNIVKLLGVCAV--GKPMCL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPSGSLKEYL---------------------PKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVES 1013
Cdd:cd05050     86 LFEYMAYGDLNEFLrhrspraqcslshstssarkcGLNPLPLSCTEQLCIAKQVAAGMAYLSERKFVHRDLATRNCLVGE 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1014 EHQVKIGDFGLTKAIETdKEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCdsdsspmalflkmIG 1093
Cdd:cd05050    166 NMVVKIADFGLSRNIYS-ADYYKASENDAIPIRWMPPESIFYNRYTTESDVWAYGVVLWEIFSYG-------------MQ 231
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1013071061 1094 PTHGqMTVTRLVNTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSF 1142
Cdd:cd05050    232 PYYG-MAHEEVIYYVRDGNVLSCPDNCPLELYNLMRLCWSKLPSDRPSF 279
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
875-1154 6.17e-50

Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER4 (ErbB4) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands that bind HER4 fall into two groups, the neuregulins (or heregulins) and some EGFR (HER1) ligands including betacellulin, HBEGF, and epiregulin. All four neuregulins (NRG1-4) interact with HER4. Upon ligand binding, HER4 forms homo- or heterodimers with other HER proteins. HER4 is essential in embryonic development. It is implicated in mammary gland, cardiac, and neural development. As a postsynaptic receptor of NRG1, HER4 plays an important role in synaptic plasticity and maturation. The impairment of NRG1/HER4 signaling may contribute to schizophrenia. The HER4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173655 [Multi-domain]  Cd Length: 303  Bit Score: 179.11  E-value: 6.17e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  875 LKRIRDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGgngIKL 954
Cdd:cd05110      9 LKRVKVLGSGAFGTVYKGIWVPEGETVKIPVAIKILNETTGPKANVEFMDEALIMASMDHPHLVRLLGVCLSPT---IQL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEY 1034
Cdd:cd05110     86 VTQLMPHGCLLDYVHEHKDNIGSQLLLNWCVQIAKGMMYLEERRLVHRDLAARNVLVKSPNHVKITDFGLARLLEGDEKE 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1035 YTVkDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCdsdsspmalflkmiGPTHGQMTVTRLVNTLKEGKRL 1114
Cdd:cd05110    166 YNA-DGGKMPIKWMALECIHYRKFTHQSDVWSYGVTIWELMTFG--------------GKPYDGIPTREIPDLLEKGERL 230
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1013071061 1115 PCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALLK 1154
Cdd:cd05110    231 PQPPICTIDVYMVMVKCWMIDADSRPKFKELAAEFSRMAR 270
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
865-1153 1.82e-49

Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The PDGFR subfamily consists of PDGFR alpha, PDGFR beta, KIT, CSF-1R, the mammalian FLT3, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. PDGFR kinase domains are autoinhibited by their juxtamembrane regions containing tyr residues. The binding to their ligands leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR subfamily receptors are important in the development of a variety of cells. PDGFRs are expressed in a many cells including fibroblasts, neurons, endometrial cells, mammary epithelial cells, and vascular smooth muscle cells. PDGFR signaling is critical in normal embryonic development, angiogenesis, and wound healing. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. Mammalian FLT3 plays an important role in the survival, proliferation, and differentiation of stem cells. The PDGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 177.68  E-value: 1.82e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  865 VDPTH--------FEKRFLKRIRDLGEGHFGKV-ELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNL-YH 934
Cdd:cd05055     19 IDPTQlpydlkweFPRNNLSFGKTLGAGAFGKVvEATAYGLSKSDAVMKVAVKMLKPTAHSSEREALMSELKIMSHLgNH 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  935 ENIVKYKGICTEDGGngIKLIMEFLPSGSLKEYLPKNKNK-INLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVES 1013
Cdd:cd05055     99 ENIVNLLGACTIGGP--ILVITEYCCYGDLLNFLRRKRESfLTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLLTH 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1014 EHQVKIGDFGLTKAIETDKEyYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSdsspmalflkmig 1093
Cdd:cd05055    177 GKIVKICDFGLARDIMNDSN-YVVKGNARLPVKWMAPESIFNCVYTFESDVWSYGILLWEIFSLGSN------------- 242
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1094 PTHGQMTVTRLVNTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALL 1153
Cdd:cd05055    243 PYPGMPVDSKFYKLIKEGYRMAQPEHAPAEIYDIMKTCWDADPLKRPTFKQIVQLIGKQL 302
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
881-1142 2.43e-49

Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes (or Fps) is a cytoplasmic (or nonreceptor) PTK containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated PTK activity. Fes kinase is expressed in myeloid, vascular endothelial, epithelial, and neuronal cells. It plays important roles in cell growth and differentiation, angiogenesis, inflammation and immunity, and cytoskeletal regulation. A recent study implicates Fes kinase as a tumor suppressor in colorectal cancer. The Fes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 175.89  E-value: 2.43e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYdpEGDNTgeQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDggNGIKLIMEFLP 960
Cdd:cd05084      4 IGRGNFGEVFSGRL--RADNT--PVAVKSCRETLPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQK--QPIYIVMELVQ 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  961 SGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAiETDKEYYTVKDD 1040
Cdd:cd05084     78 GGDFLTFLRTEGPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSRE-EEDGVYAATGGM 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1041 RDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYcdsDSSPMALflkmigPTHGQmtvTRlvNTLKEGKRLPCPPNC 1120
Cdd:cd05084    157 KQIPVKWTAPEALNYGRYSSESDVWSFGILLWETFSL---GAVPYAN------LSNQQ---TR--EAVEQGVRLPCPENC 222
                          250       260
                   ....*....|....*....|..
gi 1013071061 1121 PDEVYQLMRKCWEFQPSNRTSF 1142
Cdd:cd05084    223 PDEVYRLMEQCWEYDPRKRPSF 244
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
881-1150 8.54e-49

Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Chk is also referred to as megakaryocyte-associated tyrosine kinase (Matk). Chk inhibits Src kinases using a noncatalytic mechanism by simply binding to them. As a negative regulator of Src kinases, Chk may play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Chk is expressed in brain and hematopoietic cells. Like Csk, it is a cytoplasmic (or nonreceptor) tyr kinase containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases that are anchored to the plasma membrane, Chk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Studies in mice reveal that Chk is not functionally redundant with Csk and that it plays an important role as a regulator of immune responses. Chk also plays a role in neural differentiation in a manner independent of Src by enhancing Mapk activation via Ras-mediated signaling. The Chk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270666 [Multi-domain]  Cd Length: 254  Bit Score: 174.29  E-value: 8.54e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVElcrydpEGDNTGEQVAVKSLKPESGGNHIADlkkEIEILRNLYHENIVKYKGICTEdggNGIKLIMEFLP 960
Cdd:cd05083     14 IGEGEFGAVL------QGEYMGQKVAVKNIKCDVTAQAFLE---ETAVMTKLQHKNLVRLLGVILH---NGLYIVMELMS 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  961 SGSLKEYL-PKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDkeyytvKD 1039
Cdd:cd05083     82 KGNLVNFLrSRGRALVPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFGLAKVGSMG------VD 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1040 DRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYcdsDSSPmalflkmigptHGQMTVTRLVNTLKEGKRLPCPPN 1119
Cdd:cd05083    156 NSRLPVKWTAPEALKNKKFSSKSDVWSYGVLLWEVFSY---GRAP-----------YPKMSVKEVKEAVEKGYRMEPPEG 221
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1013071061 1120 CPDEVYQLMRKCWEFQPSNRTSFQNLIEGFE 1150
Cdd:cd05083    222 CPPDVYSIMTSCWEAEPGKRPSFKKLREKLE 252
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
866-1153 1.70e-48

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. There are many splice variants of FGFR2 which show differential expression and binding to FGF ligands. Disruption of either FGFR2 or FGFR2b is lethal in mice, due to defects in the placenta or severe impairment of tissue development including lung, limb, and thyroid, respectively. Disruption of FGFR2c in mice results in defective bone and skull development. Genetic alterations of FGFR2 are associated with many human skeletal disorders including Apert syndrome, Crouzon syndrome, Jackson-Weiss syndrome, and Pfeiffer syndrome. FGFR2 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 175.59  E-value: 1.70e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  866 DPT-HFEKRFLKRIRDLGEGHFGKV---ELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNL-YHENIVKY 940
Cdd:cd05101     16 DPKwEFPRDKLTLGKPLGEGCFGQVvmaEAVGIDKDKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIgKHKNIINL 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  941 KGICTEDGGngIKLIMEFLPSGSLKEYLPKNK---------------NKINLKQQLKYAVQICKGMDYLGSRQYVHRDLA 1005
Cdd:cd05101     96 LGACTQDGP--LYVIVEYASKGNLREYLRARRppgmeysydinrvpeEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLA 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1006 ARNVLVESEHQVKIGDFGLTKAIEtDKEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTycdsdsspm 1085
Cdd:cd05101    174 ARNVLVTENNVMKIADFGLARDIN-NIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFT--------- 243
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1013071061 1086 alflkMIGPTHGQMTVTRLVNTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALL 1153
Cdd:cd05101    244 -----LGGSPYPGIPVEELFKLLKEGHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIL 306
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
864-1149 2.57e-48

Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Hck is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Hck is present in myeloid and lymphoid cells that play a role in the development of cancer. It may be important in the oncogenic signaling of the protein Tel-Abl, which induces a chronic myelogenous leukemia (CML)-like disease. Hck also acts as a negative regulator of G-CSF-induced proliferation of granulocytic precursors, suggesting a possible role in the development of acute myeloid leukemia (AML). In addition, Hck is essential in regulating the degranulation of polymorphonuclear leukocytes. Genetic polymorphisms affect the expression level of Hck, which affects PMN mediator release and influences the development of chronic obstructive pulmonary disease (COPD). Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Hck subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 173.29  E-value: 2.57e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  864 EVDPTHFEKRFLKRIRDLGEGHFGKVELCRYdpegdNTGEQVAVKSLKPesGGNHIADLKKEIEILRNLYHENIVKYKGI 943
Cdd:cd05073      2 EKDAWEIPRESLKLEKKLGAGQFGEVWMATY-----NKHTKVAVKTMKP--GSMSVEAFLAEANVMKTLQHDKLVKLHAV 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  944 CTEDGgngIKLIMEFLPSGSLKEYLPKNK-NKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDF 1022
Cdd:cd05073     75 VTKEP---IYIITEFMAKGSLLDFLKSDEgSKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADF 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1023 GLTKAIETDKeyYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSdsspmalflkmigPTHGqMTVT 1102
Cdd:cd05073    152 GLARVIEDNE--YTAREGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLMEIVTYGRI-------------PYPG-MSNP 215
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1103 RLVNTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSF---QNLIEGF 1149
Cdd:cd05073    216 EVIRALERGYRMPRPENCPEELYNIMMRCWKNRPEERPTFeyiQSVLDDF 265
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
879-1153 5.47e-48

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Many FGFR3 splice variants have been reported with the IIIb and IIIc isoforms being the predominant forms. FGFR3 IIIc is the isoform expressed in chondrocytes, the cells affected in dwarfism, while IIIb is expressed in epithelial cells. FGFR3 ligands include FGF1, FGF2, FGF4, FGF8, FGF9, and FGF23. It is a negative regulator of long bone growth. In the cochlear duct and in the lens, FGFR3 is involved in differentiation while it appears to have a role in cell proliferation in epithelial cells. Germline mutations in FGFR3 are associated with skeletal disorders including several forms of dwarfism. Some missense mutations are associated with multiple myeloma and carcinomas of the bladder and cervix. Overexpression of FGFR3 is found in thyroid carcinoma. FGFR3 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 174.82  E-value: 5.47e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGHFGKV---ELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNL-YHENIVKYKGICTEDGGngIKL 954
Cdd:cd05100     18 KPLGEGCFGQVvmaEAIGIDKDKPNKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQDGP--LYV 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPSGSLKEYLPKNK---------------NKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKI 1019
Cdd:cd05100     96 LVEYASKGNLREYLRARRppgmdysfdtcklpeEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKI 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1020 GDFGLTKAIEtDKEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTycdsdsspmalflkmIGPT-HGQ 1098
Cdd:cd05100    176 ADFGLARDVH-NIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFT---------------LGGSpYPG 239
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1013071061 1099 MTVTRLVNTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALL 1153
Cdd:cd05100    240 IPVEELFKLLKEGHRMDKPANCTHELYMIMRECWHAVPSQRPTFKQLVEDLDRVL 294
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
870-1149 1.06e-47

Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER3 contains an impaired tyr kinase domain, which lacks crucial residues for catalytic activity against exogenous substrates but is still able to bind ATP and autophosphorylate. HER3 binds the neuregulin ligands, NRG1 and NRG2, and it relies on its heterodimerization partners for activity following ligand binding. The HER2-HER3 heterodimer constitutes a high affinity co-receptor capable of potent mitogenic signaling. HER3 participates in a signaling pathway involved in the proliferation, survival, adhesion, and motility of tumor cells. The HER3 subfamily is part of a larger superfamily that includes other pseudokinases and the the catalytic domains of active kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173656 [Multi-domain]  Cd Length: 279  Bit Score: 172.06  E-value: 1.06e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  870 FEKRFLKRIRDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTedgG 949
Cdd:cd05111      4 FKETELRKLKVLGSGVFGTVHKGIWIPEGDSIKIPVAIKVIQDRSGRQSFQAVTDHMLAIGSLDHAYIVRLLGICP---G 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  950 NGIKLIMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIE 1029
Cdd:cd05111     81 ASLQLVTQLLPLGSLLDHVRQHRGSLGPQLLLNWCVQIAKGMYYLEEHRMVHRNLAARNVLLKSPSQVQVADFGVADLLY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1030 TDKEYYtVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYcdsDSSPMAlflkmigpthgQMTVTRLVNTLK 1109
Cdd:cd05111    161 PDDKKY-FYSEAKTPIKWMALESIHFGKYTHQSDVWSYGVTVWEMMTF---GAEPYA-----------GMRLAEVPDLLE 225
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1013071061 1110 EGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGF 1149
Cdd:cd05111    226 KGERLAQPQICTIDVYMVMVKCWMIDENIRPTFKELANEF 265
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
881-1145 1.50e-47

Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; Fer kinase; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fer kinase is a member of the Fes subfamily of proteins which are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. Fer kinase is expressed in a wide variety of tissues, and is found to reside in both the cytoplasm and the nucleus. It plays important roles in neuronal polarization and neurite development, cytoskeletal reorganization, cell migration, growth factor signaling, and the regulation of cell-cell interactions mediated by adherens junctions and focal adhesions. Fer kinase also regulates cell cycle progression in malignant cells.


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 170.57  E-value: 1.50e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDpegDNTgeQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDggNGIKLIMEFLP 960
Cdd:cd05085      4 LGKGNFGEVYKGTLK---DKT--PVAVKTCKEDLPQELKIKFLSEARILKQYDHPNIVKLIGVCTQR--QPIYIVMELVP 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  961 SGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKaiETDKEYYTVKDD 1040
Cdd:cd05085     77 GGDFLSFLRKKKDELKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSR--QEDDGVYSSSGL 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1041 RDSPVFWYAPECLMQSKFYIASDVWSFGVTLHElltycdsdsspmaLFLKMIGPTHGqMTVTRLVNTLKEGKRLPCPPNC 1120
Cdd:cd05085    155 KQIPIKWTAPEALNYGRYSSESDVWSFGILLWE-------------TFSLGVCPYPG-MTNQQAREQVEKGYRMSAPQRC 220
                          250       260
                   ....*....|....*....|....*
gi 1013071061 1121 PDEVYQLMRKCWEFQPSNRTSFQNL 1145
Cdd:cd05085    221 PEDIYKIMQRCWDYNPENRPKFSEL 245
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
881-1074 6.39e-47

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 167.45  E-value: 6.39e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDpegdNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDggNGIKLIMEFLP 960
Cdd:cd00180      1 LGKGSFGKVYKARDK----ETGKKVAVKVIPKEKLKKLLEELLREIEILKKLNHPNIVKLYDVFETE--NFLYLVMEYCE 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  961 SGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIeTDKEYYTVKDD 1040
Cdd:cd00180     75 GGSLKDLLKENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDL-DSDDSLLKTTG 153
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1013071061 1041 RDSPVFWYAPECLMQSKFYIASDVWSFGVTLHEL 1074
Cdd:cd00180    154 GTTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL 187
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
870-1147 6.89e-47

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The VEGFR subfamily consists of VEGFR1 (Flt1), VEGFR2 (Flk1), VEGFR3 (Flt4), and similar proteins. VEGFR subfamily members are receptor PTKss (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. There are five VEGF ligands in mammals, which bind, in an overlapping pattern to the three VEGFRs, which can form homo or heterodimers. VEGFRs regulate the cardiovascular system. They are critical for vascular development during embryogenesis and blood vessel formation in adults. They induce cellular functions common to other growth factor receptors such as cell migration, survival, and proliferation. The VEGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 170.36  E-value: 6.89e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  870 FEKRFLKRIRDLGEGHFGKV-ELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNL-YHENIVKYKGICTED 947
Cdd:cd05054      4 FPRDRLKLGKPLGRGAFGKViQASAFGIDKSATCRTVAVKMLKEGATASEHKALMTELKILIHIgHHLNVVNLLGACTKP 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  948 GGNgIKLIMEFLPSGSLKEYL-------------------------PKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHR 1002
Cdd:cd05054     84 GGP-LMVIVEFCKFGNLSNYLrskreefvpyrdkgardveeeedddELYKEPLTLEDLICYSFQVARGMEFLASRKCIHR 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1003 DLAARNVLVESEHQVKIGDFGLTKAIETDKEYYTVKDDRdSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSds 1082
Cdd:cd05054    163 DLAARNILLSENNVVKICDFGLARDIYKDPDYVRKGDAR-LPLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFSLGAS-- 239
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1013071061 1083 spmalflkmigPTHGQMTVTRLVNTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIE 1147
Cdd:cd05054    240 -----------PYPGVQMDEEFCRRLKEGTRMRAPEYTTPEIYQIMLDCWHGEPKERPTFSELVE 293
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
879-1145 3.31e-46

Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes a subset of Src-like PTKs including Src, Fyn, Yrk, and Yes, which are all widely expressed. Yrk has been detected only in chickens. It is primarily found in neuronal and epithelial cells and in macrophages. It may play a role in inflammation and in response to injury. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. They are also implicated in acute inflammatory responses and osteoclast function. The Src/Fyn-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 166.63  E-value: 3.31e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGHFGKVELCRYdpegdNTGEQVAVKSLKPesGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGgngIKLIMEF 958
Cdd:cd14203      1 VKLGQGCFGEVWMGTW-----NGTTKVAIKTLKP--GTMSPEAFLEEAQIMKKLRHDKLVQLYAVVSEEP---IYIVTEF 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  959 LPSGSLKEYLPKNKNK-INLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKeyYTV 1037
Cdd:cd14203     71 MSKGSLLDFLKDGEGKyLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNE--YTA 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1038 KDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTycdsdsspmalflKMIGPTHGqMTVTRLVNTLKEGKRLPCP 1117
Cdd:cd14203    149 RQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVT-------------KGRVPYPG-MNNREVLEQVERGYRMPCP 214
                          250       260
                   ....*....|....*....|....*...
gi 1013071061 1118 PNCPDEVYQLMRKCWEFQPSNRTSFQNL 1145
Cdd:cd14203    215 PGCPESLHELMCQCWRKDPEERPTFEYL 242
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
876-1139 3.76e-46

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 166.54  E-value: 3.76e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  876 KRIRDLGEGHFGKVELCRYDpegdNTGEQVAVKSLK-PESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDggNGIKL 954
Cdd:cd06606      3 KKGELLGKGSFGSVYLALNL----DTGELMAVKEVElSGDSEEELEALEREIRILSSLKHPNIVRYLGTERTE--NTLNI 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPSGSLKEYLPKNKnKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEY 1034
Cdd:cd06606     77 FLEYVPGGSLASLLKKFG-KLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKRLAEIATG 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1035 YTVKDDRDSPvFWYAPECLMQSKFYIASDVWSFGVTLHELLTYC---DSDSSPMALFLKMIGPTHgqmtvtrlvntlkeg 1111
Cdd:cd06606    156 EGTKSLRGTP-YWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKppwSELGNPVAALFKIGSSGE--------------- 219
                          250       260
                   ....*....|....*....|....*....
gi 1013071061 1112 krLPC-PPNCPDEVYQLMRKCWEFQPSNR 1139
Cdd:cd06606    220 --PPPiPEHLSEEAKDFLRKCLQRDPKKR 246
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
864-1153 4.67e-46

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The EphA2 receptor is overexpressed in tumor cells and tumor blood vessels in a variety of cancers including breast, prostate, lung, and colon. As a result, it is an attractive target for drug design since its inhibition could affect several aspects of tumor progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 133194 [Multi-domain]  Cd Length: 268  Bit Score: 166.69  E-value: 4.67e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  864 EVDPTHFEKRflkriRDLGEGHFGKVELCRYDPEGDNTgEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGI 943
Cdd:cd05063      1 EIHPSHITKQ-----KVIGAGEFGEVFRGILKMPGRKE-VAVAIKTLKPGYTEKQRQDFLSEASIMGQFSHHNIIRLEGV 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  944 CTEdgGNGIKLIMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFG 1023
Cdd:cd05063     75 VTK--FKPAMIITEYMENGALDKYLRDHDGEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFG 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1024 LTKAIETDKEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSdsspmalflkmigpTHGQMTVTR 1103
Cdd:cd05063    153 LSRVLEDDPEGTYTTSGGKIPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSFGER--------------PYWDMSNHE 218
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1104 LVNTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALL 1153
Cdd:cd05063    219 VMKAINDGFRLPAPMDCPSAVYQLMLQCWQQDRARRPRFVDIVNLLDKLL 268
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
870-1145 5.35e-46

Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR-like proteins are members of the DDR subfamily, which are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 167.46  E-value: 5.35e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  870 FEKRFLKRIRDLGEGHFGKVELCRYD----------PEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVK 939
Cdd:cd05097      2 FPRQQLRLKEKLGEGQFGEVHLCEAEglaeflgegaPEFDGQPVLVAVKMLRADVTKTARNDFLKEIKIMSRLKNPNIIR 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  940 YKGICTEDggNGIKLIMEFLPSGSLKEYLPK-----------NKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARN 1008
Cdd:cd05097     82 LLGVCVSD--DPLCMITEYMENGDLNQFLSQreiestfthanNIPSVSIANLLYMAVQIASGMKYLASLNFVHRDLATRN 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1009 VLVESEHQVKIGDFGLTKAIETDkEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCdsDSSPMALF 1088
Cdd:cd05097    160 CLVGNHYTIKIADFGMSRNLYSG-DYYRIQGRAVLPIRWMAWESILLGKFTTASDVWAFGVTLWEMFTLC--KEQPYSLL 236
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1013071061 1089 lkmigpTHGQMTVTRLVNTLKEGKR--LPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNL 1145
Cdd:cd05097    237 ------SDEQVIENTGEFFRNQGRQiyLSQTPLCPSPVFKLMMRCWSRDIKDRPTFNKI 289
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
869-1154 1.16e-45

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkC is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkC to its ligand, neurotrophin 3 (NT3), results in receptor oligomerization and activation of the catalytic domain. TrkC is broadly expressed in the nervous system and in some non-neural tissues including the developing heart. NT3/TrkC signaling plays an important role in the innervation of the cardiac conducting system and the development of smooth muscle cells. Mice deficient with NT3 and TrkC have multiple heart defects. NT3/TrkC signaling is also critical for the development and maintenance of enteric neurons that are important for the control of gut peristalsis. The TrkC subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 166.34  E-value: 1.16e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  869 HFEKRFLKRIRDLGEGHFGKVELCR-YDPEGDNTGEQVAVKSLKPESGGNHiADLKKEIEILRNLYHENIVKYKGICTEd 947
Cdd:cd05094      1 HIKRRDIVLKRELGEGAFGKVFLAEcYNLSPTKDKMLVAVKTLKDPTLAAR-KDFQREAELLTNLQHDHIVKFYGVCGD- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  948 gGNGIKLIMEFLPSGSLKEYLP---------------KNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVE 1012
Cdd:cd05094     79 -GDPLIMVFEYMKHGDLNKFLRahgpdamilvdgqprQAKGELGLSQMLHIATQIASGMVYLASQHFVHRDLATRNCLVG 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1013 SEHQVKIGDFGLTKAIETdKEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYcdsDSSPMAlflkmi 1092
Cdd:cd05094    158 ANLLVKIGDFGMSRDVYS-TDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTY---GKQPWF------ 227
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1013071061 1093 gpthgQMTVTRLVNTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALLK 1154
Cdd:cd05094    228 -----QLSNTEVIECITQGRVLERPRVCPKEVYDIMLGCWQREPQQRLNIKEIYKILHALGK 284
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
870-1145 1.44e-45

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR2 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR2 results in a slow but sustained receptor activation. DDR2 binds mostly to fibrillar collagens as well as collagen X. DDR2 is widely expressed in many tissues with the highest levels found in skeletal muscle, skin, kidney and lung. It is important in cell proliferation and development. Mice, with a deletion of DDR2, suffer from dwarfism and delayed healing of epidermal wounds. DDR2 also contributes to collagen (type I) regulation by inhibiting fibrillogenesis and altering the morphology of collagen fibers. It is also expressed in immature dendritic cells (DCs), where it plays a role in DC activation and function. The DDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 166.32  E-value: 1.44e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  870 FEKRFLKRIRDLGEGHFGKVELCryDPEG-----------DNTGEQ---VAVKSLKPESGGNHIADLKKEIEILRNLYHE 935
Cdd:cd05095      2 FPRKLLTFKEKLGEGQFGEVHLC--EAEGmekfmdkdfalEVSENQpvlVAVKMLRADANKNARNDFLKEIKIMSRLKDP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  936 NIVKYKGICTEDggNGIKLIMEFLPSGSLKEYLPKNKNKINLKQ----------QLKY-AVQICKGMDYLGSRQYVHRDL 1004
Cdd:cd05095     80 NIIRLLAVCITD--DPLCMITEYMENGDLNQFLSRQQPEGQLALpsnaltvsysDLRFmAAQIASGMKYLSSLNFVHRDL 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1005 AARNVLVESEHQVKIGDFGLTKAIETDkEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSDSsp 1084
Cdd:cd05095    158 ATRNCLVGKNYTIKIADFGMSRNLYSG-DYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETLTFCREQP-- 234
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1013071061 1085 malflkmigptHGQMTVTRLVNTLKEGKR-------LPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNL 1145
Cdd:cd05095    235 -----------YSQLSDEQVIENTGEFFRdqgrqtyLPQPALCPDSVYKLMLSCWRRDTKDRPSFQEI 291
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
881-1145 2.59e-45

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR1 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR1 results in a slow but sustained receptor activation. DDR1 binds to all collagens tested to date (types I-IV). It is widely expressed in many tissues. It is abundant in the brain and is also found in keratinocytes, colonic mucosa epithelium, lung epithelium, thyroid follicles, and the islets of Langerhans. During embryonic development, it is found in the developing neuroectoderm. DDR1 is a key regulator of cell morphogenesis, differentiation and proliferation. It is important in the development of the mammary gland, the vasculator and the kidney. DDR1 is also found in human leukocytes, where it facilitates cell adhesion, migration, maturation, and cytokine production. The DDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133227 [Multi-domain]  Cd Length: 304  Bit Score: 165.88  E-value: 2.59e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDPEGDNTGEQ------------VAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDg 948
Cdd:cd05096     13 LGEGQFGEVHLCEVVNPQDLPTLQfpfnvrkgrpllVAVKILRPDANKNARNDFLKEVKILSRLKDPNIIRLLGVCVDE- 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  949 gNGIKLIMEFLPSGSLKEYL----------PKNKNK--------INLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVL 1010
Cdd:cd05096     92 -DPLCMITEYMENGDLNQFLsshhlddkeeNGNDAVppahclpaISYSSLLHVALQIASGMKYLSSLNFVHRDLATRNCL 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1011 VESEHQVKIGDFGLTKAIETDkEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSDSspmalflk 1090
Cdd:cd05096    171 VGENLTIKIADFGMSRNLYAG-DYYRIQGRAVLPIRWMAWECILMGKFTTASDVWAFGVTLWEILMLCKEQP-------- 241
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1013071061 1091 migptHGQMTVTRLVNTLKEGKR-------LPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNL 1145
Cdd:cd05096    242 -----YGELTDEQVIENAGEFFRdqgrqvyLFRPPPCPQGLYELMLQCWSRDCRERPSFSDI 298
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
875-1146 6.04e-45

Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Itk, also known as Tsk or Emt, is a member of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Itk contains the Tec homology (TH) domain containing one proline-rich region and a zinc-binding region. Itk is expressed in T-cells and mast cells, and is important in their development and differentiation. Of the three Tec kinases expressed in T-cells, Itk plays the predominant role in T-cell receptor (TCR) signaling. It is activated by phosphorylation upon TCR crosslinking and is involved in the pathway resulting in phospholipase C-gamma1 activation and actin polymerization. It also plays a role in the downstream signaling of the T-cell costimulatory receptor CD28, the T-cell surface receptor CD2, and the chemokine receptor CXCR4. In addition, Itk is crucial for the development of T-helper(Th)2 effector responses. The Itk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133243 [Multi-domain]  Cd Length: 256  Bit Score: 163.20  E-value: 6.04e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  875 LKRIRDLGEGHFGKVELCRYDPEgdntgEQVAVKSLKpeSGGNHIADLKKEIEILRNLYHENIVKYKGICTEDggNGIKL 954
Cdd:cd05112      6 LTFVQEIGSGQFGLVHLGYWLNK-----DKVAIKTIR--EGAMSEEDFIEEAEVMMKLSHPKLVQLYGVCLEQ--APICL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKey 1034
Cdd:cd05112     77 VFEFMEHGCLSDYLRTQRGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMTRFVLDDQ-- 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1035 YTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTycdSDSSPmalflkmigptHGQMTVTRLVNTLKEGKRL 1114
Cdd:cd05112    155 YTSSTGTKFPVKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFS---EGKIP-----------YENRSNSEVVEDINAGFRL 220
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1013071061 1115 PCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLI 1146
Cdd:cd05112    221 YKPRLASTHVYEIMNHCWKERPEDRPSFSLLL 252
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
881-1146 6.20e-45

Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie proteins, consisting of Tie1 and Tie2, are receptor PTKs (RTKs) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2, while no specific ligand has been identified for Tie1. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. In vivo studies of Tie1 show that it is critical in vascular development. The Tie subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 163.67  E-value: 6.20e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDPEGDNTgeQVAVKSLKPESGGNHIADLKKEIEILRNL-YHENIVKYKGICTEDGGngIKLIMEFL 959
Cdd:cd05047      3 IGEGNFGQVLKARIKKDGLRM--DAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGY--LYLAIEYA 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  960 PSGSLKEYLPKNK---------------NKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGL 1024
Cdd:cd05047     79 PHGNLLDFLRKSRvletdpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1025 TKAietdKEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTycdsdsspmalflkMIGPTHGQMTVTRL 1104
Cdd:cd05047    159 SRG----QEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVS--------------LGGTPYCGMTCAEL 220
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1013071061 1105 VNTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLI 1146
Cdd:cd05047    221 YEKLPQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQIL 262
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
879-1153 9.14e-45

Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyro3 (or Sky) is predominantly expressed in the central nervous system and the brain, and functions as a neurotrophic factor. It is also expressed in osteoclasts and has a role in bone resorption. Tyro3 is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Tyro3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 163.55  E-value: 9.14e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGHFGKVELCRYDPEgDNTGEQVAVKSLKPE-SGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGNG----IK 953
Cdd:cd05074     15 RMLGKGEFGSVREAQLKSE-DGSFQKVAVKMLKADiFSSSDIEEFLREAACMKEFDHPNVIKLIGVSLRSRAKGrlpiPM 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  954 LIMEFLPSGSLKEYLPKNK---NKINLKQQ--LKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAI 1028
Cdd:cd05074     94 VILPFMKHGDLHTFLLMSRigeEPFTLPLQtlVRFMIDIASGMEYLSSKNFIHRDLAARNCMLNENMTVCVADFGLSKKI 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1029 ETDkEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTycdSDSSPMAlflkmigpthgQMTVTRLVNTL 1108
Cdd:cd05074    174 YSG-DYYRQGCASKLPVKWLALESLADNVYTTHSDVWAFGVTMWEIMT---RGQTPYA-----------GVENSEIYNYL 238
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1013071061 1109 KEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALL 1153
Cdd:cd05074    239 IKGNRLKQPPDCLEDVYELMCQCWSPEPKCRPSFQHLRDQLELIW 283
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
873-1145 1.96e-44

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror kinases are expressed in many tissues during development. Avian Ror1 was found to be involved in late limb development. Studies in mice reveal that Ror1 is important in the regulation of neurite growth in central neurons, as well as in respiratory development. Loss of Ror1 also enhances the heart and skeletal abnormalities found in Ror2-deficient mice. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 162.87  E-value: 1.96e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  873 RFLKrirDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDggNGI 952
Cdd:cd05090      8 RFME---ELGECAFGKIYKGHLYLPGMDHAQLVAIKTLKDYNNPQQWNEFQQEASLMTELHHPNIVCLLGVVTQE--QPV 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  953 KLIMEFLPSGSLKEYL----PKN------------KNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQ 1016
Cdd:cd05090     83 CMLFEFMNQGDLHEFLimrsPHSdvgcssdedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILVGEQLH 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1017 VKIGDFGLTKAIETdKEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCdsdsspmalflkmIGPTH 1096
Cdd:cd05090    163 VKISDLGLSREIYS-SDYYRVQNKSLLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFG-------------LQPYY 228
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1013071061 1097 GqMTVTRLVNTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNL 1145
Cdd:cd05090    229 G-FSNQEVIEMVRKRQLLPCSEDCPPRMYSLMTECWQEIPSRRPRFKDI 276
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
869-1154 2.08e-44

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkB is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkB to its ligands, brain-derived neurotrophic factor (BDNF) or neurotrophin 4 (NT4), results in receptor oligomerization and activation of the catalytic domain. TrkB is broadly expressed in the nervous system and in some non-neural tissues. It plays important roles in cell proliferation, differentiation, and survival. BDNF/Trk signaling plays a key role in regulating activity-dependent synaptic plasticity. TrkB also contributes to protection against gp120-induced neuronal cell death. TrkB overexpression is associated with poor prognosis in neuroblastoma (NB) and other human cancers. It acts as a suppressor of anoikis (detachment-induced apoptosis) and contributes to tumor metastasis. The TrkB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 162.90  E-value: 2.08e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  869 HFEKRFLKRIRDLGEGHFGKVELCR-YDPEGDNTGEQVAVKSLKpESGGNHIADLKKEIEILRNLYHENIVKYKGICTEd 947
Cdd:cd05093      1 HIKRHNIVLKRELGEGAFGKVFLAEcYNLCPEQDKILVAVKTLK-DASDNARKDFHREAELLTNLQHEHIVKFYGVCVE- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  948 gGNGIKLIMEFLPSGSLKEYLPKNK------------NKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEH 1015
Cdd:cd05093     79 -GDPLIMVFEYMKHGDLNKFLRAHGpdavlmaegnrpAELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENL 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1016 QVKIGDFGLTKAIETdKEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSdsspmalflkmigPT 1095
Cdd:cd05093    158 LVKIGDFGMSRDVYS-TDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQ-------------PW 223
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1013071061 1096 HgQMTVTRLVNTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALLK 1154
Cdd:cd05093    224 Y-QLSNNEVIECITQGRVLQRPRTCPKEVYDLMLGCWQREPHMRLNIKEIHSLLQNLAK 281
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
879-1153 3.49e-44

Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of most class EphA receptors including EphA3, EphA4, EphA5, and EphA7, but excluding EphA1, EphA2 and EphA10. Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. One exception is EphA4, which also binds ephrins-B2/B3. EphA receptors and ephrin-A ligands are expressed in multiple areas of the developing brain, especially in the retina and tectum. They are part of a system controlling retinotectal mapping. EphRs comprise the largest subfamily of receptor PTKs (RTKs). EphRs contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 161.57  E-value: 3.49e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGHFGKVELCRYDPEGDNTgEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEdgGNGIKLIMEF 958
Cdd:cd05066     10 KVIGAGEFGEVCSGRLKLPGKRE-IPVAIKTLKAGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTR--SKPVMIVTEY 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  959 LPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKE-YYTV 1037
Cdd:cd05066     87 MENGSLDAFLRKHDGQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDDPEaAYTT 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1038 KDDRdSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSdsspmalflkmigpTHGQMTVTRLVNTLKEGKRLPCP 1117
Cdd:cd05066    167 RGGK-IPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGER--------------PYWEMSNQDVIKAIEEGYRLPAP 231
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1013071061 1118 PNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALL 1153
Cdd:cd05066    232 MDCPAALHQLMLDCWQKDRNERPKFEQIVSILDKLI 267
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
883-1148 4.73e-44

Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase (RTK) containing an extracellular region with two leucine-rich motifs, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. The extracellular region of Ryk shows homology to the N-terminal domain of Wnt inhibitory factor-1 (WIF) and serves as the ligand (Wnt) binding domain of Ryk. Ryk is expressed in many different tissues both during development and in adults, suggesting a widespread function. It acts as a chemorepulsive axon guidance receptor of Wnt glycoproteins and is responsible for the establishment of axon tracts during the development of the central nervous system. In addition, studies in mice reveal that Ryk is essential in skeletal, craniofacial, and cardiac development. Thus, it appears Ryk is involved in signal transduction despite its lack of kinase activity. Ryk may function as an accessory protein that modulates the signals coming from catalytically active partner RTKs such as the Eph receptors. The Ryk subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270639 [Multi-domain]  Cd Length: 279  Bit Score: 161.47  E-value: 4.73e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  883 EGHFGKVELCRYDPEGDNTgEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGNGiKLIMEFLPSG 962
Cdd:cd05043     16 EGTFGRIFHGILRDEKGKE-EEVLVKTVKDHASEIQVTMLLQESSLLYGLSHQNLLPILHVCIEDGEKP-MVLYPYMNWG 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  963 SLKEYLPKNK-----NKINLKQQ--LKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDkEYY 1035
Cdd:cd05043     94 NLKLFLQQCRlseanNPQALSTQqlVHMALQIACGMSYLHRRGVIHKDIAARNCVIDDELQVKITDNALSRDLFPM-DYH 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1036 TVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLT-----YCDSDSSPMAlflkmigpthgqmtvtrlvNTLKE 1110
Cdd:cd05043    173 CLGDNENRPIKWMSLESLVNKEYSSASDVWSFGVLLWELMTlgqtpYVEIDPFEMA-------------------AYLKD 233
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1013071061 1111 GKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEG 1148
Cdd:cd05043    234 GYRLAQPINCPDELFAVMACCWALDPEERPSFQQLVQC 271
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
881-1154 7.32e-44

Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Mer (or Mertk) is named after its original reported expression pattern (monocytes, epithelial, and reproductive tissues). It is required for the ingestion of apoptotic cells by phagocytes such as macrophages, retinal pigment epithelial cells, and dendritic cells. Mer is also important in maintaining immune homeostasis. Mer is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Mer subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271106 [Multi-domain]  Cd Length: 284  Bit Score: 160.87  E-value: 7.32e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDPEgDNTGEQVAVKSLKPE-SGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGNGIK---LIM 956
Cdd:cd14204     15 LGEGEFGSVMEGELQQP-DGTNHKVAVKTMKLDnFSQREIEEFLSEAACMKDFNHPNVIRLLGVCLEVGSQRIPkpmVIL 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  957 EFLPSGSLKEYLPKNKNK-----INLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETD 1031
Cdd:cd14204     94 PFMKYGDLHSFLLRSRLGsgpqhVPLQTLLKFMIDIALGMEYLSSRNFLHRDLAARNCMLRDDMTVCVADFGLSKKIYSG 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1032 kEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTycdsdsspmalflKMIGPTHGQMTvTRLVNTLKEG 1111
Cdd:cd14204    174 -DYYRQGRIAKMPVKWIAVESLADRVYTVKSDVWAFGVTMWEIAT-------------RGMTPYPGVQN-HEIYDYLLHG 238
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1013071061 1112 KRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALLK 1154
Cdd:cd14204    239 HRLKQPEDCLDELYDIMYSCWRSDPTDRPTFTQLRENLEKLLE 281
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
879-1153 1.21e-43

Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The TAM subfamily consists of Tyro3 (or Sky), Axl, Mer (or Mertk), and similar proteins. TAM subfamily members are receptor tyr kinases (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. TAM proteins are implicated in a variety of cellular effects including survival, proliferation, migration, and phagocytosis. They are also associated with several types of cancer as well as inflammatory, autoimmune, vascular, and kidney diseases. The TAM subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270631 [Multi-domain]  Cd Length: 273  Bit Score: 160.01  E-value: 1.21e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGHFGKVELCRYDPEgDNTGEQVAVKSLKPE-SGGNHIADLKKEIEILRNLYHENIVKYKGIC-TEDGGNGIK--- 953
Cdd:cd05035      5 KILGEGEFGSVMEAQLKQD-DGSQLKVAVKTMKVDiHTYSEIEEFLSEAACMKDFDHPNVMRLIGVCfTASDLNKPPspm 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  954 LIMEFLPSGSLKEYL-----PKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAI 1028
Cdd:cd05035     84 VILPFMKHGDLHSYLlysrlGGLPEKLPLQTLLKFMVDIAKGMEYLSNRNFIHRDLAARNCMLDENMTVCVADFGLSRKI 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1029 ETDkEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTycdSDSSPMAlflkmiGPTHGQMtvtrlVNTL 1108
Cdd:cd05035    164 YSG-DYYRQGRISKMPVKWIALESLADNVYTSKSDVWSFGVTMWEIAT---RGQTPYP------GVENHEI-----YDYL 228
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1013071061 1109 KEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALL 1153
Cdd:cd05035    229 RNGNRLKQPEDCLDEVYFLMYFCWTVDPKDRPTFTKLREVLENIL 273
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
865-1146 1.95e-43

Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow kinase on the X chromosome; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Btk and Bmx (also named Etk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Btk contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Btk is expressed in B-cells, and a variety of myeloid cells including mast cells, platelets, neutrophils, and dendrictic cells. It interacts with a variety of partners, from cytosolic proteins to nuclear transcription factors, suggesting a diversity of functions. Stimulation of a diverse array of cell surface receptors, including antigen engagement of the B-cell receptor, leads to PH-mediated membrane translocation of Btk and subsequent phosphorylation by Src kinase and activation. Btk plays an important role in the life cycle of B-cells including their development, differentiation, proliferation, survival, and apoptosis. Mutations in Btk cause the primary immunodeficiency disease, X-linked agammaglobulinaemia (XLA) in humans. Bmx is primarily expressed in bone marrow and the arterial endothelium, and plays an important role in ischemia-induced angiogenesis. It facilitates arterial growth, capillary formation, vessel maturation, and bone marrow-derived endothelial progenitor cell mobilization. The Btk/Bmx subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 158.89  E-value: 1.95e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  865 VDPTHfekrfLKRIRDLGEGHFGKVELCRYDPEGDntgeqVAVKSLKpeSGGNHIADLKKEIEILRNLYHENIVKYKGIC 944
Cdd:cd05113      1 IDPKD-----LTFLKELGTGQFGVVKYGKWRGQYD-----VAIKMIK--EGSMSEDEFIEEAKVMMNLSHEKLVQLYGVC 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  945 TEDggNGIKLIMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGL 1024
Cdd:cd05113     69 TKQ--RPIFIITEYMANGCLLNYLREMRKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGL 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1025 TKAIETDKeyYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYcdsdsspmalflkmigpthGQMTVTRL 1104
Cdd:cd05113    147 SRYVLDDE--YTSSVGSKFPVRWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSL-------------------GKMPYERF 205
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1013071061 1105 VNT-----LKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLI 1146
Cdd:cd05113    206 TNSetvehVSQGLRLYRPHLASEKVYTIMYSCWHEKADERPTFKILL 252
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
875-1147 2.93e-43

Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte Tyrosine Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyr residues in protein substrates. ALK and LTK are orphan receptor PTKs (RTKs) whose ligands are not yet well-defined. ALK appears to play an important role in mammalian neural development as well as visceral muscle differentiation in Drosophila. ALK is aberrantly expressed as fusion proteins, due to chromosomal translocations, in about 60% of anaplastic large cell lymphomas (ALCLs). ALK fusion proteins are also found in rare cases of diffuse large B cell lymphomas (DLBCLs). LTK is mainly expressed in B lymphocytes and neuronal tissues. It is important in cell proliferation and survival. Transgenic mice expressing TLK display retarded growth and high mortality rate. In addition, a polymorphism in mouse and human LTK is implicated in the pathogenesis of systemic lupus erythematosus. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. They are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The ALK/LTK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270632 [Multi-domain]  Cd Length: 277  Bit Score: 159.09  E-value: 2.93e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  875 LKRIRDLGEGHFGKVELCRYDPE-GDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGNGIk 953
Cdd:cd05036      8 LTLIRALGQGAFGEVYEGTVSGMpGDPSPLQVAVKTLPELCSEQDEMDFLMEALIMSKFNHPNIVRCIGVCFQRLPRFI- 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  954 lIMEFLPSGSLKEYLPKNKNK------INLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLV---ESEHQVKIGDFGL 1024
Cdd:cd05036     87 -LLELMAGGDLKSFLRENRPRpeqpssLTMLDLLQLAQDVAKGCRYLEENHFIHRDIAARNCLLtckGPGRVAKIGDFGM 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1025 TKAIETdKEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHEL--LTYcdsdsspmalflkMIGPTHGQMTVT 1102
Cdd:cd05036    166 ARDIYR-ADYYRKGGKAMLPVKWMPPEAFLDGIFTSKTDVWSFGVLLWEIfsLGY-------------MPYPGKSNQEVM 231
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1013071061 1103 RLVNtlkEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIE 1147
Cdd:cd05036    232 EFVT---SGGRMDPPKNCPGPVYRIMTQCWQHIPEDRPNFSTILE 273
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
881-1146 2.53e-42

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinases 12 and 13; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K12 is also called MAPK upstream kinase (MUK), dual leucine zipper-bearing kinase (DLK) or leucine-zipper protein kinase (ZPK). It is involved in the c-Jun N-terminal kinase (JNK) pathway that directly regulates axonal regulation through the phosphorylation of microtubule-associated protein 1B (MAP1B). It also regulates the differentiation of many cell types including adipocytes and may play a role in adipogenesis. MAP3K13, also called leucine zipper-bearing kinase (LZK), directly phosphorylates and activates MKK7, which in turn activates the JNK pathway. It also activates NF-kB through IKK activation and this activity is enhanced by antioxidant protein-1 (AOP-1). MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAP2Ks (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K12/13 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270961 [Multi-domain]  Cd Length: 237  Bit Score: 154.96  E-value: 2.53e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYdpegdnTGEQVAVKSLKPEsggnhiadlkKEIEI--LRNLYHENIVKYKGICTEDGGNGIklIMEF 958
Cdd:cd14059      1 LGSGAQGAVFLGKF------RGEEVAVKKVRDE----------KETDIkhLRKLNHPNIIKFKGVCTQAPCYCI--LMEY 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  959 LPSGSLKEYLpKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIeTDKeyyTVK 1038
Cdd:cd14059     63 CPYGQLYEVL-RAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKEL-SEK---STK 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1039 DDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLT----YCDSDSSPMalfLKMIGPthgqmtvtrlvNTLkegkRL 1114
Cdd:cd14059    138 MSFAGTVAWMAPEVIRNEPCSEKVDIWSFGVVLWELLTgeipYKDVDSSAI---IWGVGS-----------NSL----QL 199
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1013071061 1115 PCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLI 1146
Cdd:cd14059    200 PVPSTCPDGFKLLMKQCWNSKPRNRPSFRQIL 231
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
878-1147 2.54e-42

Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. InsR is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the insulin ligand to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR signaling plays an important role in many cellular processes including glucose homeostasis, glycogen synthesis, lipid and protein metabolism, ion and amino acid transport, cell cycle and proliferation, cell differentiation, gene transcription, and nitric oxide synthesis. Insulin resistance, caused by abnormalities in InsR signaling, has been described in diabetes, hypertension, cardiovascular disease, metabolic syndrome, heart failure, and female infertility. The InsR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133192 [Multi-domain]  Cd Length: 288  Bit Score: 156.67  E-value: 2.54e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKV------ELCRYDPEgdntgEQVAVKSLkpesggNHIADLKKEIE------ILRNLYHENIVKYKGICT 945
Cdd:cd05061     11 LRELGQGSFGMVyegnarDIIKGEAE-----TRVAVKTV------NESASLRERIEflneasVMKGFTCHHVVRLLGVVS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  946 EdgGNGIKLIMEFLPSGSLKEYL----PKNKNKI-----NLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQ 1016
Cdd:cd05061     80 K--GQPTLVVMELMAHGDLKSYLrslrPEAENNPgrpppTLQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFT 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1017 VKIGDFGLTKAI-ETDkeYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSdsspmalflkmigPT 1095
Cdd:cd05061    158 VKIGDFGMTRDIyETD--YYRKGGKGLLPVRWMAPESLKDGVFTTSSDMWSFGVVLWEITSLAEQ-------------PY 222
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1013071061 1096 HGqMTVTRLVNTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIE 1147
Cdd:cd05061    223 QG-LSNEQVLKFVMDGGYLDQPDNCPERVTDLMRMCWQFNPKMRPTFLEIVN 273
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
881-1149 8.73e-42

Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src (or c-Src) is a cytoplasmic (or non-receptor) PTK, containing an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region with a conserved tyr. It is activated by autophosphorylation at the tyr kinase domain, and is negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). c-Src is the vertebrate homolog of the oncogenic protein (v-Src) from Rous sarcoma virus. Together with other Src subfamily proteins, it is involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. Src also play a role in regulating cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Elevated levels of Src kinase activity have been reported in a variety of human cancers. Several inhibitors of Src have been developed as anti-cancer drugs. Src is also implicated in acute inflammatory responses and osteoclast function. The Src subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 154.84  E-value: 8.73e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYdpegdNTGEQVAVKSLKPesGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGgngIKLIMEFLP 960
Cdd:cd05071     17 LGQGCFGEVWMGTW-----NGTTRVAIKTLKP--GTMSPEAFLQEAQVMKKLRHEKLVQLYAVVSEEP---IYIVTEYMS 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  961 SGSLKEYLPKNKNK-INLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKeyYTVKD 1039
Cdd:cd05071     87 KGSLLDFLKGEMGKyLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIEDNE--YTARQ 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1040 DRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTycdsdsspmalflKMIGPTHGqMTVTRLVNTLKEGKRLPCPPN 1119
Cdd:cd05071    165 GAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTT-------------KGRVPYPG-MVNREVLDQVERGYRMPCPPE 230
                          250       260       270
                   ....*....|....*....|....*....|
gi 1013071061 1120 CPDEVYQLMRKCWEFQPSNRTSFQNLiEGF 1149
Cdd:cd05071    231 CPESLHDLMCQCWRKEPEERPTFEYL-QAF 259
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
881-1143 9.49e-42

Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Yes (or c-Yes) is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. c-Yes kinase is the cellular homolog of the oncogenic protein (v-Yes) encoded by the Yamaguchi 73 and Esh sarcoma viruses. It displays functional overlap with other Src subfamily members, particularly Src. It also shows some unique functions such as binding to occludins, transmembrane proteins that regulate extracellular interactions in tight junctions. Yes also associates with a number of proteins in different cell types that Src does not interact with, like JAK2 and gp130 in pre-adipocytes, and Pyk2 in treated pulmonary vein endothelial cells. Although the biological function of Yes remains unclear, it appears to have a role in regulating cell-cell interactions and vesicle trafficking in polarized cells. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Yes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 154.84  E-value: 9.49e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYdpegdNTGEQVAVKSLKPesGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGgngIKLIMEFLP 960
Cdd:cd05069     20 LGQGCFGEVWMGTW-----NGTTKVAIKTLKP--GTMMPEAFLQEAQIMKKLRHDKLVPLYAVVSEEP---IYIVTEFMG 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  961 SGSLKEYLPKNKNK-INLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKeyYTVKD 1039
Cdd:cd05069     90 KGSLLDFLKEGDGKyLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNE--YTARQ 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1040 DRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTycdsdsspmalflKMIGPTHGqMTVTRLVNTLKEGKRLPCPPN 1119
Cdd:cd05069    168 GAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVT-------------KGRVPYPG-MVNREVLEQVERGYRMPCPQG 233
                          250       260
                   ....*....|....*....|....
gi 1013071061 1120 CPDEVYQLMRKCWEFQPSNRTSFQ 1143
Cdd:cd05069    234 CPESLHELMKLCWKKDPDERPTFE 257
FERM_F1 pfam18379
FERM F1 ubiquitin-like domain; This is an F1 lobe domain consisting of a ubiquitin like fold ...
36-129 4.36e-41

FERM F1 ubiquitin-like domain; This is an F1 lobe domain consisting of a ubiquitin like fold found in FERM region of Jak-family tyrosine kinases. Multidomain JAK molecules interact with receptors through their FERM and SH2-like domains, triggering a series of phosphorylation events, resulting in the activation of their kinase domains. Overall, the FERM region maintains the typical three-lobed architecture, with an F1 lobe consisting of a ubiquitin-like fold, an F2 lobe consisting of an acyl-CoA binding protein fold, and an F3 lobe consisting of a pleckstrin-homology (PH) fold.


Pssm-ID: 465733  Cd Length: 96  Bit Score: 146.16  E-value: 4.36e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061   36 VEVIFYLSDRE----PLRLGSGEYTAEELCIRAAQACRISPLCHNLFALYDENTKLWYAPNRTITVDDKMSLRLHYRMRF 111
Cdd:pfam18379    1 LQVHLYWSGPGdgetYLSYPPGEYTAEELCIDAAKACGITPVYHNLFALYDEDDRVWYPPNHVFHIDESTSLTLHFRIRF 80
                           90
                   ....*....|....*...
gi 1013071061  112 YFTNWHGTNDNEQsvWRH 129
Cdd:pfam18379   81 YFPNWHGLGESEP--YRY 96
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
881-1145 1.26e-40

Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; Tie1; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie1 is a receptor tyr kinase (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. No specific ligand has been identified for Tie1, although the angiopoietin, Ang-1, binds to Tie1 through integrins at high concentrations. In vivo studies of Tie1 show that it is critical in vascular development.


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 152.08  E-value: 1.26e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVelCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNL-YHENIVKYKGICTEDGGngIKLIMEFL 959
Cdd:cd05089     10 IGEGNFGQV--IKAMIKKDGLKMNAAIKMLKEFASENDHRDFAGELEVLCKLgHHPNIINLLGACENRGY--LYIAIEYA 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  960 PSGSLKEYLPKNK---------------NKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGL 1024
Cdd:cd05089     86 PYGNLLDFLRKSRvletdpafakehgtaSTLTSQQLLQFASDVAKGMQYLSEKQFIHRDLAARNVLVGENLVSKIADFGL 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1025 TKAietdKEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTycdsdsspmalflkMIGPTHGQMTVTRL 1104
Cdd:cd05089    166 SRG----EEVYVKKTMGRLPVRWMAIESLNYSVYTTKSDVWSFGVLLWEIVS--------------LGGTPYCGMTCAEL 227
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1013071061 1105 VNTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNL 1145
Cdd:cd05089    228 YEKLPQGYRMEKPRNCDDEVYELMRQCWRDRPYERPPFSQI 268
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
881-1153 1.31e-40

Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EphB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphB receptors play important roles in synapse formation and plasticity, spine morphogenesis, axon guidance, and angiogenesis. In the intestinal epithelium, EphBs are Wnt signaling target genes that control cell compartmentalization. They function as suppressors of colon cancer progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion. The EphB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 151.18  E-value: 1.31e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDPEGDNTgEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDggNGIKLIMEFLP 960
Cdd:cd05065     12 IGAGEFGEVCRGRLKLPGKRE-IFVAIKTLKSGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTKS--RPVMIITEFME 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  961 SGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKE--YYTVK 1038
Cdd:cd05065     89 NGALDSFLRQNDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRFLEDDTSdpTYTSS 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1039 DDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSdsspmalflkmigpTHGQMTVTRLVNTLKEGKRLPCPP 1118
Cdd:cd05065    169 LGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGER--------------PYWDMSNQDVINAIEQDYRLPPPM 234
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1013071061 1119 NCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALL 1153
Cdd:cd05065    235 DCPTALHQLMLDCWQKDRNLRPKFGQIVNTLDKMI 269
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
870-1154 3.25e-40

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR2 (or Flk1) binds the ligands VEGFA, VEGFC, VEGFD and VEGFE. VEGFR2 signaling is implicated in all aspects of normal and pathological vascular endothelial cell biology. It induces a variety of cellular effects including migration, survival, and proliferation. It is critical in regulating embryonic vascular development and angiogenesis. VEGFR2 is the major signal transducer in pathological angiogenesis including cancer and diabetic retinopathy, and is a target for inhibition in cancer therapy. The carboxyl terminus of VEGFR2 plays an important role in its autophosphorylation and activation. VEGFR2 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 152.44  E-value: 3.25e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  870 FEKRFLKRIRDLGEGHFGKV-ELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNL-YHENIVKYKGICTED 947
Cdd:cd05103      4 FPRDRLKLGKPLGRGAFGQViEADAFGIDKTATCRTVAVKMLKEGATHSEHRALMSELKILIHIgHHLNVVNLLGACTKP 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  948 GGNgIKLIMEFLPSGSLKEYLPKNKNKI----------------------NLKQQLK----------------------- 982
Cdd:cd05103     84 GGP-LMVIVEFCKFGNLSAYLRSKRSEFvpyktkgarfrqgkdyvgdisvDLKRRLDsitssqssassgfveekslsdve 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  983 ---------------------YAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYTvKDDR 1041
Cdd:cd05103    163 eeeagqedlykdfltledlicYSFQVAKGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKDPDYVR-KGDA 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1042 DSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSdsspmalflkmigPTHGQMTVTRLVNTLKEGKRLPCPPNCP 1121
Cdd:cd05103    242 RLPLKWMAPETIFDRVYTIQSDVWSFGVLLWEIFSLGAS-------------PYPGVKIDEEFCRRLKEGTRMRAPDYTT 308
                          330       340       350
                   ....*....|....*....|....*....|...
gi 1013071061 1122 DEVYQLMRKCWEFQPSNRTSFQNLIEGFEALLK 1154
Cdd:cd05103    309 PEMYQTMLDCWHGEPSQRPTFSELVEHLGNLLQ 341
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
589-845 4.21e-40

Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 149.22  E-value: 4.21e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061   589 LGRGTRTHIYSGTLmdykddEGTSEEKKIKVILKVLDPSHRDISLA-FFEAASMMRQVSHKHIVYLYGVCvRDVENIM-V 666
Cdd:smart00219    7 LGEGAFGEVYKGKL------KGKGGKKKVEVAVKTLKEDASEQQIEeFLREARIMRKLDHPNVVKLLGVC-TEEEPLYiV 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061   667 EEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGipitv 746
Cdd:smart00219   80 MEYMEGGDLLSYLRKNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLV-------VKISDFG----- 147
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061   747 LSRQ--------ECIERIP--WIAPECVEDSKnLSVAADKWSFGTTLWEICYNGEIP---LKDKTLIEKERFYESRCRPv 813
Cdd:smart00219  148 LSRDlydddyyrKRGGKLPirWMAPESLKEGK-FTSKSDVWSFGVLLWEIFTLGEQPypgMSNEEVLEYLKNGYRLPQP- 225
                           250       260       270
                    ....*....|....*....|....*....|...
gi 1013071061   814 tPSC-KELADLMTRCMNYDPNQRPFFRAIMRDI 845
Cdd:smart00219  226 -PNCpPELYDLMLQCWAEDPEDRPTFSELVEIL 257
FERM_C_TYK2 cd13335
FERM domain C-lobe of Non-receptor tyrosine-protein kinase TYK2; Tyk2 functions primarily in ...
281-426 9.39e-40

FERM domain C-lobe of Non-receptor tyrosine-protein kinase TYK2; Tyk2 functions primarily in IL-12 and type I-IFN signaling as well as transduction of IL-23, IL-10, and IL-6 signals. A mutation in the Tyk2 gene has been associated with hyperimmunoglobulin E syndrome (HIES), a primary immunodeficiency characterized by elevated serum immunoglobulin E. Tyk2 has been shown to interact with FYN, PTPN6, IFNAR1, Ku80 and GNB2L1. JAK (also called Just Another Kinase) is a family of intracellular, non-receptor tyrosine kinases that transduce cytokine-mediated signals via the JAK-STAT pathway. The JAK family in mammals consists of 4 members: JAK1, JAK2, JAK3 and TYK2. JAKs are composed of seven JAK homology (JH) domains (JH1-JH7) . The C-terminal JH1 domain is the main catalytic domain, followed by JH2, which is often referred to as a pseudokinase domain, followed by JH3-JH4 which is homologous to the SH2 domain, and lastly JH5-JH7 which is a FERM domain. Named after Janus, the two-faced Roman god of doorways, JAKs possess two near-identical phosphate-transferring domains; one which displays the kinase activity (JH1), while the other negatively regulates the kinase activity of the first (JH2). The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 275414  Cd Length: 158  Bit Score: 144.57  E-value: 9.39e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  281 YGAEIFETSMLLISSENEMNWFHSN----------DGGNVLYYEVMVTGNLGIQWRHKP-NVVSVEKEKNKLKRKKLENK 349
Cdd:cd13335      1 FGTETFPVLHLDLRADGEKSGSYLNgghtegnppeETINPPTHEVMVSGTDGIQWRKVSaERSQSDSYSRHYFMKVMRQK 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1013071061  350 HKKDEEKNKIREE-WNNFSYFPEITHIVIKESVVSINKQDNKKMELKLSSHEEALSFVSLVDGYFRLTADAHHYLCTD 426
Cdd:cd13335     81 SQKSEQPALNEEPkWVIFCDFQEITHIVIQGINVCISRQDNKCMEISLPSSIQALSFVSLLDGYFRLTADSNHYLCHE 158
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
589-845 1.35e-39

Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase.


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 147.70  E-value: 1.35e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061   589 LGRGTRTHIYSGTLmdykddEGTSEEKKIKVILKVLDPSHRDISLA-FFEAASMMRQVSHKHIVYLYGVCvRDVENIM-V 666
Cdd:smart00221    7 LGEGAFGEVYKGTL------KGKGDGKEVEVAVKTLKEDASEQQIEeFLREARIMRKLDHPNIVKLLGVC-TEEEPLMiV 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061   667 EEFVEGGPLDLFMH-RKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGipit 745
Cdd:smart00221   80 MEYMPGGDLLDYLRkNRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLV-------VKISDFG---- 148
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061   746 vLSRQE--------CIERIP--WIAPECVEDSKnLSVAADKWSFGTTLWEICYNGEIP---LKDKTLIEKERFYESRCRP 812
Cdd:smart00221  149 -LSRDLydddyykvKGGKLPirWMAPESLKEGK-FTSKSDVWSFGVLLWEIFTLGEEPypgMSNAEVLEYLKKGYRLPKP 226
                           250       260       270
                    ....*....|....*....|....*....|....
gi 1013071061   813 vtPSC-KELADLMTRCMNYDPNQRPFFRAIMRDI 845
Cdd:smart00221  227 --PNCpPELYKLMLQCWAEDPEDRPTFSELVEIL 258
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
879-1154 2.75e-39

Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Axl is widely expressed in a variety of organs and cells including epithelial, mesenchymal, hematopoietic, as well as non-transformed cells. It is important in many cellular functions such as survival, anti-apoptosis, proliferation, migration, and adhesion. Axl was originally isolated from patients with chronic myelogenous leukemia and a chronic myeloproliferative disorder. It is overexpressed in many human cancers including colon, squamous cell, thyroid, breast, and lung carcinomas. Axl is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to its ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Axl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270660 [Multi-domain]  Cd Length: 277  Bit Score: 147.46  E-value: 2.75e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGHFGKVElcrydpEG----DNTGEQVAVKSLKPE-SGGNHIADLKKEIEILRNLYHENIVKYKGICTE----DGG 949
Cdd:cd05075      6 KTLGEGEFGSVM------EGqlnqDDSVLKVAVKTMKIAiCTRSEMEDFLSEAVCMKEFDHPNVMRLIGVCLQntesEGY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  950 NGIKLIMEFLPSGSLKEYLPKNK---NKINLKQQL--KYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGL 1024
Cdd:cd05075     80 PSPVVILPFMKHGDLHSFLLYSRlgdCPVYLPTQMlvKFMTDIASGMEYLSSKNFIHRDLAARNCMLNENMNVCVADFGL 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1025 TKAIeTDKEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSdsspmalflkmigPTHGqMTVTRL 1104
Cdd:cd05075    160 SKKI-YNGDYYRQGRISKMPVKWIAIESLADRVYTTKSDVWSFGVTMWEIATRGQT-------------PYPG-VENSEI 224
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1105 VNTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALLK 1154
Cdd:cd05075    225 YDYLRQGNRLKQPPDCLDGLYELMSSCWLLNPKDRPSFETLRCELEKILK 274
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
881-1154 3.59e-39

Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie2 is a receptor PTK (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie2 is expressed mainly in endothelial cells and hematopoietic stem cells. It is also found in a subset of tumor-associated monocytes and eosinophils. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. Tie2 signaling plays key regulatory roles in vascular integrity and quiescence, and in inflammation. The Tie2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133219 [Multi-domain]  Cd Length: 303  Bit Score: 148.22  E-value: 3.59e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDPEGDNTgeQVAVKSLKPESGGNHIADLKKEIEILRNL-YHENIVKYKGICTEDGGngIKLIMEFL 959
Cdd:cd05088     15 IGEGNFGQVLKARIKKDGLRM--DAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGY--LYLAIEYA 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  960 PSGSLKEYLPKNK---------------NKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGL 1024
Cdd:cd05088     91 PHGNLLDFLRKSRvletdpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGL 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1025 TKAietdKEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTycdsdsspmalflkMIGPTHGQMTVTRL 1104
Cdd:cd05088    171 SRG----QEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVS--------------LGGTPYCGMTCAEL 232
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1105 VNTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALLK 1154
Cdd:cd05088    233 YEKLPQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLE 282
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
873-1145 3.78e-39

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror2 plays important roles in skeletal and heart formation. Ror2-deficient mice show widespread bone abnormalities, ventricular defects in the heart, and respiratory dysfunction. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Ror2 is also implicated in neural development. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 147.47  E-value: 3.78e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  873 RFLKrirDLGEGHFGKVelcrYDPE--GDNTGEQ---VAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTED 947
Cdd:cd05091      9 RFME---ELGEDRFGKV----YKGHlfGTAPGEQtqaVAIKTLKDKAEGPLREEFRHEAMLRSRLQHPNIVCLLGVVTKE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  948 ggNGIKLIMEFLPSGSLKEYL----PKN-----------KNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVE 1012
Cdd:cd05091     82 --QPMSMIFSYCSHGDLHEFLvmrsPHSdvgstdddktvKSTLEPADFLHIVTQIAAGMEYLSSHHVVHKDLATRNVLVF 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1013 SEHQVKIGDFGLTKAIETdKEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCdsdsspmalflkmI 1092
Cdd:cd05091    160 DKLNVKISDLGLFREVYA-ADYYKLMGNSLLPIRWMSPEAIMYGKFSIDSDIWSYGVVLWEVFSYG-------------L 225
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1013071061 1093 GPTHGqMTVTRLVNTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNL 1145
Cdd:cd05091    226 QPYCG-YSNQDVIEMIRNRQVLPCPDDCPAWVYTLMLECWNEFPSRRPRFKDI 277
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
870-1147 5.33e-39

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR1 (or Flt1) binds VEGFA, VEGFB, and placenta growth factor (PLGF). It regulates monocyte and macrophage migration, vascular permeability, haematopoiesis, and the recruitment of haematopietic progenitor cells from the bone marrow. VEGFR1 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 148.61  E-value: 5.33e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  870 FEKRFLKRIRDLGEGHFGKV-ELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNL-YHENIVKYKGICTED 947
Cdd:cd14207      4 FARERLKLGKSLGRGAFGKVvQASAFGIKKSPTCRVVAVKMLKEGATASEYKALMTELKILIHIgHHLNVVNLLGACTKS 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  948 GGNgIKLIMEFLPSGSLKEYLPKNKN------------------------------------------------------ 973
Cdd:cd14207     84 GGP-LMVIVEYCKYGNLSNYLKSKRDffvtnkdtslqeelikekkeaeptggkkkrlesvtssesfassgfqedkslsdv 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  974 -------------KINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYTvKDD 1040
Cdd:cd14207    163 eeeeedsgdfykrPLTMEDLISYSFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLARDIYKNPDYVR-KGD 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1041 RDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSdsspmalflkmigPTHGQMTVTRLVNTLKEGKRLPCPPNC 1120
Cdd:cd14207    242 ARLPLKWMAPESIFDKIYSTKSDVWSYGVLLWEIFSLGAS-------------PYPGVQIDEDFCSKLKEGIRMRAPEFA 308
                          330       340
                   ....*....|....*....|....*..
gi 1013071061 1121 PDEVYQLMRKCWEFQPSNRTSFQNLIE 1147
Cdd:cd14207    309 TSEIYQIMLDCWQGDPNERPRFSELVE 335
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
881-1147 7.43e-39

Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase kinase kinase (MAPKKK) epsilon, and related proteins. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Cdc7 is essential for cell division by playing a key role in the initiation of septum formation and cytokinesis. Budding yeast Cdc15 functions to coordinate mitotic exit with cytokinesis. Arabidopsis MAPKKK epsilon is required for pollen development in the plasma membrane. The Cdc7-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270797 [Multi-domain]  Cd Length: 254  Bit Score: 145.45  E-value: 7.43e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVelcrYDPEGDNTGEQVAVKSLKPES-GGNHIADLKKEIEILRNLYHENIVKYKGiCTEDGGNgIKLIMEFL 959
Cdd:cd06627      8 IGRGAFGSV----YKGLNLNTGEFVAIKQISLEKiPKSDLKSVMGEIDLLKKLNHPNIVKYIG-SVKTKDS-LYIILEYV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  960 PSGSLKEYLpKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGL-TKAIETDKEYYTVK 1038
Cdd:cd06627     82 ENGSLASII-KKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVaTKLNEVEKDENSVV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1039 ddrDSPvFWYAPECLMQSKFYIASDVWSFGVTLHELLT----YCDSDssPM-ALFlkmigpthgqmtvtRLVNTlkegKR 1113
Cdd:cd06627    161 ---GTP-YWMAPEVIEMSGVTTASDIWSVGCTVIELLTgnppYYDLQ--PMaALF--------------RIVQD----DH 216
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1013071061 1114 LPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIE 1147
Cdd:cd06627    217 PPLPENISPELRDFLLQCFQKDPTLRPSAKELLK 250
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
875-1147 8.05e-39

Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular carcinoma and Resting lymphocyte kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tec and Rlk (also named Txk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. Instead of PH, Rlk contains an N-terminal cysteine-rich region. In addition to PH, Tec also contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells. Tec is more widely-expressed than other Tec-like subfamily kinases. It is found in endothelial cells, both B- and T-cells, and a variety of myeloid cells including mast cells, erythroid cells, platelets, macrophages and neutrophils. Rlk is expressed in T-cells and mast cell lines. Tec and Rlk are both key components of T-cell receptor (TCR) signaling. They are important in TCR-stimulated proliferation, IL-2 production and phopholipase C-gamma1 activation. The Tec/Rlk subfamily is part of a larger superfamily, that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 145.77  E-value: 8.05e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  875 LKRIRDLGEGHFGKVELCRYdpegdNTGEQVAVKSLKpeSGGNHIADLKKEIEILRNLYHENIVKYKGICTEDggNGIKL 954
Cdd:cd05114      6 LTFMKELGSGLFGVVRLGKW-----RAQYKVAIKAIR--EGAMSEEDFIEEAKVMMKLTHPKLVQLYGVCTQQ--KPIYI 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKey 1034
Cdd:cd05114     77 VTEFMENGCLLNYLRQRRGKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTRYVLDDQ-- 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1035 YTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCdsdsspmalflKMIGPTHGQMTVTRLVNtlkEGKRL 1114
Cdd:cd05114    155 YTSSSGAKFPVKWSPPEVFNYSKFSSKSDVWSFGVLMWEVFTEG-----------KMPFESKSNYEVVEMVS---RGHRL 220
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1013071061 1115 PCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIE 1147
Cdd:cd05114    221 YRPKLASKSVYEVMYSCWHEKPEGRPTFADLLR 253
FERM_C_JAK cd13196
FERM domain C-lobe of Janus kinase (JAK); JAK (also called Just Another Kinase) is a family of ...
282-426 1.45e-38

FERM domain C-lobe of Janus kinase (JAK); JAK (also called Just Another Kinase) is a family of intracellular, non-receptor tyrosine kinases that transduce cytokine-mediated signals via the JAK-STAT pathway. The JAK family in mammals consists of 4 members: JAK1, JAK2, JAK3 and TYK2. JAKs are composed of seven JAK homology (JH) domains (JH1-JH7) . The C-terminal JH1 domain is the main catalytic domain, followed by JH2, which is often referred to as a pseudokinase domain, followed by JH3-JH4 which is homologous to the SH2 domain, and lastly JH5-JH7 which is a FERM domain. Named after Janus, the two-faced Roman god of doorways, JAKs possess two near-identical phosphate-transferring domains; one which displays the kinase activity (JH1), while the other negatively regulates the kinase activity of the first (JH2). The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 275394  Cd Length: 109  Bit Score: 139.48  E-value: 1.45e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  282 GAEIFETSMLLISSenemnwfhsnDGGNVLYYEVMVTGNLGIQWRHKPNVvsvekeknklkrkklenkhkkdeeknkiRE 361
Cdd:cd13196      1 LSEKYKATMLEGGS----------KEASEIPVEVLVSGDEGIKWLRTPNT----------------------------ES 42
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1013071061  362 EWNNFSYFPEITHIVIKES--VVSINKQDNKKMELKLSSHEEALSFVSLVDGYFRLTADAHHYLCTD 426
Cdd:cd13196     43 DWQTLCDIPELCHISIKQEsgTVEISRKDGKPLELEFSSHAEALSFVSLVDGYYRLTCDWTHYLCKD 109
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
875-1149 2.00e-38

Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fyn and Yrk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Fyn, together with Lck, plays a critical role in T-cell signal transduction by phosphorylating ITAM (immunoreceptor tyr activation motif) sequences on T-cell receptors, ultimately leading to the proliferation and differentiation of T-cells. In addition, Fyn is involved in the myelination of neurons, and is implicated in Alzheimer's and Parkinson's diseases. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Fyn/Yrk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase.


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 145.21  E-value: 2.00e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  875 LKRIRDLGEGHFGKVELCRYdpegdNTGEQVAVKSLKPesGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGgngIKL 954
Cdd:cd05070     11 LQLIKRLGNGQFGEVWMGTW-----NGNTKVAIKTLKP--GTMSPESFLEEAQIMKKLKHDKLVQLYAVVSEEP---IYI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPSGSLKEYLPKNKNK-INLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKe 1033
Cdd:cd05070     81 VTEYMSKGSLLDFLKDGEGRaLKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIEDNE- 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1034 yYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTycdsdsspmalflKMIGPTHGqMTVTRLVNTLKEGKR 1113
Cdd:cd05070    160 -YTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVT-------------KGRVPYPG-MNNREVLEQVERGYR 224
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1013071061 1114 LPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLiEGF 1149
Cdd:cd05070    225 MPCPQDCPISLHELMIHCWKKDPEERPTFEYL-QGF 259
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
876-1139 5.67e-38

Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPKK kinases (MAPKKKs), or MAPKKK kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli. The STE family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 143.11  E-value: 5.67e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  876 KRIRDLGEGHFGKVelcrYDPEGDNTGEQVAVKSLKPESGgNHIADLKKEIEILRNLYHENIVKYkgICTEDGGNGIKLI 955
Cdd:cd05122      3 EILEKIGKGGFGVV----YKARHKKTGQIVAIKKINLESK-EKKESILNEIAILKKCKHPNIVKY--YGSYLKKDELWIV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  956 MEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKeyy 1035
Cdd:cd05122     76 MEFCSGGSLKDLLKNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQLSDGK--- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1036 tvkdDRDSPV---FWYAPECLMQSKFYIASDVWSFGVTLHELLT----YcdSDSSPMALfLKMIgPTHGQMTvtrlvntl 1108
Cdd:cd05122    153 ----TRNTFVgtpYWMAPEVIQGKPYGFKADIWSLGITAIEMAEgkppY--SELPPMKA-LFLI-ATNGPPG-------- 216
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1013071061 1109 kegkrLPCPPNCPDEVYQLMRKCWEFQPSNR 1139
Cdd:cd05122    217 -----LRNPKKWSKEFKDFLKKCLQKDPEKR 242
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
879-1146 9.18e-38

Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. IGF-1R is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the ligand (IGF-1 or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, which stimulates downstream kinase activities and biological function. IGF-1R signaling is important in the differentiation, growth, and survival of normal cells. In cancer cells, where it is frequently overexpressed, IGF-1R is implicated in proliferation, the suppression of apoptosis, invasion, and metastasis. IGF-1R is being developed as a therapeutic target in cancer treatment. The IGF-1R subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133193 [Multi-domain]  Cd Length: 277  Bit Score: 143.25  E-value: 9.18e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGHFGKV-ELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEdgGNGIKLIME 957
Cdd:cd05062     12 RELGQGSFGMVyEGIAKGVVKDEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQ--GQPTLVIME 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  958 FLPSGSLKEYL----PKNKNKI-----NLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAI 1028
Cdd:cd05062     90 LMTRGDLKSYLrslrPEMENNPvqappSLKKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFTVKIGDFGMTRDI 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1029 -ETDkeYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSdsspmalflkmigPTHGqMTVTRLVNT 1107
Cdd:cd05062    170 yETD--YYRKGGKGLLPVRWMSPESLKDGVFTTYSDVWSFGVVLWEIATLAEQ-------------PYQG-MSNEQVLRF 233
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1013071061 1108 LKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLI 1146
Cdd:cd05062    234 VMEGGLLDKPDNCPDMLFELMRMCWQYNPKMRPSFLEII 272
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
876-1147 1.04e-37

Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MEKK3, MEKK2, and related proteins; all contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKK) that activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270795 [Multi-domain]  Cd Length: 260  Bit Score: 142.49  E-value: 1.04e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  876 KRIRDLGEGHFGKVELCrYDPegdNTGEQVAVKSLKPE----SGGNHIADLKKEIEILRNLYHENIVKYKGiCTEDGGNg 951
Cdd:cd06625      3 KQGKLLGQGAFGQVYLC-YDA---DTGRELAVKQVEIDpintEASKEVKALECEIQLLKNLQHERIVQYYG-CLQDEKS- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  952 IKLIMEFLPSGSLKEYLpKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETD 1031
Cdd:cd06625     77 LSIFMEYMPGGSVKDEI-KAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGASKRLQTI 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1032 KEYYTVKDDRDSPvFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCD--SDSSPMALFLKMI-GPTHGQMtvtrlvntl 1108
Cdd:cd06625    156 CSSTGMKSVTGTP-YWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPpwAEFEPMAAIFKIAtQPTNPQL--------- 225
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1013071061 1109 kegkrlpcPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIE 1147
Cdd:cd06625    226 --------PPHVSEDARDFLSLIFVRNKKQRPSAEELLS 256
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
879-1145 1.84e-37

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphA10, which contains an inactive tyr kinase domain, may function to attenuate signals of co-clustered active receptors. EphA10 is mainly expressed in the testis. Ephrin/EphR interaction results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. EphRs comprise the largest subfamily of receptor tyr kinases (RTKs). In general, class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The EphA10 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133195 [Multi-domain]  Cd Length: 266  Bit Score: 141.98  E-value: 1.84e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGHFGkvELCRYDPEGDNTGE-QVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEdgGNGIKLIME 957
Cdd:cd05064     11 RILGTGRFG--ELCRGCLKLPSKRElPVAIHTLRAGCSDKQRRGFLAEALTLGQFDHSNIVRLEGVITR--GNTMMIVTE 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  958 FLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYTV 1037
Cdd:cd05064     87 YMSNGALDSFLRKHEGQLVAGQLMGMLPGLASGMKYLSEMGYVHKGLAAHKVLVNSDLVCKISGFRRLQEDKSEAIYTTM 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1038 KDdrDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSdsspmalflkmigpTHGQMTVTRLVNTLKEGKRLPCP 1117
Cdd:cd05064    167 SG--KSPVLWAAPEAIQYHHFSSASDVWSFGIVMWEVMSYGER--------------PYWDMSGQDVIKAVEDGFRLPAP 230
                          250       260
                   ....*....|....*....|....*...
gi 1013071061 1118 PNCPDEVYQLMRKCWEFQPSNRTSFQNL 1145
Cdd:cd05064    231 RNCPNLLHQLMLDCWQKERGERPRFSQI 258
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
863-1153 2.39e-37

Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. CSF-1R, also called c-Fms, is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of CSF-1R to its ligand, CSF-1, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. It leads to increases in gene transcription and protein translation, and induces cytoskeletal remodeling. CSF-1R signaling leads to a variety of cellular responses including survival, proliferation, and differentiation of target cells. It plays an important role in innate immunity, tissue development and function, and the pathogenesis of some diseases including atherosclerosis and cancer. CSF-1R signaling is also implicated in mammary gland development during pregnancy and lactation. Aberrant CSF-1/CSF-1R expression correlates with tumor cell invasiveness, poor clinical prognosis, and bone metastasis in breast cancer. Although the structure of the human CSF-1R catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. The CSF-1R subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133237 [Multi-domain]  Cd Length: 374  Bit Score: 144.99  E-value: 2.39e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  863 TEVDPTH--------FEKRFLKRIRDLGEGHFGKV-ELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNL- 932
Cdd:cd05106     20 TFIDPTQlpynekweFPRDNLQFGKTLGAGAFGKVvEATAFGLGKEDNVLRVAVKMLKASAHTDEREALMSELKILSHLg 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  933 YHENIVKYKGICTEDGGngIKLIMEFLPSGSLKEYLPKN---------------------KN------------------ 973
Cdd:cd05106    100 QHKNIVNLLGACTHGGP--VLVITEYCCYGDLLNFLRKKaetflnfvmalpeisetssdyKNitlekkyirsdsgfssqg 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  974 ------------------------------KINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFG 1023
Cdd:cd05106    178 sdtyvemrpvsssssqssdskdeedtedswPLDLDDLLRFSSQVAQGMDFLASKNCIHRDVAARNVLLTDGRVAKICDFG 257
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1024 LTKAIETDKEyYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSdsspmalflkmigPTHGQMTVTR 1103
Cdd:cd05106    258 LARDIMNDSN-YVVKGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGKS-------------PYPGILVNSK 323
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1104 LVNTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALL 1153
Cdd:cd05106    324 FYKMVKRGYQMSRPDFAPPEIYSIMKMCWNLEPTERPTFSQISQLIQRQL 373
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
881-1152 2.50e-37

Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Mammals have four MLKs (MLK1-4), mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 141.38  E-value: 2.50e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDpegdntGEQVAVKSLKPESGGNH---IADLKKEIEILRNLYHENIVKYKGICTEDggNGIKLIME 957
Cdd:cd14061      2 IGVGGFGKVYRGIWR------GEEVAVKAARQDPDEDIsvtLENVRQEARLFWMLRHPNIIALRGVCLQP--PNLCLVME 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  958 FLPSGSLKEYLpkNKNKINLKQQLKYAVQICKGMDYLGSRQYV---HRDLAARNVL----VESE----HQVKIGDFGLTK 1026
Cdd:cd14061     74 YARGGALNRVL--AGRKIPPHVLVDWAIQIARGMNYLHNEAPVpiiHRDLKSSNILileaIENEdlenKTLKITDFGLAR 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1027 AIetdkeYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLT----YCDSDSSPMALFLKMigpthgqmtvt 1102
Cdd:cd14061    152 EW-----HKTTRMSAAGTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTgevpYKGIDGLAVAYGVAV----------- 215
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1103 rlvNTLKegkrLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEAL 1152
Cdd:cd14061    216 ---NKLT----LPIPSTCPEPFAQLMKDCWQPDPHDRPSFADILKQLENI 258
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
878-1076 2.89e-37

Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AMPK-like subfamily is composed of AMPK, MARK, BRSK, NUAK, MELK, SNRK, TSSK, and SIK, among others. LKB1 serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. BRSKs play important roles in establishing neuronal polarity. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. The AMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270905 [Multi-domain]  Cd Length: 252  Bit Score: 140.73  E-value: 2.89e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVELCRYDPegdnTGEQVAVKSL-KPESGGNHIADLKKEIEILRNLYHENIVK-YKGICTEdggNGIKLI 955
Cdd:cd14003      5 GKTLGEGSFGKVKLARHKL----TGEKVAIKIIdKSKLKEEIEEKIKREIEIMKLLNHPNIIKlYEVIETE---NKIYLV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  956 MEFLPSGSLKEYLpKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYY 1035
Cdd:cd14003     78 MEYASGGELFDYI-VNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNEFRGGSLLK 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1013071061 1036 TVKddrDSPVFwYAPECLMQSKFY-IASDVWSFGVTLHELLT 1076
Cdd:cd14003    157 TFC---GTPAY-AAPEVLLGRKYDgPKADVWSLGVILYAMLT 194
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
589-841 8.10e-37

Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. They can be classified into receptor and non-receptor tyr kinases. PTKs play important roles in many cellular processes including, lymphocyte activation, epithelium growth and maintenance, metabolism control, organogenesis regulation, survival, proliferation, differentiation, migration, adhesion, motility, and morphogenesis. Receptor tyr kinases (RTKs) are integral membrane proteins which contain an extracellular ligand-binding region, a transmembrane segment, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain, leading to intracellular signaling. Some RTKs are orphan receptors with no known ligands. Non-receptor (or cytoplasmic) tyr kinases are distributed in different intracellular compartments and are usually multi-domain proteins containing a catalytic tyr kinase domain as well as various regulatory domains such as SH3 and SH2. PTKs are usually autoinhibited and require a mechanism for activation. In many PTKs, the phosphorylation of tyr residues in the activation loop is essential for optimal activity. Aberrant expression of PTKs is associated with many development abnormalities and cancers.The PTK family is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270623 [Multi-domain]  Cd Length: 262  Bit Score: 139.98  E-value: 8.10e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  589 LGRGTRTHIYSGTLMdykddegTSEEKKIKVILKVLDPSHRDISL-AFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVE 667
Cdd:cd00192      3 LGEGAFGEVYKGKLK-------GGDGKTVDVAVKTLKEDASESERkDFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVM 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  668 EFVEGGPLDLFMHRK--------SDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSD 739
Cdd:cd00192     76 EYMEGGDLLDFLRKSrpvfpspePSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLV-------VKISD 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  740 PG----IPITVLSRQECIERIP--WIAPECVEDSKnLSVAADKWSFGTTLWEICYNGEIP---LKDKTLIEkerFYESRC 810
Cdd:cd00192    149 FGlsrdIYDDDYYRKKTGGKLPirWMAPESLKDGI-FTSKSDVWSFGVLLWEIFTLGATPypgLSNEEVLE---YLRKGY 224
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1013071061  811 RPVTPS-C-KELADLMTRCMNYDPNQRPFFRAI 841
Cdd:cd00192    225 RLPKPEnCpDELYELMLSCWQLDPEDRPTFSEL 257
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
878-1139 1.05e-35

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 136.56  E-value: 1.05e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVELCRyDPegdNTGEQVAVKSLKPESGGNH--IADLKKEIEILRNLYHENIVKYKGICTEDGGngIKLI 955
Cdd:cd14014      5 VRLLGRGGMGEVYRAR-DT---LLGRPVAIKVLRPELAEDEefRERFLREARALARLSHPNIVRVYDVGEDDGR--PYIV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  956 MEFLPSGSLKEYLPKNKnKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYY 1035
Cdd:cd14014     79 MEYVEGGSLADLLRERG-PLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGLTQ 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1036 T--VKDdrdSPVFWyAPECLMQSKFYIASDVWSFGVTLHELLT--YCDSDSSPMALFLKmigptHGQMTVTRLVNTlkeg 1111
Cdd:cd14014    158 TgsVLG---TPAYM-APEQARGGPVDPRSDIYSLGVVLYELLTgrPPFDGDSPAAVLAK-----HLQEAPPPPSPL---- 224
                          250       260
                   ....*....|....*....|....*...
gi 1013071061 1112 krlpcPPNCPDEVYQLMRKCWEFQPSNR 1139
Cdd:cd14014    225 -----NPDVPPALDAIILRALAKDPEER 247
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
870-1154 5.96e-35

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR3 (or Flt4) preferentially binds the ligands VEGFC and VEGFD. VEGFR3 is essential for lymphatic endothelial cell (EC) development and function. It has been shown to regulate adaptive immunity during corneal transplantation. VEGFR3 is upregulated on blood vascular ECs in pathological conditions such as vascular tumors and the periphery of solid tumors. It plays a role in cancer progression and lymph node metastasis. Missense mutations in the VEGFR3 gene are associated with primary human lymphedema. VEGFR3 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 136.65  E-value: 5.96e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  870 FEKRFLKRIRDLGEGHFGKV-ELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNL-YHENIVKYKGICTED 947
Cdd:cd05102      4 FPRDRLRLGKVLGHGAFGKVvEASAFGIDKSSSCETVAVKMLKEGATASEHKALMSELKILIHIgNHLNVVNLLGACTKP 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  948 GGNgIKLIMEFLPSGSLKEYL----------------------------------PKNKNKINLKQQLK----------- 982
Cdd:cd05102     84 NGP-LMVIVEFCKYGNLSNFLrakregfspyrersprtrsqvrsmveavradrrsRQGSDRVASFTESTsstnqprqevd 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  983 --------------YAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYTvKDDRDSPVFWY 1048
Cdd:cd05102    163 dlwqspltmedlicYSFQVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKDPDYVR-KGSARLPLKWM 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1049 APECLMQSKFYIASDVWSFGVTLHELLTYCDSdsspmalflkmigPTHGQMTVTRLVNTLKEGKRLPCPPNCPDEVYQLM 1128
Cdd:cd05102    242 APESIFDKVYTTQSDVWSFGVLLWEIFSLGAS-------------PYPGVQINEEFCQRLKDGTRMRAPEYATPEIYRIM 308
                          330       340
                   ....*....|....*....|....*.
gi 1013071061 1129 RKCWEFQPSNRTSFQNLIEGFEALLK 1154
Cdd:cd05102    309 LSCWHGDPKERPTFSDLVEILGDLLQ 334
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
879-1153 6.45e-35

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR alpha is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR alpha forms homodimers or heterodimers with PDGFR beta, depending on the nature of the PDGF ligand. PDGF-AA, PDGF-AB, and PDGF-CC induce PDGFR alpha homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR alpha signaling is important in the formation of lung alveoli, intestinal villi, mesenchymal dermis, and hair follicles, as well as in the development of oligodendrocytes, retinal astrocytes, neural crest cells, and testicular cells. Aberrant PDGFR alpha expression is associated with some human cancers. Mutations in PDGFR alpha have been found within a subset of gastrointestinal stromal tumors (GISTs). An active fusion protein FIP1L1-PDGFR alpha, derived from interstitial deletion, is associated with idiopathic hypereosinophilic syndrome and chronic eosinophilic leukemia. The PDGFR alpha subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173653 [Multi-domain]  Cd Length: 400  Bit Score: 138.62  E-value: 6.45e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGHFGKV-ELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNL-YHENIVKYKGICTEDGGngIKLIM 956
Cdd:cd05105     43 RILGSGAFGKVvEGTAYGLSRSQPVMKVAVKMLKPTARSSEKQALMSELKIMTHLgPHLNIVNLLGACTKSGP--IYIIT 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  957 EFLPSGSLKEYLPKNKNK---------------------------------------INLKQQ----------------- 980
Cdd:cd05105    121 EYCFYGDLVNYLHKNRDNflsrhpekpkkdldifginpadestrsyvilsfenkgdyMDMKQAdttqyvpmleikeasky 200
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  981 ---------------------------------------LKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGD 1021
Cdd:cd05105    201 sdiqrsnydrpasykgsndsevknllsddgseglttldlLSFTYQVARGMEFLASKNCVHRDLAARNVLLAQGKIVKICD 280
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1022 FGLTKAIETDKEYYTvKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSdsspmalflkmigPTHGQMTV 1101
Cdd:cd05105    281 FGLARDIMHDSNYVS-KGSTFLPVKWMAPESIFDNLYTTLSDVWSYGILLWEIFSLGGT-------------PYPGMIVD 346
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1013071061 1102 TRLVNTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALL 1153
Cdd:cd05105    347 STFYNKIKSGYRMAKPDHATQEVYDIMVKCWNSEPEKRPSFLHLSDIVESLL 398
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
876-1076 2.51e-34

Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. CDKs are partly regulated by their subcellular localization, which defines substrate phosphorylation and the resulting specific function. CDK1, CDK2, CDK4, and CDK6 have well-defined functions in the cell cycle, such as the regulation of the early G1 phase by CDK4 or CDK6, the G1/S phase transition by CDK2, or the entry of mitosis by CDK1. They also exhibit overlapping cyclin specificity and functions in certain conditions. Knockout mice with a single CDK deleted remain viable with specific phenotypes, showing that some CDKs can compensate for each other. For example, CDK4 can compensate for the loss of CDK6, however, double knockout mice with both CDK4 and CDK6 deleted die in utero. CDK8 and CDK9 are mainly involved in transcription while CDK5 is implicated in neuronal function. CDK7 plays essential roles in both the cell cycle as a CDK-Activating Kinase (CAK) and in transcription as a component of the general transcription factor TFIIH. The CDK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270823 [Multi-domain]  Cd Length: 282  Bit Score: 133.38  E-value: 2.51e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  876 KRIRDLGEGHFGKVELCRydpegD-NTGEQVAVKSLKPESG--GNHIADLKkEIEILRNLYHENIVKYKGICTEDggNGI 952
Cdd:cd07829      2 EKLEKLGEGTYGVVYKAK-----DkKTGEIVALKKIRLDNEeeGIPSTALR-EISLLKELKHPNIVKLLDVIHTE--NKL 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  953 KLIMEFLPSgSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDK 1032
Cdd:cd07829     74 YLVFEYCDQ-DLKKYLDKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGLARAFGIPL 152
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1013071061 1033 EYYTvkddrdSPV--FWY-APECLMQSKFY-IASDVWSFGVTLHELLT 1076
Cdd:cd07829    153 RTYT------HEVvtLWYrAPEILLGSKHYsTAVDIWSVGCIFAELIT 194
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
37-286 1.18e-33

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 128.57  E-value: 1.18e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061    37 EVIFYLSDREPLRLGSG-EYTAEELCIRAAQACRIspLCHNLFALYDENTKL----WYAPNRTITVDDKMS--LRLHYRM 109
Cdd:smart00295    1 VLKVYLLDGTTLEFEVDsSTTAEELLETVCRKLGI--RESEYFGLQFEDPDEdlrhWLDPAKTLLDQDVKSepLTLYFRV 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061   110 RFYFTNwhgtndneqsvwrhspkkqkngyekkkipDATPLLDASSLEYLFAQGQYDLVKCLAPIRdpkteqdghdiENEC 189
Cdd:smart00295   79 KFYPPD-----------------------------PNQLKEDPTRLNLLYLQVRNDILEGRLPCP-----------EEEA 118
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061   190 LGMAVLAISHYAMMKKMQLPELPKDISYKRYIPETLNKSirQRNLLTRMRINNVFKDFlkefnnkticdSSVSTHDLKVK 269
Cdd:smart00295  119 LLLAALALQAEFGDYDEELHDLRGELSLKRFLPKQLLDS--RKLKEWRERIVELHKEL-----------IGLSPEEAKLK 185
                           250
                    ....*....|....*..
gi 1013071061   270 YLATLETLTkHYGAEIF 286
Cdd:smart00295  186 YLELARKLP-TYGVELF 201
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
865-1150 1.32e-33

Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. Kit signaling is involved in major cellular functions including cell survival, proliferation, differentiation, adhesion, and chemotaxis. Mutations in Kit, which result in constitutive ligand-independent activation, are found in human cancers such as gastrointestinal stromal tumor (GIST) and testicular germ cell tumor (TGCT). The aberrant expression of Kit and/or SCF is associated with other tumor types such as systemic mastocytosis and cancers of the breast, neurons, lung, prostate, colon, and rectum. Although the structure of the human Kit catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. Kit is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of Kit to its ligand, the stem-cell factor (SCF), leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. The Kit subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270682 [Multi-domain]  Cd Length: 375  Bit Score: 133.88  E-value: 1.32e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  865 VDPTH--------FEKRFLKRIRDLGEGHFGKV-ELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNL-YH 934
Cdd:cd05104     19 IDPTQlpydhkweFPRDRLRFGKTLGAGAFGKVvEATAYGLAKADSAMTVAVKMLKPSAHSTEREALMSELKVLSYLgNH 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  935 ENIVKYKGICT-------------------------------------------------EDGGNGIKLIMEFLPSGSLk 965
Cdd:cd05104     99 INIVNLLGACTvggptlviteyccygdllnflrrkrdsficpkfedlaeaalyrnllhqrEMACDSLNEYMDMKPSVSY- 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  966 eYLPKNKNK-------------------------INLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIG 1020
Cdd:cd05104    178 -VVPTKADKrrgvrsgsyvdqdvtseileedelaLDTEDLLSFSYQVAKGMEFLASKNCIHRDLAARNILLTHGRITKIC 256
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1021 DFGLTKAIETDKEyYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSDSSPM---ALFLKMIgpthg 1097
Cdd:cd05104    257 DFGLARDIRNDSN-YVVKGNARLPVKWMAPESIFECVYTFESDVWSYGILLWEIFSLGSSPYPGMpvdSKFYKMI----- 330
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1013071061 1098 qmtvtrlvntlKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFE 1150
Cdd:cd05104    331 -----------KEGYRMDSPEFAPSEMYDIMRSCWDADPLKRPTFKQIVQLIE 372
SH2_Jak_family cd09921
Src homology 2 (SH2) domain in the Janus kinase (Jak) family; The Janus kinases (Jak) are a ...
426-527 1.56e-33

Src homology 2 (SH2) domain in the Janus kinase (Jak) family; The Janus kinases (Jak) are a family of 4 non-receptor tyrosine kinases (Jak1, Jak2, Jak3, Tyk2) which respond to cytokine or growth factor receptor activation. To transduce cytokine signaling, a series of conformational changes occur in the receptor-Jak complex upon extracellular ligand binding. This results in trans-activation of the receptor-associated Jaks followed by phosphorylation of receptor tail tyrosine sites. The Signal Transducers and Activators of Transcription (STAT) are then recruited to the receptor tail, become phosphorylated and translocate to the nucleus to regulate transcription. Jaks have four domains: the pseudokinase domain, the catalytic tyrosine kinase domain, the FERM (band four-point-one, ezrin, radixin, and moesin) domain, and the SH2 (Src Homology-2) domain. The Jak kinases are regulated by several enzymatic and non-enzymatic mechanisms. First, the Jak kinase domain is regulated by phosphorylation of the activation loop which is associated with the catalytically competent kinase conformation and is distinct from the inactive kinase conformation. Second, the pseudokinase domain directly modulates Jak catalytic activity with the FERM domain maintaining an active state. Third, the suppressor of cytokine signaling (SOCS) family and tyrosine phosphatases directly regulate Jak activity. Dysregulation of Jak activity can manifest as either a reduction or an increase in kinase activity resulting in immunodeficiency, inflammatory diseases, hematological defects, autoimmune and myeloproliferative disorders, and susceptibility to infection. Altered Jak regulation occurs by many mechanisms, including: gene translocations, somatic or inherited point mutations, receptor mutations, and alterations in the activity of Jak regulators such as SOCS or phosphatases. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198177  Cd Length: 97  Bit Score: 124.32  E-value: 1.56e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  426 DVAPPLIVHNIQNGCHGPICTEYAINKLRQEGSEEGMYVLRWSCTDFDNILMTVTCFEKSEQvqgaqkQFKNFQIEVQKG 505
Cdd:cd09921      1 DVATPSLVELIELRCHGPIGGEFSYRKLKERGNKPGSYILRESETEYDTYYIDVCVKDGSRF------QTKTFKIEKKEG 74
                           90       100
                   ....*....|....*....|...
gi 1013071061  506 -RYSLHGSDRSFPSLGDLMSHLK 527
Cdd:cd09921     75 gVFFLDGDSREYPSLRDLLNSLQ 97
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
882-1152 2.42e-33

Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated protein Triple Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLTK, also called zipper sterile-alpha-motif kinase (ZAK), contains a catalytic kinase domain and a leucine zipper. There are two alternatively-spliced variants, MLTK-alpha and MLTK-beta. MLTK-alpha contains a sterile-alpha-motif (SAM) at the C-terminus. MLTK regulates the c-Jun N-terminal kinase, extracellular signal-regulated kinase, p38 MAPK, and NF-kB pathways. ZAK is the MAP3K involved in the signaling cascade that leads to the ribotoxic stress response initiated by cellular damage due to Shiga toxins and ricin. It may also play a role in cell transformation and cancer development. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals.The MLTK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 129.31  E-value: 2.42e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  882 GEGHFGKVELCRYDPEGdntgEQVAVKSLKpesggnhiaDLKKEIEILRNLYHENIVKYKGICTEDGGNGIklIMEFLPS 961
Cdd:cd14060      2 GGGSFGSVYRAIWVSQD----KEVAVKKLL---------KIEKEAEILSVLSHRNIIQFYGAILEAPNYGI--VTEYASY 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  962 GSLKEYLPKNKN-KINLKQQLKYAVQICKGMDYLGSR---QYVHRDLAARNVLVESEHQVKIGDFGLTKAIEtdkeyYTV 1037
Cdd:cd14060     67 GSLFDYLNSNESeEMDMDQIMTWATDIAKGMHYLHMEapvKVIHRDLKSRNVVIAADGVLKICDFGASRFHS-----HTT 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1038 KDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTycdsDSSPmalFLKMIGpthgqMTVTRLVntLKEGKRLPCP 1117
Cdd:cd14060    142 HMSLVGTFPWMAPEVIQSLPVSETCDTYSYGVVLWEMLT----REVP---FKGLEG-----LQVAWLV--VEKNERPTIP 207
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1013071061 1118 PNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEAL 1152
Cdd:cd14060    208 SSCPRSFAELMRRCWEADVKERPSFKQIIGILESM 242
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
878-1152 4.59e-33

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 134.76  E-value: 4.59e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVELCRyDPEgdnTGEQVAVKSLKPESGGNH--IADLKKEIEILRNLYHENIVKYKGICTEDGGngIKLI 955
Cdd:COG0515     12 LRLLGRGGMGVVYLAR-DLR---LGRPVALKVLRPELAADPeaRERFRREARALARLNHPNIVRVYDVGEEDGR--PYLV 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  956 MEFLPSGSLKEYLpKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYy 1035
Cdd:COG0515     86 MEYVEGESLADLL-RRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATLT- 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1036 tvkddRDSPVFW---Y-APECLMQSKFYIASDVWSFGVTLHELLT----YcdSDSSPMALFLKMIgptHGQMTVTRLVNt 1107
Cdd:COG0515    164 -----QTGTVVGtpgYmAPEQARGEPVDPRSDVYSLGVTLYELLTgrppF--DGDSPAELLRAHL---REPPPPPSELR- 232
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1013071061 1108 lkegkrlpcpPNCPDEVYQLMRKCWEFQPSNRtsFQNLIEGFEAL 1152
Cdd:COG0515    233 ----------PDLPPALDAIVLRALAKDPEER--YQSAAELAAAL 265
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
881-1152 1.03e-32

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK4 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The specific function of MLK4 is yet to be determined. Mutations in the kinase domain of MLK4 have been detected in colorectal cancers. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 128.23  E-value: 1.03e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVElcrydpEGDNTGEQVAVKSLK--PESGGNHIAD-LKKEIEILRNLYHENIVKYKGICTEDggNGIKLIME 957
Cdd:cd14146      2 IGVGGFGKVY------RATWKGQEVAVKAARqdPDEDIKATAEsVRQEAKLFSMLRHPNIIKLEGVCLEE--PNLCLVME 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  958 FLPSGSLKEYL--------PKNKNKINLKQQLKYAVQICKGMDYLGSRQYV---HRDLAARNVLV--ESEHQ------VK 1018
Cdd:cd14146     74 FARGGTLNRALaaanaapgPRRARRIPPHILVNWAVQIARGMLYLHEEAVVpilHRDLKSSNILLleKIEHDdicnktLK 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1019 IGDFGLTKaietdkEYY-TVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLT----YCDSDSSPMALFLKmig 1093
Cdd:cd14146    154 ITDFGLAR------EWHrTTKMSAAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTgevpYRGIDGLAVAYGVA--- 224
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1013071061 1094 pthgqmtvtrlVNTLKegkrLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEAL 1152
Cdd:cd14146    225 -----------VNKLT----LPIPSTCPEPFAKLMKECWEQDPHIRPSFALILEQLTAI 268
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
881-1149 1.19e-32

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated Kinase-1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAK1 is also known as mitogen-activated protein kinase kinase kinase 7 (MAPKKK7 or MAP3K7), TAK, or MEKK7. As a MAPKKK, it is an important mediator of cellular responses to extracellular signals. It regulates both the c-Jun N-terminal kinase and p38 MAPK cascades by activating the MAPK kinases, MKK4 and MKK3/6. In addition, TAK1 plays diverse roles in immunity and development, in different biological contexts, through many signaling pathways including TGFbeta/BMP, Wnt/Fz, and NF-kB. It is also implicated in the activation of the tumor suppressor kinase, LKB1. The TAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270960 [Multi-domain]  Cd Length: 253  Bit Score: 127.55  E-value: 1.19e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYdpegdnTGEQVAVKSLKPESggnHIADLKKEIEILRNLYHENIVKYKGICTEdgGNGIKLIMEFLP 960
Cdd:cd14058      1 VGRGSFGVVCKARW------RNQIVAVKIIESES---EKKAFEVEVRQLSRVDHPNIIKLYGACSN--QKPVCLVMEYAE 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  961 SGSLKEYL--PKNKNKINLKQQLKYAVQICKGMDYLGS---RQYVHRDLAARNVLVESEHQV-KIGDFGLTKAIETDKey 1034
Cdd:cd14058     70 GGSLYNVLhgKEPKPIYTAAHAMSWALQCAKGVAYLHSmkpKALIHRDLKPPNLLLTNGGTVlKICDFGTACDISTHM-- 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1035 ytvKDDRDSPVfWYAPECLMQSKFYIASDVWSFGVTLHELLTycdsDSSPmalFLKMIGPThgqmtvTRLVNTLKEGKRL 1114
Cdd:cd14058    148 ---TNNKGSAA-WMAPEVFEGSKYSEKCDVFSWGIILWEVIT----RRKP---FDHIGGPA------FRIMWAVHNGERP 210
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1013071061 1115 PCPPNCPDEVYQLMRKCWEFQPSNRTSFQNlIEGF 1149
Cdd:cd14058    211 PLIKNCPKPIESLMTRCWSKDPEKRPSMKE-IVKI 244
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
878-1076 3.99e-32

Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC family consists of Cyclin-Dependent protein Kinases (CDKs), Mitogen-activated protein kinases (MAPKs) such as Extracellular signal-regulated kinase (ERKs), c-Jun N-terminal kinases (JNKs), and p38, and other kinases. CDKs belong to a large subfamily of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Other members of the CMGC family include casein kinase 2 (CK2), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK), Glycogen Synthase Kinase 3 (GSK3), among many others. The CMGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 125.81  E-value: 3.99e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVELCRydpegD-NTGEQVAVKSLKPESGGNHIADlkKEIEILRNLY----HENIVKYKGICTEDGGNGI 952
Cdd:cd05118      4 LRKIGEGAFGTVWLAR-----DkVTGEKVAIKKIKNDFRHPKAAL--REIKLLKHLNdvegHPNIVKLLDVFEHRGGNHL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  953 KLIMEFLPSgSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEH-QVKIGDFGLTKaIETD 1031
Cdd:cd05118     77 CLVFELMGM-NLYELIKDYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLELgQLKLADFGLAR-SFTS 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1013071061 1032 KEYYtvkdDRDSPVFWYAPECLMQSKFY-IASDVWSFGVTLHELLT 1076
Cdd:cd05118    155 PPYT----PYVATRWYRAPEVLLGAKPYgSSIDIWSLGCILAELLT 196
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
881-1091 5.65e-32

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK2 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK2 also activates ERK1/2, c-Jun N-terminal kinase (JNK) and p38 through their respective MAPKKs MEK1/2, JNK-activating kinase 2 (JNKK2), and MKK3/6. MEKK2 plays roles in T cell receptor signaling, immune synapse formation, cytokine gene expression, as well as in EGF and FGF receptor signaling. The MEKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 125.93  E-value: 5.65e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCrYDPEgdnTGEQVAVKSLK--PES--GGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGNGIKLIM 956
Cdd:cd06652     10 LGQGAFGRVYLC-YDAD---TGRELAVKQVQfdPESpeTSKEVNALECEIQLLKNLLHERIVQYYGCLRDPQERTLSIFM 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  957 EFLPSGSLKEYLpKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYT 1036
Cdd:cd06652     86 EYMPGGSIKDQL-KSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGASKRLQTICLSGT 164
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1013071061 1037 -VKDDRDSPvFWYAPECLMQSKFYIASDVWSFGVTLHELLTycdsDSSPMALFLKM 1091
Cdd:cd06652    165 gMKSVTGTP-YWMSPEVISGEGYGRKADIWSVGCTVVEMLT----EKPPWAEFEAM 215
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
881-1139 7.68e-32

Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent Protein Kinase Kinase, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Both LKB1 and CaMKKs can phosphorylate and activate AMP-activated protein kinase (AMPK). LKB1, also called STK11, serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMPK. Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The LKB1/CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 125.74  E-value: 7.68e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRydpegD-NTGEQVAVKSLK-------------PESGGNHIADLKKEIEILRNLYHENIVKYKGICTE 946
Cdd:cd14008      1 LGRGSFGKVKLAL-----DtETGQLYAIKIFNksrlrkrregkndRGKIKNALDDVRREIAIMKKLDHPNIVRLYEVIDD 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  947 DGGNGIKLIMEFLPSGSLKEyLPKNKNKINLKQQL--KYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGL 1024
Cdd:cd14008     76 PESDKLYLVLEYCEGGPVME-LDSGDRVPPLPEETarKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFGV 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1025 TKAIETDKEYytVKDDRDSPVFwYAPE-CLMQSKFYI--ASDVWSFGVTLhelltYCdsdsspMaLFLKM--IGPTHGQM 1099
Cdd:cd14008    155 SEMFEDGNDT--LQKTAGTPAF-LAPElCDGDSKTYSgkAADIWALGVTL-----YC------L-VFGRLpfNGDNILEL 219
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1013071061 1100 tvtrLVNTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNR 1139
Cdd:cd14008    220 ----YEAIQNQNDEFPIPPELSPELKDLLRRMLEKDPEKR 255
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
881-1147 1.02e-31

Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of plant MAPK kinase kinases (MAPKKKs) including Arabidopsis thaliana MEKK1 and MAPKKK3. Arabidopsis thaliana MEKK1 activates MPK4, a MAPK that regulates systemic acquired resistance. MEKK1 also participates in the regulation of temperature-sensitive and tissue-specific cell death. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The plant MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270802 [Multi-domain]  Cd Length: 259  Bit Score: 125.21  E-value: 1.02e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVelcrYDPEGDNTGEQVAVKSLKPESGGNH----IADLKKEIEILRNLYHENIVKYKGICTEDGGNGIKLim 956
Cdd:cd06632      8 LGSGSFGSV----YEGFNGDTGDFFAVKEVSLVDDDKKsresVKQLEQEIALLSKLRHPNIVQYYGTEREEDNLYIFL-- 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  957 EFLPSGSL----KEYLPKNKNKINLkqqlkYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETdk 1032
Cdd:cd06632     82 EYVPGGSIhkllQRYGAFEEPVIRL-----YTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKHVEA-- 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1033 eYYTVKDDRDSPvFWYAPECLMQ--SKFYIASDVWSFGVTLHELLTYcdsdsspmalflkmiGPTHGQMT-VTRLVNTLK 1109
Cdd:cd06632    155 -FSFAKSFKGSP-YWMAPEVIMQknSGYGLAVDIWSLGCTVLEMATG---------------KPPWSQYEgVAAIFKIGN 217
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1013071061 1110 EGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIE 1147
Cdd:cd06632    218 SGELPPIPDHLSPDAKDFIRLCLQRDPEDRPTASQLLE 255
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
881-1146 1.08e-31

Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Schizosaccharomyces pombe Byr2, Saccharomyces cerevisiae and Cryptococcus neoformans Ste11, and related proteins. They contain an N-terminal SAM (sterile alpha-motif) domain, which mediates protein-protein interaction, and a C-terminal catalytic domain. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Byr2 is regulated by Ras1. It responds to pheromone signaling and controls mating through the MAPK pathway. Budding yeast Ste11 functions in MAPK cascades that regulate mating, high osmolarity glycerol, and filamentous growth responses. The Byr2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270798 [Multi-domain]  Cd Length: 267  Bit Score: 125.34  E-value: 1.08e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELcrydpeGDN--TGEQVAVKSLKPESGGNHIAD--------LKKEIEILRNLYHENIVKYKGICTEdgGN 950
Cdd:cd06628      8 IGSGSFGSVYL------GMNasSGELMAVKQVELPSVSAENKDrkksmldaLQREIALLRELQHENIVQYLGSSSD--AN 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  951 GIKLIMEFLPSGSLKEYLpKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIET 1030
Cdd:cd06628     80 HLNIFLEYVPGGSVATLL-NNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISKKLEA 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1031 DKEYYTVKDDRDS---PVFWYAPECLMQSKFYIASDVWSFGvtlhelltyCdsdsspmaLFLKMIGPTHGQMTVTRLVNT 1107
Cdd:cd06628    159 NSLSTKNNGARPSlqgSVFWMAPEVVKQTSYTRKADIWSLG---------C--------LVVEMLTGTHPFPDCTQMQAI 221
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1013071061 1108 LKEG-KRLPC-PPNCPDEVYQLMRKCWEFQPSNRTSFQNLI 1146
Cdd:cd06628    222 FKIGeNASPTiPSNISSEARDFLEKTFEIDHNKRPTADELL 262
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
881-1152 1.57e-31

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK2 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K10. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK2 is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease. MLK2 also binds to normal huntingtin (Htt), which is important in neuronal transcription, development, and survival. MLK2 does not bind to the polyglutamine-expanded Htt, which is implicated in the pathogeneis of Huntington's disease, leading to neuronal toxicity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271050 [Multi-domain]  Cd Length: 258  Bit Score: 124.71  E-value: 1.57e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVElcrydpEGDNTGEQVAVKSLK--PESGGNHIAD-LKKEIEILRNLYHENIVKYKGICTEDggNGIKLIME 957
Cdd:cd14148      2 IGVGGFGKVY------KGLWRGEEVAVKAARqdPDEDIAVTAEnVRQEARLFWMLQHPNIIALRGVCLNP--PHLCLVME 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  958 FLPSGSLKEYLPKNKnkINLKQQLKYAVQICKGMDYLGSRQYV---HRDLAARNVLVE--------SEHQVKIGDFGLTK 1026
Cdd:cd14148     74 YARGGALNRALAGKK--VPPHVLVNWAVQIARGMNYLHNEAIVpiiHRDLKSSNILILepienddlSGKTLKITDFGLAR 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1027 aietdkEYY-TVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLT----YCDSDSSPMALFLKMigpthgqmtv 1101
Cdd:cd14148    152 ------EWHkTTKMSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTgevpYREIDALAVAYGVAM---------- 215
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1013071061 1102 trlvNTLKegkrLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEAL 1152
Cdd:cd14148    216 ----NKLT----LPIPSTCPEPFARLLEECWDPDPHGRPDFGSILKRLEDI 258
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
879-1153 2.13e-31

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR beta is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR beta forms homodimers or heterodimers with PDGFR alpha, depending on the nature of the PDGF ligand. PDGF-BB and PDGF-DD induce PDGFR beta homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR beta signaling leads to a variety of cellular effects including the stimulation of cell growth and chemotaxis, as well as the inhibition of apoptosis and GAP junctional communication. It is critical in normal angiogenesis as it is involved in the recruitment of pericytes and smooth muscle cells essential for vessel stability. Aberrant PDGFR beta expression is associated with some human cancers. The continuously-active fusion proteins of PDGFR beta with COL1A1 and TEL are associated with dermatofibrosarcoma protuberans (DFSP) and a subset of chronic myelomonocytic leukemia (CMML), respectively. The PDGFR beta subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133238 [Multi-domain]  Cd Length: 401  Bit Score: 128.20  E-value: 2.13e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGHFGKV-ELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNL-YHENIVKYKGICTEDGGngIKLIM 956
Cdd:cd05107     43 RTLGSGAFGRVvEATAHGLSHSQSTMKVAVKMLKSTARSSEKQALMSELKIMSHLgPHLNIVNLLGACTKGGP--IYIIT 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  957 EFLPSGSLKEYLPKNKNKI------------------------------------------------------NLKQQLK 982
Cdd:cd05107    121 EYCRYGDLVDYLHRNKHTFlqyyldknrddgslisggstplsqrkshvslgsesdggymdmskdesadyvpmqDMKGTVK 200
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  983 YA-------------------------------------------VQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKI 1019
Cdd:cd05107    201 YAdiessnyespydqylpsapertrrdtlinespalsymdlvgfsYQVANGMEFLASKNCVHRDLAARNVLICEGKLVKI 280
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1020 GDFGLTKAIETDKEYYTvKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTycdsdsspmalflkMIGPTHGQM 1099
Cdd:cd05107    281 CDFGLARDIMRDSNYIS-KGSTFLPLKWMAPESIFNNLYTTLSDVWSFGILLWEIFT--------------LGGTPYPEL 345
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1013071061 1100 TVTRLV-NTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALL 1153
Cdd:cd05107    346 PMNEQFyNAIKRGYRMAKPAHASDEIYEIMQKCWEEKFEIRPDFSQLVHLVGDLL 400
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
876-1141 2.45e-31

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek family is composed of 11 different mammalian members (Nek1-11) with similarity to the catalytic domain of Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants that were prevented from entering mitosis. Neks contain a conserved N-terminal catalytic domain and a more divergent C-terminal regulatory region of various sizes and structures. They are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270855 [Multi-domain]  Cd Length: 258  Bit Score: 123.73  E-value: 2.45e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  876 KRIRDLGEGHFGKVELCRydpeGDNTGEQVAVK--SLKpESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGgngiK 953
Cdd:cd08215      3 EKIRVIGKGSFGSAYLVR----RKSDGKLYVLKeiDLS-NMSEKEREEALNEVKLLSKLKHPNIVKYYESFEENG----K 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  954 L--IMEFLPSGSLKEYLPKNKNKINL---KQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAI 1028
Cdd:cd08215     74 LciVMEYADGGDLAQKIKKQKKKGQPfpeEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISKVL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1029 ETDKE---------YYtvkddrdspvfwYAPEcLMQSKFY-IASDVWSFGVTLHELLTycdsdsspmalfLKmigPTHGQ 1098
Cdd:cd08215    154 ESTTDlaktvvgtpYY------------LSPE-LCENKPYnYKSDIWALGCVLYELCT------------LK---HPFEA 205
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1013071061 1099 MTVTRLVNTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTS 1141
Cdd:cd08215    206 NNLPALVYKIVKGQYPPIPSQYSSELRDLVNSMLQKDPEKRPS 248
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
876-1141 3.13e-31

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK7 plays essential roles in the cell cycle and in transcription. It associates with cyclin H and MAT1 and acts as a CDK-Activating Kinase (CAK) by phosphorylating and activating cell cycle CDKs (CDK1/2/4/6). In the brain, it activates CDK5. CDK7 is also a component of the general transcription factor TFIIH, which phosphorylates the C-terminal domain (CTD) of RNA polymerase II when it is bound with unphosphorylated DNA, as present in the pre-initiation complex. Following phosphorylation, the CTD dissociates from the DNA which allows transcription initiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270833 [Multi-domain]  Cd Length: 298  Bit Score: 124.99  E-value: 3.13e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  876 KRIRDLGEGHFGKVELCRYDpegdNTGEQVAVKSLKPesggNHIADLK--------KEIEILRNLYHENIVKYKGICTED 947
Cdd:cd07841      3 EKGKKLGEGTYAVVYKARDK----ETGRIVAIKKIKL----GERKEAKdginftalREIKLLQELKHPNIIGLLDVFGHK 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  948 GGngIKLIMEFLPSgSLkEYLPKNKNKINLKQQLK-YAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTK 1026
Cdd:cd07841     75 SN--INLVFEFMET-DL-EKVIKDKSIVLTPADIKsYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLAR 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1027 AIETDKEYYTVKddrdspVF--WY-APECLMQSKFY-IASDVWSFGVTLHELLT-----YCDSDSSPMALFLKMIG-PTH 1096
Cdd:cd07841    151 SFGSPNRKMTHQ------VVtrWYrAPELLFGARHYgVGVDMWSVGCIFAELLLrvpflPGDSDIDQLGKIFEALGtPTE 224
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1013071061 1097 GQMT-VTRLVNTLKEGKRLPCP-----PNCPDEVYQLMRKCWEFQPSNRTS 1141
Cdd:cd07841    225 ENWPgVTSLPDYVEFKPFPPTPlkqifPAASDDALDLLQRLLTLNPNKRIT 275
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
876-1076 1.53e-30

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK3 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. In addition, MEKK3 is involved in interleukin-1 receptor and Toll-like receptor 4 signaling. It is also a specific regulator of the proinflammatory cytokines IL-6 and GM-CSF in some immune cells. MEKK3 also regulates calcineurin, which plays a critical role in T cell activation, apoptosis, skeletal myocyte differentiation, and cardiac hypertrophy. The MEKK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270817 [Multi-domain]  Cd Length: 271  Bit Score: 122.11  E-value: 1.53e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  876 KRIRDLGEGHFGKVELCrYDPEgdnTGEQVAVKSLK--PES--GGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGNG 951
Cdd:cd06651     10 RRGKLLGQGAFGRVYLC-YDVD---TGRELAAKQVQfdPESpeTSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAEKT 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  952 IKLIMEFLPSGSLKEYLpKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETD 1031
Cdd:cd06651     86 LTIFMEYMPGGSVKDQL-KAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTI 164
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1013071061 1032 KEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd06651    165 CMSGTGIRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLT 209
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
881-1091 1.79e-30

Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized proteins with similarity to MEKK3, MEKK2, and related proteins; they contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKKs), proteins that phosphorylate and activate MAPK kinases (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MEKK2 and MEKK3 activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270819 [Multi-domain]  Cd Length: 264  Bit Score: 121.67  E-value: 1.79e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCrYDPEgdnTGEQVAVKSL--KPES--GGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGNGIKLIM 956
Cdd:cd06653     10 LGRGAFGEVYLC-YDAD---TGRELAVKQVpfDPDSqeTSKEVNALECEIQLLKNLRHDRIVQYYGCLRDPEEKKLSIFV 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  957 EFLPSGSLKEYLpKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYT 1036
Cdd:cd06653     86 EYMPGGSVKDQL-KAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRIQTICMSGT 164
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1013071061 1037 -VKDDRDSPvFWYAPECLMQSKFYIASDVWSFGVTLHELLTycdsDSSPMALFLKM 1091
Cdd:cd06653    165 gIKSVTGTP-YWMSPEVISGEGYGRKADVWSVACTVVEMLT----EKPPWAEYEAM 215
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
881-1152 5.24e-30

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK3 is a mitogen-activated protein kinase kinase kinases (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK3 activates multiple MAPK pathways and plays a role in apoptosis, proliferation, migration, and differentiation, depending on the cellular context. It is highly expressed in breast cancer cells and its signaling through c-Jun N-terminal kinase has been implicated in the migration, invasion, and malignancy of cancer cells. MLK3 also functions as a negative regulator of Inhibitor of Nuclear Factor-KappaB Kinase (IKK) and consequently, it also impacts inflammation and immunity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271049 [Multi-domain]  Cd Length: 267  Bit Score: 120.52  E-value: 5.24e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVElcrydpEGDNTGEQVAVKSLK--PESGGNHIAD-LKKEIEILRNLYHENIVKYKGICTEDggNGIKLIME 957
Cdd:cd14147     11 IGIGGFGKVY------RGSWRGELVAVKAARqdPDEDISVTAEsVRQEARLFAMLAHPNIIALKAVCLEE--PNLCLVME 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  958 FLPSGSLKEYLPKNKnkINLKQQLKYAVQICKGMDYLGSRQYV---HRDLAARNVLV-------ESEHQ-VKIGDFGLTK 1026
Cdd:cd14147     83 YAAGGPLSRALAGRR--VPPHVLVNWAVQIARGMHYLHCEALVpviHRDLKSNNILLlqpiendDMEHKtLKITDFGLAR 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1027 aietdKEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLT----YCDSDSSPMALFLKmigpthgqmtvt 1102
Cdd:cd14147    161 -----EWHKTTQMSAAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTgevpYRGIDCLAVAYGVA------------ 223
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1103 rlVNTLKegkrLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEAL 1152
Cdd:cd14147    224 --VNKLT----LPIPSTCPEPFAQLMADCWAQDPHRRPDFASILQQLEAL 267
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
881-1152 8.66e-30

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK1 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K9. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Little is known about the specific function of MLK1. It is capable of activating the c-Jun N-terminal kinase pathway. Mice lacking both MLK1 and MLK2 are viable, fertile, and have normal life spans. There could be redundancy in the function of MLKs. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271047 [Multi-domain]  Cd Length: 270  Bit Score: 119.76  E-value: 8.66e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDpegdntGEQVAVKSLK---PESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDggNGIKLIME 957
Cdd:cd14145     14 IGIGGFGKVYRAIWI------GDEVAVKAARhdpDEDISQTIENVRQEAKLFAMLKHPNIIALRGVCLKE--PNLCLVME 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  958 FLPSGSLKEYLpkNKNKINLKQQLKYAVQICKGMDYLGSRQYV---HRDLAARNVL----VE----SEHQVKIGDFGLTK 1026
Cdd:cd14145     86 FARGGPLNRVL--SGKRIPPDILVNWAVQIARGMNYLHCEAIVpviHRDLKSSNILilekVEngdlSNKILKITDFGLAR 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1027 aietdKEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLT----YCDSDSSPMALFLKMigpthgqmtvt 1102
Cdd:cd14145    164 -----EWHRTTKMSAAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTgevpFRGIDGLAVAYGVAM----------- 227
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1103 rlvNTLKegkrLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEAL 1152
Cdd:cd14145    228 ---NKLS----LPIPSTCPEPFARLMEDCWNPDPHSRPPFTNILDQLTAI 270
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
881-1076 1.44e-29

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270687 [Multi-domain]  Cd Length: 258  Bit Score: 118.73  E-value: 1.44e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDpegdNTGEQVAVKSLKPESGGNH-IADLKKEIEILRNLYHENIVKYKGIcTEDGGNgIKLIMEFL 959
Cdd:cd05117      8 LGRGSFGVVRLAVHK----KTGEEYAVKIIDKKKLKSEdEEMLRREIEILKRLDHPNIVKLYEV-FEDDKN-LYLVMELC 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  960 PSGSLKEYLpKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQ---VKIGDFGLTKAIETDKEYYT 1036
Cdd:cd05117     82 TGGELFDRI-VKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPdspIKIIDFGLAKIFEEGEKLKT 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1013071061 1037 VKddrDSPVFWyAPECLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd05117    161 VC---GTPYYV-APEVLKGKGYGKKCDIWSLGVILYILLC 196
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
577-851 1.55e-29

Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. FAK is a cytoplasmic (or nonreceptor) PTK that contains an autophosphorylation site and a FERM domain at the N-terminus, a central tyr kinase domain, proline-rich regions, and a C-terminal FAT (focal adhesion targeting) domain. FAK activity is dependent on integrin-mediated cell adhesion, which facilitates N-terminal autophosphorylation. Full activation is achieved by the phosphorylation of its two adjacent A-loop tyrosines. FAK is important in mediating signaling initiated at sites of cell adhesions and at growth factor receptors. Through diverse molecular interactions, FAK functions as a biosensor or integrator to control cell motility. It is a key regulator of cell survival, proliferation, migration and invasion, and thus plays an important role in the development and progression of cancer. Src binds to autophosphorylated FAK forming the FAK-Src dual kinase complex, which is activated in a wide variety of tumor cells and generates signals promoting growth and metastasis. FAK is being developed as a target for cancer therapy. The FAK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 119.06  E-value: 1.55e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  577 RILKKDLVQGEHLGRGTRTHIYSGTLMDYKDDegtseekKIKVILKV----LDPSHRDislAFFEAASMMRQVSHKHIVY 652
Cdd:cd05056      2 EIQREDITLGRCIGEGQFGDVYQGVYMSPENE-------KIAVAVKTckncTSPSVRE---KFLQEAYIMRQFDHPHIVK 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  653 LYGVCVRDVENImVEEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAregiDSECg 732
Cdd:cd05056     72 LIGVITENPVWI-VMELAPLGELRSYLQVNKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVS----SPDC- 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  733 pfIKLSDPGipitvLSR--------QECIERIP--WIAPECVeDSKNLSVAADKWSFGTTLWEICYNGEIP---LKDKTL 799
Cdd:cd05056    146 --VKLGDFG-----LSRymedesyyKASKGKLPikWMAPESI-NFRRFTSASDVWMFGVCMWEILMLGVKPfqgVKNNDV 217
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1013071061  800 IEK----ERFyesrcrPVTPSC-KELADLMTRCMNYDPNQRPFFRAIMRDINKLEEQ 851
Cdd:cd05056    218 IGRiengERL------PMPPNCpPTLYSLMTKCWAYDPSKRPRFTELKAQLSDILQE 268
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
881-1076 2.00e-29

Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. Some IRAKs may also play roles in T- and B-cell signaling, and adaptive immunity. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK-1, -2, and -4 are ubiquitously expressed and are active kinases, while IRAK-M is only induced in monocytes and macrophages and is an inactive kinase. Variations in IRAK genes are linked to diverse diseases including infection, sepsis, cancer, and autoimmune diseases. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase domain in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. This subfamily includes plant receptor-like kinases (RLKs) including Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1). BAK1 functions in BR (brassinosteroid)-regulated plant development and in pathways involved in plant resistance to pathogen infection and herbivore attack. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The IRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 118.91  E-value: 2.00e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYdpegdNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGNGikLIMEFLP 960
Cdd:cd14066      1 IGSGGFGTVYKGVL-----ENGTVVAVKRLNEMNCAASKKEFLTELEMLGRLRHPNLVRLLGYCLESDEKL--LVYEYMP 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  961 SGSLKEYLPKNKNKINL--KQQLKYAVQICKGMDYL---GSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEyy 1035
Cdd:cd14066     74 NGSLEDRLHCHKGSPPLpwPQRLKIAKGIARGLEYLheeCPPPIIHGDIKSSNILLDEDFEPKLTDFGLARLIPPSES-- 151
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1013071061 1036 TVKDDRDSPVFWY-APECLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd14066    152 VSKTSAVKGTIGYlAPEYIRTGRVSTKSDVYSFGVVLLELLT 193
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
881-1142 2.29e-29

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP kinases serve as essential sensors of cellular stress. They are involved in regulating NF-kappaB and MAPK signaling, and are implicated in mediating cellular processes such as apoptosis, necroptosis, differentiation, and survival. RIP kinases contain a homologous N-terminal kinase domain and varying C-terminal domains. Higher vertebrates contain multiple RIP kinases, with mammals harboring at least five members. RIP1 and RIP2 harbor C-terminal domains from the Death domain (DD) superfamily while RIP4 contains ankyrin (ANK) repeats. RIP3 contain a RIP homotypic interaction motif (RHIM) that facilitates binding to RIP1. RIP1 and RIP3 are important in apoptosis and necroptosis, while RIP2 and RIP4 play roles in keratinocyte differentiation and inflammatory immune responses. The RIP subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270880 [Multi-domain]  Cd Length: 263  Bit Score: 118.32  E-value: 2.29e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDpegdNTGEQVAVKSLKPESG-GNHIADLKKEIEILRNLYHENIVKYKGICTEDGGNGikLIMEFL 959
Cdd:cd13978      1 LGSGGFGTVSKARHV----SWFGMVAIKCLHSSPNcIEERKALLKEAEKMERARHSYVLPLLGVCVERRSLG--LVMEYM 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  960 PSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYL--GSRQYVHRDLAARNVLVESEHQVKIGDFGLTK---AIETDKEY 1034
Cdd:cd13978     75 ENGSLKSLLEREIQDVPWSLRFRIIHEIALGMNFLhnMDPPLLHHDLKPENILLDNHFHVKISDFGLSKlgmKSISANRR 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1035 YTVKDDRDSPVFwYAPECL--MQSKFYIASDVWSFGVTLHELLT----YCDSDSSpmalFLKMIGPTHGQMTVtrlVNTL 1108
Cdd:cd13978    155 RGTENLGGTPIY-MAPEAFddFNKKPTSKSDVYSFAIVIWAVLTrkepFENAINP----LLIMQIVSKGDRPS---LDDI 226
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1013071061 1109 KEgkrlPCPPNCPDEVYQLMRKCWEFQPSNRTSF 1142
Cdd:cd13978    227 GR----LKQIENVQELISLMIRCWDGNPDARPTF 256
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
577-848 2.30e-29

Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of Csk, Chk, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. They negatively regulate the activity of Src kinases that are anchored to the plasma membrane. To inhibit Src kinases, Csk and Chk are translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Chk inhibit Src kinases using a noncatalytic mechanism by simply binding to them. As negative regulators of Src kinases, Csk and Chk play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. The Csk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 118.22  E-value: 2.30e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  577 RILKKDLVQGEHLGRGTRTHIYSGTLmdykddegtseeKKIKVILKVLDPSHRDISlAFFEAASMMRQVSHKHIVYLYGV 656
Cdd:cd05039      2 AINKKDLKLGELIGKGEFGDVMLGDY------------RGQKVAVKCLKDDSTAAQ-AFLAEASVMTTLRHPNLVQLLGV 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  657 CVRDVENIMVEEFVEGGPL-DLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfI 735
Cdd:cd05039     69 VLEGNGLYIVTEYMAKGSLvDYLRSRGRAVITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDNV-------A 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  736 KLSDPGipitvLSRQECIER------IPWIAPECVEDSKnLSVAADKWSFGTTLWEICYNG-----EIPLKD-KTLIEKE 803
Cdd:cd05039    142 KVSDFG-----LAKEASSNQdggklpIKWTAPEALREKK-FSTKSDVWSFGILLWEIYSFGrvpypRIPLKDvVPHVEKG 215
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1013071061  804 rfYESRCRPVTPscKELADLMTRCMNYDPNQRPFFRAIMRDINKL 848
Cdd:cd05039    216 --YRMEAPEGCP--PEVYKVMKNCWELDPAKRPTFKQLREKLEHI 256
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
881-1147 3.81e-29

Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. Members of this subfamily include LIMK, Testicular or testis-specific protein kinase (TESK), and similar proteins. LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270967 [Multi-domain]  Cd Length: 252  Bit Score: 117.59  E-value: 3.81e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVelcrYDPEGDNTGEQVAVKSLKPESGGNHIAdlkKEIEILRNLYHENIVKYKGICTEDggNGIKLIMEFLP 960
Cdd:cd14065      1 LGKGFFGEV----YKVTHRETGKVMVMKELKRFDEQRSFL---KEVKLMRRLSHPNILRFIGVCVKD--NKLNFITEYVN 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  961 SGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVK---IGDFGLTKAIetdKEYYTV 1037
Cdd:cd14065     72 GGTLEELLKSMDEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVREANRGRnavVADFGLAREM---PDEKTK 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1038 KDDRDSPV------FWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSDsspmalflkmigPTHGQMTVTRLVNTlkEG 1111
Cdd:cd14065    149 KPDRKKRLtvvgspYWMAPEMLRGESYDEKVDVFSFGIVLCEIIGRVPAD------------PDYLPRTMDFGLDV--RA 214
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1013071061 1112 KRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIE 1147
Cdd:cd14065    215 FRTLYVPDCPPSFLPLAIRCCQLDPEKRPSFVELEH 250
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
586-845 4.50e-29

Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes (or Fps) is a cytoplasmic (or nonreceptor) PTK containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated PTK activity. Fes kinase is expressed in myeloid, vascular endothelial, epithelial, and neuronal cells. It plays important roles in cell growth and differentiation, angiogenesis, inflammation and immunity, and cytoskeletal regulation. A recent study implicates Fes kinase as a tumor suppressor in colorectal cancer. The Fes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 117.34  E-value: 4.50e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  586 GEHLGRGTRTHIYSGTLmdykddEGTSEEKKIKVILKVLDPSHRDislAFFEAASMMRQVSHKHIVYLYGVCVRDVENIM 665
Cdd:cd05084      1 GERIGRGNFGEVFSGRL------RADNTPVAVKSCRETLPPDLKA---KFLQEARILKQYSHPNIVRLIGVCTQKQPIYI 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  666 VEEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGipit 745
Cdd:cd05084     72 VMELVQGGDFLTFLRTEGPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNV-------LKISDFG---- 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  746 vLSRQEC---------IERIP--WIAPECVEDSKnLSVAADKWSFGTTLWEICYNGEIPLKDKTLIEKERFYESRCR-PV 813
Cdd:cd05084    141 -MSREEEdgvyaatggMKQIPvkWTAPEALNYGR-YSSESDVWSFGILLWETFSLGAVPYANLSNQQTREAVEQGVRlPC 218
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1013071061  814 TPSC-KELADLMTRCMNYDPNQRPFFRAIMRDI 845
Cdd:cd05084    219 PENCpDEVYRLMEQCWEYDPRKRPSFSTVHQDL 251
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
875-1076 4.62e-29

Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and similar proteins; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include MAPKKs from plants, kinetoplastids, alveolates, and mycetozoa. The MAPKK, LmxPK4, from Leishmania mexicana, is important in differentiation and virulence. Dictyostelium discoideum MEK1 is required for proper chemotaxis; MEK1 null mutants display severe defects in cell polarization and directional movement. Plants contain multiple MAPKKs like other eukaryotes. The Arabidopsis genome encodes for 10 MAPKKs while poplar and rice contain 13 MAPKKs each. The functions of these proteins have not been fully elucidated. There is evidence to suggest that MAPK cascades are involved in plant stress responses. In Arabidopsis, MKK3 plays a role in pathogen signaling; MKK2 is involved in cold and salt stress signaling; MKK4/MKK5 participates in innate immunity; and MKK7 regulates basal and systemic acquired resistance. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 117.69  E-value: 4.62e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  875 LKRIRDLGEGHFGKVELCRYDPegdnTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGngIKL 954
Cdd:cd06623      3 LERVKVLGQGSSGVVYKVRHKP----TGKIYALKKIHVDGDEEFRKQLLRELKTLRSCESPYVVKCYGAFYKEGE--ISI 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPSGSLKEYLPKNKnKINlKQQLKY-AVQICKGMDYL-GSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIEtdk 1032
Cdd:cd06623     77 VLEYMDGGSLADLLKKVG-KIP-EPVLAYiARQILKGLDYLhTKRHIIHRDIKPSNLLINSKGEVKIADFGISKVLE--- 151
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1013071061 1033 eyyTVKDDRDSPVFWYA---PECLmQSKFY-IASDVWSFGVTLHELLT 1076
Cdd:cd06623    152 ---NTLDQCNTFVGTVTymsPERI-QGESYsYAADIWSLGLTLLECAL 195
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
589-845 4.88e-29

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 115.83  E-value: 4.88e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  589 LGRGTRTHIYsgtlmdykddEGTSEEKKIKVILKVLDPSHRDISLAFFEA-ASMMRQVSHKHIVYLYGVCVRDVENIMVE 667
Cdd:cd00180      1 LGKGSFGKVY----------KARDKETGKKVAVKVIPKEKLKKLLEELLReIEILKKLNHPNIVKLYDVFETENFLYLVM 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  668 EFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGI----- 742
Cdd:cd00180     71 EYCEGGSLKDLLKENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGT-------VKLADFGLakdld 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  743 PITVLSRQECIERIPWIAPECVEDSKNLSVAADKWSFGTTLWEIcyngeiplkdktliekerfyesrcrpvtpscKELAD 822
Cdd:cd00180    144 SDDSLLKTTGGTTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL-------------------------------EELKD 192
                          250       260
                   ....*....|....*....|...
gi 1013071061  823 LMTRCMNYDPNQRPFFRAIMRDI 845
Cdd:cd00180    193 LIRRMLQYDPKKRPSAKELLEHL 215
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
587-845 6.14e-29

Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Syk-like subfamily is composed of Syk, ZAP-70, Shark, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. They are involved in the signaling downstream of activated receptors (including B-cell, T-cell, and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. Syk is important in B-cell receptor signaling, while Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor signaling. Syk also plays a central role in Fc receptor-mediated phagocytosis in the adaptive immune system. Shark is exclusively expressed in ectodermally derived epithelia, and is localized preferentially to the apical surface of the epithelial cells, it may play a role in a signaling pathway for epithelial cell polarity. The Syk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 117.07  E-value: 6.14e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  587 EHLGRGTRTHIYSGTlmdYKDDEGtseeKKIKVILKVLDPSHRDISLA-FFEAASMMRQVSHKHIVYLYGVCVRDvENIM 665
Cdd:cd05060      1 KELGHGNFGSVRKGV---YLMKSG----KEVEVAVKTLKQEHEKAGKKeFLREASVMAQLDHPCIVRLIGVCKGE-PLML 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  666 VEEFVEGGPLDLFMHRKSDVltTPWKFKV-AKQLASALSYLEDKDLVHGNVCTKNLLLAREGidsecgpFIKLSDPGipi 744
Cdd:cd05060     73 VMELAPLGPLLKYLKKRREI--PVSDLKElAHQVAMGMAYLESKHFVHRDLAARNVLLVNRH-------QAKISDFG--- 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  745 tvLSRQ----------ECIERIP--WIAPECVEDSKnLSVAADKWSFGTTLWEICYNGEIPLKDKTLIEKERFYESRCRP 812
Cdd:cd05060    141 --MSRAlgagsdyyraTTAGRWPlkWYAPECINYGK-FSSKSDVWSYGVTLWEAFSYGAKPYGEMKGPEVIAMLESGERL 217
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1013071061  813 VTPS-C-KELADLMTRCMNYDPNQRPFFRAI---MRDI 845
Cdd:cd05060    218 PRPEeCpQEIYSIMLSCWKYRPEDRPTFSELestFRRD 255
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
586-845 6.59e-29

Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; Fer kinase; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fer kinase is a member of the Fes subfamily of proteins which are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. Fer kinase is expressed in a wide variety of tissues, and is found to reside in both the cytoplasm and the nucleus. It plays important roles in neuronal polarization and neurite development, cytoskeletal reorganization, cell migration, growth factor signaling, and the regulation of cell-cell interactions mediated by adherens junctions and focal adhesions. Fer kinase also regulates cell cycle progression in malignant cells.


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 116.64  E-value: 6.59e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  586 GEHLGRGTRTHIYSGTLMDykddegtseekKIKVILKVLDPS-HRDISLAFFEAASMMRQVSHKHIVYLYGVCVRDVENI 664
Cdd:cd05085      1 GELLGKGNFGEVYKGTLKD-----------KTPVAVKTCKEDlPQELKIKFLSEARILKQYDHPNIVKLIGVCTQRQPIY 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  665 MVEEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGipi 744
Cdd:cd05085     70 IVMELVPGGDFLSFLRKKKDELKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNA-------LKISDFG--- 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  745 tvLSRQE--------CIERIP--WIAPECVEDSKnLSVAADKWSFGTTLWEICYNGEIP---LKDKTLIEK-ERFYESRC 810
Cdd:cd05085    140 --MSRQEddgvysssGLKQIPikWTAPEALNYGR-YSSESDVWSFGILLWETFSLGVCPypgMTNQQAREQvEKGYRMSA 216
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1013071061  811 RPVTPscKELADLMTRCMNYDPNQRPFFRAIMRDI 845
Cdd:cd05085    217 PQRCP--EDIYKIMQRCWDYNPENRPKFSELQKEL 249
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
881-1150 1.23e-28

Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Raf kinases act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Aberrant expression or activation of components in this pathway are associated with tumor initiation, progression, and metastasis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain, and a catalytic kinase domain. Vertebrates have three Raf isoforms (A-, B-, and C-Raf) with different expression profiles, modes of regulation, and abilities to function in the ERK cascade, depending on cellular context and stimuli. They have essential and non-overlapping roles during embryo- and organogenesis. Knockout of each isoform results in a lethal phenotype or abnormality in most mouse strains. The Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270964 [Multi-domain]  Cd Length: 253  Bit Score: 115.95  E-value: 1.23e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYdpEGDntgeqVAVKSLKPES-GGNHIADLKKEIEILRNLYHENIVKYKGICTEdggNGIKLIMEFL 959
Cdd:cd14062      1 IGSGSFGTVYKGRW--HGD-----VAVKKLNVTDpTPSQLQAFKNEVAVLRKTRHVNILLFMGYMTK---PQLAIVTQWC 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  960 PSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTkaieTDKEYYTVKD 1039
Cdd:cd14062     71 EGSSLYKHLHVLETKFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLA----TVKTRWSGSQ 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1040 DRDSP---VFWYAPECL-MQSK--FYIASDVWSFGVTLHELLT----YCDSDSSPMALFLKMIGPTHGQMTVTRlvntlk 1109
Cdd:cd14062    147 QFEQPtgsILWMAPEVIrMQDEnpYSFQSDVYAFGIVLYELLTgqlpYSHINNRDQILFMVGRGYLRPDLSKVR------ 220
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1013071061 1110 egkrlpcpPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFE 1150
Cdd:cd14062    221 --------SDTPKALRRLMEDCIKFQRDERPLFPQILASLE 253
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
878-1145 2.35e-28

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk3, also called lemur tyrosine kinase 3 (Lmtk3) is a receptor kinase containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. The function of Aatyk3 is still unknown. The Aatyk3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271108 [Multi-domain]  Cd Length: 276  Bit Score: 115.82  E-value: 2.35e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVELCryDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDggNGIKLIME 957
Cdd:cd14206      2 LQEIGNGWFGKVILG--EIFSDYTPAQVVVKELRVSAGPLEQRKFISEAQPYRSLQHPNILQCLGLCTET--IPFLLIME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  958 FLPSGSLKEYLPKNKNKINLKQQL---------KYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAi 1028
Cdd:cd14206     78 FCQLGDLKRYLRAQRKADGMTPDLptrdlrtlqRMAYEITLGLLHLHKNNYIHSDLALRNCLLTSDLTVRIGDYGLSHN- 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1029 ETDKEYYTVKDDRDSPVFWYAPECL--MQSKFYIA-----SDVWSFGVTLHELLTYCD------SDSSPMALFLKmigpt 1095
Cdd:cd14206    157 NYKEDYYLTPDRLWIPLRWVAPELLdeLHGNLIVVdqskeSNVWSLGVTIWELFEFGAqpyrhlSDEEVLTFVVR----- 231
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1096 HGQMTVTRlvntlkegKRLPCPPNcpDEVYQLMRKCWeFQPSNRTSFQNL 1145
Cdd:cd14206    232 EQQMKLAK--------PRLKLPYA--DYWYEIMQSCW-LPPSQRPSVEEL 270
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
871-1152 3.63e-28

Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A-Raf cooperates with C-Raf in regulating ERK transient phosphorylation that is associated with cyclin D expression and cell cycle progression. Mice deficient in A-Raf are born alive but show neurological and intestinal defects. A-Raf demonstrates low kinase activity to MEK, compared with B- and C-Raf, and may also have alternative functions other than in the ERK signaling cascade. It regulates the M2 type pyruvate kinase, a key glycolytic enzyme. It also plays a role in endocytic membrane trafficking. A-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The A-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271052 [Multi-domain]  Cd Length: 265  Bit Score: 115.11  E-value: 3.63e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  871 EKRFLKRIrdlGEGHFGKVELCRYdpEGDntgeqVAVKSLK-PESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGg 949
Cdd:cd14150      1 EVSMLKRI---GTGSFGTVFRGKW--HGD-----VAVKILKvTEPTPEQLQAFKNEMQVLRKTRHVNILLFMGFMTRPN- 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  950 ngIKLIMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTkaie 1029
Cdd:cd14150     70 --FAIITQWCEGSSLYRHLHVTETRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLA---- 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1030 TDKEYYTVKDDRDSP---VFWYAPECL-MQ--SKFYIASDVWSFGVTLHELLT----YCDSDSSPMALFlkMIGPTHGQM 1099
Cdd:cd14150    144 TVKTRWSGSQQVEQPsgsILWMAPEVIrMQdtNPYSFQSDVYAYGVVLYELMSgtlpYSNINNRDQIIF--MVGRGYLSP 221
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1013071061 1100 TVTRLVNtlkegkrlpcppNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEAL 1152
Cdd:cd14150    222 DLSKLSS------------NCPKAMKRLLIDCLKFKREERPLFPQILVSIELL 262
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
589-848 3.80e-28

Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are PTKs, catalyzing the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jaks are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 115.56  E-value: 3.80e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  589 LGRGTRTHIYSGTLmDYKDDeGTSEEkkikVILKVLDPSHRDISLAFFE-AASMMRQVSHKHIVYLYGVCVRDVENIM-- 665
Cdd:cd05038     12 LGEGHFGSVELCRY-DPLGD-NTGEQ----VAVKSLQPSGEEQHMSDFKrEIEILRTLDHEYIVKYKGVCESPGRRSLrl 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  666 VEEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGIP-I 744
Cdd:cd05038     86 IMEYLPSGSLRDYLQRHRDQIDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILVESEDL-------VKISDFGLAkV 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  745 TVLSRQECIERIP------WIAPECVEDSKnLSVAADKWSFGTTLWEICYNGEIPLKDKTLIEK---------------E 803
Cdd:cd05038    159 LPEDKEYYYVKEPgespifWYAPECLRESR-FSSASDVWSFGVTLYELFTYGDPSQSPPALFLRmigiaqgqmivtrllE 237
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1013071061  804 RFYESRCRPVTPSC-KELADLMTRCMNYDPNQRPFFRAIMRDINKL 848
Cdd:cd05038    238 LLKSGERLPRPPSCpDEVYDLMKECWEYEPQDRPSFSDLILIIDRL 283
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
611-842 3.92e-28

Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes Ack1, thirty-eight-negative kinase 1 (Tnk1), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal catalytic domain, an SH3 domain, a Cdc42-binding CRIB domain, and a proline-rich region. They are mainly expressed in brain and skeletal tissues and are involved in the regulation of cell adhesion and growth, receptor degradation, and axonal guidance. Ack1 is also associated with androgen-independent prostate cancer progression. Tnk1 regulates TNFalpha signaling and may play an important role in cell death. The Ack-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 114.75  E-value: 3.92e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  611 TSEEKKIKVILKVLD---PSHRDISLAFFEAASMMRQVSHKHIVYLYGVcVRDVENIMVEEFVEGGPL--DLFMHRKSDV 685
Cdd:cd05040     18 TPSGKVIQVAVKCLKsdvLSQPNAMDDFLKEVNAMHSLDHPNLIRLYGV-VLSSPLMMVTELAPLGSLldRLRKDQGHFL 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  686 LTTPWKFkvAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGipitvLSRQECIER---------- 755
Cdd:cd05040     97 ISTLCDY--AVQIANGMAYLESKRFIHRDLAARNILLASKDK-------VKIGDFG-----LMRALPQNEdhyvmqehrk 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  756 --IPWIAPECVEdSKNLSVAADKWSFGTTLWEICYNGEIP---LKDKTLIEK-ERFYESRCRPvtPSC-KELADLMTRCM 828
Cdd:cd05040    163 vpFAWCAPESLK-TRKFSHASDVWMFGVTLWEMFTYGEEPwlgLNGSQILEKiDKEGERLERP--DDCpQDIYNVMLQCW 239
                          250
                   ....*....|....
gi 1013071061  829 NYDPNQRPFFRAIM 842
Cdd:cd05040    240 AHKPADRPTFVALR 253
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
617-842 4.74e-28

Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed mainly of MAP3Ks and similar proteins, including TGF-beta Activated Kinase-1 (TAK1, also called MAP3K7), MAP3K12, MAP3K13, Mixed lineage kinase (MLK), MLK-Like mitogen-activated protein Triple Kinase (MLTK), and Raf (Rapidly Accelerated Fibrosarcoma) kinases. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Also included in this subfamily is the pseudokinase Kinase Suppressor of Ras (KSR), which is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway.


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 114.17  E-value: 4.74e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  617 IKViLKVLDPSHRDISlAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSDVLTTPWKFKVAK 696
Cdd:cd13999     21 IKK-LKVEDDNDELLK-EFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSLYDLLHKKKIPLSWSLRLKIAL 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  697 QLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGipitvLSRQE---------CIERIPWIAPECVEDS 767
Cdd:cd13999     99 DIARGMNYLHSPPIIHRDLKSLNILLDENFT-------VKIADFG-----LSRIKnsttekmtgVVGTPRWMAPEVLRGE 166
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1013071061  768 KNlSVAADKWSFGTTLWEICyNGEIPLKDKTLIEK--ERFYESRCRPVTPSC-KELADLMTRCMNYDPNQRPFFRAIM 842
Cdd:cd13999    167 PY-TEKADVYSFGIVLWELL-TGEVPFKELSPIQIaaAVVQKGLRPPIPPDCpPELSKLIKRCWNEDPEKRPSFSEIV 242
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
879-1145 1.09e-27

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Aatyk subfamily is also referred to as the lemur tyrosine kinase (Lmtk) subfamily. It consists of Aatyk1 (Lmtk1), Aatyk2 (Lmtk2, Brek), Aatyk3 (Lmtk3), and similar proteins. Aatyk proteins are mostly receptor PTKs (RTKs) containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk1 does not contain a transmembrane segment and is a cytoplasmic (or nonreceptor) kinase. Aatyk proteins are classified as PTKs based on overall sequence similarity and the phylogenetic tree. However, analysis of catalytic residues suggests that Aatyk proteins may be multispecific kinases, functioning also as serine/threonine kinases. They are involved in neural differentiation, nerve growth factor (NGF) signaling, apoptosis, and spermatogenesis. The Aatyk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270638 [Multi-domain]  Cd Length: 269  Bit Score: 113.84  E-value: 1.09e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGHFGKVELCRYDpeGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEdgGNGIKLIMEF 958
Cdd:cd05042      1 QEIGNGWFGKVLLGEIY--SGTSVAQVVVKELKASANPKEQDTFLKEGQPYRILQHPNILQCLGQCVE--AIPYLLVMEF 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  959 LPSGSLKEYLPKNKNKINLKQQL----KYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLtkAIETDKEY 1034
Cdd:cd05042     77 CDLGDLKAYLRSEREHERGDSDTrtlqRMACEVAAGLAHLHKLNFVHSDLALRNCLLTSDLTVKIGDYGL--AHSRYKED 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1035 YTVKDDRD-SPVFWYAPECL--MQSKFYIA-----SDVWSFGVTLHELLtycDSDSSPMalflkmigPTHGQMTVtrLVN 1106
Cdd:cd05042    155 YIETDDKLwFPLRWTAPELVteFHDRLLVVdqtkySNIWSLGVTLWELF---ENGAQPY--------SNLSDLDV--LAQ 221
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1013071061 1107 TLKEGK-RLPCPP---NCPDEVYQLMRKCWeFQPSNRTSFQNL 1145
Cdd:cd05042    222 VVREQDtKLPKPQlelPYSDRWYEVLQFCW-LSPEQRPAAEDV 263
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
876-1076 3.22e-27

Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK9 and CDK12 from higher eukaryotes, yeast BUR1, C-type plant CDKs (CdkC), and similar proteins. CDK9, BUR1, and CdkC are functionally equivalent. They act as a kinase for the C-terminal domain of RNA polymerase II and participate in regulating mutliple steps of gene expression including transcription elongation and RNA processing. CDK9 and CdkC associate with T-type cyclins while BUR1 associates with the cyclin BUR2. CDK12 is a unique CDK that contains an arginine/serine-rich (RS) domain, which is predominantly found in splicing factors. CDK12 interacts with cyclins L1 and L2, and participates in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270832 [Multi-domain]  Cd Length: 291  Bit Score: 113.04  E-value: 3.22e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  876 KRIRDLGEGHFGKVelcrYDPEGDNTGEQVAVKSLKPESG--GNHIADLKkEIEILRNLYHENIVKYKGICTEDG----G 949
Cdd:cd07840      2 EKIAQIGEGTYGQV----YKARNKKTGELVALKKIRMENEkeGFPITAIR-EIKLLQKLDHPNVVRLKEIVTSKGsakyK 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  950 NGIKLIMEFLP---SGslkeyLPKNKNKINLKQQLK-YAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLT 1025
Cdd:cd07840     77 GSIYMVFEYMDhdlTG-----LLDNPEVKFTESQIKcYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGLA 151
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1013071061 1026 KAIETDKEY-YTVKddrdspV--FWY-APECLMQSKFY-IASDVWSFGVTLHELLT 1076
Cdd:cd07840    152 RPYTKENNAdYTNR------VitLWYrPPELLLGATRYgPEVDMWSVGCILAELFT 201
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
878-1074 6.03e-27

Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Pek1/Skh1 from Schizosaccharomyces pombe and MKK2 from Saccharomyces cerevisiae, and related proteins. Both fission yeast Pek1 and baker's yeast MKK2 are components of the cell integrity MAPK pathway. In fission yeast, Pek1 phosphorylates and activates Pmk1/Spm1 and is regulated by the MAPKK kinase Mkh1. In baker's yeast, the pathway involves the MAPK Slt2, the MAPKKs MKK1 and MKK2, and the MAPKK kinase Bck1. The cell integrity MAPK cascade is activated by multiple stress conditions, and is essential in cell wall construction, morphogenesis, cytokinesis, and ion homeostasis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 112.13  E-value: 6.03e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVELCRYDpegdNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGNGIKLIME 957
Cdd:cd06621      6 LSSLGEGAGGSVTKCRLR----NTKTIFALKTITTDPNPDVQKQILRELEINKSCASPYIVKYYGAFLDEQDSSIGIAME 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  958 FLPSGSL----KEYLpKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLT-KAIETDK 1032
Cdd:cd06621     82 YCEGGSLdsiyKKVK-KKGGRIGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGVSgELVNSLA 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1013071061 1033 EYYTvkddrdSPVFWYAPECLMQSKFYIASDVWSFGVTLHEL 1074
Cdd:cd06621    161 GTFT------GTSYYMAPERIQGGPYSITSDVWSLGLTLLEV 196
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
874-1147 9.53e-27

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. PAK deregulation is associated with tumor development. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). Group II PAKs contain a PBD and a catalytic domain, but lack other motifs found in group I PAKs. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. Group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX; no such binding has been demonstrated for group II PAKs. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270789 [Multi-domain]  Cd Length: 255  Bit Score: 110.38  E-value: 9.53e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  874 FLKRIRDLGEGHFGKVELCRYDpegdNTGEQVAVKSLKPESggNHIADLKKEIEILRNLYHENIVKYKGiCTEDGGNgIK 953
Cdd:cd06614      1 LYKNLEKIGEGASGEVYKATDR----ATGKEVAIKKMRLRK--QNKELIINEILIMKECKHPNIVDYYD-SYLVGDE-LW 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  954 LIMEFLPSGSLKEYLPKNKNKINlKQQLKYAV-QICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFG----LTKAi 1028
Cdd:cd06614     73 VVMEYMDGGSLTDIITQNPVRMN-ESQIAYVCrEVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGfaaqLTKE- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1029 etdkeyytvKDDRDSPV---FWYAPECLMQSKFYIASDVWSFGVTLHELltyCDS-----DSSPM-ALFLkmigpthgqm 1099
Cdd:cd06614    151 ---------KSKRNSVVgtpYWMAPEVIKRKDYGPKVDIWSLGIMCIEM---AEGeppylEEPPLrALFL---------- 208
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1013071061 1100 TVTRLVNTLKEGKRLpcPPNCPDevyqLMRKCWEFQPSNRTSFQNLIE 1147
Cdd:cd06614    209 ITTKGIPPLKNPEKW--SPEFKD----FLNKCLVKDPEKRPSAEELLQ 250
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
881-1146 9.60e-27

Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDKL1-5 and similar proteins. Some CDKLs, like CDKL1 and CDKL3, may be implicated in transformation and others, like CDKL3 and CDKL5, are associated with mental retardation when impaired. CDKL2 plays a role in learning and memory. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270827 [Multi-domain]  Cd Length: 288  Bit Score: 111.64  E-value: 9.60e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDpegdNTGEQVAVKSLKPESGGNHIADLK-KEIEILRNLYHENIVKYKGICTEDGGngIKLIMEFL 959
Cdd:cd07833      9 VGEGAYGVVLKCRNK----ATGEIVAIKKFKESEDDEDVKKTAlREVKVLRQLRHENIVNLKEAFRRKGR--LYLVFEYV 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  960 PSgSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKE-YYTvk 1038
Cdd:cd07833     83 ER-TLLELLEASPGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFARALTARPAsPLT-- 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1039 ddrdSPVF--WY-APECLMQSKFY-IASDVWSFGVTLHELLT-----YCDSDSSPMALFLKMIGPTHGQMTVTRLVNTLK 1109
Cdd:cd07833    160 ----DYVAtrWYrAPELLVGDTNYgKPVDVWAIGCIMAELLDgeplfPGDSDIDQLYLIQKCLGPLPPSHQELFSSNPRF 235
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1013071061 1110 EGKRLPCPPN-----------CPDEVYQLMRKCWEFQPSNRTSFQNLI 1146
Cdd:cd07833    236 AGVAFPEPSQpeslerrypgkVSSPALDFLKACLRMDPKERLTCDELL 283
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
881-1152 1.01e-26

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK2 activation is induced by transforming growth factor-beta l (TGFb-l) and shares the same subcellular location as the cofilin family member twinfilin, which may be its biological substrate. LIMK2 plays a role in spermatogenesis, and may contribute to tumor progression and metastasis formation in some cancer cells. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 111.19  E-value: 1.01e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDPegdnTGEQVAVKSL---KPESGGNHIadlkKEIEILRNLYHENIVKYKGICTEDggNGIKLIME 957
Cdd:cd14222      1 LGKGFFGQAIKVTHKA----TGKVMVMKELircDEETQKTFL----TEVKVMRSLDHPNVLKFIGVLYKD--KRLNLLTE 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  958 FLPSGSLKEYLpKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAI--------- 1028
Cdd:cd14222     71 FIEGGTLKDFL-RADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveekkkppp 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1029 --ETDKEYYTVKDDRD-------SPvFWYAPECLMQSKFYIASDVWSFGVTLHELL--TYCDSDSSPMALFLKMigptHG 1097
Cdd:cd14222    150 dkPTTKKRTLRKNDRKkrytvvgNP-YWMAPEMLNGKSYDEKVDIFSFGIVLCEIIgqVYADPDCLPRTLDFGL----NV 224
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1013071061 1098 QMTVTRLVntlkegkrlpcPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEAL 1152
Cdd:cd14222    225 RLFWEKFV-----------PKDCPPAFFPLAAICCRLEPDSRPAFSKLEDSFEAL 268
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
878-1139 1.15e-26

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk1 (or simply Aatyk) is also called lemur tyrosine kinase 1 (Lmtk1). It is a cytoplasmic (or nonreceptor) kinase containing a long C-terminal region. The expression of Aatyk1 is upregulated during growth arrest and apoptosis in myeloid cells. Aatyk1 has been implicated in neural differentiation, and is a regulator of the Na-K-2Cl cotransporter, a membrane protein involved in cell proliferation and survival, epithelial transport, and blood pressure control. The Aatyk1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270670 [Multi-domain]  Cd Length: 271  Bit Score: 110.85  E-value: 1.15e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVELCRYDPEGDNTgeQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDggNGIKLIME 957
Cdd:cd05087      2 LKEIGHGWFGKVFLGEVNSGLSST--QVVVKELKASASVQDQMQFLEEAQPYRALQHTNLLQCLAQCAEV--TPYLLVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  958 FLPSGSLKEYLPKNKNKINLK------QQLkyAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETD 1031
Cdd:cd05087     78 FCPLGDLKGYLRSCRAAESMApdpltlQRM--ACEVACGLLHLHRNNFVHSDLALRNCLLTADLTVKIGDYGLSHCKYKE 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1032 kEYYTVKDDRDSPVFWYAPECL--MQSKFYIA-----SDVWSFGVTLHELLtycDSDSSPMalflkmigPTHGQMTVtrL 1104
Cdd:cd05087    156 -DYFVTADQLWVPLRWIAPELVdeVHGNLLVVdqtkqSNVWSLGVTIWELF---ELGNQPY--------RHYSDRQV--L 221
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1013071061 1105 VNTLKEGK-RLPCPP---NCPDEVYQLMRKCWeFQPSNR 1139
Cdd:cd05087    222 TYTVREQQlKLPKPQlklSLAERWYEVMQFCW-LQPEQR 259
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
881-1075 2.00e-26

Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MELK is a cell cycle dependent protein which functions in cytokinesis, cell cycle, apoptosis, cell proliferation, and mRNA processing. It is found upregulated in many types of cancer cells, playing an indispensable role in cancer cell survival. It makes an attractive target in the design of inhibitors for use in the treatment of a wide range of human cancer. The MELK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270980 [Multi-domain]  Cd Length: 257  Bit Score: 109.78  E-value: 2.00e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDPegdnTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVK-YKGICTEdggNGIKLIMEFL 959
Cdd:cd14078     11 IGSGGFAKVKLATHIL----TGEKVAIKIMDKKALGDDLPRVKTEIEALKNLSHQHICRlYHVIETD---NKIFMVLEYC 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  960 PSGSLKEYLPKnKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYtVKD 1039
Cdd:cd14078     84 PGGELFDYIVA-KDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLCAKPKGGMDHH-LET 161
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1013071061 1040 DRDSPVFwYAPEcLMQSKFYIAS--DVWSFGVTLHELL 1075
Cdd:cd14078    162 CCGSPAY-AAPE-LIQGKPYIGSeaDVWSMGVLLYALL 197
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
881-1146 4.65e-26

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. In the case of Jak2, the presumed pseudokinase (repeat 1) domain exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270633 [Multi-domain]  Cd Length: 259  Bit Score: 108.72  E-value: 4.65e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDPEGDNTGEQVAV--KSLKpeSGGNHIADLKKE-IEILRNLYHENIVKYKGICTEDGGngiKLIME 957
Cdd:cd05037      7 LGQGTFTNIYDGILREVGDGRVQEVEVllKVLD--SDHRDISESFFEtASLMSQISHKHLVKLYGVCVADEN---IMVQE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  958 FLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQ------VKIGDFGLTKAIETd 1031
Cdd:cd05037     82 YVRYGPLDKYLRRMGNNVPLSWKLQVAKQLASALHYLEDKKLIHGNVRGRNILLAREGLdgyppfIKLSDPGVPITVLS- 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1032 keyytvKDDRDSPVFWYAPECL--MQSKFYIASDVWSFGVTLHELLTYCDS-----DSSPMALFlkmigpthgqmtvtrl 1104
Cdd:cd05037    161 ------REERVDRIPWIAPECLrnLQANLTIAADKWSFGTTLWEICSGGEEplsalSSQEKLQF---------------- 218
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1013071061 1105 vntLKEGKRLPCpPNCPdEVYQLMRKCWEFQPSNRTSFQNLI 1146
Cdd:cd05037    219 ---YEDQHQLPA-PDCA-ELAELIMQCWTYEPTKRPSFRAIL 255
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
587-845 4.66e-26

Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; Fes subfamily; catalytic (c) domain. Fes subfamily members include Fes (or Fps), Fer, and similar proteins. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes subfamily proteins are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated tyr kinase activity. Fes and Fer kinases play roles in haematopoiesis, inflammation and immunity, growth factor signaling, cytoskeletal regulation, cell migration and adhesion, and the regulation of cell-cell interactions. Fes and Fer show redundancy in their biological functions.


Pssm-ID: 270637 [Multi-domain]  Cd Length: 251  Bit Score: 108.30  E-value: 4.66e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  587 EHLGRGTRTHIYSGTLmdykddEGTSEEKKIKVILKVLDPSHRDislAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMV 666
Cdd:cd05041      1 EKIGRGNFGDVYRGVL------KPDNTEVAVKTCRETLPPDLKR---KFLQEARILKQYDHPNIVKLIGVCVQKQPIMIV 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  667 EEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGipitv 746
Cdd:cd05041     72 MELVPGGSLLTFLRKKGARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNV-------LKISDFG----- 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  747 LSRQE---------CIERIP--WIAPECVEDSKnLSVAADKWSFGTTLWEICYNGEIPLKDKTLIEKERFYESRCR-PVT 814
Cdd:cd05041    140 MSREEedgeytvsdGLKQIPikWTAPEALNYGR-YTSESDVWSFGILLWEIFSLGATPYPGMSNQQTREQIESGYRmPAP 218
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1013071061  815 PSCKE-LADLMTRCMNYDPNQRPFFRAIMRDI 845
Cdd:cd05041    219 ELCPEaVYRLMLQCWAYDPENRPSFSEIYNEL 250
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
875-1089 5.95e-26

Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST3, MST4, STK25, Schizosaccharomyces pombe Nak1 and Sid1, Saccharomyces cerevisiae sporulation-specific protein 1 (SPS1), and related proteins. Nak1 is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Sid1 is a component in the septation initiation network (SIN) signaling pathway, and plays a role in cytokinesis. SPS1 plays a role in regulating proteins required for spore wall formation. MST4 plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. STK25 may play a role in the regulation of cell migration and polarization. The MST3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 108.87  E-value: 5.95e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  875 LKRIRDLGEGHFGKVELCRYDpegdNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEdggnGIKL 954
Cdd:cd06609      3 FTLLERIGKGSFGEVYKGIDK----RTNQVVAIKVIDLEEAEDEIEDIQQEIQFLSQCDSPYITKYYGSFLK----GSKL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 --IMEFLPSGSLKEYLpknknKINLKQQLKYAV---QICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIE 1029
Cdd:cd06609     75 wiIMEYCGGGSVLDLL-----KPGPLDETYIAFilrEVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSGQLT 149
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1030 --TDKeyytvkddRDSPV---FWYAPECLMQSKFYIASDVWSFGVTLHELLT----YCDSDssPM-ALFL 1089
Cdd:cd06609    150 stMSK--------RNTFVgtpFWMAPEVIKQSGYDEKADIWSLGITAIELAKgeppLSDLH--PMrVLFL 209
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
881-1074 6.21e-26

Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST1, MST2, and related proteins including Drosophila Hippo and Dictyostelium discoideum Krs1 (kinase responsive to stress 1). MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 activates the mitogen-activated protein kinases (MAPKs) p38 and c-Jun N-terminal kinase (JNK) through MKK7 and MEKK1 by acting as a MAPK kinase kinase kinase. Activation of JNK by MST1 leads to caspase activation and apoptosis. MST1 has also been implicated in cell proliferation and differentiation. Krs1 may regulate cell growth arrest and apoptosis in response to cellular stress. The MST1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 108.12  E-value: 6.21e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDPegdnTGEQVAVKSLKPESGgnhIADLKKEIEILRNLYHENIVKYKGICTEDggNGIKLIMEFLP 960
Cdd:cd06612     11 LGEGSYGSVYKAIHKE----TGQVVAIKVVPVEED---LQEIIKEISILKQCDSPYIVKYYGSYFKN--TDLWIVMEYCG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  961 SGSLKEYLpkNKNKINLKQQLKYAV--QICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGL-TKAIETDKEYYTV 1037
Cdd:cd06612     82 AGSVSDIM--KITNKTLTEEEIAAIlyQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVsGQLTDTMAKRNTV 159
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1013071061 1038 KddrDSPvFWYAPECLMQSKFYIASDVWSFGVTLHEL 1074
Cdd:cd06612    160 I---GTP-FWMAPEVIQEIGYNNKADIWSLGITAIEM 192
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
578-845 7.15e-26

Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Tec-like subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases form the second largest subfamily of nonreceptor PTKs and are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. Tec kinases play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. Mutations in Btk cause the severe B-cell immunodeficiency, X-linked agammaglobulinaemia (XLA). The Tec-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 107.92  E-value: 7.15e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  578 ILKKDLVQGEHLGRGTRTHIYSGTLMDykddegtseekKIKVILKVLdpshRDISLA---FFEAASMMRQVSHKHIVYLY 654
Cdd:cd05059      1 IDPSELTFLKELGSGQFGVVHLGKWRG-----------KIDVAIKMI----KEGSMSeddFIEEAKVMMKLSHPKLVQLY 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  655 GVCVRDVENIMVEEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpf 734
Cdd:cd05059     66 GVCTKQRPIFIVTEYMANGCLLNYLRERRGKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNV------- 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  735 IKLSDPGIPITVLSRQECIER-----IPWIAPECVEDSKnLSVAADKWSFGTTLWEICYNGEIPLKDKT-------LIEK 802
Cdd:cd05059    139 VKVSDFGLARYVLDDEYTSSVgtkfpVKWSPPEVFMYSK-FSSKSDVWSFGVLMWEVFSEGKMPYERFSnsevvehISQG 217
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1013071061  803 ERFYESRCRPvtpscKELADLMTRCMNYDPNQRPFFRAIMRDI 845
Cdd:cd05059    218 YRLYRPHLAP-----TEVYTIMYSCWHEKPEERPTFKILLSQL 255
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
873-1076 8.66e-26

Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNKs comprise a subfamily of STKs with an unusual placement of a catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. They are also involved in cell signaling, survival, proliferation, and organ development. WNKs are activated by hyperosmotic or low-chloride hypotonic stress and they function upstream of SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. There are four vertebrate WNKs which show varying expression patterns. WNK1 and WNK2 are widely expressed while WNK3 and WNK4 show a more restricted expression pattern. Because mutations in human WNK1 and WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension (due to increased sodium reabsorption) and hyperkalemia (due to impaired renal potassium secretion), there are more studies conducted on these two proteins, compared to WNK2 and WNK3. The WNK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 107.70  E-value: 8.66e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  873 RFLKRIRDLGEGHFGKVELCrYDPEgdnTGEQVA---VKSLKPESggNHIADLKKEIEILRNLYHENIVKYKGICTEDGG 949
Cdd:cd13983      1 RYLKFNEVLGRGSFKTVYRA-FDTE---EGIEVAwneIKLRKLPK--AERQRFKQEIEILKSLKHPNIIKFYDSWESKSK 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  950 NGIKLIMEFLPSGSLKEYLPKNKNkINLKQQLKYAVQICKGMDYLGSRQY--VHRDLAARNVLVESEH-QVKIGDFGLTK 1026
Cdd:cd13983     75 KEVIFITELMTSGTLKQYLKRFKR-LKLKVIKSWCRQILEGLNYLHTRDPpiIHRDLKCDNIFINGNTgEVKIGDLGLAT 153
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1027 AIETDKEYYTVkddrDSPVFwYAPEcLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd13983    154 LLRQSFAKSVI----GTPEF-MAPE-MYEEHYDEKVDIYAFGMCLLEMAT 197
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
881-1090 1.67e-25

Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. In response to decreased ATP levels, it enhances energy-producing processes and inhibits energy-consuming pathways. Once activated, AMPK phosphorylates a broad range of downstream targets, with effects in carbohydrate metabolism and uptake, lipid and fatty acid biosynthesis, carbon energy storage, and inflammation, among others. Defects in energy homeostasis underlie many human diseases including Type 2 diabetes, obesity, heart disease, and cancer. As a result, AMPK has emerged as a therapeutic target in the treatment of these diseases. The AMPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270981 [Multi-domain]  Cd Length: 256  Bit Score: 106.97  E-value: 1.67e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDPegdnTGEQVAVKSL------KPESGGNhiadLKKEIEILRNLYHENIVK-YKGICTEDGgngIK 953
Cdd:cd14079     10 LGVGSFGKVKLAEHEL----TGHKVAVKILnrqkikSLDMEEK----IRREIQILKLFRHPHIIRlYEVIETPTD---IF 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  954 LIMEFLPSGSLKEYLPKnKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKaIETDKE 1033
Cdd:cd14079     79 MVMEYVSGGELFDYIVQ-KGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLSN-IMRDGE 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1013071061 1034 YytVKDDRDSPVFwYAPEcLMQSKFYIAS--DVWSFGVTLHELLtyC-----DSDSSPMaLFLK 1090
Cdd:cd14079    157 F--LKTSCGSPNY-AAPE-VISGKLYAGPevDVWSCGVILYALL--CgslpfDDEHIPN-LFKK 213
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
881-1143 1.86e-25

Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes yeast ATG1 and metazoan homologs including vertebrate ULK1-3. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. It is involved in nutrient sensing and signaling, the assembly of autophagy factors and the execution of autophagy. In metazoans, ATG1 homologs display additional functions. Unc-51 and ULKs have been implicated in neuronal and axonal development. The ATG1/ULK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270911 [Multi-domain]  Cd Length: 251  Bit Score: 106.54  E-value: 1.86e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDpegdNTGEQVAVKSLKPES-GGNHIADLKKEIEILRNLYHENIVKYKGIctEDGGNGIKLIMEFL 959
Cdd:cd14009      1 IGRGSFATVWKGRHK----QTGEVVAIKEISRKKlNKKLQENLESEIAILKSIKHPNIVRLYDV--QKTEDFIYLVLEYC 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  960 PSGSLKEYLPKNKnKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVES---EHQVKIGDFGLTKAIETDKEYYT 1036
Cdd:cd14009     75 AGGDLSQYIRKRG-RLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTsgdDPVLKIADFGFARSLQPASMAET 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1037 VkddRDSPvFWYAPECLMQSKFYIASDVWSFGVTLHELLTycdsdsspmalflkmiG--PTHGQMTVTRLVNTLKEGKRL 1114
Cdd:cd14009    154 L---CGSP-LYMAPEILQFQKYDAKADLWSVGAILFEMLV----------------GkpPFRGSNHVQLLRNIERSDAVI 213
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1013071061 1115 PCP------PNCPDEVYQLMRKcwefQPSNRTSFQ 1143
Cdd:cd14009    214 PFPiaaqlsPDCKDLLRRLLRR----DPAERISFE 244
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
875-1139 2.36e-25

The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GSK3 is a mutifunctional kinase involved in many cellular processes including cell division, proliferation, differentiation, adhesion, and apoptosis. In plants, GSK3 plays a role in the response to osmotic stress. In Caenorhabditis elegans, it plays a role in regulating normal oocyte-to-embryo transition and response to oxidative stress. In Chlamydomonas reinhardtii, GSK3 regulates flagellar length and assembly. In mammals, there are two isoforms, GSK3alpha and GSK3beta, which show both distinct and redundant functions. The two isoforms differ mainly in their N-termini. They are both involved in axon formation and in Wnt signaling.They play distinct roles in cardiogenesis, with GSKalpha being essential in cardiomyocyte survival, and GSKbeta regulating heart positioning and left-right symmetry. GSK3beta was first identified as a regulator of glycogen synthesis, but has since been determined to play other roles. It regulates the degradation of beta-catenin and IkB. Beta-catenin is the main effector of Wnt, which is involved in normal haematopoiesis and stem cell function. IkB is a central inhibitor of NF-kB, which is critical in maintaining leukemic cell growth. GSK3beta is enriched in the brain and is involved in regulating neuronal signaling pathways. It is implicated in the pathogenesis of many diseases including Type II diabetes, obesity, mood disorders, Alzheimer's disease, osteoporosis, and some types of cancer, among others. The GSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271039 [Multi-domain]  Cd Length: 293  Bit Score: 107.59  E-value: 2.36e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  875 LKRIRDLGEGHFGKVELCRYDpegdNTGEQVAVKSLKPESGGNHiadlkKEIEILRNLYHENIVKYKGICTEDGGNGIK- 953
Cdd:cd14137      6 YTIEKVIGSGSFGVVYQAKLL----ETGEVVAIKKVLQDKRYKN-----RELQIMRRLKHPNIVKLKYFFYSSGEKKDEv 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  954 ---LIMEFLPSgSLKEYLpknKNKINLKQQL-----K-YAVQICKGMDYLGSRQYVHRDLAARNVLVESE-HQVKIGDFG 1023
Cdd:cd14137     77 ylnLVMEYMPE-TLYRVI---RHYSKNKQTIpiiyvKlYSYQLFRGLAYLHSLGICHRDIKPQNLLVDPEtGVLKLCDFG 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1024 LTKAIETDKE--------YYtvkddRdspvfwyAPECLMQSKFYIAS-DVWSFGVTLHELLT----YC-DSDSSPMALFL 1089
Cdd:cd14137    153 SAKRLVPGEPnvsyicsrYY-----R-------APELIFGATDYTTAiDIWSAGCVLAELLLgqplFPgESSVDQLVEII 220
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1013071061 1090 KMIG-PTHGQ---MTVTRLVNTLKEGKRLP----CPPNCPDEVYQLMRKCWEFQPSNR 1139
Cdd:cd14137    221 KVLGtPTREQikaMNPNYTEFKFPQIKPHPwekvFPKRTPPDAIDLLSKILVYNPSKR 278
FERM_C_JAK2 cd13333
FERM domain C-lobe of Janus kinase (JAK) 2; JAK2 has been implicated in signaling by members ...
315-426 2.91e-25

FERM domain C-lobe of Janus kinase (JAK) 2; JAK2 has been implicated in signaling by members of the type II cytokine receptor family, the GM-CSF receptor family, the gp130 receptor family, and the single chain receptors. JAK2 orthologs have been identified in all mammals. Mutations in JAK2 have been implicated in polycythemia vera, essential thrombocythemia, myelofibrosis as well as other myeloproliferative disorders. JAK2 gene fusions with the PCM1 and TEL(ETV6) (TEL-JAK2) genes have been found in leukemia patients. Researcher are targetting JAK2 inhibitors in the treatment of patients with prostate cancer. JAK2 has been shown to interact with a variety of proteins including growth hormone receptor, STAT5A, STAT5B, interleukin 5 receptor alpha subunit, interleukin 12 receptor, SOCS3, PTPN6,PTPN11, Grb2, VAV1, and YES1. JAK (also called Just Another Kinase) is a family of intracellular, non-receptor tyrosine kinases that transduce cytokine-mediated signals via the JAK-STAT pathway. The JAK family in mammals consists of 4 members: JAK1, JAK2, JAK3 and TYK2. JAKs are composed of seven JAK homology (JH) domains (JH1-JH7) . The C-terminal JH1 domain is the main catalytic domain, followed by JH2, which is often referred to as a pseudokinase domain, followed by JH3-JH4 which is homologous to the SH2 domain, and lastly JH5-JH7 which is a FERM domain. Named after Janus, the two-faced Roman god of doorways, JAKs possess two near-identical phosphate-transferring domains; one which displays the kinase activity (JH1), while the other negatively regulates the kinase activity of the first (JH2). The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270141  Cd Length: 113  Bit Score: 101.42  E-value: 2.91e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  315 VMVTGNLGIQWRHKpnvvsvekeknklkrkklenKHKKDEEKnkirEEWNNFSYFPEITHIVIKES---------VVSIN 385
Cdd:cd13333     17 IVVTGNGGIQWSRG--------------------KHKETEAE----QDLQTYCDFPEVIDISIKQAnkegssesrVVTIN 72
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1013071061  386 KQDNKKMELKLSSHEEALSFVSLVDGYFRLTADAHHYLCTD 426
Cdd:cd13333     73 KQDGKNLELEFSSLSEALSFVSLIDGYYRLTTDAHHYLCKE 113
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
881-1086 3.04e-25

Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. YSK4 is a putative MAPKKK, whose mammalian gene has been isolated. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The YSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 106.37  E-value: 3.04e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVeLCRYDpegdNTGEQVAVKSLKPESGGNHIAD-----LKKEIEILRNLYHENIVKYKGICTEDggNGIKLI 955
Cdd:cd06631      9 LGKGAYGTV-YCGLT----STGQLIAVKQVELDTSDKEKAEkeyekLQEEVDLLKTLKHVNIVGYLGTCLED--NVVSIF 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  956 MEFLPSGSLKEYLpknkNKINLKQQL---KYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDK 1032
Cdd:cd06631     82 MEFVPGGSIASIL----ARFGALEEPvfcRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGCAKRLCINL 157
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1033 EYYT----VKDDRDSPvFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCD--SDSSPMA 1086
Cdd:cd06631    158 SSGSqsqlLKSMRGTP-YWMAPEVINETGHGRKSDIWSIGCTVFEMATGKPpwADMNPMA 216
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
586-844 3.84e-25

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 105.69  E-value: 3.84e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061   586 GEHLGRGTRTHIYSGTlmdykdDEGTSEekkiKVILKVLDPSHRDISLAFFEA-ASMMRQVSHKHIVYLYGVCVRDVENI 664
Cdd:smart00220    4 LEKLGEGSFGKVYLAR------DKKTGK----LVAIKVIKKKKIKKDRERILReIKILKKLKHPNIVRLYDVFEDEDKLY 73
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061   665 MVEEFVEGGPLDLFMHRKsDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVctK--NLLLAREGIdsecgpfIKLSDPGi 742
Cdd:smart00220   74 LVMEYCEGGDLFDLLKKR-GRLSEDEARFYLRQILSALEYLHSKGIVHRDL--KpeNILLDEDGH-------VKLADFG- 142
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061   743 pitvLSRQECIER--------IPWIAPECVeDSKNLSVAADKWSFGTTLWEICYnGEIPLKD--------KTLIEKERFY 806
Cdd:smart00220  143 ----LARQLDPGEklttfvgtPEYMAPEVL-LGKGYGKAVDIWSLGVILYELLT-GKPPFPGddqllelfKKIGKPKPPF 216
                           250       260       270
                    ....*....|....*....|....*....|....*...
gi 1013071061   807 ESRCRPVTPSCKelaDLMTRCMNYDPNQRPFFRAIMRD 844
Cdd:smart00220  217 PPPEWDISPEAK---DLIRKLLVKDPEKRLTAEEALQH 251
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
589-846 4.66e-25

Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily contains c-ros, Sevenless, and similar proteins. The proto-oncogene c-ros encodes an orphan receptor PTK (RTK) with an unknown ligand. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. C-ros is expressed in embryonic cells of the kidney, intestine and lung, but disappears soon after birth. It persists only in the adult epididymis. Male mice bearing inactive mutations of c-ros lack the initial segment of the epididymis and are infertile. The Drosophila protein, Sevenless, is required for the specification of the R7 photoreceptor cell during eye development. The c-ros subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 105.96  E-value: 4.66e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  589 LGRGTRTHIYSGTLMDYkDDEGTSEekkIKVILKVLDPSHRDISLA-FFEAASMMRQVSHKHIVYLYGVCVRDVENIMVE 667
Cdd:cd05044      3 LGSGAFGEVFEGTAKDI-LGDGSGE---TKVAVKTLRKGATDQEKAeFLKEAHLMSNFKHPNILKLLGVCLDNDPQYIIL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  668 EFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASAL------SYLEDKDLVHGNVCTKNLLLAREGIDSECgpfIKLSDPG 741
Cdd:cd05044     79 ELMEGGDLLSYLRAARPTAFTPPLLTLKDLLSICVdvakgcVYLEDMHFVHRDLAARNCLVSSKDYRERV---VKIGDFG 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  742 IPITVLS----RQECIERIP--WIAPECVEDSKnLSVAADKWSFGTTLWEICYNGEIPLKDKTLIEKERFYESRCRPVTP 815
Cdd:cd05044    156 LARDIYKndyyRKEGEGLLPvrWMAPESLVDGV-FTTQSDVWAFGVLMWEILTLGQQPYPARNNLEVLHFVRAGGRLDQP 234
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1013071061  816 -SC-KELADLMTRCMNYDPNQRPFFRAIMRDIN 846
Cdd:cd05044    235 dNCpDDLYELMLRCWSTDPEERPSFARILEQLQ 267
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
881-1152 6.06e-25

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. Vertebrate have two members, LIMK1 and LIMK2. The LIMK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 105.67  E-value: 6.06e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDpegdNTGEQVAVKSL---KPESGGNHIadlkKEIEILRNLYHENIVKYKGICTEDggNGIKLIME 957
Cdd:cd14154      1 LGKGFFGQAIKVTHR----ETGEVMVMKELirfDEEAQRNFL----KEVKVMRSLDHPNVLKFIGVLYKD--KKLNLITE 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  958 FLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKE---- 1033
Cdd:cd14154     71 YIPGGTLKDVLKDMARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLARLIVEERLpsgn 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1034 -------YYTVKDDRD-------SPvFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSDSSPMalflkmigPTHGQM 1099
Cdd:cd14154    151 mspsetlRHLKSPDRKkrytvvgNP-YWMAPEMLNGRSYDEKVDIFSFGIVLCEIIGRVEADPDYL--------PRTKDF 221
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1013071061 1100 TVTrlvntlKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEAL 1152
Cdd:cd14154    222 GLN------VDSFREKFCAGCPPPFFKLAFLCCDLDPEKRPPFETLEEWLEAL 268
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
881-1139 8.42e-25

Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Saccharomyces cerevisiae Bck1 and Schizosaccharomyces pombe Mkh1, and related proteins. Budding yeast Bck1 is part of the cell integrity MAPK pathway, which is activated by stresses and aggressions to the cell wall. The MAPKKK Bck1, MAPKKs Mkk1 and Mkk2, and the MAPK Slt2 make up the cascade that is important in the maintenance of cell wall homeostasis. Fission yeast Mkh1 is involved in MAPK cascades regulating cell morphology, cell wall integrity, salt resistance, and filamentous growth in response to stress. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The Bck1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270799 [Multi-domain]  Cd Length: 270  Bit Score: 105.16  E-value: 8.42e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRydpeGDNTGEQVAVK--SLKPESGGNH-------IADLKKEIEILRNLYHENIVKYKGIctEDGGNG 951
Cdd:cd06629      9 IGKGTYGRVYLAM----NATTGEMLAVKqvELPKTSSDRAdsrqktvVDALKSEIDTLKDLDHPNIVQYLGF--EETEDY 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  952 IKLIMEFLPSGSLKEYLPKNKNkinLKQQL--KYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAie 1029
Cdd:cd06629     83 FSIFLEYVPGGSIGSCLRKYGK---FEEDLvrFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGISKK-- 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1030 TDKEYYTVKD-DRDSPVFWYAPECLM-QSKFYIAS-DVWSFGVTLHELLTyCDSDSSPMALFLKMigpthgqmtvtrlvn 1106
Cdd:cd06629    158 SDDIYGNNGAtSMQGSVFWMAPEVIHsQGQGYSAKvDIWSLGCVVLEMLA-GRRPWSDDEAIAAM--------------- 221
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1013071061 1107 tLKEGKRLPCPPNCPD-----EVYQLMRKCWEFQPSNR 1139
Cdd:cd06629    222 -FKLGNKRSAPPVPEDvnlspEALDFLNACFAIDPRDR 258
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
578-841 1.01e-24

Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The InsR subfamily is composed of InsR, Insulin-like Growth Factor-1 Receptor (IGF-1R), and similar proteins. InsR and IGF-1R are receptor PTKs (RTKs) composed of two alphabeta heterodimers. Binding of the ligand (insulin, IGF-1, or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR and IGF-1R, which share 84% sequence identity in their kinase domains, display physiologically distinct yet overlapping functions in cell growth, differentiation, and metabolism. InsR activation leads primarily to metabolic effects while IGF-1R activation stimulates mitogenic pathways. In cells expressing both receptors, InsR/IGF-1R hybrids are found together with classical receptors. Both receptors can interact with common adaptor molecules such as IRS-1 and IRS-2. The InsR-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 105.12  E-value: 1.01e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  578 ILKKDLVQGEHLGRGTRTHIYSGTLMDYKDDEGtseekKIKVILKVL--DPSHRDIsLAFFEAASMMRQVSHKHIVYLYG 655
Cdd:cd05032      3 LPREKITLIRELGQGSFGMVYEGLAKGVVKGEP-----ETRVAIKTVneNASMRER-IEFLNEASVMKEFNCHHVVRLLG 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  656 VCVRDVENIMVEEFVEGGPLD--LFMHR-------KSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREG 726
Cdd:cd05032     77 VVSTGQPTLVVMELMAKGDLKsyLRSRRpeaennpGLGPPTLQKFIQMAAEIADGMAYLAAKKFVHRDLAARNCMVAEDL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  727 IdsecgpfIKLSDPG----IPITVLSRQECIERIP--WIAPECVEDSKnLSVAADKWSFGTTLWEICYNGEIPLKDKTLI 800
Cdd:cd05032    157 T-------VKIGDFGmtrdIYETDYYRKGGKGLLPvrWMAPESLKDGV-FTTKSDVWSFGVVLWEMATLAEQPYQGLSNE 228
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1013071061  801 EKERFYESRCRPVTPSC--KELADLMTRCMNYDPNQRPFFRAI 841
Cdd:cd05032    229 EVLKFVIDGGHLDLPENcpDKLLELMRMCWQYNPKMRPTFLEI 271
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
879-1141 1.29e-24

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK3 is represented in this cd. The SnRK3 group contains members also known as CBL-interacting protein kinase, salt overly sensitive 2, SOS3-interacting proteins and protein kinase S. These kinases interact with calcium-binding proteins such as SOS3, SCaBPs, and CBL proteins, and are involved in responses to salt stress and in sugar and ABA signaling. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271133 [Multi-domain]  Cd Length: 256  Bit Score: 104.41  E-value: 1.29e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGHFGKVELCRYDpegdNTGEQVAVKSLKPESGGNH--IADLKKEIEILRNLYHENIVKYKGICTEDggNGIKLIM 956
Cdd:cd14663      6 RTLGEGTFAKVKFARNT----KTGESVAIKIIDKEQVAREgmVEQIKREIAIMKLLRHPNIVELHEVMATK--TKIFFVM 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  957 EFLPSGSLKEYLPKNKnKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGL---TKAIETDKE 1033
Cdd:cd14663     80 ELVTGGELFSKIAKNG-RLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLsalSEQFRQDGL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1034 YYTVKddrDSPVFwYAPECLMQsKFYI--ASDVWSFGVTLHELLTYC--DSDSSPMALFLKMigpthgqmtvtrlvntlk 1109
Cdd:cd14663    159 LHTTC---GTPNY-VAPEVLAR-RGYDgaKADIWSCGVILFVLLAGYlpFDDENLMALYRKI------------------ 215
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1013071061 1110 EGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTS 1141
Cdd:cd14663    216 MKGEFEYPRWFSPGAKSLIKRILDPNPSTRIT 247
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
875-1145 3.22e-24

Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Byr1 from Schizosaccharomyces pombe, FUZ7 from Ustilago maydis, and related proteins. Byr1 phosphorylates its downstream target, the MAPK Spk1, and is regulated by the MAPKK kinase Byr2. The Spk1 cascade is pheromone-responsive and is essential for sporulation and sexual differentiation in fission yeast. FUZ7 phosphorylates and activates its target, the MAPK Crk1, which is required in mating and virulence in U. maydis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The Byr-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 104.06  E-value: 3.22e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  875 LKRIRDLGEGHFGKVELCRYDPegdnTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGNgIKL 954
Cdd:cd06620      7 LETLKDLGAGNGGSVSKVLHIP----TGTIMAKKVIHIDAKSSVRKQILRELQILHECHSPYIVSFYGAFLNENNN-III 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPSGSLKEYLPKNKnKINLKQQLKYAVQICKGMDYLgSRQY--VHRDLAARNVLVESEHQVKIGDFGLTKAIETdk 1032
Cdd:cd06620     82 CMEYMDCGSLDKILKKKG-PFPEEVLGKIAVAVLEGLTYL-YNVHriIHRDIKPSNILVNSKGQIKLCDFGVSGELIN-- 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1033 eyyTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLT----------YCDSDSSPMALFlkmigpthgqMTVT 1102
Cdd:cd06620    158 ---SIADTFVGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALgefpfagsndDDDGYNGPMGIL----------DLLQ 224
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1013071061 1103 RLVNtlKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNL 1145
Cdd:cd06620    225 RIVN--EPPPRLPKDRIFPKDLRDFVDRCLLKDPRERPSPQLL 265
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
875-1093 3.47e-24

Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the cAMP-dependent protein kinases, PKA and PRKX, and similar proteins. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. PRKX is also reulated by the R subunit and is is present in many tissues including fetal and adult brain, kidney, and lung. It is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PKA-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270732 [Multi-domain]  Cd Length: 290  Bit Score: 104.20  E-value: 3.47e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  875 LKRIRDLGEGHFGKVELCRYDpegdNTGEQVAVKSLKPESggnhIADLKK------EIEILRNLYHENIVKYKGICTEDg 948
Cdd:cd05580      3 FEFLKTLGTGSFGRVRLVKHK----DSGKYYALKILKKAK----IIKLKQvehvlnEKRILSEVRHPFIVNLLGSFQDD- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  949 gNGIKLIMEFLPSGSLKEYLPKNkNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAI 1028
Cdd:cd05580     74 -RNLYMVMEYVPGGELFSLLRRS-GRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAKRV 151
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1013071061 1029 EtdKEYYTVKDDRDspvfWYAPEcLMQSKFY-IASDVWSFGVTLHELLTYCDS--DSSPMALFLKMIG 1093
Cdd:cd05580    152 K--DRTYTLCGTPE----YLAPE-IILSKGHgKAVDWWALGILIYEMLAGYPPffDENPMKIYEKILE 212
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
881-1154 4.22e-24

Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TESK proteins phosphorylate cofilin and induce actin cytoskeletal reorganization. In the Drosphila eye, TESK is required for epithelial cell organization. Mammals contain two TESK proteins, TESK1 and TESK2, which are highly expressed in testis and play roles in spermatogenesis. TESK1 is found in testicular germ cells while TESK2 is expressed mainly in nongerminal Sertoli cells. TESK1 is stimulated by integrin-mediated signaling pathways. It regulates cell spreading and focal adhesion formation. The TESK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 102.94  E-value: 4.22e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDPEGdntgeQVAVksLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGngIKLIMEFLP 960
Cdd:cd14155      1 IGSGFFSEVYKVRHRTSG-----QVMA--LKMNTLSSNRANMLREVQLMNRLSHPNILRFMGVCVHQGQ--LHALTEYIN 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  961 SGSLKEYLPKNKNkINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESE---HQVKIGDFGLTKAIetdkeyyTV 1037
Cdd:cd14155     72 GGNLEQLLDSNEP-LSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIKRDengYTAVVGDFGLAEKI-------PD 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1038 KDDRDSPV------FWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSDSS--PMALFLKMIGPTHGQMTvtrlvntlk 1109
Cdd:cd14155    144 YSDGKEKLavvgspYWMAPEVLRGEPYNEKADVFSYGIILCEIIARIQADPDylPRTEDFGLDYDAFQHMV--------- 214
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1013071061 1110 egkrlpcpPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALLK 1154
Cdd:cd14155    215 --------GDCPPDFLQLAFNCCNMDPKSRPSFHDIVKTLEEILE 251
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
881-1152 5.28e-24

Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 and CDK6 partner with D-type cyclins to regulate the early G1 phase of the cell cycle. They are the first kinases activated by mitogenic signals to release cells from the G0 arrested state. CDK4 and CDK6 are both expressed ubiquitously, associate with all three D cyclins (D1, D2 and D3), and phosphorylate the retinoblastoma (pRb) protein. They are also regulated by the INK4 family of inhibitors which associate with either the CDK alone or the CDK/cyclin complex. CDK4 and CDK6 show differences in subcellular localization, sensitivity to some inhibitors, timing in activation, tumor selectivity, and possibly substrate profiles. Although CDK4 and CDK6 seem to show some redundancy, they also have discrete, nonoverlapping functions. CDK6 plays an important role in cell differentiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4/6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270831 [Multi-domain]  Cd Length: 287  Bit Score: 103.51  E-value: 5.28e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVelcrYDPEGDNTGEQVAVKSLK-PES-GGNHIADLKkEIEILRNLY---HENIVKYKGIC-TEDGGNGIK- 953
Cdd:cd07838      7 IGEGAYGTV----YKARDLQDGRFVALKKVRvPLSeEGIPLSTIR-EIALLKQLEsfeHPNVVRLLDVChGPRTDRELKl 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  954 -LIMEFL------------PSGslkeyLPKNKNKiNLKQQLkyavqiCKGMDYLGSRQYVHRDLAARNVLVESEHQVKIG 1020
Cdd:cd07838     82 tLVFEHVdqdlatyldkcpKPG-----LPPETIK-DLMRQL------LRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLA 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1021 DFGLTKAietdkeyYTVKDDRDSPV--FWY-APECLMQSKFYIASDVWSFGVTLHEL-----LTYCDSDSSPMALFLKMI 1092
Cdd:cd07838    150 DFGLARI-------YSFEMALTSVVvtLWYrAPEVLLQSSYATPVDMWSVGCIFAELfnrrpLFRGSSEADQLGKIFDVI 222
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1013071061 1093 G-PTHGQMTVTRLVN------TLKEGKRLPCPPNCPDEVyQLMRKCWEFQPSNRtsfqnlIEGFEAL 1152
Cdd:cd07838    223 GlPSEEEWPRNSALPrssfpsYTPRPFKSFVPEIDEEGL-DLLKKMLTFNPHKR------ISAFEAL 282
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
881-1148 5.44e-24

Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily are mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs) and include ASK1, ASK2, and MAPKKK15. ASK1 (also called MAPKKK5) functions in the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. It plays important roles in cytokine and stress responses, as well as in reactive oxygen species-mediated cellular responses. ASK1 is implicated in various diseases mediated by oxidative stress including inschemic heart disease, hypertension, vessel injury, brain ischemia, Fanconi anemia, asthma, and pulmonary edema, among others. ASK2 (also called MAPKKK6) functions only in a heteromeric complex with ASK1, and can activate ASK1 by direct phosphorylation. The function of MAPKKK15 is still unknown. The ASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270794 [Multi-domain]  Cd Length: 268  Bit Score: 102.87  E-value: 5.44e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVelcrYDPEGDNTGEQVAVKSLkPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGngIKLIMEFLP 960
Cdd:cd06624     16 LGKGTFGVV----YAARDLSTQVRIAIKEI-PERDSREVQPLHEEIALHSRLSHKNIVQYLGSVSEDGF--FKIFMEQVP 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  961 SGSLKEY-------LPKNKNKINLkqqlkYAVQICKGMDYLGSRQYVHRDLAARNVLVES-EHQVKIGDFGLTK---AIE 1029
Cdd:cd06624     89 GGSLSALlrskwgpLKDNENTIGY-----YTKQILEGLKYLHDNKIVHRDIKGDNVLVNTySGVVKISDFGTSKrlaGIN 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1030 TDKEYYTvkddrdsPVFWY-APECLMQSK--FYIASDVWSFGVTLHELLTycdsdSSPMALFLkmiGPTHGQMtvtrlvn 1106
Cdd:cd06624    164 PCTETFT-------GTLQYmAPEVIDKGQrgYGPPADIWSLGCTIIEMAT-----GKPPFIEL---GEPQAAM------- 221
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1013071061 1107 tLKEG--KRLP-CPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEG 1148
Cdd:cd06624    222 -FKVGmfKIHPeIPESLSEEAKSFILRCFEPDPDKRATASDLLQD 265
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
876-1076 6.31e-24

Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. PLKs derive their names from homology to polo, a kinase first identified in Drosophila. There are five mammalian PLKs (PLK1-5) from distinct genes. There is good evidence that PLK1 may function as an oncogene while PLK2-5 have tumor suppressive properties. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. PLK2 functions in G1 progression, S-phase arrest, and centriole duplication. PLK3 regulates angiogenesis and responses to DNA damage. PLK4 is required for late mitotic progression, cell survival, and embryonic development. PLK5 was first identified as a pseudogene containing a stop codon within the kinase domain, however, both murine and human genes encode expressed proteins. PLK5 functions in cell cycle arrest.


Pssm-ID: 271001 [Multi-domain]  Cd Length: 258  Bit Score: 102.25  E-value: 6.31e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  876 KRIRDLGEGHFGKVelcrYDPEGDNTGEQVAVKSLKPESGGNHIA--DLKKEIEILRNLYHENIVKYKGiCTEDGGNgIK 953
Cdd:cd14099      4 RRGKFLGKGGFAKC----YEVTDMSTGKVYAGKVVPKSSLTKPKQreKLKSEIKIHRSLKHPNIVKFHD-CFEDEEN-VY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  954 LIMEFLPSGSLKEYLPKNKnKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKE 1033
Cdd:cd14099     78 ILLELCSNGSLMELLKRRK-ALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAARLEYDGE 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1013071061 1034 -YYTVKddrDSPVFwYAPECLMQSKFY-IASDVWSFGVTLHELLT 1076
Cdd:cd14099    157 rKKTLC---GTPNY-IAPEVLEKKKGHsFEVDIWSLGVILYTLLV 197
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
617-850 6.57e-24

Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Frk and Srk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Frk, also known as Rak, is specifically expressed in liver, lung, kidney, intestine, mammary glands, and the islets of Langerhans. Rodent homologs were previously referred to as GTK (gastrointestinal tyr kinase), BSK (beta-cell Src-like kinase), or IYK (intestinal tyr kinase). Studies in mice reveal that Frk is not essential for viability. It plays a role in the signaling that leads to cytokine-induced beta-cell death in Type I diabetes. It also regulates beta-cell number during embryogenesis and early in life. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Frk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 102.48  E-value: 6.57e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  617 IKVILKVLDPSHRDISlAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSDVLTTPWKFKVAK 696
Cdd:cd05068     33 TPVAVKTLKPGTMDPE-DFLREAQIMKKLRHPKLIQLYAVCTLEEPIYIITELMKHGSLLEYLQGKGRSLQLPQLIDMAA 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  697 QLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGIPiTVLSRQECIER-------IPWIAPECVEDSKn 769
Cdd:cd05068    112 QVASGMAYLESQNYIHRDLAARNVLVGENNI-------CKVADFGLA-RVIKVEDEYEAregakfpIKWTAPEAANYNR- 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  770 LSVAADKWSFGTTLWEICYNGEIP---LKDKTLIEK-ERFYESRCRPVTPscKELADLMTRCMNYDPNQRPFFRAIMRdi 845
Cdd:cd05068    183 FSIKSDVWSFGILLTEIVTYGRIPypgMTNAEVLQQvERGYRMPCPPNCP--PQLYDIMLECWKADPMERPTFETLQW-- 258

                   ....*
gi 1013071061  846 nKLEE 850
Cdd:cd05068    259 -KLED 262
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
924-1153 6.79e-24

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK1 activation is induced by bone morphogenic protein, vascular endothelial growth factor, and thrombin. It plays roles in microtubule disassembly and cell cycle progression, and is critical in the regulation of neurite outgrowth. LIMK1 knockout mice show abnormalities in dendritic spine morphology and synaptic function. LIMK1 is one of the genes deleted in patients with Williams Syndrome, which is characterized by distinct craniofacial features, cardiovascular problems, as well as behavioral and neurological abnormalities. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 102.73  E-value: 6.79e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  924 KEIEILRNLYHENIVKYKGICTEDggNGIKLIMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRD 1003
Cdd:cd14221     39 KEVKVMRCLEHPNVLKFIGVLYKD--KRLNFITEYIKGGTLRGIIKSMDSHYPWSQRVSFAKDIASGMAYLHSMNIIHRD 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1004 LAARNVLVESEHQVKIGDFGLTKAIETDKEYYTVKDDRDSP-----------VFWYAPECLMQSKFYIASDVWSFGVTLH 1072
Cdd:cd14221    117 LNSHNCLVRENKSVVVADFGLARLMVDEKTQPEGLRSLKKPdrkkrytvvgnPYWMAPEMINGRSYDEKVDVFSFGIVLC 196
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1073 ELLTYCDSDsspmalflkmigPTHGQMTVTRLVNTLKEGKRLpCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEAL 1152
Cdd:cd14221    197 EIIGRVNAD------------PDYLPRTMDFGLNVRGFLDRY-CPPNCPPSFFPIAVLCCDLDPEKRPSFSKLEHWLETL 263

                   .
gi 1013071061 1153 L 1153
Cdd:cd14221    264 R 264
SH2_Jak_Tyk2 cd10381
Src homology 2 (SH2) domain in Tyrosine Kinase 2 (Tyk2), a member of the Janus kinases (JAK); ...
426-527 6.79e-24

Src homology 2 (SH2) domain in Tyrosine Kinase 2 (Tyk2), a member of the Janus kinases (JAK); Tyk2 is a member of the tyrosine kinase and, more specifically, the Janus kinases (JAKs) protein families. This protein associates with the cytoplasmic domain of type I and type II cytokine receptors and promulgate cytokine signals by phosphorylating receptor subunits. It is also component of both the type I and type III interferon signaling pathways. As such, it may play a role in anti-viral immunity. A mutation in this gene has been associated with hyperimmunoglobulin E syndrome (HIES) - a primary immunodeficiency characterized by elevated serum immunoglobulin E. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198244  Cd Length: 102  Bit Score: 97.27  E-value: 6.79e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  426 DVAPPLIVHNIQNGCHGPICTEYAINKLRQEGSEEGMYVLRWSCTDFDNILMTVTCFEKSEQVQGAQKQFKNFQIEVQKG 505
Cdd:cd10381      1 EVAPPRLVTSIQNGIHGPMMDPFVQAKLKKEWPEEGLYLIRWSTLDLHRLILAVAHRNPA*SNGPGGLRLRQFRIQQKGS 80
                           90       100
                   ....*....|....*....|..
gi 1013071061  506 RYSLHGSDRSFPSLGDLMSHLK 527
Cdd:cd10381     81 AFVLEGWGREFASVGDLRDALQ 102
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
878-1076 7.22e-24

Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chk1 is implicated in many major checkpoints of the cell cycle, providing a link between upstream sensors and the cell cycle engine. It plays an important role in DNA damage response and maintaining genomic stability. Chk1 acts as an effector of the sensor kinase, ATR (ATM and Rad3-related), a member of the PI3K family, which is activated upon DNA replication stress. Chk1 delays mitotic entry in response to replication blocks by inhibiting cyclin dependent kinase (Cdk) activity. In addition, Chk1 contributes to the function of centrosome and spindle-based checkpoints, inhibits firing of origins of DNA replication (Ori), and represses transcription of cell cycle proteins including cyclin B and Cdk1. The Chk1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270971 [Multi-domain]  Cd Length: 261  Bit Score: 102.41  E-value: 7.22e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVELCrydpEGDNTGEQVAVKSL-KPESGGNHIADLKKEIEILRNLYHENIVKYKGiCTEDGgNGIKLIM 956
Cdd:cd14069      6 VQTLGEGAFGEVFLA----VNRNTEEAVAVKFVdMKRAPGDCPENIKKEVCIQKMLSHKNVVRFYG-HRREG-EFQYLFL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  957 EFLPSGSLKEYL-PKNKNKINLKQqlKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGL-TKAIETDKEy 1034
Cdd:cd14069     80 EYASGGELFDKIePDVGMPEDVAQ--FYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLaTVFRYKGKE- 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1013071061 1035 yTVKDDRDSPVFWYAPEcLMQSKFYIAS--DVWSFGVTLHELLT 1076
Cdd:cd14069    157 -RLLNKMCGTLPYVAPE-LLAKKKYRAEpvDVWSCGIVLFAMLA 198
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
869-1146 9.08e-24

Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity kinase Myt1, the protein tyrosine kinase Wee1, and similar proteins. These proteins are cell cycle checkpoint kinases that are involved in the regulation of cyclin-dependent kinase CDK1, the master engine for mitosis. CDK1 is kept inactivated through phosphorylation of N-terminal thr (T14 by Myt1) and tyr (Y15 by Myt1 and Wee1) residues. Mitosis progression is ensured through activation of CDK1 by dephoshorylation and inactivation of Myt1/Wee1. The Wee1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 101.69  E-value: 9.08e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  869 HFEkrflkRIRDLGEGHFGKVELCRyDPEgdnTGEQVAVK-SLKPESGGNHIADLKKEIEILRNL-YHENIVKYkgICTE 946
Cdd:cd13997      1 HFH-----ELEQIGSGSFSEVFKVR-SKV---DGCLYAVKkSKKPFRGPKERARALREVEAHAALgQHPNIVRY--YSSW 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  947 DGGNGIKLIMEFLPSGSLKEYLPKNKNKINLKQQL--KYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGL 1024
Cdd:cd13997     70 EEGGHLYIQMELCENGSLQDALEELSPISKLSEAEvwDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1025 TKAIETDkeyytvKDDRDSPVFWYAPECLMQSKFYI-ASDVWSFGVTLHELLTycdsdSSPMalflkmigPTHGQmtvtr 1103
Cdd:cd13997    150 ATRLETS------GDVEEGDSRYLAPELLNENYTHLpKADIFSLGVTVYEAAT-----GEPL--------PRNGQ----- 205
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1013071061 1104 LVNTLKEGKrLPCPPNCP--DEVYQLMRKCWEFQPSNRTSFQNLI 1146
Cdd:cd13997    206 QWQQLRQGK-LPLPPGLVlsQELTRLLKVMLDPDPTRRPTADQLL 249
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
881-1154 9.45e-24

Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. The KSR subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 102.43  E-value: 9.45e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYdpEGDntgeqVAVKSLKPES-GGNHIADLKKEIEILRNLYHENIVKYKGICTEDggNGIKLIMEFL 959
Cdd:cd14063      8 IGKGRFGRVHRGRW--HGD-----VAIKLLNIDYlNEEQLEAFKEEVAAYKNTRHDNLVLFMGACMDP--PHLAIVTSLC 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  960 PSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESeHQVKIGDFGL---TKAIETDKEYYT 1036
Cdd:cd14063     79 KGRTLYSLIHERKEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLEN-GRVVITDFGLfslSGLLQPGRREDT 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1037 VKDDRD-----SP-------VFWYAPECLMQSKfyiASDVWSFGVTLHELLTY-----CDSDSSpmalFLKMIGPTHGQm 1099
Cdd:cd14063    158 LVIPNGwlcylAPeiiralsPDLDFEESLPFTK---ASDVYAFGTVWYELLAGrwpfkEQPAES----IIWQVGCGKKQ- 229
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1013071061 1100 tvtRLVNTlkegkrlpcppNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALLK 1154
Cdd:cd14063    230 ---SLSQL-----------DIGREVKDILMQCWAYDPEKRPTFSDLLRMLERLPK 270
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
613-839 9.82e-24

Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Csk is expressed in a wide variety of tissues. As a negative regulator of Src, Csk plays a role in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Csk is a cytoplasmic (or nonreceptor) PTK containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases, Csk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. In addition, Csk also shows Src-independent functions. It is a critical component in G-protein signaling, and plays a role in cytoskeletal reorganization and cell migration. The Csk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 101.98  E-value: 9.82e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  613 EEKKIKVILKVLdpSHRDISLAFFEAASMMRQVSHKHIVYLYGVCVRDVENI-MVEEFVEGGPL-DLFMHRKSDVLTTPW 690
Cdd:cd05082     26 DYRGNKVAVKCI--KNDATAQAFLAEASVMTQLRHSNLVQLLGVIVEEKGGLyIVTEYMAKGSLvDYLRSRGRSVLGGDC 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  691 KFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGIPITVLSRQEcIERIP--WIAPECVEDsK 768
Cdd:cd05082    104 LLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNV-------AKVSDFGLTKEASSTQD-TGKLPvkWTAPEALRE-K 174
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1013071061  769 NLSVAADKWSFGTTLWEICYNG-----EIPLKDkTLIEKERFYESRCRPVTPSCkeLADLMTRCMNYDPNQRPFFR 839
Cdd:cd05082    175 KFSTKSDVWSFGILLWEIYSFGrvpypRIPLKD-VVPRVEKGYKMDAPDGCPPA--VYDVMKNCWHLDAAMRPSFL 247
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
568-841 1.20e-23

Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The DDR subfamily consists of homologs of mammalian DDR1, DDR2, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270644 [Multi-domain]  Cd Length: 297  Bit Score: 102.80  E-value: 1.20e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  568 YPMSQLSFDrilkkdlvqgEHLGRGTRTHIY---SGTLMDYKDDEGTSEEKKIKVIL---KVLDPSHRDISLA-FFEAAS 640
Cdd:cd05051      2 FPREKLEFV----------EKLGEGQFGEVHlceANGLSDLTSDDFIGNDNKDEPVLvavKMLRPDASKNAREdFLKEVK 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  641 MMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSDVLTTPWKFK-----------VAKQLASALSYLEDKD 709
Cdd:cd05051     72 IMSQLKDPNIVRLLGVCTRDEPLCMIVEYMENGDLNQFLQKHEAETQGASATNsktlsygtllyMATQIASGMKYLESLN 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  710 LVHGNVCTKNLLLAregidseCGPFIKLSDPGIPITVLSRQEC-IE-----RIPWIAPECVEDSKnLSVAADKWSFGTTL 783
Cdd:cd05051    152 FVHRDLATRNCLVG-------PNYTIKIADFGMSRNLYSGDYYrIEgravlPIRWMAWESILLGK-FTTKSDVWAFGVTL 223
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1013071061  784 WEI-CYNGEIP---LKDKTLIEKE-RFYES----RCRPVTPSC-KELADLMTRCMNYDPNQRPFFRAI 841
Cdd:cd05051    224 WEIlTLCKEQPyehLTDEQVIENAgEFFRDdgmeVYLSRPPNCpKEIYELMLECWRRDEEDRPTFREI 291
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
610-838 1.24e-23

Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also called protein tyrosine kinase 7 (PTK7), is an orphan receptor PTK (RTK) containing an extracellular region with seven immunoglobulin domains, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Studies in mice reveal that CCK4 is essential for neural development. Mouse embryos containing a truncated CCK4 die perinatally and display craniorachischisis, a severe form of neural tube defect. The mechanism of action of the CCK4 pseudokinase is still unknown. Other pseudokinases such as HER3 rely on the activity of partner RTKs. The CCK4 subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133178 [Multi-domain]  Cd Length: 275  Bit Score: 102.16  E-value: 1.24e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  610 GTSEEKKIKVIL-KVLdpSHRD---ISLAFFEAASMMRQVSHKHIVYLYGVCvRDVE-NIMVEEFVEGGPLDLFM----- 679
Cdd:cd05046     28 GIEEEGGETLVLvKAL--QKTKdenLQSEFRRELDMFRKLSHKNVVRLLGLC-REAEpHYMILEYTDLGDLKQFLratks 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  680 ---HRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGIPITVLSRQECIER- 755
Cdd:cd05046    105 kdeKLKPPPLSTKQKVALCTQIALGMDHLSNARFVHRDLAARNCLVSSQRE-------VKVSLLSLSKDVYNSEYYKLRn 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  756 --IP--WIAPECVEDSkNLSVAADKWSFGTTLWEICYNGEIPLKDKTLIEK-ERFYESRCR-PVTPSCKE-LADLMTRCM 828
Cdd:cd05046    178 alIPlrWLAPEAVQED-DFSTKSDVWSFGVLMWEVFTQGELPFYGLSDEEVlNRLQAGKLElPVPEGCPSrLYKLMTRCW 256
                          250
                   ....*....|
gi 1013071061  829 NYDPNQRPFF 838
Cdd:cd05046    257 AVNPKDRPSF 266
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
613-841 1.32e-23

Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Zap-70 is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor (TCR) signaling. Zap-70 binds the phosphorylated ITAM (immunoreceptor tyr activation motif) sequences of the activated TCR zeta-chain through its SH2 domains, leading to its phosphorylation and activation. It then phosphorylates target proteins, which propagate the signals to downstream pathways. Zap-70 is hardly detected in normal peripheral B-cells, but is present in some B-cell malignancies. It is used as a diagnostic marker for chronic lymphocytic leukemia (CLL) as it is associated with the more aggressive subtype of the disease. The Zap-70 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 101.95  E-value: 1.32e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  613 EEKKIKVILKVL-DPSHRDISLAFFEAASMMRQVSHKHIVYLYGVCvrDVENIM-VEEFVEGGPLDLFMHRKSDVLTTPW 690
Cdd:cd05115     28 RKKQIDVAIKVLkQGNEKAVRDEMMREAQIMHQLDNPYIVRMIGVC--EAEALMlVMEMASGGPLNKFLSGKKDEITVSN 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  691 KFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREgidsecgPFIKLSDPGIPITV-------LSRQECIERIPWIAPEC 763
Cdd:cd05115    106 VVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQ-------HYAKISDFGLSKALgaddsyyKARSAGKWPLKWYAPEC 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  764 VEDSKnLSVAADKWSFGTTLWEICYNGEIPLKDKTLIEKERFYESRCRPVTP-SC-KELADLMTRCMNYDPNQRPFFRAI 841
Cdd:cd05115    179 INFRK-FSSRSDVWSYGVTMWEAFSYGQKPYKKMKGPEVMSFIEQGKRMDCPaECpPEMYALMSDCWIYKWEDRPNFLTV 257
Pkinase pfam00069
Protein kinase domain;
877-1147 1.41e-23

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 100.01  E-value: 1.41e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  877 RIRDLGEGHFGKVELCRYDpegdNTGEQVAVKSLKPEsggnHIADLKK-----EIEILRNLYHENIVKYKGICTEDggNG 951
Cdd:pfam00069    3 VLRKLGSGSFGTVYKAKHR----DTGKIVAIKKIKKE----KIKKKKDknilrEIKILKKLNHPNIVRLYDAFEDK--DN 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  952 IKLIMEFLPSGSLKEYLPKNKNkINLKQQLKYAVQICKGMdylgsrqyvhrdlaarnvlvesehqvkigdfgltkaiETD 1031
Cdd:pfam00069   73 LYLVLEYVEGGSLFDLLSEKGA-FSEREAKFIMKQILEGL-------------------------------------ESG 114
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1032 KEYYTVKDDRdspvfWY-APECLMQSKFYIASDVWSFGVTLHELLT-----YCDSDSSPMALflkmigpthgqmtvtrlv 1105
Cdd:pfam00069  115 SSLTTFVGTP-----WYmAPEVLGGNPYGPKVDVWSLGCILYELLTgkppfPGINGNEIYEL------------------ 171
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1013071061 1106 NTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIE 1147
Cdd:pfam00069  172 IIDQPYAFPELPSNLSEEAKDLLKKLLKKDPSKRLTATQALQ 213
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
876-1147 1.45e-23

Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and Ste20-related proline alanine-rich kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SPAK is also referred to as STK39 or PASK (proline-alanine-rich STE20-related kinase). OSR1 and SPAK regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. They are also implicated in cytoskeletal rearrangement, cell differentiation, transformation and proliferation. OSR1 and SPAK contain a conserved C-terminal (CCT) domain, which recognizes a unique motif ([RK]FX[VI]) present in their activating kinases (WNK1/WNK4) and their substrates. The OSR1 and SPAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270787 [Multi-domain]  Cd Length: 267  Bit Score: 101.67  E-value: 1.45e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  876 KRIRDLGEGHFGKVELCRYDPegdnTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEdgGNGIKLI 955
Cdd:cd06610      4 ELIEVIGSGATAVVYAAYCLP----KKEKVAIKRIDLEKCQTSMDELRKEIQAMSQCNHPNVVSYYTSFVV--GDELWLV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  956 MEFLPSGSLKEYLP-KNKNKIN--------LKQQLKyavqickGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTK 1026
Cdd:cd06610     78 MPLLSGGSLLDIMKsSYPRGGLdeaiiatvLKEVLK-------GLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVSA 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1027 AIET--DKEYYTVKDDRDSPVfWYAPECLMQSKFYIA-SDVWSFGVTLHELLT----YcdSDSSPMALFLkmigpthgqM 1099
Cdd:cd06610    151 SLATggDRTRKVRKTFVGTPC-WMAPEVMEQVRGYDFkADIWSFGITAIELATgaapY--SKYPPMKVLM---------L 218
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1013071061 1100 TVTRLVNTLKEGKRLpcpPNCPDEVYQLMRKCWEFQPSNRTSFQNLIE 1147
Cdd:cd06610    219 TLQNDPPSLETGADY---KKYSKSFRKMISLCLQKDPSKRPTAEELLK 263
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
577-848 1.53e-23

Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. Gain of function alterations, through their overexpression, deletions, or point mutations in their kinase domains, have been implicated in various cancers. These receptors are targets of many small molecule inhibitors and monoclonal antibodies used in cancer therapy. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 101.72  E-value: 1.53e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  577 RILKK-DLVQGEHLGRGTRTHIYSGTLMDykddEGtsEEKKIKVILKVL-DPSHRDISLAFFEAASMMRQVSHKHIVYLY 654
Cdd:cd05057      2 RIVKEtELEKGKVLGSGAFGTVYKGVWIP----EG--EKVKIPVAIKVLrEETGPKANEEILDEAYVMASVDHPHLVRLL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  655 GVCVRdvENIM-VEEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLaregidsECGP 733
Cdd:cd05057     76 GICLS--SQVQlITQLMPLGCLLDYVRNHRDNIGSQLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLV-------KTPN 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  734 FIKLSDPGIPiTVLSRQECIER-------IPWIAPECVEDSKnLSVAADKWSFGTTLWEIC------YNGeIPLKD-KTL 799
Cdd:cd05057    147 HVKITDFGLA-KLLDVDEKEYHaeggkvpIKWMALESIQYRI-YTHKSDVWSYGVTVWELMtfgakpYEG-IPAVEiPDL 223
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1013071061  800 IEK-ERFyesrcrPVTPSCK-ELADLMTRCMNYDPNQRPFFRAIMRDINKL 848
Cdd:cd05057    224 LEKgERL------PQPPICTiDVYMVLVKCWMIDAESRPTFKELANEFSKM 268
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
881-1076 1.81e-23

Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases. Members of this family include cAMP-dependent Protein Kinase (PKA), cGMP-dependent Protein Kinase (PKG), Protein Kinase C (PKC), Protein Kinase B (PKB), G protein-coupled Receptor Kinase (GRK), Serum- and Glucocorticoid-induced Kinase (SGK), and 70 kDa ribosomal Protein S6 Kinase (p70S6K or S6K), among others. AGC kinases share an activation mechanism based on the phosphorylation of up to three sites: the activation loop (A-loop), the hydrophobic motif (HM) and the turn motif. Phosphorylation at the A-loop is required of most AGC kinases, which results in a disorder-to-order transition of the A-loop. The ordered conformation results in the access of substrates and ATP to the active site. A subset of AGC kinases with C-terminal extensions containing the HM also requires phosphorylation at this site. Phosphorylation at the HM allows the C-terminal extension to form an ordered structure that packs into the hydrophobic pocket of the catalytic domain, which then reconfigures the kinase into an active bi-lobed state. In addition, growth factor-activated AGC kinases such as PKB, p70S6K, RSK, MSK, PKC, and SGK, require phosphorylation at the turn motif (also called tail or zipper site), located N-terminal to the HM at the C-terminal extension. The AGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and Phosphoinositide 3-Kinase.


Pssm-ID: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 100.67  E-value: 1.81e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRydpeGDNTGEQVAVKSLKPES--GGNHIADLKKEIEILRNLYHENIVK-YKGICTEDggngiKL--I 955
Cdd:cd05123      1 LGKGSFGKVLLVR----KKDTGKLYAMKVLRKKEiiKRKEVEHTLNERNILERVNHPFIVKlHYAFQTEE-----KLylV 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  956 MEFLPSGSLKEYLpKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYy 1035
Cdd:cd05123     72 LDYVPGGELFSHL-SKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELSSDGDR- 149
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1013071061 1036 tvkddRDSPV---FWYAPECLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd05123    150 -----TYTFCgtpEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLT 188
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
589-848 1.84e-23

Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They can be classified into two classes (EphA and EphB), according to their extracellular sequences, which largely correspond to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.The EphR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 101.29  E-value: 1.84e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  589 LGRGTRTHIYSGTLMdykddegTSEEKKIKVILKVLDPSHRD-ISLAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVE 667
Cdd:cd05033     12 IGGGEFGEVCSGSLK-------LPGKKEIDVAIKTLKSGYSDkQRLDFLTEASIMGQFDHPNVIRLEGVVTKSRPVMIVT 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  668 EFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIdseCgpfiKLSDPGipitvL 747
Cdd:cd05033     85 EYMENGSLDKFLRENDGKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLV---C----KVSDFG-----L 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  748 SRQ-ECIE--------RIP--WIAPECVEDSKnLSVAADKWSFGTTLWEICYNGEIPLKDKTLIEKERFYESRCRPVTP- 815
Cdd:cd05033    153 SRRlEDSEatyttkggKIPirWTAPEAIAYRK-FTSASDVWSFGIVMWEVMSYGERPYWDMSNQDVIKAVEDGYRLPPPm 231
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1013071061  816 SCKE-LADLMTRCMNYDPNQRPFFRAIMRDINKL 848
Cdd:cd05033    232 DCPSaLYQLMLDCWQKDRNERPTFSQIVSTLDKM 265
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
589-848 1.98e-23

Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. Some IRAKs may also play roles in T- and B-cell signaling, and adaptive immunity. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK-1, -2, and -4 are ubiquitously expressed and are active kinases, while IRAK-M is only induced in monocytes and macrophages and is an inactive kinase. Variations in IRAK genes are linked to diverse diseases including infection, sepsis, cancer, and autoimmune diseases. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase domain in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. This subfamily includes plant receptor-like kinases (RLKs) including Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1). BAK1 functions in BR (brassinosteroid)-regulated plant development and in pathways involved in plant resistance to pathogen infection and herbivore attack. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The IRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 101.20  E-value: 1.98e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  589 LGRGTRTHIYSGTLmdykdDEGTSeekkikVILKVLDPSHRDISLAFFEA-ASMMRQVSHKHIVYLYGVCVRDVENIMVE 667
Cdd:cd14066      1 IGSGGFGTVYKGVL-----ENGTV------VAVKRLNEMNCAASKKEFLTeLEMLGRLRHPNLVRLLGYCLESDEKLLVY 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  668 EFVEGGPL--DLFMHRKSDVLTTPWKFKVAKQLASALSYL---EDKDLVHGNVCTKNLLLaregiDSECGPfiKLSDPGI 742
Cdd:cd14066     70 EYMPNGSLedRLHCHKGSPPLPWPQRLKIAKGIARGLEYLheeCPPPIIHGDIKSSNILL-----DEDFEP--KLTDFGL 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  743 -----PITVLSRQECIER-IPWIAPECVEDSKnLSVAADKWSFGTTLWEIC------YNGEIPLKDKTLIE------KER 804
Cdd:cd14066    143 arlipPSESVSKTSAVKGtIGYLAPEYIRTGR-VSTKSDVYSFGVVLLELLtgkpavDENRENASRKDLVEwveskgKEE 221
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1013071061  805 FYE------SRCRPVTPSC-KELADLMTRCMNYDPNQRPFFRAIMRDINKL 848
Cdd:cd14066    222 LEDildkrlVDDDGVEEEEvEALLRLALLCTRSDPSLRPSMKEVVQMLEKL 272
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
876-1076 2.60e-23

Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK, CDK2, and CDK3. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression while the CDK1/cyclin B complex is critical for G2 to M phase transition. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. Studies in knockout mice revealed that CDK1 can compensate for the loss of the cdk2 gene as it can also bind cyclin E and drive G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270829 [Multi-domain]  Cd Length: 283  Bit Score: 101.21  E-value: 2.60e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  876 KRIRDLGEGHFGKVelcrYDPEGDNTGEQVAVKSLKPESGGNHIADLK-KEIEILRNLYHENIVKYKGICTEDggNGIKL 954
Cdd:cd07835      2 QKLEKIGEGTYGVV----YKARDKLTGEIVALKKIRLETEDEGVPSTAiREISLLKELNHPNIVRLLDVVHSE--NKLYL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPSgSLKEYLPKNKNKINLKQQLK-YAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKE 1033
Cdd:cd07835     76 VFEFLDL-DLKKYMDSSPLTGLDPPLIKsYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLARAFGVPVR 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1013071061 1034 YYTvkddRDSPVFWY-APECLMQSKFY-IASDVWSFGVTLHELLT 1076
Cdd:cd07835    155 TYT----HEVVTLWYrAPEILLGSKHYsTPVDIWSVGCIFAEMVT 195
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
878-1091 2.70e-23

Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the subfamily include SLK, STK10 (also called LOK for Lymphocyte-Oriented Kinase), SmSLK (Schistosoma mansoni SLK), and related proteins. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It also plays a role in mediating actin reorganization. STK10 is responsible in regulating the CD28 responsive element in T cells, as well as leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. SmSLK is capable of activating the MAPK Jun N-terminal kinase (JNK) pathway in human embryonic kidney cells as well as in Xenopus oocytes. It may participate in regulating MAPK cascades during host-parasite interactions. The SLK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 101.36  E-value: 2.70e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVELCRYDpegdNTGEQVAVKSLKPESGgNHIADLKKEIEILRNLYHENIVKYKGICTEDggNGIKLIME 957
Cdd:cd06611     10 IGELGDGAFGKVYKAQHK----ETGLFAAAKIIQIESE-EELEDFMVEIDILSECKHPNIVGLYEAYFYE--NKLWILIE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  958 FLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLT-KAIETDKEyyt 1036
Cdd:cd06611     83 FCDGGALDSIMLELERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSaKNKSTLQK--- 159
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1013071061 1037 vkddRDSPV---FWYAPECLMQSKF------YIAsDVWSFGVTLHEL--LTYCDSDSSPMALFLKM 1091
Cdd:cd06611    160 ----RDTFIgtpYWMAPEVVACETFkdnpydYKA-DIWSLGITLIELaqMEPPHHELNPMRVLLKI 220
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
881-1145 3.94e-23

Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LKB1, also called STK11, was first identified as a tumor suppressor responsible for Peutz-Jeghers syndrome, a disorder that leads to an increased risk of spontaneous epithelial cancer. It serves as a master upstream kinase that activates AMP-activated protein kinase (AMPK) and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. To be activated, LKB1 requires the adaptor proteins STe20-Related ADaptor (STRAD) and mouse protein 25 (MO25). The LKB1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271021 [Multi-domain]  Cd Length: 255  Bit Score: 100.02  E-value: 3.94e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVE-------LCRYdpegdntgeqvAVKSLKPES-----GGNhiADLKKEIEILRNLYHENIVKYKGICTEDG 948
Cdd:cd14119      1 LGEGSYGKVKevldtetLCRR-----------AVKILKKRKlrripNGE--ANVKREIQILRRLNHRNVIKLVDVLYNEE 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  949 GNGIKLIMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAI 1028
Cdd:cd14119     68 KQKLYMVMEYCVGGLQEMLDSAPDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVAEAL 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1029 ETDKEYYTVKDDRDSPVFwYAPECLM-QSKFY-IASDVWSFGVTLHELLT--YcdsdsspmalflkmigPTHGQmTVTRL 1104
Cdd:cd14119    148 DLFAEDDTCTTSQGSPAF-QPPEIANgQDSFSgFKVDIWSAGVTLYNMTTgkY----------------PFEGD-NIYKL 209
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1013071061 1105 VNTLKEGKrLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNL 1145
Cdd:cd14119    210 FENIGKGE-YTIPDDVDPDLQDLLRGMLEKDPEKRFTIEQI 249
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
881-1112 4.28e-23

Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes three leucine-rich repeat receptor-like kinases (LRR-RLKs): Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1), and Physcomitrella patens CLL1B clavata1-like receptor S/T protein kinase. BAK1 functions in various signaling pathways. It plays a role in BR (brassinosteroid)-regulated plant development as a co-receptor of BRASSINOSTEROID (BR) INSENSITIVE 1 (BRI1), the receptor for BRs, and is required for full activation of BR signaling. It also modulates pathways involved in plant resistance to pathogen infection (pattern-triggered immunity, PTI) and herbivore attack (wound- or herbivore feeding-induced accumulation of jasmonic acid (JA) and JA-isoleucine. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The STK_BAK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 100.26  E-value: 4.28e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVelcrYDPEGDNtGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGNgiKLIMEFLP 960
Cdd:cd14664      1 IGRGGAGTV----YKGVMPN-GTLVAVKRLKGEGTQGGDHGFQAEIQTLGMIRHRNIVRLRGYCSNPTTN--LLVYEYMP 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  961 SGSLKEYL---PKNKNKINLKQQLKYAVQICKGMDYLG---SRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIetdkey 1034
Cdd:cd14664     74 NGSLGELLhsrPESQPPLDWETRQRIALGSARGLAYLHhdcSPLIIHRDVKSNNILLDEEFEAHVADFGLAKLM------ 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1035 ytvkDDRDSPV-------FWY-APECLMQSKFYIASDVWSFGVTLHELLTycdsDSSPMALFlkmiGPTHGQMTVTRLVN 1106
Cdd:cd14664    148 ----DDKDSHVmssvagsYGYiAPEYAYTGKVSEKSDVYSYGVVLLELIT----GKRPFDEA----FLDDGVDIVDWVRG 215

                   ....*.
gi 1013071061 1107 TLKEGK 1112
Cdd:cd14664    216 LLEEKK 221
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
878-1147 4.46e-23

Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase or LOK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK10/LOK is also called polo-like kinase kinase 1 in Xenopus (xPlkk1). It is highly expressed in lymphocytes and is responsible in regulating leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. It plays a role in regulating the CD28 responsive element in T cells, and may also function as a regulator of polo-like kinase 1 (Plk1), a protein which is overexpressed in multiple tumor types. The STK10 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132975 [Multi-domain]  Cd Length: 292  Bit Score: 100.88  E-value: 4.46e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVelcrYDPEGDNTGEQVAVKSLKPESGgNHIADLKKEIEILRNLYHENIVKYKGICTEDGGngIKLIME 957
Cdd:cd06644     17 IGELGDGAFGKV----YKAKNKETGALAAAKVIETKSE-EELEDYMVEIEILATCNHPYIVKLLGAFYWDGK--LWIMIE 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  958 FLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLT-KAIETDKEyyt 1036
Cdd:cd06644     90 FCPGGAVDAIMLELDRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSaKNVKTLQR--- 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1037 vkddRDSPV---FWYAPECLM-----QSKFYIASDVWSFGVTLHElltycdsdsspmalfLKMIGPTHGQMTVTRLVntL 1108
Cdd:cd06644    167 ----RDSFIgtpYWMAPEVVMcetmkDTPYDYKADIWSLGITLIE---------------MAQIEPPHHELNPMRVL--L 225
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1013071061 1109 KEGKRLP----CPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIE 1147
Cdd:cd06644    226 KIAKSEPptlsQPSKWSMEFRDFLKTALDKHPETRPSAAQLLE 268
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
879-1076 4.51e-23

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK4 plays a critical role in NFkB activation by its interaction with MyD88, which acts as a scaffold that enables IRAK4 to phosphorylate and activate IRAK1 and/or IRAK2. It also plays an important role in type I IFN production induced by TLR7/8/9. The IRAK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 100.65  E-value: 4.51e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGHFGKVELcrydpeGDNTGEQVAVKSLKPESGGNhIADLKK----EIEILRNLYHENIVKYKGiCTEDGGNgIKL 954
Cdd:cd14158     21 NKLGEGGFGVVFK------GYINDKNVAVKKLAAMVDIS-TEDLTKqfeqEIQVMAKCQHENLVELLG-YSCDGPQ-LCL 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPSGSLKEYLP--KNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDK 1032
Cdd:cd14158     92 VYTYMPNGSLLDRLAclNDTPPLSWHMRCKIAQGTANGINYLHENNHIHRDIKSANILLDETFVPKISDFGLARASEKFS 171
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1013071061 1033 EyyTVKDDRDSPVFWY-APECLmQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd14158    172 Q--TIMTERIVGTTAYmAPEAL-RGEITPKSDIFSFGVVLLEIIT 213
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
881-1149 4.53e-23

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP1 harbors a C-terminal Death domain (DD), which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 can also recruit other kinases including MEKK1, MEKK3, and RIP3 through an intermediate domain (ID) that bears a RIP homotypic interaction motif (RHIM). RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accummulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. RIP kinases serve as essential sensors of cellular stress. The RIP1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 100.27  E-value: 4.53e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDPEGdntgeQVAVKSLKpeSGGNHI---ADLKKEIEILRNLYHENIVKYKGICTEDGGngIKLIME 957
Cdd:cd14027      1 LDSGGFGKVSLCFHRTQG-----LVVLKTVY--TGPNCIehnEALLEEGKMMNRLRHSRVVKLLGVILEEGK--YSLVME 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  958 FLPSGSLKEYLPKNKNKINLKQqlKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFG---------LTKai 1028
Cdd:cd14027     72 YMEKGNLMHVLKKVSVPLSVKG--RIILEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGlasfkmwskLTK-- 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1029 ETDKEYYTVKDDRDS---PVFWYAPECL--MQSKFYIASDVWSFGVTLHELLTYCDsdsspmalflkmigPTHGQMTVTR 1103
Cdd:cd14027    148 EEHNEQREVDGTAKKnagTLYYMAPEHLndVNAKPTEKSDVYSFAIVLWAIFANKE--------------PYENAINEDQ 213
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1104 LVNTLKEGKRlP----CPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGF 1149
Cdd:cd14027    214 IIMCIKSGNR-PdvddITEYCPREIIDLMKLCWEANPEARPTFPGIEEKF 262
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
881-1152 5.51e-23

Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This group is composed of uncharacterized proteins with similarity to LIMK and Testicular or testis-specific protein kinase (TESK). LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 99.52  E-value: 5.51e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVelcrYDPEGDNTGEQVAVKSLKPESGGNHIAdlkKEIEILRNLYHENIVKYKGICTEDGGngIKLIMEFLP 960
Cdd:cd14156      1 IGSGFFSKV----YKVTHGATGKVMVVKIYKNDVDQHKIV---REISLLQKLSHPNIVRYLGICVKDEK--LHPILEYVS 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  961 SGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVK---IGDFGLTKAIetdKEYYTV 1037
Cdd:cd14156     72 GGCLEELLAREELPLSWREKVELACDISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGReavVTDFGLAREV---GEMPAN 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1038 KDDRDSPV----FWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSDssPMALflkmigPTHGQMTVTrlVNTLKEgkr 1113
Cdd:cd14156    149 DPERKLSLvgsaFWMAPEMLRGEPYDRKVDVFSFGIVLCEILARIPAD--PEVL------PRTGDFGLD--VQAFKE--- 215
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1013071061 1114 lpCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEAL 1152
Cdd:cd14156    216 --MVPGCPEPFLDLAASCCRMDAFKRPSFAELLDELEDI 252
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
876-1139 6.98e-23

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek8 contains an N-terminal kinase catalytic domain and a C-terminal RCC1 (regulator of chromosome condensation) domain. A double point mutation in Nek8 causes cystic kidney disease in mice that genetically resembles human autosomal recessive polycystic kidney disease (ARPKD). Nek8 is also associated with a rare form of juvenile renal cystic disease, nephronophthisis type 9. It has been suggested that a defect in the ciliary localization of Nek8 contributes to the development of cysts manifested by these diseases. Nek8 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270859 [Multi-domain]  Cd Length: 256  Bit Score: 99.42  E-value: 6.98e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  876 KRIRDLGEGHFGKVELC-RYDPEGDNTGEQVAVKSLKPESGgnhiADLKKEIEILRNLYHENIVKYKGICTEDggNGIKL 954
Cdd:cd08220      3 EKIRVVGRGAYGTVYLCrRKDDNKLVIIKQIPVEQMTKEER----QAALNEVKVLSMLHHPNIIEYYESFLED--KALMI 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPSGSLKEYLPKNKNKINLKQQ-LKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQ-VKIGDFGLTKAIETDK 1032
Cdd:cd08220     77 VMEYAPGGTLFEYIQQRKGSLLSEEEiLHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTvVKIGDFGISKILSSKS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1033 EYYTVKddrDSPVFwYAPECLMQSKFYIASDVWSFGVTLHELLTY---CDSDSSPmALFLKMIGPTHGqmtvtrlvntlk 1109
Cdd:cd08220    157 KAYTVV---GTPCY-ISPELCEGKPYNQKSDIWALGCVLYELASLkraFEAANLP-ALVLKIMRGTFA------------ 219
                          250       260       270
                   ....*....|....*....|....*....|
gi 1013071061 1110 egkrlPCPPNCPDEVYQLMRKCWEFQPSNR 1139
Cdd:cd08220    220 -----PISDRYSEELRHLILSMLHLDPNKR 244
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
879-1149 7.50e-23

Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 99.39  E-value: 7.50e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGHFGKVELCRYD-PEGDNTGEQVAVKSLKPESGGNHiaDLKKEIEILRNLYHENIVKYKGICTEDGGngIKLIME 957
Cdd:cd13992      1 ASCGSGASSHTGEPKYVkKVGVYGGRTVAIKHITFSRTEKR--TILQELNQLKELVHDNLNKFIGICINPPN--IAVVTE 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  958 FLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYL-GSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYT 1036
Cdd:cd13992     77 YCTRGSLQDVLLNREIKMDWMFKSSFIKDIVKGMNYLhSSSIGYHGRLKSSNCLVDSRWVVKLTDFGLRNLLEEQTNHQL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1037 VKDDRDSPVFWYAPECLMQSKFYI----ASDVWSFGVTLHELLTYCD--SDSSPMALFLKMIgpthgqmtvtrlvntlKE 1110
Cdd:cd13992    157 DEDAQHKKLLWTAPELLRGSLLEVrgtqKGDVYSFAIILYEILFRSDpfALEREVAIVEKVI----------------SG 220
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1013071061 1111 GKRLPCP------PNCPDEVYQLMRKCWEFQPSNRTSFQnLIEGF 1149
Cdd:cd13992    221 GNKPFRPelavllDEFPPRLVLLVKQCWAENPEKRPSFK-QIKKT 264
SH2_Jak3 cd10380
Src homology 2 (SH2) domain in the Janus kinase 3 (Jak3) proteins; Jak3 is a member of the ...
426-525 9.52e-23

Src homology 2 (SH2) domain in the Janus kinase 3 (Jak3) proteins; Jak3 is a member of the Janus kinase (JAK) family of tyrosine kinases involved in cytokine receptor-mediated intracellular signal transduction. It is predominantly expressed in immune cells and transduces a signal in response to its activation via tyrosine phosphorylation by interleukin receptors. Mutations in this gene are associated with autosomal SCID (severe combined immunodeficiency disease). In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198243  Cd Length: 96  Bit Score: 93.70  E-value: 9.52e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  426 DVAPPLIVHNIQNGCHGPICTEYAINKLRQEGSEEGMYVLRWSCTDFDNILMTVtCFEKSeqvqgAQKQFKNFQIEVQKG 505
Cdd:cd10380      1 EVAPPRLLEDIENQCHGPITSEFAVNKLKKAGSEPGSFVLRRSPQDFDKFLLTV-CVQTT-----LGLDYKDCLIRKNEG 74
                           90       100
                   ....*....|....*....|
gi 1013071061  506 RYSLHGSDRSFPSLGDLMSH 525
Cdd:cd10380     75 HFSLAGVSRSFSSLKELLVT 94
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
868-1076 1.02e-22

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK10, also called PISSLRE, is essential for cell growth and proliferation, and acts through the G2/M phase of the cell cycle. CDK10 has also been identified as an important factor in endocrine therapy resistance in breast cancer. CDK10 silencing increases the transcription of c-RAF and the activation of the p42/p44 MAPK pathway, which leads to antiestrogen resistance. Patients who express low levels of CDK10 relapse early on tamoxifen. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK10 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173742 [Multi-domain]  Cd Length: 309  Bit Score: 100.13  E-value: 1.02e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  868 THFEKrfLKRIrdlGEGHFGKVelcrYDPEGDNTGEQVAVKSLK--PESGGNHIADLKkEIEILRNLYHENIVKYKGICT 945
Cdd:cd07845      7 TEFEK--LNRI---GEGTYGIV----YRARDTTSGEIVALKKVRmdNERDGIPISSLR-EITLLLNLRHPNIVELKEVVV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  946 EDGGNGIKLIMEFLPSgSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLT 1025
Cdd:cd07845     77 GKHLDSIFLVMEYCEQ-DLASLLDNMPTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGLA 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1013071061 1026 KAIETDKEYYTVKddrdSPVFWY-APECLMQSKFYIAS-DVWSFGVTLHELLT 1076
Cdd:cd07845    156 RTYGLPAKPMTPK----VVTLWYrAPELLLGCTTYTTAiDMWAVGCILAELLA 204
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
878-1076 1.27e-22

Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Yeast contains only one Aurora kinase while most higher eukaryotes have two. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2. Aurora-B is most active at the transition during metaphase to the end of mitosis. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270909 [Multi-domain]  Cd Length: 253  Bit Score: 98.32  E-value: 1.27e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVELCRYDpegdNTGEQVAVKSLKPE--SGGNHIADLKKEIEILRNLYHENIVKYKGiCTEDGGNgIKLI 955
Cdd:cd14007      5 GKPLGKGKFGNVYLAREK----KSGFIVALKVISKSqlQKSGLEHQLRREIEIQSHLRHPNILRLYG-YFEDKKR-IYLI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  956 MEFLPSGSLKEYLPKNKnKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDK--- 1032
Cdd:cd14007     79 LEYAPNGELYKELKKQK-RFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWSVHAPSNRrkt 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1033 -----EYytvkddrdspvfwYAPEcLMQSKFYIAS-DVWSFGVTLHELLT 1076
Cdd:cd14007    158 fcgtlDY-------------LPPE-MVEGKEYDYKvDIWSLGVLCYELLV 193
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
876-1076 2.21e-22

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. CDK2, together with CDK4, also regulates embryonic cell proliferation. Despite these important roles, mice deleted for the cdk2 gene are viable and normal except for being sterile. This may be due to compensation provided by CDK1 (also called Cdc2), which can also bind cyclin E and drive the G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270844 [Multi-domain]  Cd Length: 284  Bit Score: 98.73  E-value: 2.21e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  876 KRIRDLGEGHFGKVelcrYDPEGDNTGEQVAVKS--LKPESGGNHIADLKkEIEILRNLYHENIVKYKGICTEDggNGIK 953
Cdd:cd07860      3 QKVEKIGEGTYGVV----YKARNKLTGEVVALKKirLDTETEGVPSTAIR-EISLLKELNHPNIVKLLDVIHTE--NKLY 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  954 LIMEFLpSGSLKEYLP-KNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDK 1032
Cdd:cd07860     76 LVFEFL-HQDLKKFMDaSALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPV 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1013071061 1033 EYYTvkddRDSPVFWY-APECLMQSKFY-IASDVWSFGVTLHELLT 1076
Cdd:cd07860    155 RTYT----HEVVTLWYrAPEILLGCKYYsTAVDIWSLGCIFAEMVT 196
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
878-1141 2.60e-22

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Typical MAPK pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPK kinase (MAP2K or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAP3K or MKKK). Each cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. There are three typical MAPK subfamilies: Extracellular signal-Regulated Kinase (ERK), c-Jun N-terminal Kinase (JNK), and p38. Some MAPKs are atypical in that they are not regulated by MAP2Ks. These include MAPK4, MAPK6, NLK, and ERK7. The MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270828 [Multi-domain]  Cd Length: 329  Bit Score: 99.52  E-value: 2.60e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVELCrYDPEgdnTGEQVAVKSL-KPESggnHIADLKK---EIEILRNLYHENIVKYKGICTEDGG---N 950
Cdd:cd07834      5 LKPIGSGAYGVVCSA-YDKR---TGRKVAIKKIsNVFD---DLIDAKRilrEIKILRHLKHENIIGLLDILRPPSPeefN 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  951 GIKLIMEFLPSgSLKEYLpKNKNKINLkQQLKYAV-QICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIE 1029
Cdd:cd07834     78 DVYIVTELMET-DLHKVI-KSPQPLTD-DHIQYFLyQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFGLARGVD 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1030 TDK------EYYTVKddrdspvfWY-APECLMQSKFYIAS-DVWSFGVTLHELLTYCdsdsspmALF--------LKMI- 1092
Cdd:cd07834    155 PDEdkgfltEYVVTR--------WYrAPELLLSSKKYTKAiDIWSVGCIFAELLTRK-------PLFpgrdyidqLNLIv 219
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1013071061 1093 ---GPTH-------GQMTVTRLVNTL--KEGKRLP-CPPNCPDEVYQLMRKCWEFQPSNRTS 1141
Cdd:cd07834    220 evlGTPSeedlkfiSSEKARNYLKSLpkKPKKPLSeVFPGASPEAIDLLEKMLVFNPKKRIT 281
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
881-1154 2.73e-22

Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. B-Raf activates ERK with the strongest magnitude, compared with other Raf kinases. Mice embryos deficient in B-Raf die around midgestation due to vascular hemorrhage caused by apoptotic endothelial cells. Mutations in B-Raf have been implicated in initiating tumorigenesis and tumor progression, and are found in malignant cutaneous melanoma, papillary thyroid cancer, as well as in ovarian and colorectal carcinomas. Most oncogenic B-Raf mutations are located at the activation loop of the kinase and surrounding regions; the V600E mutation accounts for around 90% of oncogenic mutations. The V600E mutant constitutively activates MEK, resulting in sustained activation of ERK. B-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The B-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 98.21  E-value: 2.73e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYdpEGDNTGEQVAVKSLKPEsggnHIADLKKEIEILRNLYHENIVKYKGICTEDGgngIKLIMEFLP 960
Cdd:cd14151     16 IGSGSFGTVYKGKW--HGDVAVKMLNVTAPTPQ----QLQAFKNEVGVLRKTRHVNILLFMGYSTKPQ---LAIVTQWCE 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  961 SGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTkaieTDKEYYTVK-- 1038
Cdd:cd14151     87 GSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLA----TVKSRWSGShq 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1039 -DDRDSPVFWYAPECL-MQSK--FYIASDVWSFGVTLHELLT----YCDSDSSPMALFLKMIGPTHGQMTVTRlvntlke 1110
Cdd:cd14151    163 fEQLSGSILWMAPEVIrMQDKnpYSFQSDVYAFGIVLYELMTgqlpYSNINNRDQIIFMVGRGYLSPDLSKVR------- 235
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1013071061 1111 gkrlpcpPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALLK 1154
Cdd:cd14151    236 -------SNCPKAMKRLMAECLKKKRDERPLFPQILASIELLAR 272
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
587-841 3.00e-22

Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Ror subfamily consists of Ror1, Ror2, and similar proteins. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. Ror kinases are expressed in many tissues during development. They play important roles in bone and heart formation. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Drosophila Ror is expressed only in the developing nervous system during neurite outgrowth and neuronal differentiation, suggesting a role for Drosophila Ror in neural development. More recently, mouse Ror1 and Ror2 have also been found to play an important role in regulating neurite growth in central neurons. Ror1 and Ror2 are believed to have some overlapping and redundant functions. The Ror subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 98.22  E-value: 3.00e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  587 EHLGRGTRTHIYSGTLMDYKddegtSEEKKIKVILKVLDPSHR-DISLAFFEAASMMRQVSHKHIVYLYGVCVRDVENIM 665
Cdd:cd05048     11 EELGEGAFGKVYKGELLGPS-----SEESAISVAIKTLKENASpKTQQDFRREAELMSDLQHPNIVCLLGVCTKEQPQCM 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  666 VEEFVEGGPLDLFMHRKS---------------DVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLARegidse 730
Cdd:cd05048     86 LFEYMAHGDLHEFLVRHSphsdvgvssdddgtaSSLDQSDFLHIAIQIAAGMEYLSSHHYVHRDLAARNCLVGD------ 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  731 cGPFIKLSDPGIPITVLS----RQECIERIP--WIAPECVEDSKnLSVAADKWSFGTTLWEICYNGEIP---LKDKTLIE 801
Cdd:cd05048    160 -GLTVKISDFGLSRDIYSsdyyRVQSKSLLPvrWMPPEAILYGK-FTTESDVWSFGVVLWEIFSYGLQPyygYSNQEVIE 237
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1013071061  802 KERfyeSRCRPVTPS-C-KELADLMTRCMNYDPNQRPFFRAI 841
Cdd:cd05048    238 MIR---SRQLLPCPEdCpARVYSLMVECWHEIPSRRPRFKEI 276
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
866-1089 6.29e-22

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST4 is sometimes referred to as MASK (MST3 and SOK1-related kinase). It plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. It influences cell growth and transformation by modulating the extracellular signal-regulated kinase (ERK) pathway. MST4 may also play a role in tumor formation and progression. It localizes in the Golgi apparatus by interacting with the Golgi matrix protein GM130 and may play a role in cell migration. The MST4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 97.05  E-value: 6.29e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  866 DPthfEKRFLKRIRdLGEGHFGKVelcrYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICT 945
Cdd:cd06640      1 DP---EELFTKLER-IGKGSFGEV----FKGIDNRTQQVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYL 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  946 EdgGNGIKLIMEFLPSGSLKEYLPKNK-NKINLKQQLKyavQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGL 1024
Cdd:cd06640     73 K--GTKLWIIMEYLGGGSALDLLRAGPfDEFQIATMLK---EILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGV 147
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1013071061 1025 TKAIeTDKEYytvkdDRDSPV---FWYAPECLMQSKFYIASDVWSFGVTLHELLT--YCDSDSSPM-ALFL 1089
Cdd:cd06640    148 AGQL-TDTQI-----KRNTFVgtpFWMAPEVIQQSAYDSKADIWSLGITAIELAKgePPNSDMHPMrVLFL 212
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
878-1146 8.30e-22

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii CNK2 has both cilliary and cell cycle functions. It influences flagellar length through promoting flagellar disassembly, and it regulates cell size, through influencing the size threshold at which cells commit to mitosis. This subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily includes CNK1, and -2. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 96.31  E-value: 8.30e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVelcrYDPEGDNTGEQVAVKSLKPES-GGNHIADLKKEIEILRNLYHENIVKYKGICTEdgGNGIKLIM 956
Cdd:cd08530      5 LKKLGKGSYGSV----YKVKRLSDNQVYALKEVNLGSlSQKEREDSVNEIRLLASVNHPNIIRYKEAFLD--GNRLCIVM 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  957 EFLPSGSLKEYLPKNKNKINL-KQQL--KYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKE 1033
Cdd:cd08530     79 EYAPFGDLSKLISKRKKKRRLfPEDDiwRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGISKVLKKNLA 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1034 YYTVkddrDSPvFWYAPECLMQSKFYIASDVWSFGVTLHELLTYcdsdSSPMAlflkmigpthgQMTVTRLVNTLKEGKR 1113
Cdd:cd08530    159 KTQI----GTP-LYAAPEVWKGRPYDYKSDIWSLGCLLYEMATF----RPPFE-----------ARTMQELRYKVCRGKF 218
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1013071061 1114 LPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLI 1146
Cdd:cd08530    219 PPIPPVYSQDLQQIIRSLLQVNPKKRPSCDKLL 251
FERM_C_JAK3 cd13334
FERM domain C-lobe of Janus kinase (JAK) 3; JAK3 functions in signal transduction and ...
360-426 8.48e-22

FERM domain C-lobe of Janus kinase (JAK) 3; JAK3 functions in signal transduction and interacts with members of the STAT (signal transduction and activators of transcription) family. It is required for signaling of the type I receptors that use the common gamma chain: IL-2, IL-4, IL-7, IL-9, IL-15 and IL-21. Cytokine binding induces the association of separate cytokine receptor subunits and the activation of the receptor-associated JAKs. In the absence of cytokine, JAKs lack protein tyrosine kinase activity. Once activated, the JAKs create docking sites for the STAT transcription factors by phosphorylation of specific tyrosine residues on the cytokine receptor subunits. Unlike the ubiquitous expression of JAK1, JAK2 and Tyk2, JAK3 is predominantly expressed in hematopoietic cells, such as NK cells, T cells and B cells. Mutations of JAK3 result in severe combined immunodeficiency (SCID). In addition to its well-known roles in T cells and NK cells, JAK3 has recently been found to inhibits IL-8-mediated chemotaxis. JAK3 interacts with CD247, TIAF1, and IL2RG. JAK (also called Just Another Kinase) is a family of intracellular, non-receptor tyrosine kinases that transduce cytokine-mediated signals via the JAK-STAT pathway. The JAK family in mammals consists of 4 members: JAK1, JAK2, JAK3 and TYK2. JAKs are composed of seven JAK homology (JH) domains (JH1-JH7) . The C-terminal JH1 domain is the main catalytic domain, followed by JH2, which is often referred to as a pseudokinase domain, followed by JH3-JH4 which is homologous to the SH2 domain, and lastly JH5-JH7 which is a FERM domain. Named after Janus, the two-faced Roman god of doorways, JAKs possess two near-identical phosphate-transferring domains; one which displays the kinase activity (JH1), while the other negatively regulates the kinase activity of the first (JH2). The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 275413  Cd Length: 110  Bit Score: 91.37  E-value: 8.48e-22
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1013071061  360 REEWNNFSYFPEITHIVIKES----------VVSINKQDNKKMELKLSSHEEALSFVSLVDGYFRLTADAHHYLCTD 426
Cdd:cd13334     34 SELWQTFCDFPEIIDISIKQAcrdggpvegrIVTLTRQDNRVLEAEFPTLREALSFVSLVDGYFRLTTDSHHYFCKE 110
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
876-1076 1.06e-21

Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MARKs, also called Partitioning-defective 1 (Par1) proteins, function as regulators of diverse cellular processes in nematodes, Drosophila, yeast, and vertebrates. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. Vertebrates contain four isoforms, namely MARK1 (or Par1c), MARK2 (or Par1b), MARK3 (Par1a), and MARK4 (or MARKL1). Known substrates of MARKs include the cell cycle-regulating phosphatase Cdc25, tyrosine phosphatase PTPH1, MAPK scaffolding protein KSR1, class IIa histone deacetylases, and plakophilin 2. The MARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270974 [Multi-domain]  Cd Length: 253  Bit Score: 95.66  E-value: 1.06e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  876 KRIRDLGEGHFGKVELCRYDPegdnTGEQVAVKSL-KPESGGNHIADLKKEIEILRNLYHENIVK-YKGICTEDGgngIK 953
Cdd:cd14072      3 RLLKTIGKGNFAKVKLARHVL----TGREVAIKIIdKTQLNPSSLQKLFREVRIMKILNHPNIVKlFEVIETEKT---LY 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  954 LIMEFLPSGSLKEYLPKNKNKINLKQQLKYAvQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAietdke 1033
Cdd:cd14072     76 LVMEYASGGEVFDYLVAHGRMKEKEARAKFR-QIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNE------ 148
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1013071061 1034 yYTVKDDRD----SPVFwYAPEcLMQSKFYIAS--DVWSFGVTLHELLT 1076
Cdd:cd14072    149 -FTPGNKLDtfcgSPPY-AAPE-LFQGKKYDGPevDVWSLGVILYTLVS 194
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
877-1076 1.06e-21

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher eukaryotes; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression. CDK1/cyclin A2 has also been implicated as an important regulator of S phase events. The CDK1/cyclin B complex is critical for G2 to M phase transition. It induces mitosis by activating nuclear enzymes that regulate chromatin condensation, nuclear membrane degradation, mitosis-specific microtubule and cytoskeletal reorganization. CDK1 also associates with cyclin E and plays a role in the entry into S phase. CDK1 transcription is stable throughout the cell cycle but is modulated in some pathological conditions. It may play a role in regulating apoptosis under these conditions. In breast cancer cells, HER2 can mediate apoptosis by inactivating CDK1. Activation of CDK1 may contribute to HIV-1 induced apoptosis as well as neuronal apoptosis in neurodegenerative diseases. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270845 [Multi-domain]  Cd Length: 285  Bit Score: 96.72  E-value: 1.06e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  877 RIRDLGEGHFGKVelcrYDPEGDNTGEQVAVKSLKPESGGNHIADLK-KEIEILRNLYHENIVKYKGICTEDggNGIKLI 955
Cdd:cd07861      4 KIEKIGEGTYGVV----YKGRNKKTGQIVAMKKIRLESEEEGVPSTAiREISLLKELQHPNIVCLEDVLMQE--NRLYLV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  956 MEFLpSGSLKEYL---PKNKNkINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDK 1032
Cdd:cd07861     78 FEFL-SMDLKKYLdslPKGKY-MDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLARAFGIPV 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1013071061 1033 EYYTvkddRDSPVFWY-APECLMQSKFY-IASDVWSFGVTLHELLT 1076
Cdd:cd07861    156 RVYT----HEVVTLWYrAPEVLLGSPRYsTPVDIWSIGTIFAEMAT 197
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
872-1089 1.08e-21

Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK25 is also called Ste20/oxidant stress response kinase 1 (SOK1) or yeast Sps1/Ste20-related kinase 1 (YSK1). It is localized in the Golgi apparatus through its interaction with the Golgi matrix protein GM130. It may be involved in the regulation of cell migration and polarization. STK25 binds and phosphorylates CCM3 (cerebral cavernous malformation 3), also called PCD10 (programmed cell death 10), and may play a role in apoptosis. Human STK25 is a candidate gene responsible for pseudopseudohypoparathyroidism (PPHP), a disease that shares features with the Albright hereditary osteodystrophy (AHO) phenotype. The STK25 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 96.28  E-value: 1.08e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  872 KRFLKRIRDLGEGHFGKVelcrYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEdgGNG 951
Cdd:cd06642      3 EELFTKLERIGKGSFGEV----YKGIDNRTKEVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYITRYYGSYLK--GTK 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  952 IKLIMEFLPSGSLKEYL-PKNKNKINLKQQLKyavQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIeT 1030
Cdd:cd06642     77 LWIIMEYLGGGSALDLLkPGPLEETYIATILR---EILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQL-T 152
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1013071061 1031 DKEYytvkdDRDSPV---FWYAPECLMQSKFYIASDVWSFGVTLHELLT--YCDSDSSPM-ALFL 1089
Cdd:cd06642    153 DTQI-----KRNTFVgtpFWMAPEVIKQSAYDFKADIWSLGITAIELAKgePPNSDLHPMrVLFL 212
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
635-850 1.15e-21

Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular carcinoma and Resting lymphocyte kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tec and Rlk (also named Txk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. Instead of PH, Rlk contains an N-terminal cysteine-rich region. In addition to PH, Tec also contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells. Tec is more widely-expressed than other Tec-like subfamily kinases. It is found in endothelial cells, both B- and T-cells, and a variety of myeloid cells including mast cells, erythroid cells, platelets, macrophages and neutrophils. Rlk is expressed in T-cells and mast cell lines. Tec and Rlk are both key components of T-cell receptor (TCR) signaling. They are important in TCR-stimulated proliferation, IL-2 production and phopholipase C-gamma1 activation. The Tec/Rlk subfamily is part of a larger superfamily, that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 96.08  E-value: 1.15e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  635 FFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGN 714
Cdd:cd05114     46 FIEEAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFMENGCLLNYLRQRRGKLSRDMLLSMCQDVCEGMEYLERNNFIHRD 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  715 VCTKNLLLAREGIdsecgpfIKLSDPGIPITVLSRQ---ECIERIP--WIAPECVEDSKnLSVAADKWSFGTTLWEICYN 789
Cdd:cd05114    126 LAARNCLVNDTGV-------VKVSDFGMTRYVLDDQytsSSGAKFPvkWSPPEVFNYSK-FSSKSDVWSFGVLMWEVFTE 197
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1013071061  790 GEIPLKDKTLIEKERFYESRCRPVTP--SCKELADLMTRCMNYDPNQRPFFRAIMRDINKLEE 850
Cdd:cd05114    198 GKMPFESKSNYEVVEMVSRGHRLYRPklASKSVYEVMYSCWHEKPEGRPTFADLLRTITEIAE 260
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
615-844 1.46e-21

Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Hck is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Hck is present in myeloid and lymphoid cells that play a role in the development of cancer. It may be important in the oncogenic signaling of the protein Tel-Abl, which induces a chronic myelogenous leukemia (CML)-like disease. Hck also acts as a negative regulator of G-CSF-induced proliferation of granulocytic precursors, suggesting a possible role in the development of acute myeloid leukemia (AML). In addition, Hck is essential in regulating the degranulation of polymorphonuclear leukocytes. Genetic polymorphisms affect the expression level of Hck, which affects PMN mediator release and influences the development of chronic obstructive pulmonary disease (COPD). Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Hck subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 95.86  E-value: 1.46e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  615 KKIKVILKVLDPSHRDISlAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSDVLTTPWKFKV 694
Cdd:cd05073     34 KHTKVAVKTMKPGSMSVE-AFLAEANVMKTLQHDKLVKLHAVVTKEPIYIITEFMAKGSLLDFLKSDEGSKQPLPKLIDF 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  695 AKQLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGIPiTVLSRQECIER------IPWIAPECVeDSK 768
Cdd:cd05073    113 SAQIAEGMAFIEQRNYIHRDLRAANILVSASLV-------CKIADFGLA-RVIEDNEYTARegakfpIKWTAPEAI-NFG 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  769 NLSVAADKWSFGTTLWEICYNGEIPLKDKTLIEKERFYESRCR-PVTPSC-KELADLMTRCMNYDPNQRPFF---RAIMR 843
Cdd:cd05073    184 SFTIKSDVWSFGILLMEIVTYGRIPYPGMSNPEVIRALERGYRmPRPENCpEELYNIMMRCWKNRPEERPTFeyiQSVLD 263

                   .
gi 1013071061  844 D 844
Cdd:cd05073    264 D 264
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
871-1147 1.77e-21

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: General Control Non-derepressible-2 (GCN2) which is activated during amino acid or serum starvation; protein kinase regulated by RNA (PKR) which is activated by double stranded RNA; heme-regulated inhibitor kinase (HRI) which is activated under heme-deficient conditions; and PKR-like endoplasmic reticulum kinase (PERK) which is activated when misfolded proteins accumulate in the ER. The EIF2AK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270898 [Multi-domain]  Cd Length: 273  Bit Score: 95.82  E-value: 1.77e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  871 EKRFL---KRIRDLGEGHFGKVELCRYDPegdnTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTED 947
Cdd:cd13996      1 NSRYLndfEEIELLGSGGFGSVYKVRNKV----DGVTYAIKKIRLTEKSSASEKVLREVKALAKLNHPNIVRYYTAWVEE 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  948 GGNGIKliMEFLPSGSLKEYLPK--NKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESE-HQVKIGDFGL 1024
Cdd:cd13996     77 PPLYIQ--MELCEGGTLRDWIDRrnSSSKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDdLQVKIGDFGL 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1025 TKAIETDKEYYTVKDDRDSPV-----------FWYAPECLMQSKFYIASDVWSFGVTLHELLtycdsdsspmalflkmig 1093
Cdd:cd13996    155 ATSIGNQKRELNNLNNNNNGNtsnnsvgigtpLYASPEQLDGENYNEKADIYSLGIILFEML------------------ 216
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1013071061 1094 ptHGQMTVTRLVNTLKEGKRLPCPPNC---PDEVYQLMRKCWEFQPSNRTSFQNLIE 1147
Cdd:cd13996    217 --HPFKTAMERSTILTDLRNGILPESFkakHPKEADLIQSLLSKNPEERPSAEQLLR 271
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
619-841 2.57e-21

Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Syk is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Syk was first cloned from the spleen, and its function in hematopoietic cells is well-established. It is involved in the signaling downstream of activated receptors (including B-cell and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. More recently, Syk expression has been detected in other cell types (including epithelial cells, vascular endothelial cells, neurons, hepatocytes, and melanocytes), suggesting a variety of biological functions in non-immune cells. Syk plays a critical role in maintaining vascular integrity and in wound healing during embryogenesis. It also regulates Vav3, which is important in osteoclast function including bone development. In breast epithelial cells, where Syk acts as a negative regulator for EGFR signaling, loss of Syk expression is associated with abnormal proliferation during cancer development suggesting a potential role as a tumor suppressor. In mice, Syk has been shown to inhibit malignant transformation of mammary epithelial cells induced with murine mammary tumor virus (MMTV). The Syk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 94.64  E-value: 2.57e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  619 VILKVL-----DPSHRDISLAffeAASMMRQVSHKHIVYLYGVCvrDVENIM-VEEFVEGGPLDLFMHRKSDVlTTPWKF 692
Cdd:cd05116     25 VAVKILkneanDPALKDELLR---EANVMQQLDNPYIVRMIGIC--EAESWMlVMEMAELGPLNKFLQKNRHV-TEKNIT 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  693 KVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGidsecgpFIKLSDPGIPiTVLSRQECIER--------IPWIAPECV 764
Cdd:cd05116     99 ELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQH-------YAKISDFGLS-KALRADENYYKaqthgkwpVKWYAPECM 170
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1013071061  765 EDSKnLSVAADKWSFGTTLWEICYNGEIPLKDKTLIEKERFYESRCRPVTPS-C-KELADLMTRCMNYDPNQRPFFRAI 841
Cdd:cd05116    171 NYYK-FSSKSDVWSFGVLMWEAFSYGQKPYKGMKGNEVTQMIEKGERMECPAgCpPEMYDLMKLCWTYDVDERPGFAAV 248
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
881-1076 2.71e-21

Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of HAL4, Saccharomyces cerevisiae Ptk2/Stk2, and similar fungal proteins. Proteins in this subfamily are involved in regulating ion transporters. In budding and fission yeast, HAL4 promotes potassium ion uptake, which increases cellular resistance to other cations such as sodium, lithium, and calcium ions. HAL4 stabilizes the major high-affinity K+ transporter Trk1 at the plasma membrane under low K+ conditions, which prevents endocytosis and vacuolar degradation. Budding yeast Ptk2 phosphorylates and regulates the plasma membrane H+ ATPase, Pma1. The HAL4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270896 [Multi-domain]  Cd Length: 265  Bit Score: 95.07  E-value: 2.71e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELC-RYDPEgdnTGEQVAVKSL----KPESGGNHIADLKKEIEILRNLYHENIVKYKGICtEDGGNGIKLI 955
Cdd:cd13994      1 IGKGATSVVRIVtKKNPR---SGVLYAVKEYrrrdDESKRKDYVKRLTSEYIISSKLHHPNIVKVLDLC-QDLHGKWCLV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  956 MEFLPSGSLKEYLPKnKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTkaietdkEYY 1035
Cdd:cd13994     77 MEYCPGGDLFTLIEK-ADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTA-------EVF 148
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1013071061 1036 TVKDDRDSPVF--------WYAPEcLMQSKFY--IASDVWSFGVTLHELLT 1076
Cdd:cd13994    149 GMPAEKESPMSaglcgsepYMAPE-VFTSGSYdgRAVDVWSCGIVLFALFT 198
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
644-853 3.79e-21

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated Kinase-1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAK1 is also known as mitogen-activated protein kinase kinase kinase 7 (MAPKKK7 or MAP3K7), TAK, or MEKK7. As a MAPKKK, it is an important mediator of cellular responses to extracellular signals. It regulates both the c-Jun N-terminal kinase and p38 MAPK cascades by activating the MAPK kinases, MKK4 and MKK3/6. In addition, TAK1 plays diverse roles in immunity and development, in different biological contexts, through many signaling pathways including TGFbeta/BMP, Wnt/Fz, and NF-kB. It is also implicated in the activation of the tumor suppressor kinase, LKB1. The TAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270960 [Multi-domain]  Cd Length: 253  Bit Score: 94.04  E-value: 3.79e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  644 QVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSdvltTPWKFKVAK------QLASALSYL---EDKDLVHGN 714
Cdd:cd14058     42 RVDHPNIIKLYGACSNQKPVCLVMEYAEGGSLYNVLHGKE----PKPIYTAAHamswalQCAKGVAYLhsmKPKALIHRD 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  715 VCTKNLLLARegidseCGPFIKLSDPGIpITVLSRQECIER--IPWIAPECVEDSKnLSVAADKWSFGTTLWEICYNGEi 792
Cdd:cd14058    118 LKPPNLLLTN------GGTVLKICDFGT-ACDISTHMTNNKgsAAWMAPEVFEGSK-YSEKCDVFSWGIILWEVITRRK- 188
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1013071061  793 PLKDktlIEKERF------YESRCRPVTPSC-KELADLMTRCMNYDPNQRPFFRAIMRDINKLEEQNP 853
Cdd:cd14058    189 PFDH---IGGPAFrimwavHNGERPPLIKNCpKPIESLMTRCWSKDPEKRPSMKEIVKIMSHLMQFFP 253
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
618-836 5.12e-21

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 93.81  E-value: 5.12e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  618 KVILKVLDP--SHRDISLAFFEA-ASMMRQVSHKHIVYLYGVcVRDVENI-MVEEFVEGGPLDLFMHRKSDvLTTPWKFK 693
Cdd:cd14014     27 PVAIKVLRPelAEDEEFRERFLReARALARLSHPNIVRVYDV-GEDDGRPyIVMEYVEGGSLADLLRERGP-LPPREALR 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  694 VAKQLASALSYLEDKDLVHGNVctK--NLLLAREGIdsecgpfIKLSDPGIpiTVLSRQECIER-------IPWIAPECV 764
Cdd:cd14014    105 ILAQIADALAAAHRAGIVHRDI--KpaNILLTEDGR-------VKLTDFGI--ARALGDSGLTQtgsvlgtPAYMAPEQA 173
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1013071061  765 EDsKNLSVAADKWSFGTTLWEIC-----YNGEIPLKDKTLIEKERFY-ESRCRPVTPscKELADLMTRCMNYDPNQRP 836
Cdd:cd14014    174 RG-GPVDPRSDIYSLGVVLYELLtgrppFDGDSPAAVLAKHLQEAPPpPSPLNPDVP--PALDAIILRALAKDPEERP 248
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
881-1154 5.18e-21

Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KSR1 functions as a transducer of TNFalpha-stimulated C-Raf activation of ERK1/2 and NF-kB. Detected activity of KSR1 is cell type specific and context dependent. It is inactive in normal colon epithelial cells and becomes activated at the onset of inflammatory bowel disease (IBD). Similarly, KSR1 activity is undetectable prior to stimulation by EGF or ceramide in COS-7 or YAMC cells, respectively. KSR proteins are widely regarded as pseudokinases, however, this matter is up for debate as catalytic activity has been detected for KSR1 in some systems. The KSR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 94.65  E-value: 5.18e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDPEgdntgeqVAVKSLkpESGGN---HIADLKKEIEILRNLYHENIVKYKGICTEDggNGIKLIME 957
Cdd:cd14152      8 IGQGRWGKVHRGRWHGE-------VAIRLL--EIDGNnqdHLKLFKKEVMNYRQTRHENVVLFMGACMHP--PHLAIITS 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  958 FLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESeHQVKIGDFGL---TKAIETDKEY 1034
Cdd:cd14152     77 FCKGRTLYSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVVITDFGLfgiSGVVQEGRRE 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1035 YTVKDDRDSpVFWYAPECLM---------QSKFYIASDVWSFGVTLHELLTYC-DSDSSPMALFLKMIGPTHGqmtVTRL 1104
Cdd:cd14152    156 NELKLPHDW-LCYLAPEIVRemtpgkdedCLPFSKAADVYAFGTIWYELQARDwPLKNQPAEALIWQIGSGEG---MKQV 231
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1105 VNTLKEGKrlpcppncpdEVYQLMRKCWEFQPSNRTSFQNLIEGFEALLK 1154
Cdd:cd14152    232 LTTISLGK----------EVTEILSACWAFDLEERPSFTLLMDMLEKLPK 271
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
870-1141 5.54e-21

Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mos (or c-Mos) is a germ-cell specific kinase that plays roles in both the release of primary arrest and the induction of secondary arrest in oocytes. It is expressed towards the end of meiosis I and is quickly degraded upon fertilization. It is a component of the cytostatic factor (CSF), which is responsible for metaphase II arrest. In addition, Mos activates a phoshorylation cascade that leads to the activation of the p34 subunit of MPF (mitosis-promoting factor or maturation promoting factor), a cyclin-dependent kinase that is responsible for the release of primary arrest in meiosis I. The Mos subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270881 [Multi-domain]  Cd Length: 265  Bit Score: 93.99  E-value: 5.54e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  870 FEKRFLKRirdLGEGHFGKVELCRYdpegdnTGEQVAVKSLKPESGGNHIAD-LKKEIEILrNLYHENIVKYKGICT-ED 947
Cdd:cd13979      3 EPLRLQEP---LGSGGFGSVYKATY------KGETVAVKIVRRRRKNRASRQsFWAELNAA-RLRHENIVRVLAAETgTD 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  948 GGNGIKLIMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKA 1027
Cdd:cd13979     73 FASLGLIIMEYCGNGTLQQLIYEGSEPLPLAHRILISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCSVK 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1028 IETdkeyYTVKDDRDSPV---FWY-APECLMQSKFYIASDVWSFGVTLHELLTycdsdsspmalflkMIGPTHGQMTVTr 1103
Cdd:cd13979    153 LGE----GNEVGTPRSHIggtYTYrAPELLKGERVTPKADIYSFGITLWQMLT--------------RELPYAGLRQHV- 213
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1013071061 1104 LVNTLKEGKRLPCPPNCPDEVYQ----LMRKCWEFQPSNRTS 1141
Cdd:cd13979    214 LYAVVAKDLRPDLSGLEDSEFGQrlrsLISRCWSAQPAERPN 255
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
872-1076 5.60e-21

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 95.60  E-value: 5.60e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  872 KRFLKRIRDLGEGHFGKVELCrYDpegDNTGEQVAVKSLKPESGGNHIADLK-------------KEIEILRNLYHENIV 938
Cdd:PTZ00024     8 ERYIQKGAHLGEGTYGKVEKA-YD---TLTGKIVAIKKVKIIEISNDVTKDRqlvgmcgihfttlRELKIMNEIKHENIM 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  939 KYKGICTEdgGNGIKLIMEFLpSGSLKEYLpknKNKINLKQQLKYAV--QICKGMDYLGSRQYVHRDLAARNVLVESEHQ 1016
Cdd:PTZ00024    84 GLVDVYVE--GDFINLVMDIM-ASDLKKVV---DRKIRLTESQVKCIllQILNGLNVLHKWYFMHRDLSPANIFINSKGI 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1013071061 1017 VKIGDFGLTKAI--------ETDKEYYTVKDDRDSPV--FWY-APECLMQS-KFYIASDVWSFGVTLHELLT 1076
Cdd:PTZ00024   158 CKIADFGLARRYgyppysdtLSKDETMQRREEMTSKVvtLWYrAPELLMGAeKYHFAVDMWSVGCIFAELLT 229
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
873-1147 6.19e-21

Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of yeast Kin1, Kin2, and similar proteins. Fission yeast Kin1 is a membrane-associated kinase that is involved in regulating cell surface cohesiveness during interphase. It also plays a role during mitosis, linking actomyosin ring assembly with septum synthesis and membrane closure to ensure separation of daughter cells. Budding yeast Kin1 and Kin2 act downstream of the Rab-GTPase Sec4 and are associated with the exocytic apparatus; they play roles in the secretory pathway. The Kin1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270979 [Multi-domain]  Cd Length: 267  Bit Score: 94.05  E-value: 6.19e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  873 RFLKRIrdlGEGHFGKVELCRYDpegdNTGEQVAVK--------SLKPESGGNHIADLKKEIEILRN------LYHENIV 938
Cdd:cd14077      4 EFVKTI---GAGSMGKVKLAKHI----RTGEKCAIKiiprasnaGLKKEREKRLEKEISRDIRTIREaalsslLNHPHIC 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  939 KYKGICTEDggNGIKLIMEFLPSGSLKEYLPKNkNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVK 1018
Cdd:cd14077     77 RLRDFLRTP--NHYYMLFEYVDGGQLLDYIISH-GKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIK 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1019 IGDFGLTKAIETDKEYYTVKddrdSPVFWYAPEcLMQSKFYIAS--DVWSFGVTLHELLTYC---DSDSSPMalflkmig 1093
Cdd:cd14077    154 IIDFGLSNLYDPRRLLRTFC----GSLYFAAPE-LLQAQPYTGPevDVWSFGVVLYVLVCGKvpfDDENMPA-------- 220
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1013071061 1094 pthgqmtvtrLVNTLKEGKrLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIE 1147
Cdd:cd14077    221 ----------LHAKIKKGK-VEYPSYLSSECKSLISRMLVVDPKKRATLEQVLN 263
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
589-848 7.99e-21

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The EphA2 receptor is overexpressed in tumor cells and tumor blood vessels in a variety of cancers including breast, prostate, lung, and colon. As a result, it is an attractive target for drug design since its inhibition could affect several aspects of tumor progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 133194 [Multi-domain]  Cd Length: 268  Bit Score: 93.50  E-value: 7.99e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  589 LGRGTRTHIYSGTLMdykddegTSEEKKIKVILKVLDPSHRDISLA-FFEAASMMRQVSHKHIVYLYGVCVRDVENIMVE 667
Cdd:cd05063     13 IGAGEFGEVFRGILK-------MPGRKEVAVAIKTLKPGYTEKQRQdFLSEASIMGQFSHHNIIRLEGVVTKFKPAMIIT 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  668 EFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLARegiDSECgpfiKLSDPGIPITVL 747
Cdd:cd05063     86 EYMENGALDKYLRDHDGEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNS---NLEC----KVSDFGLSRVLE 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  748 SRQECIE-----RIP--WIAPECVEDSKNLSvAADKWSFGTTLWEICYNGEIPLKDKTLIEKERFYESRCRPVTP-SC-K 818
Cdd:cd05063    159 DDPEGTYttsggKIPirWTAPEAIAYRKFTS-ASDVWSFGIVMWEVMSFGERPYWDMSNHEVMKAINDGFRLPAPmDCpS 237
                          250       260       270
                   ....*....|....*....|....*....|
gi 1013071061  819 ELADLMTRCMNYDPNQRPFFRAIMRDINKL 848
Cdd:cd05063    238 AVYQLMLQCWQQDRARRPRFVDIVNLLDKL 267
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
635-845 8.22e-21

Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Itk, also known as Tsk or Emt, is a member of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Itk contains the Tec homology (TH) domain containing one proline-rich region and a zinc-binding region. Itk is expressed in T-cells and mast cells, and is important in their development and differentiation. Of the three Tec kinases expressed in T-cells, Itk plays the predominant role in T-cell receptor (TCR) signaling. It is activated by phosphorylation upon TCR crosslinking and is involved in the pathway resulting in phospholipase C-gamma1 activation and actin polymerization. It also plays a role in the downstream signaling of the T-cell costimulatory receptor CD28, the T-cell surface receptor CD2, and the chemokine receptor CXCR4. In addition, Itk is crucial for the development of T-helper(Th)2 effector responses. The Itk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133243 [Multi-domain]  Cd Length: 256  Bit Score: 93.48  E-value: 8.22e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  635 FFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGN 714
Cdd:cd05112     46 FIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFMEHGCLSDYLRTQRGLFSAETLLGMCLDVCEGMAYLEEASVIHRD 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  715 VCTKNLLLAREGIdsecgpfIKLSDPGIPITVLSRQECIER-----IPWIAPECVEDSkNLSVAADKWSFGTTLWEICYN 789
Cdd:cd05112    126 LAARNCLVGENQV-------VKVSDFGMTRFVLDDQYTSSTgtkfpVKWSSPEVFSFS-RYSSKSDVWSFGVLMWEVFSE 197
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1013071061  790 GEIPLKDKT---LIEK----ERFYESRCRPvtpscKELADLMTRCMNYDPNQRPFFRAIMRDI 845
Cdd:cd05112    198 GKIPYENRSnseVVEDinagFRLYKPRLAS-----THVYEIMNHCWKERPEDRPSFSLLLRQL 255
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
879-1147 8.83e-21

Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Checkpoint Kinase 2 (Chk2) plays an important role in cellular responses to DNA double-strand breaks and related lesions. It is phosphorylated and activated by ATM kinase, resulting in its dissociation from sites of damage to phosphorylate downstream targets such as BRCA1, p53, cell cycle transcription factor E2F1, the promyelocytic leukemia protein (PML) involved in apoptosis, and CDC25 phosphatases, among others. Mutations in Chk2 is linked to a variety of cancers including familial breast cancer, myelodysplastic syndromes, prostate cancer, lung cancer, and osteosarcomas. Chk2 contains an N-terminal SQ/TQ cluster domain (SCD), a central forkhead-associated (FHA) domain, and a C-terminal catalytic kinase domain. The Chk2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270986 [Multi-domain]  Cd Length: 275  Bit Score: 93.61  E-value: 8.83e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGHFGKVELCrYDPEgdnTGEQVAVKSLKPE-------SGGNHIADLKKEIEILRNLYHENIVKYKGICTEDggNG 951
Cdd:cd14084     12 RTLGSGACGEVKLA-YDKS---TCKKVAIKIINKRkftigsrREINKPRNIETEIEILKKLSHPCIIKIEDFFDAE--DD 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  952 IKLIMEFLPSGslkEYLPKNKNKINLKQQLK--YAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQ---VKIGDFGLTK 1026
Cdd:cd14084     86 YYIVLELMEGG---ELFDRVVSNKRLKEAICklYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEEeclIKITDFGLSK 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1027 AIETDKEYYTvkddRDSPVFWYAPECLM---QSKFYIASDVWSFGVtlheLLTYCDSDSSPMAlflkmigpthGQMTVTR 1103
Cdd:cd14084    163 ILGETSLMKT----LCGTPTYLAPEVLRsfgTEGYTRAVDCWSLGV----ILFICLSGYPPFS----------EEYTQMS 224
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1013071061 1104 LVNTLKEGKRLPCPP---NCPDEVYQLMRKCWEFQPSNRTSFQNLIE 1147
Cdd:cd14084    225 LKEQILSGKYTFIPKawkNVSEEAKDLVKKMLVVDPSRRPSIEEALE 271
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
875-1147 9.58e-21

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MAPKKs are dual-specificity PKs that phosphorylate their downstream targets, MAPKs, at specific threonine and tyrosine residues. The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAPK, which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK or MAP2K), which itself is phosphorylated and activated by a MAPKK kinase (MAPKKK or MKKK or MAP3K). There are three MAPK subfamilies: extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38. In mammalian cells, there are seven MAPKKs (named MKK1-7) and 20 MAPKKKs. Each MAPK subfamily can be activated by at least two cognate MAPKKs and by multiple MAPKKKs. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270782 [Multi-domain]  Cd Length: 265  Bit Score: 93.18  E-value: 9.58e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  875 LKRIRDLGEGHFGKVELCRYDPegdnTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGngIKL 954
Cdd:cd06605      3 LEYLGELGEGNGGVVSKVRHRP----SGQIMAVKVIRLEIDEALQKQILRELDVLHKCNSPYIVGFYGAFYSEGD--ISI 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPSGSLKEYLpKNKNKINLKQQLKYAVQICKGMDYLGS-RQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKe 1033
Cdd:cd06605     77 CMEYMDGGSLDKIL-KEVGRIPERILGKIAVAVVKGLIYLHEkHKIIHRDVKPSNILVNSRGQVKLCDFGVSGQLVDSL- 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1034 yytVKDDRDSPVFwYAPECLMQSKFYIASDVWSFGVTLHELLT------YCDSDSSPMALFLkmigpthgqmtVTRLVNt 1107
Cdd:cd06605    155 ---AKTFVGTRSY-MAPERISGGKYTVKSDIWSLGLSLVELATgrfpypPPNAKPSMMIFEL-----------LSYIVD- 218
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1013071061 1108 lKEGKRLPCPPNCPDEVyQLMRKCWEFQPSNRTSFQNLIE 1147
Cdd:cd06605    219 -EPPPLLPSGKFSPDFQ-DFVSQCLQKDPTERPSYKELME 256
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
872-1074 9.69e-21

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. It may also regulate paxillin and consequently, cell migration. MST3 is present in human placenta, where it plays an essential role in the oxidative stress-induced apoptosis of trophoblasts in normal spontaneous delivery. Dysregulation of trophoblast apoptosis may result in pregnancy complications such as preeclampsia and intrauterine growth retardation. The MST3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270809 [Multi-domain]  Cd Length: 277  Bit Score: 93.60  E-value: 9.69e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  872 KRFLKRIRDLGEGHFGKVelcrYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDggNG 951
Cdd:cd06641      3 EELFTKLEKIGKGSFGEV----FKGIDNRTQKVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKD--TK 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  952 IKLIMEFLPSGSLKEYL-PKNKNKINLKQQLKyavQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIeT 1030
Cdd:cd06641     77 LWIIMEYLGGGSALDLLePGPLDETQIATILR---EILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQL-T 152
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1013071061 1031 DKEyyTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHEL 1074
Cdd:cd06641    153 DTQ--IKRN*FVGTPFWMAPEVIKQSAYDSKADIWSLGITAIEL 194
PTKc_Aatyk2 cd05086
Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs ...
878-1075 1.01e-20

Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk2 is a member of the Aatyk subfamily of proteins, which are receptor kinases containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk2 is also called lemur tyrosine kinase 2 (Lmtk2) or brain-enriched kinase (Brek). It is expressed at high levels in early postnatal brain, and has been shown to play a role in nerve growth factor (NGF) signaling. Studies with knockout mice reveal that Aatyk2 is essential for late stage spermatogenesis. Although it is classified as a PTK based on sequence similarity and the phylogenetic tree, Aatyk2 has been functionally characterized as a serine/threonine kinase. The Aatyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270669 [Multi-domain]  Cd Length: 271  Bit Score: 93.39  E-value: 1.01e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVELCryDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEdgGNGIKLIME 957
Cdd:cd05086      2 IQEIGNGWFGKVLLG--EIYTGTSVARVVVKELKASANPKEQDDFLQQGEPYYILQHPNILQCVGQCVE--AIPYLLVFE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  958 FLPSGSLKEYLPKNKNKINLKQQL----KYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAiETDKE 1033
Cdd:cd05086     78 FCDLGDLKTYLANQQEKLRGDSQImllqRMACEIAAGLAHMHKHNFLHSDLALRNCYLTSDLTVKVGDYGIGFS-RYKED 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1013071061 1034 YYTVKDDRDSPVFWYAPECL--MQSKFYIA-----SDVWSFGVTLHELL 1075
Cdd:cd05086    157 YIETDDKKYAPLRWTAPELVtsFQDGLLAAeqtkySNIWSLGVTLWELF 205
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
881-1075 1.03e-20

Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CCRK was previously called p42. It is a Cyclin-Dependent Kinase (CDK)-Activating Kinase (CAK) which is essential for the activation of CDK2. It is indispensable for cell growth and has been implicated in the progression of glioblastoma multiforme. In the heart, a splice variant of CCRK with a different C-terminal half is expressed; this variant promotes cardiac cell growth and survival and is significantly down-regulated during the development of heart failure. The CCRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270826 [Multi-domain]  Cd Length: 287  Bit Score: 93.93  E-value: 1.03e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVeLCRYDPEgdnTGEQVAVKSLKPESGGNHIA-DLKKEIEILRNL-YHENIVKYKGICTEdgGNGIKLIMEF 958
Cdd:cd07832      8 IGEGAHGIV-FKAKDRE---TGETVALKKVALRKLEGGIPnQALREIKALQACqGHPYVVKLRDVFPH--GTGFVLVFEY 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  959 LPSgSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTK--AIETDKEYYT 1036
Cdd:cd07832     82 MLS-SLSEVLRDEERPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLARlfSEEDPRLYSH 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1013071061 1037 VKDDRdspvfWY-APECLMQSKFYIAS-DVWSFGVTLHELL 1075
Cdd:cd07832    161 QVATR-----WYrAPELLYGSRKYDEGvDLWAVGCIFAELL 196
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
879-1084 1.08e-20

Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kin4 is a central component of the spindle position checkpoint (SPOC), which monitors spindle position and regulates the mitotic exit network (MEN). Kin4 associates with spindle pole bodies in mother cells to inhibit MEN signaling and delay mitosis until the anaphase nucleus is properly positioned along the mother-bud axis. Kin4 activity is regulated by both the bud neck-associated kinase Elm1 and protein phosphatase 2A. The Kin4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270978 [Multi-domain]  Cd Length: 270  Bit Score: 93.32  E-value: 1.08e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGHFGKVELCRYDPEGDNT-GEQVAVKSLKPESGGN--HIADLKKEIEILRNLYHENIVKYKGICTEDGGNGIklI 955
Cdd:cd14076      7 RTLGEGEFGKVKLGWPLPKANHRsGVQVAIKLIRRDTQQEncQTSKIMREINILKGLTHPNIVRLLDVLKTKKYIGI--V 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  956 MEFLPSGSLKEYLpKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYY 1035
Cdd:cd14076     85 LEFVSGGELFDYI-LARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANTFDHFNGDL 163
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1013071061 1036 tVKDDRDSPVFwYAPECLMQSKFYIAS--DVWSFGVTLHELLT-YCDSDSSP 1084
Cdd:cd14076    164 -MSTSCGSPCY-AAPELVVSDSMYAGRkaDIWSCGVILYAMLAgYLPFDDDP 213
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
876-1076 1.65e-20

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L1, also called PITSLRE, exists in different isoforms which are named using the alias CDK11(p). The CDC2L1 gene produces two protein products, CDK11(p110) and CDK11(p58). CDC2L1 is also represented by the caspase-processed CDK11(p46). CDK11(p110), the major isoform, associates with cyclin L and is expressed throughout the cell cycle. It is involved in RNA processing and the regulation of transcription. CDK11(p58) associates with cyclin D3 and is expressed during the G2/M phase of the cell cycle. It plays roles in spindle morphogenesis, centrosome maturation, sister chromatid cohesion, and the completion of mitosis. CDK11(p46) is formed from the larger isoforms by caspases during TNFalpha- and Fas-induced apoptosis. It functions as a downstream effector kinase in apoptotic signaling pathways and interacts with eukaryotic initiation factor 3f (eIF3f), p21-activated kinase (PAK1), and Ran-binding protein (RanBPM). CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 93.44  E-value: 1.65e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  876 KRIRDLGEGHFGKVelcrYDPEGDNTGEQVAVKSLK--PESGGNHIADLKkEIEILRNLYHENIVKYKGICTEDGGNGIK 953
Cdd:cd07843      8 EKLNRIEEGTYGVV----YRARDKKTGEIVALKKLKmeKEKEGFPITSLR-EINILLKLQHPNIVTVKEVVVGSNLDKIY 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  954 LIMEFLPSgSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKE 1033
Cdd:cd07843     83 MVMEYVEH-DLKSLMETMKQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGLAREYGSPLK 161
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1013071061 1034 YYTvkddrdSPV--FWY-APECLMQSKFY-IASDVWSFGVTLHELLT 1076
Cdd:cd07843    162 PYT------QLVvtLWYrAPELLLGAKEYsTAIDMWSVGCIFAELLT 202
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
878-1076 1.71e-20

Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. TSSK6, also called SSTK, is expressed at the head of elongated sperm. TSSK1/TSSK2 double knock-out and TSSK6 null mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270982 [Multi-domain]  Cd Length: 262  Bit Score: 92.63  E-value: 1.71e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVELCRYDPEGdnTGEQVAVKslkpesggnhIADLKK------------EIEILRNLYHENIVKYKGICT 945
Cdd:cd14080      5 GKTIGEGSYSKVKLAEYTKSG--LKEKVACK----------IIDKKKapkdflekflprELEILRKLRHPNIIQVYSIFE 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  946 EdgGNGIKLIMEFLPSGSLKEYLpKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLT 1025
Cdd:cd14080     73 R--GSKVFIFMEYAEHGDLLEYI-QKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGFA 149
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1026 KAIEtdkeyytvKDDRD--SPVF-----WYAPECLmQSKFYI--ASDVWSFGVTLHELLT 1076
Cdd:cd14080    150 RLCP--------DDDGDvlSKTFcgsaaYAAPEIL-QGIPYDpkKYDIWSLGVILYIMLC 200
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
881-1152 1.99e-20

Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TNNI3K, also called cardiac ankyrin repeat kinase (CARK), is a cardiac-specific troponin I-interacting kinase that promotes cardiac myogenesis, improves cardiac performance, and protects the myocardium from ischemic injury. It contains N-terminal ankyrin repeats, a catalytic kinase domain, and a C-terminal serine-rich domain. TNNI3K exerts a disease-accelerating effect on cardiac dysfunction and reduced survival in mouse models of cardiomyopathy. The TNNI3K subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270966 [Multi-domain]  Cd Length: 254  Bit Score: 92.21  E-value: 1.99e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYdpegdnTGEQVAVKSLKPESGG--NHIADLKKEIEILRNLYHENIVKYKGICTEDGGNgIKLIMEF 958
Cdd:cd14064      1 IGSGSFGKVYKGRC------RNKIVAIKRYRANTYCskSDVDMFCREVSILCRLNHPCVIQFVGACLDDPSQ-FAIVTQY 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  959 LPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLG--SRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYT 1036
Cdd:cd14064     74 VSGGSLFSLLHEQKRVIDLQSKLIIAVDVAKGMEYLHnlTQPIIHRDLNSHNILLYEDGHAVVADFGESRFLQSLDEDNM 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1037 VKddRDSPVFWYAPECLMQS-KFYIASDVWSFGVTLHELLTycdsDSSPMAlFLKMIGPThGQMTVTRLvntlkegkRLP 1115
Cdd:cd14064    154 TK--QPGNLRWMAPEVFTQCtRYSIKADVFSYALCLWELLT----GEIPFA-HLKPAAAA-ADMAYHHI--------RPP 217
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1013071061 1116 CPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEAL 1152
Cdd:cd14064    218 IGYSIPKPISSLLMRGWNAEPESRPSFVEIVALLEPC 254
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
878-1139 2.25e-20

Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of human MAK and MAK-related kinase (MRK), Saccharomyces cerevisiae Ime2p, Schizosaccharomyces pombe Mei4-dependent protein 3 (Mde3) and Pit1, Caenorhabditis elegans dyf-5, Arabidopsis thaliana MHK, and similar proteins. These proteins play important roles during meiosis. MAK is highly expressed in testicular cells specifically in the meiotic phase, but is not essential for spermatogenesis and fertility. It functions as a coactivator of the androgen receptor in prostate cells. MRK, also called Intestinal Cell Kinase (ICK), is expressed ubiquitously, with highest expression in the ovary and uterus. A missense mutation in MRK causes endocrine-cerebro-osteodysplasia, suggesting that this protein plays an important role in the development of many organs. MAK and MRK may be involved in regulating cell cycle and cell fate. Ime2p is a meiosis-specific kinase that is important during meiotic initiation and during the later stages of meiosis. Mde3 functions downstream of the transcription factor Mei-4 which is essential for meiotic prophase I. The MAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270824 [Multi-domain]  Cd Length: 283  Bit Score: 92.60  E-value: 2.25e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVELCRYDpegdNTGEQVAVKSLKPESggNHIADLK--KEIEILRNL-YHENIVKYKGICTEDggNGIKL 954
Cdd:cd07830      4 IKQLGDGTFGSVYLARNK----ETGELVAIKKMKKKF--YSWEECMnlREVKSLRKLnEHPNIVKLKEVFREN--DELYF 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPsGSLKEYLPKNKNKINLKQQLKYAV-QICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIetdke 1033
Cdd:cd07830     76 VFEYME-GNLYQLMKDRKGKPFSESVIRSIIyQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLAREI----- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1034 yytvkddRDSPVF-------WY-APECLMQSKFYIAS-DVWSFGVTLHELLTY-------CDSDSspmalFLKM---IG- 1093
Cdd:cd07830    150 -------RSRPPYtdyvstrWYrAPEILLRSTSYSSPvDIWALGCIMAELYTLrplfpgsSEIDQ-----LYKIcsvLGt 217
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1094 PTH-----GQmtvtRLVNTLkeGKRLP-CP--------PNCPDEVYQLMRKCWEFQPSNR 1139
Cdd:cd07830    218 PTKqdwpeGY----KLASKL--GFRFPqFAptslhqliPNASPEAIDLIKDMLRWDPKKR 271
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
876-1076 2.37e-20

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Pho85 is a multifunctional CDK in yeast. It is regulated by 10 different cyclins (Pcls) and plays a role in G1 progression, cell polarity, phosphate and glycogen metabolism, gene expression, and in signaling changes in the environment. It is not essential for yeast viability and is the functional homolog of mammalian CDK5, which plays a role in central nervous system development. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The Pho85 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143341 [Multi-domain]  Cd Length: 284  Bit Score: 92.54  E-value: 2.37e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  876 KRIRDLGEGHFGKVelcrYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVK-YKGICTEdggNGIKL 954
Cdd:cd07836      3 KQLEKLGEGTYATV----YKGRNRTTGEIVALKEIHLDAEEGTPSTAIREISLMKELKHENIVRlHDVIHTE---NKLML 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLpSGSLKEYLPKNKNKINLK-QQLKYAV-QICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDK 1032
Cdd:cd07836     76 VFEYM-DKDLKKYMDTHGVRGALDpNTVKSFTyQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLARAFGIPV 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1013071061 1033 EYYTvkddRDSPVFWY-APECLMQSKFYIAS-DVWSFGVTLHELLT 1076
Cdd:cd07836    155 NTFS----NEVVTLWYrAPDVLLGSRTYSTSiDIWSVGCIMAEMIT 196
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
618-838 2.56e-20

Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lyn is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lyn is expressed in B lymphocytes and myeloid cells. It exhibits both positive and negative regulatory roles in B cell receptor (BCR) signaling. Lyn, as well as Fyn and Blk, promotes B cell activation by phosphorylating ITAMs (immunoreceptor tyr activation motifs) in CD19 and in Ig components of BCR. It negatively regulates signaling by its unique ability to phosphorylate ITIMs (immunoreceptor tyr inhibition motifs) in cell surface receptors like CD22 and CD5. Lyn also plays an important role in G-CSF receptor signaling by phosphorylating a variety of adaptor molecules. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lyn subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 92.41  E-value: 2.56e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  618 KVILKVLDPSHRDISlAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMhrKSDV---LTTPWKFKV 694
Cdd:cd05072     33 KVAVKTLKPGTMSVQ-AFLEEANLMKTLQHDKLVRLYAVVTKEEPIYIITEYMAKGSLLDFL--KSDEggkVLLPKLIDF 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  695 AKQLASALSYLEDKDLVHGNVCTKNLLLAREGIdseCgpfiKLSDPGIPiTVLSRQECIER------IPWIAPECVeDSK 768
Cdd:cd05072    110 SAQIAEGMAYIERKNYIHRDLRAANVLVSESLM---C----KIADFGLA-RVIEDNEYTARegakfpIKWTAPEAI-NFG 180
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1013071061  769 NLSVAADKWSFGTTLWEICYNGEIPLKDKT----LIEKERFYEsrcRPVTPSC-KELADLMTRCMNYDPNQRPFF 838
Cdd:cd05072    181 SFTIKSDVWSFGILLYEIVTYGKIPYPGMSnsdvMSALQRGYR---MPRMENCpDELYDIMKTCWKEKAEERPTF 252
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
589-838 3.25e-20

Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes a subset of Src-like PTKs including Src, Fyn, Yrk, and Yes, which are all widely expressed. Yrk has been detected only in chickens. It is primarily found in neuronal and epithelial cells and in macrophages. It may play a role in inflammation and in response to injury. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. They are also implicated in acute inflammatory responses and osteoclast function. The Src/Fyn-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 91.52  E-value: 3.25e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  589 LGRGTRTHIYSGTLmdykddEGTSeekkiKVILKVLDPSHRDISlAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEE 668
Cdd:cd14203      3 LGQGCFGEVWMGTW------NGTT-----KVAIKTLKPGTMSPE-AFLEEAQIMKKLRHDKLVQLYAVVSEEPIYIVTEF 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  669 FVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIdseCgpfiKLSDPGIPITV-- 746
Cdd:cd14203     71 MSKGSLLDFLKDGEGKYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLV---C----KIADFGLARLIed 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  747 ---LSRQECIERIPWIAPECVEDSKnLSVAADKWSFGTTLWEICYNGEIP---LKDKTLIEK-ERFYESRCRPVTPSckE 819
Cdd:cd14203    144 neyTARQGAKFPIKWTAPEAALYGR-FTIKSDVWSFGILLTELVTKGRVPypgMNNREVLEQvERGYRMPCPPGCPE--S 220
                          250
                   ....*....|....*....
gi 1013071061  820 LADLMTRCMNYDPNQRPFF 838
Cdd:cd14203    221 LHELMCQCWRKDPEERPTF 239
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
635-848 3.25e-20

Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Abl (or c-Abl) is a ubiquitously-expressed cytoplasmic (or nonreceptor) PTK that contains SH3, SH2, and tyr kinase domains in its N-terminal region, as well as nuclear localization motifs, a putative DNA-binding domain, and F- and G-actin binding domains in its C-terminal tail. It also contains a short autoinhibitory cap region in its N-terminus. Abl function depends on its subcellular localization. In the cytoplasm, Abl plays a role in cell proliferation and survival. In response to DNA damage or oxidative stress, Abl is transported to the nucleus where it induces apoptosis. In chronic myelogenous leukemia (CML) patients, an aberrant translocation results in the replacement of the first exon of Abl with the BCR (breakpoint cluster region) gene. The resulting BCR-Abl fusion protein is constitutively active and associates into tetramers, resulting in a hyperactive kinase sending a continuous signal. This leads to uncontrolled proliferation, morphological transformation and anti-apoptotic effects. BCR-Abl is the target of selective inhibitors, such as imatinib (Gleevec), used in the treatment of CML. Abl2, also known as ARG (Abelson-related gene), is thought to play a cooperative role with Abl in the proper development of the nervous system. The Tel-ARG fusion protein, resulting from reciprocal translocation between chromosomes 1 and 12, is associated with acute myeloid leukemia (AML). The TEL gene is a frequent fusion partner of other tyr kinase oncogenes, including Tel/Abl, Tel/PDGFRbeta, and Tel/Jak2, found in patients with leukemia and myeloproliferative disorders. The Abl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 91.71  E-value: 3.25e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  635 FFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFV-EGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHG 713
Cdd:cd05052     49 FLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMpYGNLLDYLRECNREELNAVVLLYMATQIASAMEYLEKKNFIHR 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  714 NVCTKNLLLAREGIdsecgpfIKLSDPGIPI-----TVLSRQECIERIPWIAPECVEDSKnLSVAADKWSFGTTLWEICY 788
Cdd:cd05052    129 DLAARNCLVGENHL-------VKVADFGLSRlmtgdTYTAHAGAKFPIKWTAPESLAYNK-FSIKSDVWAFGVLLWEIAT 200
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1013071061  789 NGEIPLKDKTLIEK----ERFYESRCRPVTPSckELADLMTRCMNYDPNQRPFFRAIMRDINKL 848
Cdd:cd05052    201 YGMSPYPGIDLSQVyellEKGYRMERPEGCPP--KVYELMRACWQWNPSDRPSFAEIHQALETM 262
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
876-1145 3.31e-20

Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Nak1, Saccharomyces cerevisiae Kic1p (kinase that interacts with Cdc31p) and related proteins. Nak1 (also called N-rich kinase 1), is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Kic1p is required by budding yeast for cell integrity and morphogenesis. Kic1p interacts with Cdc31p, the yeast homologue of centrin, and phosphorylates substrates in a Cdc31p-dependent manner. The Nak1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 92.15  E-value: 3.31e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  876 KRIRDLGEGHFGKVelcrYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYH---ENIVKYKGiCTEDGGNgI 952
Cdd:cd06917      4 RRLELVGRGSYGAV----YRGYHVKTGRVVALKVLNLDTDDDDVSDIQKEVALLSQLKLgqpKNIIKYYG-SYLKGPS-L 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  953 KLIMEFLPSGSLKEYLPKNKnkinLKQqlKYAVQICK----GMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTK-- 1026
Cdd:cd06917     78 WIIMDYCEGGSIRTLMRAGP----IAE--RYIAVIMRevlvALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAAsl 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1027 AIETDKEYYTVkddrDSPvFWYAPECLMQSKFY-IASDVWSFGVTLHELLTycdsDSSPMAlflkmigpTHGQMTVTRLV 1105
Cdd:cd06917    152 NQNSSKRSTFV----GTP-YWMAPEVITEGKYYdTKADIWSLGITTYEMAT----GNPPYS--------DVDALRAVMLI 214
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1013071061 1106 NTLKegkrlpcPPNCPDEVYQ-LMRK----CWEFQPSNRTSFQNL 1145
Cdd:cd06917    215 PKSK-------PPRLEGNGYSpLLKEfvaaCLDEEPKDRLSADEL 252
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
881-1141 3.59e-20

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type I Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of type I receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation through trans-phosphorylation by type II receptors, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. They are inhibited by the immunophilin FKBP12, which is thought to control leaky signaling caused by receptor oligomerization in the absence of ligand. The TGFbR-I subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 92.34  E-value: 3.59e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYdpegdnTGEQVAVK---SLKPESggnhiadLKKEIEILRN--LYHENIVKYKG--ICTEDGGNGIK 953
Cdd:cd14056      3 IGKGRYGEVWLGKY------RGEKVAVKifsSRDEDS-------WFRETEIYQTvmLRHENILGFIAadIKSTGSWTQLW 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  954 LIMEFLPSGSLKEYLpkNKNKINLKQQLKYAVQICKGMDYL-----GSR---QYVHRDLAARNVLVESEHQVKIGDFGLt 1025
Cdd:cd14056     70 LITEYHEHGSLYDYL--QRNTLDTEEALRLAYSAASGLAHLhteivGTQgkpAIAHRDLKSKNILVKRDGTCCIADLGL- 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1026 kAIETDKEYYTVKDDRDSPV---FWYAPECLMQS----KF--YIASDVWSFGVTLHELLTYCDSDS--SPMAL-FLKMIG 1093
Cdd:cd14056    147 -AVRYDSDTNTIDIPPNPRVgtkRYMAPEVLDDSinpkSFesFKMADIYSFGLVLWEIARRCEIGGiaEEYQLpYFGMVP 225
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1013071061 1094 --PTHGQMtvTRLVNTlkEGKRLPCPP---NCP--DEVYQLMRKCWEFQPSNRTS 1141
Cdd:cd14056    226 sdPSFEEM--RKVVCV--EKLRPPIPNrwkSDPvlRSMVKLMQECWSENPHARLT 276
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
617-838 4.36e-20

Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, and Yes. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, and Lyn show a limited expression pattern. The Src-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270630 [Multi-domain]  Cd Length: 248  Bit Score: 90.80  E-value: 4.36e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  617 IKVILKVLDPSHRDISlAFFEAASMMRQVSHKHIVYLYGVCVrDVENI-MVEEFVEGGPL-DLFMHRKSDVLTTPWKFKV 694
Cdd:cd05034     20 TKVAVKTLKPGTMSPE-AFLQEAQIMKKLRHDKLVQLYAVCS-DEEPIyIVTELMSKGSLlDYLRTGEGRALRLPQLIDM 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  695 AKQLASALSYLEDKDLVHGNVCTKNLLLARegidsecGPFIKLSDPGipitvLSR--QECI------ERIP--WIAPECV 764
Cdd:cd05034     98 AAQIASGMAYLESRNYIHRDLAARNILVGE-------NNVCKVADFG-----LARliEDDEytaregAKFPikWTAPEAA 165
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1013071061  765 EDSKnLSVAADKWSFGTTLWEICYNGEIP---LKDKTLIEK-ERFYESRCRPVTPSckELADLMTRCMNYDPNQRPFF 838
Cdd:cd05034    166 LYGR-FTIKSDVWSFGILLYEIVTYGRVPypgMTNREVLEQvERGYRMPKPPGCPD--ELYDIMLQCWKKEPEERPTF 240
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
881-1152 4.54e-20

Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. C-Raf, also known as Raf-1 or c-Raf-1, is ubiquitously expressed and was the first Raf identified. It was characterized as the acquired oncogene from an acutely transforming murine sarcoma virus (3611-MSV) and the transforming agent from the avian retrovirus MH2. C-Raf-deficient mice embryos die around midgestation with increased apoptosis of embryonic tissues, especially in the fetal liver. One of the main functions of C-Raf is restricting caspase activation to promote survival in response to specific stimuli such as Fas stimulation, macrophage apoptosis, and erythroid differentiation. C-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The C-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 92.02  E-value: 4.54e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYdpEGDntgeqVAVKSLK-----PEsggnHIADLKKEIEILRNLYHENIVKYKGICTEDGgngIKLI 955
Cdd:cd14149     20 IGSGSFGTVYKGKW--HGD-----VAVKILKvvdptPE----QFQAFRNEVAVLRKTRHVNILLFMGYMTKDN---LAIV 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  956 MEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTkaieTDKEYY 1035
Cdd:cd14149     86 TQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLA----TVKSRW 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1036 TVKDDRDSP---VFWYAPECL-MQ--SKFYIASDVWSFGVTLHELLT----YCDSDSSPMALFlkMIGPTHGQMTVTRLV 1105
Cdd:cd14149    162 SGSQQVEQPtgsILWMAPEVIrMQdnNPFSFQSDVYSYGIVLYELMTgelpYSHINNRDQIIF--MVGRGYASPDLSKLY 239
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1013071061 1106 NtlkegkrlpcppNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEAL 1152
Cdd:cd14149    240 K------------NCPKAMKRLVADCIKKVKEERPLFPQILSSIELL 274
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
878-1089 7.01e-20

Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAP4K3, MAP4K1, MAP4K2, MAP4K5, and related proteins. Vertebrate members contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K1, also called haematopoietic progenitor kinase 1 (HPK1), is a hematopoietic-specific STK involved in many cellular signaling cascades including MAPK, antigen receptor, apoptosis, growth factor, and cytokine signaling. It participates in the regulation of T cell receptor signaling and T cell-mediated immune responses. MAP4K2 was referred to as germinal center (GC) kinase because of its preferred location in GC B cells. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. It is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). The MAP4K3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 90.83  E-value: 7.01e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVelcrYDPEGDNTGEQVAVKSLKPESGGNhIADLKKEIEILRNLYHENIVKYKGicTEDGGNGIKLIME 957
Cdd:cd06613      5 IQRIGSGTYGDV----YKARNIATGELAAVKVIKLEPGDD-FEIIQQEISMLKECRHPNIVAYFG--SYLRRDKLWIVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  958 FLPSGSLKEYLpkNKNKINLKQQLKYavqIC----KGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETdke 1033
Cdd:cd06613     78 YCGGGSLQDIY--QVTGPLSELQIAY---VCretlKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSAQLTA--- 149
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1013071061 1034 yyTVKdDRDSPV---FWYAPECL---MQSKFYIASDVWSFGVTLHEL--LTYCDSDSSPM-ALFL 1089
Cdd:cd06613    150 --TIA-KRKSFIgtpYWMAPEVAaveRKGGYDGKCDIWALGITAIELaeLQPPMFDLHPMrALFL 211
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
578-847 8.08e-20

Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Trk subfamily consists of TrkA, TrkB, TrkC, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, the nerve growth factor (NGF) family of neutrotrophins, leads to Trk receptor oligomerization and activation of the catalytic domain. Trk receptors are mainly expressed in the peripheral and central nervous systems. They play important roles in cell fate determination, neuronal survival and differentiation, as well as in the regulation of synaptic plasticity. Altered expression of Trk receptors is associated with many human diseases. The Trk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 90.99  E-value: 8.08e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  578 ILKKDLVQGEHLGRGTRTHIYSGTLMDYKddegtSEEKKIKVILKVL-DPSHRDISLAFFEAASMMRQVSHKHIVYLYGV 656
Cdd:cd05049      2 IKRDTIVLKRELGEGAFGKVFLGECYNLE-----PEQDKMLVAVKTLkDASSPDARKDFEREAELLTNLQHENIVKFYGV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  657 CVRDVENIMVEEFVEGGPLDLFMHR---------KSDVLTTPWK----FKVAKQLASALSYLEDKDLVHGNVCTKNLLLA 723
Cdd:cd05049     77 CTEGDPLLMVFEYMEHGDLNKFLRShgpdaaflaSEDSAPGELTlsqlLHIAVQIASGMVYLASQHFVHRDLATRNCLVG 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  724 regidseCGPFIKLSDPGIPITVLS----RQECIERIP--WIAPECVEDSKnLSVAADKWSFGTTLWEICYNGEIP---L 794
Cdd:cd05049    157 -------TNLVVKIGDFGMSRDIYStdyyRVGGHTMLPirWMPPESILYRK-FTTESDVWSFGVVLWEIFTYGKQPwfqL 228
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1013071061  795 KDKTLIE--KERFYESRCRPVTPsckELADLMTRCMNYDPNQRPFFRAIMRDINK 847
Cdd:cd05049    229 SNTEVIEciTQGRLLQRPRTCPS---EVYAVMLGCWKREPQQRLNIKDIHKRLQE 280
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
614-848 8.32e-20

Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of most class EphA receptors including EphA3, EphA4, EphA5, and EphA7, but excluding EphA1, EphA2 and EphA10. Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. One exception is EphA4, which also binds ephrins-B2/B3. EphA receptors and ephrin-A ligands are expressed in multiple areas of the developing brain, especially in the retina and tectum. They are part of a system controlling retinotectal mapping. EphRs comprise the largest subfamily of receptor PTKs (RTKs). EphRs contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 90.70  E-value: 8.32e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  614 EKKIKVILKVL-----DPSHRDislaFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSDVLTT 688
Cdd:cd05066     30 KREIPVAIKTLkagytEKQRRD----FLSEASIMGQFDHPNIIHLEGVVTRSKPVMIVTEYMENGSLDAFLRKHDGQFTV 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  689 PWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLlaregIDSECgpFIKLSDPGIPITVLSRQECIE-----RIP--WIAP 761
Cdd:cd05066    106 IQLVGMLRGIASGMKYLSDMGYVHRDLAARNIL-----VNSNL--VCKVSDFGLSRVLEDDPEAAYttrggKIPirWTAP 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  762 ECVEDSKnLSVAADKWSFGTTLWEICYNGEIPLKDKTLIEKERFYESRCR-PVTPSCK-ELADLMTRCMNYDPNQRPFFR 839
Cdd:cd05066    179 EAIAYRK-FTSASDVWSYGIVMWEVMSYGERPYWEMSNQDVIKAIEEGYRlPAPMDCPaALHQLMLDCWQKDRNERPKFE 257

                   ....*....
gi 1013071061  840 AIMRDINKL 848
Cdd:cd05066    258 QIVSILDKL 266
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
882-1076 1.01e-19

Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK36, also called Fused (or Fu) kinase, is involved in the Hedgehog signaling pathway. It is activated by the Smoothened (SMO) signal transducer, resulting in the stabilization of GLI transcription factors and the phosphorylation of SUFU to facilitate the nuclear accumulation of GLI. In Drosophila, Fused kinase is maternally required for proper segmentation during embryonic development and for the development of legs and wings during the larval stage. In mice, STK36 is not necessary for embryonic development, although mice deficient in STK36 display growth retardation postnatally. The STK36 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270904 [Multi-domain]  Cd Length: 253  Bit Score: 90.00  E-value: 1.01e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  882 GEGHFGKVelcrYDPEGDNTGEQVAVKSLkPESGGN--HIADLKKEIEILRNLYHENIVK-YKGICTEdggNGIKLIMEF 958
Cdd:cd14002     10 GEGSFGKV----YKGRRKYTGQVVALKFI-PKRGKSekELRNLRQEIEILRKLNHPNIIEmLDSFETK---KEFVVVTEY 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  959 lPSGSLKEYLPKNKNkINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYT-V 1037
Cdd:cd14002     82 -AQGELFQILEDDGT-LPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFARAMSCNTLVLTsI 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1013071061 1038 KddrDSPVFwYAPEcLMQSKFY-IASDVWSFGVTLHELLT 1076
Cdd:cd14002    160 K---GTPLY-MAPE-LVQEQPYdHTADLWSLGCILYELFV 194
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
874-1147 1.14e-19

Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It acts as a MAPK kinase kinase by phosphorylating ASK1, resulting in the phosphorylation of p38. SLK also plays a role in mediating actin reorganization. It is part of a microtubule-associated complex that is targeted at adhesion sites, and is required in focal adhesion turnover and in regulating cell migration. The SLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 90.47  E-value: 1.14e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  874 FLKRIRDLGEGHFGKVelcrYDPEGDNTGEQVAVKSLKPESGgNHIADLKKEIEILRNLYHENIVKYKGICTEDggNGIK 953
Cdd:cd06643      6 FWEIVGELGDGAFGKV----YKAQNKETGILAAAKVIDTKSE-EELEDYMVEIDILASCDHPNIVKLLDAFYYE--NNLW 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  954 LIMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKaietdKE 1033
Cdd:cd06643     79 ILIEFCAGGAVDAVMLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSA-----KN 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1034 YYTVKdDRDSPV---FWYAPECLM--QSK---FYIASDVWSFGVTLHElltycdsdsspmalfLKMIGPTHGQMTVTRLV 1105
Cdd:cd06643    154 TRTLQ-RRDSFIgtpYWMAPEVVMceTSKdrpYDYKADVWSLGVTLIE---------------MAQIEPPHHELNPMRVL 217
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1013071061 1106 ntLKEGKRLP----CPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIE 1147
Cdd:cd06643    218 --LKIAKSEPptlaQPSRWSPEFKDFLRKCLEKNVDARWTTSQLLQ 261
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
875-1073 1.16e-19

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 92.19  E-value: 1.16e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  875 LKRIRDLGEGHFGKVELCRYDPegdnTGEQVAVKSLKpesgGNHIADLK----KEIEILRNLYHENIVKYKGIctEDGGN 950
Cdd:PLN00034    76 LERVNRIGSGAGGTVYKVIHRP----TGRLYALKVIY----GNHEDTVRrqicREIEILRDVNHPNVVKCHDM--FDHNG 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  951 GIKLIMEFLPSGSLKeylpknKNKINLKQQLK-YAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIE 1029
Cdd:PLN00034   146 EIQVLLEFMDGGSLE------GTHIADEQFLAdVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRILA 219
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1013071061 1030 tdkeyyTVKDDRDSPV---FWYAPEC----LMQSKF--YiASDVWSFGVTLHE 1073
Cdd:PLN00034   220 ------QTMDPCNSSVgtiAYMSPERintdLNHGAYdgY-AGDIWSLGVSILE 265
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
614-848 1.31e-19

Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EphB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphB receptors play important roles in synapse formation and plasticity, spine morphogenesis, axon guidance, and angiogenesis. In the intestinal epithelium, EphBs are Wnt signaling target genes that control cell compartmentalization. They function as suppressors of colon cancer progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion. The EphB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 90.31  E-value: 1.31e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  614 EKKIKVILKVL-----DPSHRDislaFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSDVLTT 688
Cdd:cd05065     30 KREIFVAIKTLksgytEKQRRD----FLSEASIMGQFDHPNIIHLEGVVTKSRPVMIITEFMENGALDSFLRQNDGQFTV 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  689 PWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGI----DSECGPFIK--LSDPgipiTVLSRQECIERIPWIAPE 762
Cdd:cd05065    106 IQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVckvsDFGLSRFLEddTSDP----TYTSSLGGKIPIRWTAPE 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  763 CVEDSKNLSvAADKWSFGTTLWEICYNGEIPLKDKTLIEKERFYESRCR-PVTPSCKE-LADLMTRCMNYDPNQRPFFRA 840
Cdd:cd05065    182 AIAYRKFTS-ASDVWSYGIVMWEVMSYGERPYWDMSNQDVINAIEQDYRlPPPMDCPTaLHQLMLDCWQKDRNLRPKFGQ 260

                   ....*...
gi 1013071061  841 IMRDINKL 848
Cdd:cd05065    261 IVNTLDKM 268
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
618-844 1.36e-19

Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lck and Blk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lck is expressed in T-cells and natural killer cells. It plays a critical role in T-cell maturation, activation, and T-cell receptor (TCR) signaling. Lck phosphorylates ITAM (immunoreceptor tyr activation motif) sequences on several subunits of TCRs, leading to the activation of different second messenger cascades. Phosphorylated ITAMs serve as binding sites for other signaling factor such as Syk and ZAP-70, leading to their activation and propagation of downstream events. In addition, Lck regulates drug-induced apoptosis by interfering with the mitochondrial death pathway. The apototic role of Lck is independent of its primary function in T-cell signaling. Blk is expressed specifically in B-cells. It is involved in pre-BCR (B-cell receptor) signaling. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lck/Blk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 89.95  E-value: 1.36e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  618 KVILKVLDPSHRDISlAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQ 697
Cdd:cd05067     33 KVAIKSLKQGSMSPD-AFLAEANLMKQLQHQRLVRLYAVVTQEPIYIITEYMENGSLVDFLKTPSGIKLTINKLLDMAAQ 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  698 LASALSYLEDKDLVHGNVCTKNLLLAREgidSECgpfiKLSDPGIPiTVLSRQECIER------IPWIAPECVeDSKNLS 771
Cdd:cd05067    112 IAEGMAFIEERNYIHRDLRAANILVSDT---LSC----KIADFGLA-RLIEDNEYTARegakfpIKWTAPEAI-NYGTFT 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  772 VAADKWSFGTTLWEICYNGEIPLKDKT---LIEK-ERFYESRCRPVTPscKELADLMTRCMNYDPNQRP---FFRAIMRD 844
Cdd:cd05067    183 IKSDVWSFGILLTEIVTHGRIPYPGMTnpeVIQNlERGYRMPRPDNCP--EELYQLMRLCWKERPEDRPtfeYLRSVLED 260
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
635-841 1.50e-19

Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR-like proteins are members of the DDR subfamily, which are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 90.42  E-value: 1.50e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  635 FFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRK-----------------SDVLttpwkfKVAKQ 697
Cdd:cd05097     64 FLKEIKIMSRLKNPNIIRLLGVCVSDDPLCMITEYMENGDLNQFLSQReiestfthannipsvsiANLL------YMAVQ 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  698 LASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGIPITVLS------RQECIERIPWIAPECVEDSKnLS 771
Cdd:cd05097    138 IASGMKYLASLNFVHRDLATRNCLVGNHYT-------IKIADFGMSRNLYSgdyyriQGRAVLPIRWMAWESILLGK-FT 209
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  772 VAADKWSFGTTLWEI---CynGEIP---LKDKTLIEKE-RFYESRCRPV----TPSC-KELADLMTRCMNYDPNQRPFFR 839
Cdd:cd05097    210 TASDVWAFGVTLWEMftlC--KEQPyslLSDEQVIENTgEFFRNQGRQIylsqTPLCpSPVFKLMMRCWSRDIKDRPTFN 287

                   ..
gi 1013071061  840 AI 841
Cdd:cd05097    288 KI 289
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
877-1147 1.53e-19

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek1 is associated with centrosomes throughout the cell cycle. It is involved in the formation of primary cilium and in the maintenance of centrosomes. It cycles through the nucleus and may be capable of relaying signals between the cilium and the nucleus. Nek1 is implicated in the development of polycystic kidney disease, which is characterized by benign polycystic tumors formed by abnormal overgrowth of renal epithelial cells. It appears also to be involved in DNA damage response, and may be important for both correct DNA damage checkpoint activation and DNA repair. Nek1 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 89.48  E-value: 1.53e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  877 RIRDLGEGHFGKVELCRYDpegdNTGEQVAVKSLK-PESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGngIKLI 955
Cdd:cd08218      4 RIKKIGEGSFGKALLVKSK----EDGKQYVIKEINiSKMSPKEREESRKEVAVLSKMKHPNIVQYQESFEENGN--LYIV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  956 MEFLPSGSLKEYLPKNKNKINLKQQ-LKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETdkey 1034
Cdd:cd08218     78 MDYCDGGDLYKRINAQRGVLFPEDQiLDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARVLNS---- 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1035 yTVKDDRD---SPvFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDS-DSSPMA-LFLKMIgpthgqmtvtrlvntlk 1109
Cdd:cd08218    154 -TVELARTcigTP-YYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAfEAGNMKnLVLKII----------------- 214
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1013071061 1110 EGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIE 1147
Cdd:cd08218    215 RGSYPPVPSRYSYDLRSLVSQLFKRNPRDRPSINSILE 252
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
641-844 1.85e-19

Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent Protein Kinase Kinase, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Both LKB1 and CaMKKs can phosphorylate and activate AMP-activated protein kinase (AMPK). LKB1, also called STK11, serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMPK. Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The LKB1/CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 89.53  E-value: 1.85e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  641 MMRQVSHKHIVYLYGVcVRDVEN---IMVEEFVEGGPLdlfMHRKSD----VLTTPWKFKVAKQLASALSYLEDKDLVHG 713
Cdd:cd14008     57 IMKKLDHPNIVRLYEV-IDDPESdklYLVLEYCEGGPV---MELDSGdrvpPLPEETARKYFRDLVLGLEYLHENGIVHR 132
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  714 NVCTKNLLLAREGIdsecgpfIKLSDPGIPITVLSRQECIERIP----WIAPE-CVEDSKNLSV-AADKWSFGTTLWEIC 787
Cdd:cd14008    133 DIKPENLLLTADGT-------VKISDFGVSEMFEDGNDTLQKTAgtpaFLAPElCDGDSKTYSGkAADIWALGVTLYCLV 205
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1013071061  788 YnGEIPLKDKTL------IEKERFYESRCRPVTPsckELADLMTRCMNYDPNQRPFFRAIMRD 844
Cdd:cd14008    206 F-GRLPFNGDNIlelyeaIQNQNDEFPIPPELSP---ELKDLLRRMLEKDPEKRITLKEIKEH 264
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
922-1145 2.99e-19

Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-A binds and is activated by the atrial and B-type natriuretic peptides, ANP and BNP, which are important in blood pressure regulation and cardiac pathophysiology. GC-B binds the C-type natriuretic peptide, CNP, which is a potent vasorelaxant and functions in vascular remodeling and bone growth regulation. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-A/B subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270944 [Multi-domain]  Cd Length: 279  Bit Score: 89.19  E-value: 2.99e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  922 LKKEIEILRNLYHENIVKYKGICTeDGGNgIKLIMEFLPSGSLKEYLpKNKNkINLKQQLKYAV--QICKGMDYLGSRQY 999
Cdd:cd14042     49 VLKELKHMRDLQHDNLTRFIGACV-DPPN-ICILTEYCPKGSLQDIL-ENED-IKLDWMFRYSLihDIVKGMHYLHDSEI 124
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1000 V-HRDLAARNVLVESEHQVKIGDFGLTKAIETDK------EYYTVKddrdspvFWYAPECLMQSkfYIAS------DVWS 1066
Cdd:cd14042    125 KsHGNLKSSNCVVDSRFVLKITDFGLHSFRSGQEppddshAYYAKL-------LWTAPELLRDP--NPPPpgtqkgDVYS 195
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1067 FGVTLHELLT------YCDSDSSPMalflkmigpthgQMTVTRLVNTLKEGKRLPCPPN-CPDEVYQLMRKCWEFQPSNR 1139
Cdd:cd14042    196 FGIILQEIATrqgpfyEEGPDLSPK------------EIIKKKVRNGEKPPFRPSLDELeCPDEVLSLMQRCWAEDPEER 263

                   ....*.
gi 1013071061 1140 TSFQNL 1145
Cdd:cd14042    264 PDFSTL 269
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
878-1146 3.31e-19

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek3 is primarily localized in the cytoplasm and shows no cell cycle-dependent changes in its activity. It is present in the axons of neurons and affects morphogenesis and polarity through its regulation of microtubule acetylation. Nek3 modulates the signaling of the prolactin receptor through its activation of Vav2 and contributes to prolactin-mediated motility of breast cancer cells. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 88.49  E-value: 3.31e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVELCRYDpegdNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGngIKLIME 957
Cdd:cd08219      5 LRVVGEGSFGRALLVQHV----NSDQKYAMKEIRLPKSSSAVEDSRKEAVLLAKMKHPNIVAFKESFEADGH--LYIVME 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  958 FLPSGSLKEYLPKNKNKINLKQQ-LKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYT 1036
Cdd:cd08219     79 YCDGGDLMQKIKLQRGKLFPEDTiLQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLTSPGAYAC 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1037 VKddRDSPvFWYAPECLMQSKFYIASDVWSFGVTLHELLT--YCDSDSSPMALFLKMIgpthgqmtvtrlvntlkEGKRL 1114
Cdd:cd08219    159 TY--VGTP-YYVPPEIWENMPYNNKSDIWSLGCILYELCTlkHPFQANSWKNLILKVC-----------------QGSYK 218
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1013071061 1115 PCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLI 1146
Cdd:cd08219    219 PLPSHYSYELRSLIKQMFKRNPRSRPSATTIL 250
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
578-853 3.56e-19

Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Mer (or Mertk) is named after its original reported expression pattern (monocytes, epithelial, and reproductive tissues). It is required for the ingestion of apoptotic cells by phagocytes such as macrophages, retinal pigment epithelial cells, and dendritic cells. Mer is also important in maintaining immune homeostasis. Mer is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Mer subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271106 [Multi-domain]  Cd Length: 284  Bit Score: 89.22  E-value: 3.56e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  578 ILKKDLVQGEHLGRGTRTHIYSGTLmdyKDDEGTSEEKKIKViLKVLDPSHRDISlAFFEAASMMRQVSHKHIVYLYGVC 657
Cdd:cd14204      4 IDRNLLSLGKVLGEGEFGSVMEGEL---QQPDGTNHKVAVKT-MKLDNFSQREIE-EFLSEAACMKDFNHPNVIRLLGVC 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  658 V-----RDVENIMVEEFVEGGPLDLFMHR-------KSDVLTTPWKFKVakQLASALSYLEDKDLVHGNVCTKNLLLaRE 725
Cdd:cd14204     79 LevgsqRIPKPMVILPFMKYGDLHSFLLRsrlgsgpQHVPLQTLLKFMI--DIALGMEYLSSRNFLHRDLAARNCML-RD 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  726 GIdSECgpfikLSDPGIPITVLS----RQECIERIP--WIAPECVEDsKNLSVAADKWSFGTTLWEICYNGEIPLKDktl 799
Cdd:cd14204    156 DM-TVC-----VADFGLSKKIYSgdyyRQGRIAKMPvkWIAVESLAD-RVYTVKSDVWAFGVTMWEIATRGMTPYPG--- 225
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1013071061  800 IEKERFYE-----SRCRPVTPSCKELADLMTRCMNYDPNQRPFFRAIMRDINKLEEQNP 853
Cdd:cd14204    226 VQNHEIYDyllhgHRLKQPEDCLDELYDIMYSCWRSDPTDRPTFTQLRENLEKLLESLP 284
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
634-847 3.62e-19

Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Chk is also referred to as megakaryocyte-associated tyrosine kinase (Matk). Chk inhibits Src kinases using a noncatalytic mechanism by simply binding to them. As a negative regulator of Src kinases, Chk may play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Chk is expressed in brain and hematopoietic cells. Like Csk, it is a cytoplasmic (or nonreceptor) tyr kinase containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases that are anchored to the plasma membrane, Chk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Studies in mice reveal that Chk is not functionally redundant with Csk and that it plays an important role as a regulator of immune responses. Chk also plays a role in neural differentiation in a manner independent of Src by enhancing Mapk activation via Ras-mediated signaling. The Chk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270666 [Multi-domain]  Cd Length: 254  Bit Score: 88.39  E-value: 3.62e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  634 AFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHG 713
Cdd:cd05083     45 AFLEETAVMTKLQHKNLVRLLGVILHNGLYIVMELMSKGNLVNFLRSRGRALVPVIQLLQFSLDVAEGMEYLESKKLVHR 124
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  714 NVCTKNLLLAREGIdsecgpfIKLSDPGIPiTVLSRQECIERIP--WIAPECVEDSKnLSVAADKWSFGTTLWEICYNGE 791
Cdd:cd05083    125 DLAARNILVSEDGV-------AKISDFGLA-KVGSMGVDNSRLPvkWTAPEALKNKK-FSSKSDVWSYGVLLWEVFSYGR 195
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1013071061  792 IPLKDKTLIEKERFYESRCRPVTP-SCK-ELADLMTRCMNYDPNQRPFFRAIMRDINK 847
Cdd:cd05083    196 APYPKMSVKEVKEAVEKGYRMEPPeGCPpDVYSIMTSCWEAEPGKRPSFKKLREKLEK 253
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
879-1151 3.68e-19

Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes cyclin G-Associated Kinase (GAK), Drosophila melanogaster Numb-Associated Kinase (NAK)-like proteins, and similar protein kinases. GAK plays regulatory roles in clathrin-mediated membrane trafficking, the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses. NAK plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. The GAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270887 [Multi-domain]  Cd Length: 272  Bit Score: 88.93  E-value: 3.68e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGHFGKVelcrYDPEGDNTGEQVAVKslkpESGGNHIADLK---KEIEILRNL-YHENIVKYKG--ICTEDGGNGI 952
Cdd:cd13985      6 KQLGEGGFSYV----YLAHDVNTGRRYALK----RMYFNDEEQLRvaiKEIEIMKRLcGHPNIVQYYDsaILSSEGRKEV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  953 KLIMEFLPsGSLKEYLPKN-KNKINLKQQLKYAVQICKGMDYLGSRQ--YVHRDLAARNVLVESEHQVKIGDFGltKAIE 1029
Cdd:cd13985     78 LLLMEYCP-GSLVDILEKSpPSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFG--SATT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1030 TDKEYYTVKD--------DRDSPVFWYAPECL-MQSKFYIA--SDVWSFGVTLHELLTYCD--SDSSPMA-LFLKMIGPT 1095
Cdd:cd13985    155 EHYPLERAEEvniieeeiQKNTTPMYRAPEMIdLYSKKPIGekADIWALGCLLYKLCFFKLpfDESSKLAiVAGKYSIPE 234
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1013071061 1096 HgqmtvtrlvntlkegkrlpcpPNCPDEVYQLMRKCWEFQPSNRTS-FQ--NLIEGFEA 1151
Cdd:cd13985    235 Q---------------------PRYSPELHDLIRHMLTPDPAERPDiFQviNIITKDTK 272
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
878-1141 3.90e-19

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 11; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek11 is involved, through direct phosphorylation, in regulating the degradation of Cdc25A (Cell Division Cycle 25 homolog A), which plays a role in cell cycle progression and in activating cyclin dependent kinases. Nek11 is activated by CHK1 (CHeckpoint Kinase 1) and may be involved in the G2/M checkpoint. Nek11 may also play a role in the S-phase checkpoint as well as in DNA replication and genotoxic stress responses. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270861 [Multi-domain]  Cd Length: 260  Bit Score: 88.63  E-value: 3.90e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVELCRyDPEGDNTGE-----QVAVKSLKPesggNHIADLKKEIEILRNLYHENIVKYKGICTEDGGNGI 952
Cdd:cd08222      5 VRKLGSGNFGTVYLVS-DLKATADEElkvlkEISVGELQP----DETVDANREAKLLSKLDHPAIVKFHDSFVEKESFCI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  953 klIMEFLPSGSL----KEYlPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESeHQVKIGDFGLTKAI 1028
Cdd:cd08222     80 --VTEYCEGGDLddkiSEY-KKSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLKN-NVIKVGDFGISRIL 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1029 ETDKEYYTVKddRDSPvFWYAPECLMQSKFYIASDVWSFGVTLHEL--LTYCDSDSSPMALFLKMIgpthgqmtvtrlvn 1106
Cdd:cd08222    156 MGTSDLATTF--TGTP-YYMSPEVLKHEGYNSKSDIWSLGCILYEMccLKHAFDGQNLLSVMYKIV-------------- 218
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1013071061 1107 tlkEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTS 1141
Cdd:cd08222    219 ---EGETPSLPDKYSKELNAIYSRMLNKDPALRPS 250
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
881-1075 4.14e-19

Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. It phosphorylates Cre-Responsive Element Binding protein (CREB), facilitating the binding of CREB to the specific cis cAMP responsive element (CRE), which is important in activating genes related to germ cell differentiation. Mutations in the human TSSK4 gene is associated with infertile Chinese men with impaired spermatogenesis. The TSSK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271064 [Multi-domain]  Cd Length: 259  Bit Score: 88.51  E-value: 4.14e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDpegdNTGEQVAVKSL-KPESGGNHIAD-LKKEIEILRNLYHENIVK-YKGICTEdggNGIKLIME 957
Cdd:cd14162      8 LGHGSYAVVKKAYST----KHKCKVAIKIVsKKKAPEDYLQKfLPREIEVIKGLKHPNLICfYEAIETT---SRVYIIME 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  958 FLPSGSLKEYLPKNKNkINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYTV 1037
Cdd:cd14162     81 LAENGDLLDYIRKNGA-LPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFARGVMKTKDGKPK 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1013071061 1038 KDDRDSPVFWYAPECLMQSKFY--IASDVWSFGVTLHELL 1075
Cdd:cd14162    160 LSETYCGSYAYASPEILRGIPYdpFLSDIWSMGVVLYTMV 199
PTK_Jak2_rpt1 cd05078
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely ...
881-1146 4.72e-19

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely expressed in many tissues. It is essential for the signaling of hormone-like cytokines such as growth hormone, erythropoietin, thrombopoietin, and prolactin, as well as some IFNs and cytokines that signal through the IL-3 and gp130 receptors. Disruption of Jak2 in mice results in an embryonic lethal phenotype with multiple defects including erythropoietic and cardiac abnormalities. It is the only Jak gene that results in a lethal phenotype when disrupted in mice. A mutation in the pseudokinase domain of Jak2, V617F, is present in many myeloproliferative diseases, including almost all patients with polycythemia vera, and 50% of patients with essential thrombocytosis and myelofibrosis. Jak2 is a cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Despite this, the presumed pseudokinase (repeat 1) domain of Jak2 exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. Inactivation of the repeat 1 domain increased Jak2 basal activity, suggesting that it modulates the kinase activity of the C-terminal catalytic (repeat 2) domain. The Jak2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270663 [Multi-domain]  Cd Length: 262  Bit Score: 88.47  E-value: 4.72e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKV------ELCRYdpeGDNTGEQVAVKSLKpESGGNHIADLKKEIEILRNLYHENIVKYKGICTedGGNGIKL 954
Cdd:cd05078      7 LGQGTFTKIfkgirrEVGDY---GQLHETEVLLKVLD-KAHRNYSESFFEAASMMSQLSHKHLVLNYGVCV--CGDENIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEy 1034
Cdd:cd05078     81 VQEYVKFGSLDTYLKKNKNCINILWKLEVAKQLAWAMHFLEEKTLVHGNVCAKNILLIREEDRKTGNPPFIKLSDPGIS- 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1035 YTV--KDDRDSPVFWYAPECLMQSK-FYIASDVWSFGVTLHELltYCDSDsSPMAlflkmigpthgQMTVTRLVNTLKEG 1111
Cdd:cd05078    160 ITVlpKDILLERIPWVPPECIENPKnLSLATDKWSFGTTLWEI--CSGGD-KPLS-----------ALDSQRKLQFYEDR 225
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1013071061 1112 KRLPCPPNCpdEVYQLMRKCWEFQPSNRTSFQNLI 1146
Cdd:cd05078    226 HQLPAPKWT--ELANLINNCMDYEPDHRPSFRAII 258
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
583-853 4.83e-19

Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Axl is widely expressed in a variety of organs and cells including epithelial, mesenchymal, hematopoietic, as well as non-transformed cells. It is important in many cellular functions such as survival, anti-apoptosis, proliferation, migration, and adhesion. Axl was originally isolated from patients with chronic myelogenous leukemia and a chronic myeloproliferative disorder. It is overexpressed in many human cancers including colon, squamous cell, thyroid, breast, and lung carcinomas. Axl is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to its ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Axl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270660 [Multi-domain]  Cd Length: 277  Bit Score: 88.53  E-value: 4.83e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  583 LVQGEHLGRGTRTHIYSGTLmdykddegTSEEKKIKVILKVLDPS--HRDISLAFFEAASMMRQVSHKHIVYLYGVCVRD 660
Cdd:cd05075      2 LALGKTLGEGEFGSVMEGQL--------NQDDSVLKVAVKTMKIAicTRSEMEDFLSEAVCMKEFDHPNVMRLIGVCLQN 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  661 VEN------IMVEEFVEGGPLDLFM--HRKSDV---LTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLaREGIDs 729
Cdd:cd05075     74 TESegypspVVILPFMKHGDLHSFLlySRLGDCpvyLPTQMLVKFMTDIASGMEYLSSKNFIHRDLAARNCML-NENMN- 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  730 ecgpfIKLSDPGIPITVLS----RQECIERIP--WIAPECVEDsKNLSVAADKWSFGTTLWEICYNGEIPLKDktlIEKE 803
Cdd:cd05075    152 -----VCVADFGLSKKIYNgdyyRQGRISKMPvkWIAIESLAD-RVYTTKSDVWSFGVTMWEIATRGQTPYPG---VENS 222
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1013071061  804 RFYE-----SRCRPvTPSCKE-LADLMTRCMNYDPNQRPFFRAIMRDINKLEEQNP 853
Cdd:cd05075    223 EIYDylrqgNRLKQ-PPDCLDgLYELMSSCWLLNPKDRPSFETLRCELEKILKDLP 277
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
921-1074 4.87e-19

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 is required for the transition from metaphase to anaphase. It also plays important roles in mitotic spindle formation and cytokinesis. Activated by Nek9 during mitosis, Nek6 phosphorylates Eg5, a kinesin that is important for spindle bipolarity. Nek6 localizes to spindle microtubules during metaphase and anaphase, and to the midbody during cytokinesis. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 88.55  E-value: 4.87e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  921 DLKKEIEILRNLYHENIVKYKGICTEDggNGIKLIMEFLPSGSLKE---YLPKNKNKINLKQQLKYAVQICKGMDYLGSR 997
Cdd:cd08228     48 DCVKEIDLLKQLNHPNVIKYLDSFIED--NELNIVLELADAGDLSQmikYFKKQKRLIPERTVWKYFVQLCSAVEHMHSR 125
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1013071061  998 QYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKeyyTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHEL 1074
Cdd:cd08228    126 RVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKT---TAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEM 199
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
582-848 5.19e-19

Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. RET is a receptor PTK (RTK) containing an extracellular region with four cadherin-like repeats, a calcium-binding site, and a cysteine-rich domain, a transmembrane segment, and an intracellular catalytic domain. It is part of a multisubunit complex that binds glial-derived neurotropic factor (GDNF) family ligands (GFLs) including GDNF, neurturin, artemin, and persephin. GFLs bind RET along with four GPI-anchored coreceptors, bringing two RET molecules together, leading to autophosphorylation, activation, and intracellular signaling. RET is essential for the development of the sympathetic, parasympathetic and enteric nervous systems, and the kidney. RET disruption by germline mutations causes diseases in humans including congenital aganglionosis of the gastrointestinal tract (Hirschsprung's disease) and three related inherited cancers: multiple endocrine neoplasia type 2A (MEN2A), MEN2B, and familial medullary thyroid carcinoma. The RET subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 88.87  E-value: 5.19e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  582 DLVQGEHLGRGTRTHIYSGTLMDYKDDEGTSeekkiKVILKVLDPSHRDISL-AFFEAASMMRQVSHKHIVYLYGVCVRD 660
Cdd:cd05045      1 NLVLGKTLGEGEFGKVVKATAFRLKGRAGYT-----TVAVKMLKENASSSELrDLLSEFNLLKQVNHPHVIKLYGACSQD 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  661 VENIMVEEFVEGGPLDLFMH--RK---------------------------SDVLTTPWkfkvakQLASALSYLEDKDLV 711
Cdd:cd05045     76 GPLLLIVEYAKYGSLRSFLResRKvgpsylgsdgnrnssyldnpderaltmGDLISFAW------QISRGMQYLAEMKLV 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  712 HGNVCTKNLLLARegidsecGPFIKLSDPGIPITVLSRQECIE----RIP--WIAPECVEDSKNLSvAADKWSFGTTLWE 785
Cdd:cd05045    150 HRDLAARNVLVAE-------GRKMKISDFGLSRDVYEEDSYVKrskgRIPvkWMAIESLFDHIYTT-QSDVWSFGVLLWE 221
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1013071061  786 ICYNGEIPLKDktlIEKERFYE------SRCRPVTPScKELADLMTRCMNYDPNQRPFFRAIMRDINKL 848
Cdd:cd05045    222 IVTLGGNPYPG---IAPERLFNllktgyRMERPENCS-EEMYNLMLTCWKQEPDKRPTFADISKELEKM 286
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
925-1146 5.21e-19

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii FA2 was discovered in a genetic screen for deflagellation-defective mutants. It is essential for basal-body/centriole-associated microtubule severing, and plays a role in cell cycle progression. No cellular function has yet been ascribed to CNK4. The Chlamydomonas reinhardtii FA2-like subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily contains FA2 and CNK4. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 87.85  E-value: 5.21e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  925 EIEILRNLYHENIVKYKGICTEdgGNGIKLIMEFLPSGSLKEYLPKNKNK-INLKQQLKYAVQICKGMDYLGSRQYVHRD 1003
Cdd:cd08529     49 EARVLSKLNSPYVIKYYDSFVD--KGKLNIVMEYAENGDLHSLIKSQRGRpLPEDQIWKFFIQTLLGLSHLHSKKILHRD 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1004 LAARNVLVESEHQVKIGDFGLTKAIETDKEYytVKDDRDSPvFWYAPEcLMQSKFYIA-SDVWSFGVTLHELLTY---CD 1079
Cdd:cd08529    127 IKSMNIFLDKGDNVKIGDLGVAKILSDTTNF--AQTIVGTP-YYLSPE-LCEDKPYNEkSDVWALGCVLYELCTGkhpFE 202
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1013071061 1080 SDSSpMALFLKMIgpthgqmtvtrlvntlkEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLI 1146
Cdd:cd08529    203 AQNQ-GALILKIV-----------------RGKYPPISASYSQDLSQLIDSCLTKDYRQRPDTTELL 251
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
876-1139 5.24e-19

Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Dusty protein kinase is also called Receptor-interacting protein kinase 5 (RIPK5 or RIP5) or RIP-homologous kinase. It is widely distributed in the central nervous system, and may be involved in inducing both caspase-dependent and caspase-independent cell death. The Dusty subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 88.32  E-value: 5.24e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  876 KRIRDLGEGHFGKVELCrydpegDNTG--EQVAVKSLKPeSGGNHIADLKKEIEILRNL-YHENIVKYKGICTE---DGG 949
Cdd:cd13975      3 KLGRELGRGQYGVVYAC------DSWGghFPCALKSVVP-PDDKHWNDLALEFHYTRSLpKHERIVSLHGSVIDysyGGG 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  950 NGIK--LIMEFLpSGSLKEYLpknKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKA 1027
Cdd:cd13975     76 SSIAvlLIMERL-HRDLYTGI---KAGLSLEERLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGFCKP 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1028 ietdkEYYTVKDDRDSPVFwYAPEcLMQSKFYIASDVWSFGVtlheLLTYCDSDSS--PMAlFLKMIGPTHgqmtvtrLV 1105
Cdd:cd13975    152 -----EAMMSGSIVGTPIH-MAPE-LFSGKYDNSVDVYAFGI----LFWYLCAGHVklPEA-FEQCASKDH-------LW 212
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1013071061 1106 NTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNR 1139
Cdd:cd13975    213 NNVRKGVRPERLPVFDEECWNLMEACWSGDPSQR 246
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
580-841 5.35e-19

Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The PDGFR subfamily consists of PDGFR alpha, PDGFR beta, KIT, CSF-1R, the mammalian FLT3, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. PDGFR kinase domains are autoinhibited by their juxtamembrane regions containing tyr residues. The binding to their ligands leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR subfamily receptors are important in the development of a variety of cells. PDGFRs are expressed in a many cells including fibroblasts, neurons, endometrial cells, mammary epithelial cells, and vascular smooth muscle cells. PDGFR signaling is critical in normal embryonic development, angiogenesis, and wound healing. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. Mammalian FLT3 plays an important role in the survival, proliferation, and differentiation of stem cells. The PDGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 89.08  E-value: 5.35e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  580 KKDLVQGEHLGRGTRTHIYSGTLMdykddeGTSEEKK-IKVILKVLDPS-HRDISLAFFEAASMMRQV-SHKHIVYLYGV 656
Cdd:cd05055     34 RNNLSFGKTLGAGAFGKVVEATAY------GLSKSDAvMKVAVKMLKPTaHSSEREALMSELKIMSHLgNHENIVNLLGA 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  657 CVRDVENIMVEEFVEGGPLDLFMHRKSDVLTTPWK-FKVAKQLASALSYLEDKDLVHGNVCTKNLLLARegidsecGPFI 735
Cdd:cd05055    108 CTIGGPILVITEYCCYGDLLNFLRRKRESFLTLEDlLSFSYQVAKGMAFLASKNCIHRDLAARNVLLTH-------GKIV 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  736 KLSDPGIPITVLSRQECI----ERIP--WIAPECVEDSKnLSVAADKWSFGTTLWEICYNGEIPLKDktLIEKERFY--- 806
Cdd:cd05055    181 KICDFGLARDIMNDSNYVvkgnARLPvkWMAPESIFNCV-YTFESDVWSYGILLWEIFSLGSNPYPG--MPVDSKFYkli 257
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1013071061  807 ESRCRPVTP--SCKELADLMTRCMNYDPNQRPFFRAI 841
Cdd:cd05055    258 KEGYRMAQPehAPAEIYDIMKTCWDADPLKRPTFKQI 294
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
884-1099 5.61e-19

Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as ACVR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. Vertebrates contain two ACVR2 proteins, ACVR2a (or ActRIIA) and ACVR2b (or ActRIIB). The ACVR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 88.54  E-value: 5.61e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  884 GHFGKVELCRYdpegdnTGEQVAVKSLKPESGGNHIADlkKEIEILRNLYHENIVKYkgICTEDGGNGIK----LIMEFL 959
Cdd:cd14053      6 GRFGAVWKAQY------LNRLVAVKIFPLQEKQSWLTE--REIYSLPGMKHENILQF--IGAEKHGESLEaeywLITEFH 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  960 PSGSLKEYLpKNkNKINLKQQLKYAVQICKGMDYL-----GSRQYV-----HRDLAARNVLVESEHQVKIGDFGLTKAIE 1029
Cdd:cd14053     76 ERGSLCDYL-KG-NVISWNELCKIAESMARGLAYLhedipATNGGHkpsiaHRDFKSKNVLLKSDLTACIADFGLALKFE 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1030 TDKE----YYTVKDDRdspvfWYAPECL-----MQSKFYIASDVWSFGVTLHELLTYCDSDSSP----MALFLKMIG--P 1094
Cdd:cd14053    154 PGKScgdtHGQVGTRR-----YMAPEVLegainFTRDAFLRIDMYAMGLVLWELLSRCSVHDGPvdeyQLPFEEEVGqhP 228

                   ....*
gi 1013071061 1095 THGQM 1099
Cdd:cd14053    229 TLEDM 233
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
578-846 5.93e-19

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkA is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkA to its ligand, nerve growth factor (NGF), results in receptor oligomerization and activation of the catalytic domain. TrkA is expressed mainly in neural-crest-derived sensory and sympathetic neurons of the peripheral nervous system, and in basal forebrain cholinergic neurons of the central nervous system. It is critical for neuronal growth, differentiation and survival. Alternative TrkA splicing has been implicated as a pivotal regulator of neuroblastoma (NB) behavior. Normal TrkA expression is associated with better NB prognosis, while the hypoxia-regulated TrkAIII splice variant promotes NB pathogenesis and progression. Aberrant TrkA expression has also been demonstrated in non-neural tumors including prostate, breast, lung, and pancreatic cancers. The TrkA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 88.48  E-value: 5.93e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  578 ILKKDLVQGEHLGRGTRTHIYSGTLMDYkddegTSEEKKIKVILKVLDPSHRDISLAFFEAASMMRQVSHKHIVYLYGVC 657
Cdd:cd05092      2 IKRRDIVLKWELGEGAFGKVFLAECHNL-----LPEQDKMLVAVKALKEATESARQDFQREAELLTVLQHQHIVRFYGVC 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  658 VRDVENIMVEEFVEGGPLDLFMHRKS--------------DVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLA 723
Cdd:cd05092     77 TEGEPLIMVFEYMRHGDLNRFLRSHGpdakildggegqapGQLTLGQMLQIASQIASGMVYLASLHFVHRDLATRNCLVG 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  724 RegidsecGPFIKLSDPGIPITVLSRQ------ECIERIPWIAPECVEDSKnLSVAADKWSFGTTLWEICYNGEIP---L 794
Cdd:cd05092    157 Q-------GLVVKIGDFGMSRDIYSTDyyrvggRTMLPIRWMPPESILYRK-FTTESDIWSFGVVLWEIFTYGKQPwyqL 228
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1013071061  795 KDKTLIE---KERFYEsrcRPVT-PSckELADLMTRCMNYDPNQrpffRAIMRDIN 846
Cdd:cd05092    229 SNTEAIEcitQGRELE---RPRTcPP--EVYAIMQGCWQREPQQ----RHSIKDIH 275
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
578-838 7.01e-19

Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fyn and Yrk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Fyn, together with Lck, plays a critical role in T-cell signal transduction by phosphorylating ITAM (immunoreceptor tyr activation motif) sequences on T-cell receptors, ultimately leading to the proliferation and differentiation of T-cells. In addition, Fyn is involved in the myelination of neurons, and is implicated in Alzheimer's and Parkinson's diseases. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Fyn/Yrk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase.


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 88.20  E-value: 7.01e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  578 ILKKDLVQGEHLGRGTRTHIYSGTLmdykddegtseEKKIKVILKVLDPSHRDISlAFFEAASMMRQVSHKHIVYLYGVC 657
Cdd:cd05070      6 IPRESLQLIKRLGNGQFGEVWMGTW-----------NGNTKVAIKTLKPGTMSPE-SFLEEAQIMKKLKHDKLVQLYAVV 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  658 VRDVENIMVEEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLARegidsecGPFIKL 737
Cdd:cd05070     74 SEEPIYIVTEYMSKGSLLDFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGN-------GLICKI 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  738 SDPGIPITV-----LSRQECIERIPWIAPECVEDSKnLSVAADKWSFGTTLWEICYNGEIP---LKDKTLIEK-ERFYES 808
Cdd:cd05070    147 ADFGLARLIedneyTARQGAKFPIKWTAPEAALYGR-FTIKSDVWSFGILLTELVTKGRVPypgMNNREVLEQvERGYRM 225
                          250       260       270
                   ....*....|....*....|....*....|
gi 1013071061  809 RCRPVTPSckELADLMTRCMNYDPNQRPFF 838
Cdd:cd05070    226 PCPQDCPI--SLHELMIHCWKKDPEERPTF 253
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
589-838 7.74e-19

Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src (or c-Src) is a cytoplasmic (or non-receptor) PTK, containing an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region with a conserved tyr. It is activated by autophosphorylation at the tyr kinase domain, and is negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). c-Src is the vertebrate homolog of the oncogenic protein (v-Src) from Rous sarcoma virus. Together with other Src subfamily proteins, it is involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. Src also play a role in regulating cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Elevated levels of Src kinase activity have been reported in a variety of human cancers. Several inhibitors of Src have been developed as anti-cancer drugs. Src is also implicated in acute inflammatory responses and osteoclast function. The Src subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 88.21  E-value: 7.74e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  589 LGRGTRTHIYSGTLmdykddEGTSeekkiKVILKVLDPSHRDISlAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEE 668
Cdd:cd05071     17 LGQGCFGEVWMGTW------NGTT-----RVAIKTLKPGTMSPE-AFLQEAQVMKKLRHEKLVQLYAVVSEEPIYIVTEY 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  669 FVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLareGIDSECgpfiKLSDPGIPITV-- 746
Cdd:cd05071     85 MSKGSLLDFLKGEMGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILV---GENLVC----KVADFGLARLIed 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  747 ---LSRQECIERIPWIAPECVEDSKnLSVAADKWSFGTTLWEICYNGEIP----LKDKTLIEKERFYESRCRPVTPSckE 819
Cdd:cd05071    158 neyTARQGAKFPIKWTAPEAALYGR-FTIKSDVWSFGILLTELTTKGRVPypgmVNREVLDQVERGYRMPCPPECPE--S 234
                          250
                   ....*....|....*....
gi 1013071061  820 LADLMTRCMNYDPNQRPFF 838
Cdd:cd05071    235 LHDLMCQCWRKEPEERPTF 253
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
877-1076 9.75e-19

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK4 is a MAPK kinase kinase that phosphorylates and activates the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. MEKK4 also plays roles in the re-polarization of the actin cytoskeleton in response to osmotic stress, in the proper closure of the neural tube, in cardiovascular development, and in immune responses. The MEKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270796 [Multi-domain]  Cd Length: 265  Bit Score: 87.36  E-value: 9.75e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  877 RIRDLGEGHFGKVELCRydpeGDNTGEQVAVKSLK-PESGGNHIADLKKEIEILRNLYHENIVKYKGIctEDGGNGIKLI 955
Cdd:cd06626      4 RGNKIGEGTFGKVYTAV----NLDTGELMAMKEIRfQDNDPKTIKEIADEMKVLEGLDHPNLVRYYGV--EVHREEVYIF 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  956 MEFLPSGSLKEYLpknKNKINLKQQL--KYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAI---ET 1030
Cdd:cd06626     78 MEYCQEGTLEELL---RHGRILDEAVirVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAVKLknnTT 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1013071061 1031 DKEYYTVKDDRDSPVFwYAPECLMQSKF--YI-ASDVWSFGVTLHELLT 1076
Cdd:cd06626    155 TMAPGEVNSLVGTPAY-MAPEVITGNKGegHGrAADIWSLGCVVLEMAT 202
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
576-838 9.88e-19

Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase (RTK) containing an extracellular region with two leucine-rich motifs, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. The extracellular region of Ryk shows homology to the N-terminal domain of Wnt inhibitory factor-1 (WIF) and serves as the ligand (Wnt) binding domain of Ryk. Ryk is expressed in many different tissues both during development and in adults, suggesting a widespread function. It acts as a chemorepulsive axon guidance receptor of Wnt glycoproteins and is responsible for the establishment of axon tracts during the development of the central nervous system. In addition, studies in mice reveal that Ryk is essential in skeletal, craniofacial, and cardiac development. Thus, it appears Ryk is involved in signal transduction despite its lack of kinase activity. Ryk may function as an accessory protein that modulates the signals coming from catalytically active partner RTKs such as the Eph receptors. The Ryk subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270639 [Multi-domain]  Cd Length: 279  Bit Score: 87.89  E-value: 9.88e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  576 DRILKKDLVQgehlgRGTRTHIYSGTlmdYKDDEGTSEEkkikVILKVLDPSHRDISLA-FFEAASMMRQVSHKHIVYLY 654
Cdd:cd05043      6 ERVTLSDLLQ-----EGTFGRIFHGI---LRDEKGKEEE----VLVKTVKDHASEIQVTmLLQESSLLYGLSHQNLLPIL 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  655 GVCVRDVENIMVEEFVEG-GPLDLFMHRKSDV-------LTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLlareg 726
Cdd:cd05043     74 HVCIEDGEKPMVLYPYMNwGNLKLFLQQCRLSeannpqaLSTQQLVHMALQIACGMSYLHRRGVIHKDIAARNCV----- 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  727 IDSECgpFIKLSDpgipiTVLSRQ------ECI---ERIP--WIAPECVEDsKNLSVAADKWSFGTTLWEICYNGEIPLK 795
Cdd:cd05043    149 IDDEL--QVKITD-----NALSRDlfpmdyHCLgdnENRPikWMSLESLVN-KEYSSASDVWSFGVLLWELMTLGQTPYV 220
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1013071061  796 DKTLIEKERFYESRCRPVTP-SC-KELADLMTRCMNYDPNQRPFF 838
Cdd:cd05043    221 EIDPFEMAAYLKDGYRLAQPiNCpDELFAVMACCWALDPEERPSF 265
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
619-843 1.05e-18

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR1 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR1 results in a slow but sustained receptor activation. DDR1 binds to all collagens tested to date (types I-IV). It is widely expressed in many tissues. It is abundant in the brain and is also found in keratinocytes, colonic mucosa epithelium, lung epithelium, thyroid follicles, and the islets of Langerhans. During embryonic development, it is found in the developing neuroectoderm. DDR1 is a key regulator of cell morphogenesis, differentiation and proliferation. It is important in the development of the mammary gland, the vasculator and the kidney. DDR1 is also found in human leukocytes, where it facilitates cell adhesion, migration, maturation, and cytokine production. The DDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133227 [Multi-domain]  Cd Length: 304  Bit Score: 88.07  E-value: 1.05e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  619 VILKVLDP-SHRDISLAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFM-HRKSD------------ 684
Cdd:cd05096     49 VAVKILRPdANKNARNDFLKEVKILSRLKDPNIIRLLGVCVDEDPLCMITEYMENGDLNQFLsSHHLDdkeengndavpp 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  685 -----VLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGIPITVLS------RQECI 753
Cdd:cd05096    129 ahclpAISYSSLLHVALQIASGMKYLSSLNFVHRDLATRNCLVGENLT-------IKIADFGMSRNLYAgdyyriQGRAV 201
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  754 ERIPWIAPECVEDSKnLSVAADKWSFGTTLWEI---CYngEIP---LKDKTLIEKE-RFYESRCRPV----TPSCKE-LA 821
Cdd:cd05096    202 LPIRWMAWECILMGK-FTTASDVWAFGVTLWEIlmlCK--EQPygeLTDEQVIENAgEFFRDQGRQVylfrPPPCPQgLY 278
                          250       260
                   ....*....|....*....|..
gi 1013071061  822 DLMTRCMNYDPNQRPFFRAIMR 843
Cdd:cd05096    279 ELMLQCWSRDCRERPSFSDIHA 300
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
881-1076 1.11e-18

Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. ULK2 is ubiquitously expressed and is essential in autophagy induction. ULK1 and ULK2 have unique and cell-type specific roles, but also display partially redundant roles in starvation-induced autophagy. They both display neuron-specific functions: ULK1 is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, and axon branching; ULK2 plays a role in axon development. The ULK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271022 [Multi-domain]  Cd Length: 256  Bit Score: 87.04  E-value: 1.11e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDpegDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVK-YKgiCTEDgGNGIKLIMEFL 959
Cdd:cd14120      1 IGHGAFAVVFKGRHR---KKPDLPVAIKCITKKNLSKSQNLLGKEIKILKELSHENVVAlLD--CQET-SSSVYLVMEYC 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  960 PSGSLKEYLPK----NKNKINLkqqlkYAVQICKGMDYLGSRQYVHRDLAARNVLVE---------SEHQVKIGDFGLTK 1026
Cdd:cd14120     75 NGGDLADYLQAkgtlSEDTIRV-----FLQQIAAAMKALHSKGIVHRDLKPQNILLShnsgrkpspNDIRLKIADFGFAR 149
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1027 AIETDKEYYTVKddrDSPVFwYAPECLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd14120    150 FLQDGMMAATLC---GSPMY-MAPEVIMSLQYDAKADLWSIGTIVYQCLT 195
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
878-1075 1.12e-18

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK6 is regulated by D-type cyclins and INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein, implicating it to function in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the cytoplasm. It is also present in the ruffling edge of spreading fibroblasts and may play a role in cell spreading. It binds to the p21 inhibitor without any effect on its own activity and it is overexpressed in squamous cell carcinomas and neuroblastomas. CDK6 has also been shown to inhibit cell differentiation in many cell types. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270846 [Multi-domain]  Cd Length: 290  Bit Score: 87.78  E-value: 1.12e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVELCRydpEGDNTGEQVAVKSLK--PESGGNHIADLKkEIEILRNLY---HENIVKYKGICT---EDGG 949
Cdd:cd07862      6 VAEIGEGAYGKVFKAR---DLKNGGRFVALKRVRvqTGEEGMPLSTIR-EVAVLRHLEtfeHPNVVRLFDVCTvsrTDRE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  950 NGIKLIMEFLPSgSLKEYLPKNKNKINLKQQLK-YAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKai 1028
Cdd:cd07862     82 TKLTLVFEHVDQ-DLTTYLDKVPEPGVPTETIKdMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLAR-- 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1029 etdkeYYTVKDDRDSPV--FWY-APECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd07862    159 -----IYSFQMALTSVVvtLWYrAPEVLLQSSYATPVDLWSVGCIFAEMF 203
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
877-1076 1.29e-18

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-3 shows a restricted pattern of expression and is present in brain, kidney, and intestine. It is elevated in Alzheimer's disease (AD) and has been shown to associate with paired helical filaments (PHFs) and stimulate Tau phosphorylation. As AD progresses, phosphorylated Tau aggregates and forms PHFs, which leads to the formation of neurofibrillary tangles. In human glioma cells, PCTAIRE-3 induces cell cycle arrest and cell death. PCTAIRE-3 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270853 [Multi-domain]  Cd Length: 288  Bit Score: 87.76  E-value: 1.29e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  877 RIRDLGEGHFGKVelcrYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDggNGIKLIM 956
Cdd:cd07871      9 KLDKLGEGTYATV----FKGRSKLTENLVALKEIRLEHEEGAPCTAIREVSLLKNLKHANIVTLHDIIHTE--RCLTLVF 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  957 EFLPSgSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYT 1036
Cdd:cd07871     83 EYLDS-DLKQYLDNCGNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLARAKSVPTKTYS 161
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1013071061 1037 vkddRDSPVFWY-APECLMQSKFYIAS-DVWSFGVTLHELLT 1076
Cdd:cd07871    162 ----NEVVTLWYrPPDVLLGSTEYSTPiDMWGVGCILYEMAT 199
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
583-848 1.68e-18

Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The TAM subfamily consists of Tyro3 (or Sky), Axl, Mer (or Mertk), and similar proteins. TAM subfamily members are receptor tyr kinases (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. TAM proteins are implicated in a variety of cellular effects including survival, proliferation, migration, and phagocytosis. They are also associated with several types of cancer as well as inflammatory, autoimmune, vascular, and kidney diseases. The TAM subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270631 [Multi-domain]  Cd Length: 273  Bit Score: 86.82  E-value: 1.68e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  583 LVQGEHLGRGTRTHIYSGTLmdyKDDEGTSEEKKIKVIlKVLDPSHRDISlAFFEAASMMRQVSHKHIVYLYGVCVRDVE 662
Cdd:cd05035      1 LKLGKILGEGEFGSVMEAQL---KQDDGSQLKVAVKTM-KVDIHTYSEIE-EFLSEAACMKDFDHPNVMRLIGVCFTASD 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  663 N------IMVEEFVEGGPLDLFMHrKSDVLTTPWKFKVAKQL------ASALSYLEDKDLVHGNVCTKNLLLAREGidSE 730
Cdd:cd05035     76 LnkppspMVILPFMKHGDLHSYLL-YSRLGGLPEKLPLQTLLkfmvdiAKGMEYLSNRNFIHRDLAARNCMLDENM--TV 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  731 CgpfikLSDPGIPITVLS----RQECIERIP--WIAPECVEDsKNLSVAADKWSFGTTLWEICYNGEIPLKDktlIEKER 804
Cdd:cd05035    153 C-----VADFGLSRKIYSgdyyRQGRISKMPvkWIALESLAD-NVYTSKSDVWSFGVTMWEIATRGQTPYPG---VENHE 223
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1013071061  805 FYE-----SRCRPVTPSCKELADLMTRCMNYDPNQRPFFRAIMRDINKL 848
Cdd:cd05035    224 IYDylrngNRLKQPEDCLDEVYFLMYFCWTVDPKDRPTFTKLREVLENI 272
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
878-1141 1.79e-18

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK1, also called ARK5 (AMPK-related protein kinase 5), regulates cell proliferation and displays tumor suppression through direct interaction and phosphorylation of p53. It is also involved in cell senescence and motility. High NUAK1 expression is associated with invasiveness of nonsmall cell lung cancer (NSCLC) and breast cancer cells. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. The NUAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270975 [Multi-domain]  Cd Length: 254  Bit Score: 86.29  E-value: 1.79e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVELCRYDpegdNTGEQVAVKSLKP-----ESGGNHIadlKKEIEILRNLYHENIVK-YKGICTEDGgng 951
Cdd:cd14073      6 LETLGKGTYGKVKLAIER----ATGREVAIKSIKKdkiedEQDMVRI---RREIEIMSSLNHPHIIRiYEVFENKDK--- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  952 IKLIMEFLPSGSLKEYLpKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETD 1031
Cdd:cd14073     76 IVIVMEYASGGELYDYI-SERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLSNLYSKD 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1032 KEYYTVKddrDSPVfwYA-PEcLMQSKFYIASDV--WSFGVTLHELLtycdsdsspmalflkmigptHGQM-----TVTR 1103
Cdd:cd14073    155 KLLQTFC---GSPL--YAsPE-IVNGTPYQGPEVdcWSLGVLLYTLV--------------------YGTMpfdgsDFKR 208
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1013071061 1104 LVNTLKEGK-RLPCPPNcpdEVYQLMRKCWEFQPSNRTS 1141
Cdd:cd14073    209 LVKQISSGDyREPTQPS---DASGLIRWMLTVNPKRRAT 244
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
637-842 1.80e-18

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK1 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K9. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Little is known about the specific function of MLK1. It is capable of activating the c-Jun N-terminal kinase pathway. Mice lacking both MLK1 and MLK2 are viable, fertile, and have normal life spans. There could be redundancy in the function of MLKs. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271047 [Multi-domain]  Cd Length: 270  Bit Score: 86.63  E-value: 1.80e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  637 EAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKS---DVLTTpWkfkvAKQLASALSYLEDKDLV-- 711
Cdd:cd14145     54 QEAKLFAMLKHPNIIALRGVCLKEPNLCLVMEFARGGPLNRVLSGKRippDILVN-W----AVQIARGMNYLHCEAIVpv 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  712 -HGNVCTKN-LLLAREGIDSECGPFIKLSDPGIPIT--VLSRQECIERIPWIAPECVEDSKnLSVAADKWSFGTTLWEIc 787
Cdd:cd14145    129 iHRDLKSSNiLILEKVENGDLSNKILKITDFGLAREwhRTTKMSAAGTYAWMAPEVIRSSM-FSKGSDVWSYGVLLWEL- 206
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1013071061  788 YNGEIPLK--DKTLIEKERFYESRCRPVTPSCKE-LADLMTRCMNYDPNQRPFFRAIM 842
Cdd:cd14145    207 LTGEVPFRgiDGLAVAYGVAMNKLSLPIPSTCPEpFARLMEDCWNPDPHSRPPFTNIL 264
SH2_Jak2 cd10379
Src homology 2 (SH2) domain in the Janus kinase 2 (Jak2) proteins; Jak2 is a protein tyrosine ...
426-523 1.81e-18

Src homology 2 (SH2) domain in the Janus kinase 2 (Jak2) proteins; Jak2 is a protein tyrosine kinase involved in a specific subset of cytokine receptor signaling pathways. It has been found to be constitutively associated with the prolactin receptor and is required for responses to gamma interferon. Mice that do not express an active protein for this gene exhibit embryonic lethality associated with the absence of definitive erythropoiesis. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198242  Cd Length: 97  Bit Score: 81.38  E-value: 1.81e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  426 DVAPPLIVHNIQNGCHGPICTEYAINKLRQEGSEEGMYVLRWSCTDFDNILMTVTcFEKSEQVqgaqkQFKNFQI-EVQK 504
Cdd:cd10379      1 EVAPPRLLEAIQSYCHGPISMEFAISKLRKAGNQTGLYILRCSPKDYNKYFLTFA-VEREGAL-----EYKHCLItKNEN 74
                           90
                   ....*....|....*....
gi 1013071061  505 GRYSLHGSDRSFPSLGDLM 523
Cdd:cd10379     75 GEYNLSGAKKSFGSLKDLL 93
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
878-1153 1.95e-18

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 partners with all three D-type cyclins (D1, D2, and D3) and is also regulated by INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein and plays a role in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the nucleus. CDK4 also shows kinase activity towards Smad3, a signal transducer of TGF-beta signaling which modulates transcription and plays a role in cell proliferation and apoptosis. CDK4 is inhibited by the p21 inhibitor and is specifically mutated in human melanoma. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143368 [Multi-domain]  Cd Length: 288  Bit Score: 86.94  E-value: 1.95e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVELCRyDPEgdnTGEQVAVKSLKPESGGNHIA-DLKKEIEILRNLY---HENIVKYKGICTE---DGGN 950
Cdd:cd07863      5 VAEIGVGAYGTVYKAR-DPH---SGHFVALKSVRVQTNEDGLPlSTVREVALLKRLEafdHPNIVRLMDVCATsrtDRET 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  951 GIKLIMEFLPSgSLKEYL--------PKNKNKINLKQQLKyavqickGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDF 1022
Cdd:cd07863     81 KVTLVFEHVDQ-DLRTYLdkvpppglPAETIKDLMRQFLR-------GLDFLHANCIVHRDLKPENILVTSGGQVKLADF 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1023 GLTKaietdkeYYTVKDDRDSPV--FWY-APECLMQSKFYIASDVWSFGVTLHELLT----YC-DSDSSPMALFLKMIG- 1093
Cdd:cd07863    153 GLAR-------IYSCQMALTPVVvtLWYrAPEVLLQSTYATPVDMWSVGCIFAEMFRrkplFCgNSEADQLGKIFDLIGl 225
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1013071061 1094 PTHGQMTVTRlvnTLKEGKRLP--------CPPNCPDEVYQLMRKCWEFQPSNRtsfqnlIEGFEALL 1153
Cdd:cd07863    226 PPEDDWPRDV---TLPRGAFSPrgprpvqsVVPEIEESGAQLLLEMLTFNPHKR------ISAFRALQ 284
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
878-1147 1.97e-18

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The specific function of Nek5 is unknown. Nek5 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 86.55  E-value: 1.97e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVELCRydpeGDNTGEQVAVKSLKPESGGNHIADL-KKEIEILRNLYHENIVKYKGICTEDGGngIKLIM 956
Cdd:cd08225      5 IKKIGEGSFGKIYLAK----AKSDSEHCVIKEIDLTKMPVKEKEAsKKEVILLAKMKHPNIVTFFASFQENGR--LFIVM 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  957 EFLPSGSLKEYLPKNKNKINLKQQ-LKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQV-KIGDFGLTKAIETDKEY 1034
Cdd:cd08225     79 EYCDGGDLMKRINRQRGVLFSEDQiLSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVaKLGDFGIARQLNDSMEL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1035 -YTVKddrDSPvFWYAPECLMQSKFYIASDVWSFGVTLHELLTycdsdsspmalfLKMigPTHGQmTVTRLVNTLKEGKR 1113
Cdd:cd08225    159 aYTCV---GTP-YYLSPEICQNRPYNNKTDIWSLGCVLYELCT------------LKH--PFEGN-NLHQLVLKICQGYF 219
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1013071061 1114 LPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIE 1147
Cdd:cd08225    220 APISPNFSRDLRSLISQLFKVSPRDRPSITSILK 253
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
881-1078 2.15e-18

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. NUAK2 is implicated in regulating actin stress fiber assembly through its association with myosin phosphatase Rho-interacting protein (MRIP), which leads to an increase in myosin regulatory light chain (MLC) phosphorylation. It is also associated with tumor growth, migration, and oncogenicity of melanoma cells. The NUAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271063 [Multi-domain]  Cd Length: 255  Bit Score: 86.16  E-value: 2.15e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRydpegDNTGEQVAVKSL-----KPESGGNHIadlKKEIEILRNLYHENIVKYKGICteDGGNGIKLI 955
Cdd:cd14161     11 LGKGTYGRVKKAR-----DSSGRLVAIKSIrkdriKDEQDLLHI---RREIEIMSSLNHPHIISVYEVF--ENSSKIVIV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  956 MEFLPSGSLKEYLpKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYY 1035
Cdd:cd14161     81 MEYASRGDLYDYI-SERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLSNLYNQDKFLQ 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1013071061 1036 TVKddrDSPVfwYAPECLMQSKFYIASDV--WSFGVTLHELLTYC 1078
Cdd:cd14161    160 TYC---GSPL--YASPEIVNGRPYIGPEVdsWSLGVLLYILVHGT 199
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
879-1076 2.23e-18

Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BRSK1, also called SAD-B or SAD1 (Synapses of Amphids Defective homolog 1), and BRSK2, also called SAD-A, are highly expressed in mammalian forebrain. They play important roles in establishing neuronal polarity. BRSK1/2 double knock-out mice die soon after birth, showing thin cerebral cortices due to disordered subplate layers and neurons that lack distinct axons and dendrites. BRSK1 regulates presynaptic neurotransmitter release. Its activity fluctuates during cell cysle progression and it acts as a regulator of centrosome duplication. BRSK2 is also abundant in pancreatic islets, where it is involved in the regulation of glucose-stimulated insulin secretion. The BRSK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270983 [Multi-domain]  Cd Length: 255  Bit Score: 86.15  E-value: 2.23e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGHFGKVELCRYDpegdNTGEQVAVKSLKPE--SGGNHIADLKKEIEILRNLYHENIVKYKGIcTEDGGNgIKLIM 956
Cdd:cd14081      7 KTLGKGQTGLVKLAKHC----VTGQKVAIKIVNKEklSKESVLMKVEREIAIMKLIEHPNVLKLYDV-YENKKY-LYLVL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  957 EFLPSGSLKEYLPKnKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYT 1036
Cdd:cd14081     81 EYVSGGELFDYLVK-KGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMASLQPEGSLLET 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1013071061 1037 vkdDRDSPvFWYAPECLMQSKFY-IASDVWSFGVTLHELLT 1076
Cdd:cd14081    160 ---SCGSP-HYACPEVIKGEKYDgRKADIWSCGVILYALLV 196
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
619-838 2.30e-18

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP kinases serve as essential sensors of cellular stress. They are involved in regulating NF-kappaB and MAPK signaling, and are implicated in mediating cellular processes such as apoptosis, necroptosis, differentiation, and survival. RIP kinases contain a homologous N-terminal kinase domain and varying C-terminal domains. Higher vertebrates contain multiple RIP kinases, with mammals harboring at least five members. RIP1 and RIP2 harbor C-terminal domains from the Death domain (DD) superfamily while RIP4 contains ankyrin (ANK) repeats. RIP3 contain a RIP homotypic interaction motif (RHIM) that facilitates binding to RIP1. RIP1 and RIP3 are important in apoptosis and necroptosis, while RIP2 and RIP4 play roles in keratinocyte differentiation and inflammatory immune responses. The RIP subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270880 [Multi-domain]  Cd Length: 263  Bit Score: 86.35  E-value: 2.30e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  619 VILKVL--DPSHRDISLAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSDVLTTPWKFKVAK 696
Cdd:cd13978     21 VAIKCLhsSPNCIEERKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGSLKSLLEREIQDVPWSLRFRIIH 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  697 QLASALSYLE--DKDLVHGNVCTKNLLLAREgidsecgpF-IKLSDPGIPITVLSRQECIER---------IPWIAPECV 764
Cdd:cd13978    101 EIALGMNFLHnmDPPLLHHDLKPENILLDNH--------FhVKISDFGLSKLGMKSISANRRrgtenlggtPIYMAPEAF 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  765 ED-SKNLSVAADKWSFGTTLWEIcYNGEIPLKDKTLIEKERFYESR---------CRP-VTPSCKELADLMTRCMNYDPN 833
Cdd:cd13978    173 DDfNKKPTSKSDVYSFAIVIWAV-LTRKEPFENAINPLLIMQIVSKgdrpslddiGRLkQIENVQELISLMIRCWDGNPD 251

                   ....*
gi 1013071061  834 QRPFF 838
Cdd:cd13978    252 ARPTF 256
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
878-1076 2.58e-18

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK12 is also called Cdc2-related protein kinase 7 (CRK7) or Cdc2-related kinase arginine/serine-rich (CrkRS). It is a unique CDK that contains an RS domain, which is predominantly found in splicing factors. CDK12 is widely expressed in tissues. It interacts with cyclins L1 and L2, and plays roles in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK12 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 87.17  E-value: 2.58e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVelcrYDPEGDNTGEQVAVKS--LKPESGGNHIADLKkEIEILRNLYHENIVKYKGICTE--------- 946
Cdd:cd07864     12 IGIIGEGTYGQV----YKAKDKDTGELVALKKvrLDNEKEGFPITAIR-EIKILRQLNHRSVVNLKEIVTDkqdaldfkk 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  947 DGGNgIKLIMEFLPS---GSLKEYLpKNKNKINLKQQLKyavQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFG 1023
Cdd:cd07864     87 DKGA-FYLVFEYMDHdlmGLLESGL-VHFSEDHIKSFMK---QLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLADFG 161
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1013071061 1024 LTKAIETD-KEYYTVKddrdSPVFWY-APECLMQSKFYIAS-DVWSFGVTLHELLT 1076
Cdd:cd07864    162 LARLYNSEeSRPYTNK----VITLWYrPPELLLGEERYGPAiDVWSCGCILGELFT 213
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
578-838 2.77e-18

Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyro3 (or Sky) is predominantly expressed in the central nervous system and the brain, and functions as a neurotrophic factor. It is also expressed in osteoclasts and has a role in bone resorption. Tyro3 is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Tyro3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 86.51  E-value: 2.77e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  578 ILKKDLVQGEHLGRGTRTHIYSGTLmdyKDDEGTSEEKKIKViLKVLDPSHRDISlAFFEAASMMRQVSHKHIVYLYGVC 657
Cdd:cd05074      6 IQEQQFTLGRMLGKGEFGSVREAQL---KSEDGSFQKVAVKM-LKADIFSSSDIE-EFLREAACMKEFDHPNVIKLIGVS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  658 VRDVEN------IMVEEFVEGGPLDLF--MHRKSD-----VLTTPWKFKVakQLASALSYLEDKDLVHGNVCTKNLLLAR 724
Cdd:cd05074     81 LRSRAKgrlpipMVILPFMKHGDLHTFllMSRIGEepftlPLQTLVRFMI--DIASGMEYLSSKNFIHRDLAARNCMLNE 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  725 EGIdsecgpfIKLSDPGIPITVLS----RQECIERIP--WIAPECVEDskNL-SVAADKWSFGTTLWEICYNGEIPLKDk 797
Cdd:cd05074    159 NMT-------VCVADFGLSKKIYSgdyyRQGCASKLPvkWLALESLAD--NVyTTHSDVWAFGVTMWEIMTRGQTPYAG- 228
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1013071061  798 tlIEKERFYE-----SRCRPvTPSC-KELADLMTRCMNYDPNQRPFF 838
Cdd:cd05074    229 --VENSEIYNylikgNRLKQ-PPDClEDVYELMCQCWSPEPKCRPSF 272
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
613-853 2.80e-18

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkB is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkB to its ligands, brain-derived neurotrophic factor (BDNF) or neurotrophin 4 (NT4), results in receptor oligomerization and activation of the catalytic domain. TrkB is broadly expressed in the nervous system and in some non-neural tissues. It plays important roles in cell proliferation, differentiation, and survival. BDNF/Trk signaling plays a key role in regulating activity-dependent synaptic plasticity. TrkB also contributes to protection against gp120-induced neuronal cell death. TrkB overexpression is associated with poor prognosis in neuroblastoma (NB) and other human cancers. It acts as a suppressor of anoikis (detachment-induced apoptosis) and contributes to tumor metastasis. The TrkB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 86.63  E-value: 2.80e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  613 EEKKIKVILKVLDPSHRDISLAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFM--HRKSDV----- 685
Cdd:cd05093     32 EQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGDLNKFLraHGPDAVlmaeg 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  686 -----LTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGIPITVLSRQ------ECIE 754
Cdd:cd05093    112 nrpaeLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLL-------VKIGDFGMSRDVYSTDyyrvggHTML 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  755 RIPWIAPECVEdSKNLSVAADKWSFGTTLWEICYNGEIP---LKDKTLIEKERFYESRCRPVTPScKELADLMTRCMNYD 831
Cdd:cd05093    185 PIRWMPPESIM-YRKFTTESDVWSLGVVLWEIFTYGKQPwyqLSNNEVIECITQGRVLQRPRTCP-KEVYDLMLGCWQRE 262
                          250       260
                   ....*....|....*....|..
gi 1013071061  832 PNQRPFFRAIMRDINKLEEQNP 853
Cdd:cd05093    263 PHMRLNIKEIHSLLQNLAKASP 284
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
910-1149 2.98e-18

Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-2D is allso called Retinal Guanylyl Cyclase 1 (RETGC-1) or Rod Outer Segment membrane Guanylate Cyclase (ROS-GC). It is found in the photoreceptors of the retina where it anchors the reciprocal feedback loop between calcium and cGMP, which regulates the dark, light, and recovery phases in phototransduction. It is also found in other sensory neurons and may be a universal transduction component that plays a role in the perception of all senses. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-2D subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270945 [Multi-domain]  Cd Length: 267  Bit Score: 85.92  E-value: 2.98e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  910 LKPESGGNHIADLKKEIEI---LRNLYHENIVKYKGiCTEDGGNgIKLIMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQ 986
Cdd:cd14043     28 LKKFPGGSHTELRPSTKNVfskLRELRHENVNLFLG-LFVDCGI-LAIVSEHCSRGSLEDLLRNDDMKLDWMFKSSLLLD 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  987 ICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYTVKDDRDspVFWYAPECL----MQSKFYIAS 1062
Cdd:cd14043    106 LIKGMRYLHHRGIVHGRLKSRNCVVDGRFVLKITDYGYNEILEAQNLPLPEPAPEE--LLWTAPELLrdprLERRGTFPG 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1063 DVWSFGVTLHELLT----YCDSDSSPMALFLKMIGPthgqmtvtrlvntlkegkrlpcPPNC---------PDEVYQLMR 1129
Cdd:cd14043    184 DVFSFAIIMQEVIVrgapYCMLGLSPEEIIEKVRSP----------------------PPLCrpsvsmdqaPLECIQLMK 241
                          250       260
                   ....*....|....*....|
gi 1013071061 1130 KCWEFQPSNRTSFQNLIEGF 1149
Cdd:cd14043    242 QCWSEAPERRPTFDQIFDQF 261
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
881-1147 3.11e-18

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL2, also called p56 KKIAMRE, is expressed in testis, kidney, lung, and brain. It functions mainly in mature neurons and plays an important role in learning and memory. Inactivation of CDKL3, also called NKIAMRE (NKIATRE in rat), by translocation is associated with mild mental retardation. It has been reported that CDKL3 is lost in leukemic cells having a chromosome arm 5q deletion, and may contribute to the transformed phenotype. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270836 [Multi-domain]  Cd Length: 286  Bit Score: 86.32  E-value: 3.11e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDpegdNTGEQVAVKSL---KPESGGNHIAdlKKEIEILRNLYHENIVKYKGICTEDggNGIKLIME 957
Cdd:cd07846      9 VGEGSYGMVMKCRHK----ETGQIVAIKKFlesEDDKMVKKIA--MREIKMLKQLRHENLVNLIEVFRRK--KRWYLVFE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  958 FLPSGSLKEyLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYTv 1037
Cdd:cd07846     81 FVDHTVLDD-LEKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYT- 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1038 kdDRDSPVFWYAPECLM-QSKFYIASDVWSFGVTLHELLTY-----CDSDSSPMALFLKMIG---PTHGQMTvtrLVNTL 1108
Cdd:cd07846    159 --DYVATRWYRAPELLVgDTKYGKAVDVWAVGCLVTEMLTGeplfpGDSDIDQLYHIIKCLGnliPRHQELF---QKNPL 233
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1013071061 1109 KEGKRLPCP----------PNCPDEVYQLMRKCWEFQPSNRTSFQNLIE 1147
Cdd:cd07846    234 FAGVRLPEVkeveplerryPKLSGVVIDLAKKCLHIDPDKRPSCSELLH 282
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
589-841 3.29e-18

Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Yes (or c-Yes) is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. c-Yes kinase is the cellular homolog of the oncogenic protein (v-Yes) encoded by the Yamaguchi 73 and Esh sarcoma viruses. It displays functional overlap with other Src subfamily members, particularly Src. It also shows some unique functions such as binding to occludins, transmembrane proteins that regulate extracellular interactions in tight junctions. Yes also associates with a number of proteins in different cell types that Src does not interact with, like JAK2 and gp130 in pre-adipocytes, and Pyk2 in treated pulmonary vein endothelial cells. Although the biological function of Yes remains unclear, it appears to have a role in regulating cell-cell interactions and vesicle trafficking in polarized cells. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Yes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 86.28  E-value: 3.29e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  589 LGRGTRTHIYSGTLmdykddEGTSeekkiKVILKVLDPSHRdISLAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEE 668
Cdd:cd05069     20 LGQGCFGEVWMGTW------NGTT-----KVAIKTLKPGTM-MPEAFLQEAQIMKKLRHDKLVPLYAVVSEEPIYIVTEF 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  669 FVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGIPITV-- 746
Cdd:cd05069     88 MGKGSLLDFLKEGDGKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLV-------CKIADFGLARLIed 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  747 ---LSRQECIERIPWIAPECVEDSKnLSVAADKWSFGTTLWEICYNGEIP---LKDKTLIEK-ERFYESRCRPVTPscKE 819
Cdd:cd05069    161 neyTARQGAKFPIKWTAPEAALYGR-FTIKSDVWSFGILLTELVTKGRVPypgMVNREVLEQvERGYRMPCPQGCP--ES 237
                          250       260
                   ....*....|....*....|..
gi 1013071061  820 LADLMTRCMNYDPNQRPFFRAI 841
Cdd:cd05069    238 LHELMKLCWKKDPDERPTFEYI 259
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
881-1076 3.66e-18

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), Bypass UAS Requirement 1, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BUR1, also called SGV1, is a yeast CDK that is functionally equivalent to mammalian CDK9. It associates with the cyclin BUR2. BUR genes were orginally identified in a genetic screen as factors involved in general transcription. The BUR1/BUR2 complex phosphorylates the C-terminal domain of RNA polymerase II. In addition, this complex regulates histone modification by phosporylating Rad6 and mediating the association of the Paf1 complex with chromatin. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The BUR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270849 [Multi-domain]  Cd Length: 311  Bit Score: 86.60  E-value: 3.66e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVelcrYDPEGDNTGEQVAVKSL--KPESGGNHIADLKkEIEILRNLYHENIVKYKGICTEDGGNGIKLIMEF 958
Cdd:cd07866     16 LGEGTFGEV----YKARQIKTGRVVALKKIlmHNEKDGFPITALR-EIKILKKLKHPNVVPLIDMAVERPDKSKRKRGSV 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  959 ---LP------SGSLkeylpkNKNKINLKQ-QLK-YAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKA 1027
Cdd:cd07866     91 ymvTPymdhdlSGLL------ENPSVKLTEsQIKcYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADFGLARP 164
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1013071061 1028 IETDK------------EYYTVKDDRdspvfWY-APECLMQSKFY-IASDVWSFGVTLHELLT 1076
Cdd:cd07866    165 YDGPPpnpkggggggtrKYTNLVVTR-----WYrPPELLLGERRYtTAVDIWGIGCVFAEMFT 222
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
880-1084 3.96e-18

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. It is Ca2+/calmodulin (CaM)-regulated and actin-associated protein that contains an N-terminal kinase domain followed by an autoinhibitory CaM binding region and a large C-terminal extension with multiple functional domains including ankyrin (ANK) repeats, a cytoskeletal binding domain, a Death domain, and a serine-rich tail. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. The DAPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 85.84  E-value: 3.96e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  880 DLGEGHFGKVELCRYDpegdNTGEQVAVKSLKPESG-----GNHIADLKKEIEILRNLYHENIVKYKGIctEDGGNGIKL 954
Cdd:cd14194     12 ELGSGQFAVVKKCREK----STGLQYAAKFIKKRRTkssrrGVSREDIEREVSILKEIQHPNVITLHEV--YENKTDVIL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPSGSLKEYLPKnKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEH----QVKIGDFGLTKAIET 1030
Cdd:cd14194     86 ILELVAGGELFDFLAE-KESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNvpkpRIKIIDFGLAHKIDF 164
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1013071061 1031 DKEYytvKDDRDSPVFwYAPECLMQSKFYIASDVWSFGVTLHELLtycdSDSSP 1084
Cdd:cd14194    165 GNEF---KNIFGTPEF-VAPEIVNYEPLGLEADMWSIGVITYILL----SGASP 210
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
877-1076 4.35e-18

Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIM1 is a widely-expressed kinase belonging to the AMP-activated protein kinase (AMPK) subfamily. Although present in most tissues, NIM1 kinase activity is only observed in the brain and testis. NIM1 is capable of autophosphorylating and activating itself, but may be present in other tissues in the inactive form. The physiological function of NIM1 has yet to be elucidated. The NIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270977 [Multi-domain]  Cd Length: 255  Bit Score: 85.47  E-value: 4.35e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  877 RIR-DLGEGHFGKVELCRYDPegdnTGEQVAVKSL-KPESGGNHIADLKKEIEILRNLYHENIVK-YKGICTEdggNGIK 953
Cdd:cd14075      5 RIRgELGSGNFSQVKLGIHQL----TKEKVAIKILdKTKLDQKTQRLLSREISSMEKLHHPNIIRlYEVVETL---SKLH 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  954 LIMEFLPSGSLKEYLpKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGL-TKAIETDk 1032
Cdd:cd14075     78 LVMEYASGGELYTKI-STEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGFsTHAKRGE- 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1013071061 1033 eyyTVKDDRDSPVFwYAPEcLMQSKFYIAS--DVWSFGVTLHELLT 1076
Cdd:cd14075    156 ---TLNTFCGSPPY-AAPE-LFKDEHYIGIyvDIWALGVLLYFMVT 196
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
635-845 4.63e-18

Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow kinase on the X chromosome; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Btk and Bmx (also named Etk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Btk contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Btk is expressed in B-cells, and a variety of myeloid cells including mast cells, platelets, neutrophils, and dendrictic cells. It interacts with a variety of partners, from cytosolic proteins to nuclear transcription factors, suggesting a diversity of functions. Stimulation of a diverse array of cell surface receptors, including antigen engagement of the B-cell receptor, leads to PH-mediated membrane translocation of Btk and subsequent phosphorylation by Src kinase and activation. Btk plays an important role in the life cycle of B-cells including their development, differentiation, proliferation, survival, and apoptosis. Mutations in Btk cause the primary immunodeficiency disease, X-linked agammaglobulinaemia (XLA) in humans. Bmx is primarily expressed in bone marrow and the arterial endothelium, and plays an important role in ischemia-induced angiogenesis. It facilitates arterial growth, capillary formation, vessel maturation, and bone marrow-derived endothelial progenitor cell mobilization. The Btk/Bmx subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 85.32  E-value: 4.63e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  635 FFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGN 714
Cdd:cd05113     46 FIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMANGCLLNYLREMRKRFQTQQLLEMCKDVCEAMEYLESKQFLHRD 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  715 VCTKNLLLAREGIdsecgpfIKLSDPGIPITVLSRQ---ECIERIP--WIAPECVEDSKnLSVAADKWSFGTTLWEICYN 789
Cdd:cd05113    126 LAARNCLVNDQGV-------VKVSDFGLSRYVLDDEytsSVGSKFPvrWSPPEVLMYSK-FSSKSDVWAFGVLMWEVYSL 197
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1013071061  790 GEIP---LKDKTLIEK----ERFYesrcRPVTPSCKELAdLMTRCMNYDPNQRPFFRAIMRDI 845
Cdd:cd05113    198 GKMPyerFTNSETVEHvsqgLRLY----RPHLASEKVYT-IMYSCWHEKADERPTFKILLSNI 255
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
903-1144 4.99e-18

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK3 mRNA is up-regulated in fibroblasts after Ras-induced senescence, and its overexpression induces both autophagy and senescence in a fibroblast cell line. ULK3, through its kinase activity, positively regulates Gli proteins, mediators of the Sonic hedgehog (Shh) signaling pathway that is implicated in tissue homeostasis maintenance and neurogenesis. It is inhibited by binding to Suppressor of Fused (Sufu). The ULK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271023 [Multi-domain]  Cd Length: 252  Bit Score: 85.03  E-value: 4.99e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  903 EQVAVK-----SLKPESGGNhiadLKKEIEILRNLYHENIVKYKGIcTEDGGNgIKLIMEFLPSGSLKEY------LPKN 971
Cdd:cd14121     22 EVVAVKcvsksSLNKASTEN----LLTEIELLKKLKHPHIVELKDF-QWDEEH-IYLIMEYCSGGDLSRFirsrrtLPES 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  972 KNKINLkQQLKYAVQickgmdYLGSRQYVHRDLAARNVLVESEHQV--KIGDFGLTKAIETDKEYYTVkddRDSPVFwYA 1049
Cdd:cd14121     96 TVRRFL-QQLASALQ------FLREHNISHMDLKPQNLLLSSRYNPvlKLADFGFAQHLKPNDEAHSL---RGSPLY-MA 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1050 PECLMQSKFYIASDVWSFGVTLHElltycdsdsspmALFLKmigPTHGQMTVTRLVNTLKEGK--RLPCPP----NCPDE 1123
Cdd:cd14121    165 PEMILKKKYDARVDLWSVGVILYE------------CLFGR---APFASRSFEELEEKIRSSKpiEIPTRPelsaDCRDL 229
                          250       260
                   ....*....|....*....|.
gi 1013071061 1124 VYQLMRKcwefQPSNRTSFQN 1144
Cdd:cd14121    230 LLRLLQR----DPDRRISFEE 246
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
619-843 5.26e-18

Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Musk is a receptor PTK (RTK) containing an extracellular region with four immunoglobulin-like domains and a cysteine-rich cluster, a transmembrane segment, and an intracellular catalytic domain. Musk is expressed and concentrated in the postsynaptic membrane in skeletal muscle. It is essential for the establishment of the neuromuscular junction (NMJ), a peripheral synapse that conveys signals from motor neurons to muscle cells. Agrin, a large proteoglycan released from motor neurons, stimulates Musk autophosphorylation and activation, leading to the clustering of acetylcholine receptors (AChRs). To date, there is no evidence to suggest that agrin binds directly to Musk. Mutations in AChR, Musk and other partners are responsible for diseases of the NMJ, such as the autoimmune syndrome myasthenia gravis. The Musk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 85.65  E-value: 5.26e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  619 VILKVL-DPSHRDISLAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSDV------------ 685
Cdd:cd05050     38 VAVKMLkEEASADMQADFQREAALMAEFDHPNIVKLLGVCAVGKPMCLLFEYMAYGDLNEFLRHRSPRaqcslshstssa 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  686 ---------LTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGIPITVLSRQECI--- 753
Cdd:cd05050    118 rkcglnplpLSCTEQLCIAKQVAAGMAYLSERKFVHRDLATRNCLVGENMV-------VKIADFGLSRNIYSADYYKase 190
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  754 -ERIP--WIAPECVEDSKnLSVAADKWSFGTTLWEICYNGEIPLkdKTLIEKERFYESR------CRPVTPSckELADLM 824
Cdd:cd05050    191 nDAIPirWMPPESIFYNR-YTTESDVWAYGVVLWEIFSYGMQPY--YGMAHEEVIYYVRdgnvlsCPDNCPL--ELYNLM 265
                          250
                   ....*....|....*....
gi 1013071061  825 TRCMNYDPNQRPFFRAIMR 843
Cdd:cd05050    266 RLCWSKLPSDRPSFASINR 284
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
881-1076 5.75e-18

Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This family is composed of MLCKs and related MLCK-like kinase domains from giant STKs such as titin, obscurin, SPEG, Unc-89, Trio, kalirin, and Twitchin. Also included in this family are Death-Associated Protein Kinases (DAPKs) and Death-associated protein kinase-Related Apoptosis-inducing protein Kinase (DRAKs). MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. Titin, obscurin, Twitchin, and SPEG are muscle proteins involved in the contractile apparatus. The giant STKs are multidomain proteins containing immunoglobulin (Ig), fibronectin type III (FN3), SH3, RhoGEF, PH and kinase domains. Titin, obscurin, Twitchin, and SPEG contain many Ig domain repeats at the N-terminus, while Trio and Kalirin contain spectrin-like repeats. The MLCK-like family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270908 [Multi-domain]  Cd Length: 247  Bit Score: 84.63  E-value: 5.75e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDpegdNTGEQVAVKSLKPESGGNhiADLKKEIEILRNLYHENIVK----YKGictedgGNGIKLIM 956
Cdd:cd14006      1 LGRGRFGVVKRCIEK----ATGREFAAKFIPKRDKKK--EAVLREISILNQLQHPRIIQlheaYES------PTELVLIL 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  957 EFLPSGSLKEYLpKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVES--EHQVKIGDFGLTKAIETDKEY 1034
Cdd:cd14006     69 ELCSGGELLDRL-AERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADrpSPQIKIIDFGLARKLNPGEEL 147
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1013071061 1035 YTVKddrDSPVFwYAPECLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd14006    148 KEIF---GTPEF-VAPEIVNGEPVSLATDMWSIGVLTYVLLS 185
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
875-1145 6.10e-18

Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Pat1 (also called Ran1), Saccharomyces cerevisiae VHS1 and KSP1, and similar fungal STKs. Pat1 blocks Mei2, an RNA-binding protein which is indispensable in the initiation of meiosis. Pat1 is inactivated and Mei2 activated, which initiates meiosis, under nutrient-deprived conditions through a signaling cascade involving Ste11. Meiosis induced by Pat1 inactivation may show different characteristics than normal meiosis including aberrant positioning of centromeres. VHS1 was identified in a screen for suppressors of cell cycle arrest at the G1/S transition, while KSP1 may be involved in regulating PRP20, which is required for mRNA export and maintenance of nuclear structure. The Pat1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 85.09  E-value: 6.10e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  875 LKRIRDLGEGHFGKVelcrYDPEGDNTGEQVAVKSL-KPESGGNHIADLKK-----EIEILRNLY-HENIVKY-KGICTE 946
Cdd:cd13993      2 YQLISPIGEGAYGVV----YLAVDLRTGRKYAIKCLyKSGPNSKDGNDFQKlpqlrEIDLHRRVSrHPNIITLhDVFETE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  947 DGgngIKLIMEFLPSGSLKEYLpKNKNKINLKQQL--KYAVQICKGMDYLGSRQYVHRDLAARNVLVE-SEHQVKIGDFG 1023
Cdd:cd13993     78 VA---IYIVLEYCPNGDLFEAI-TENRIYVGKTELikNVFLQLIDAVKHCHSLGIYHRDIKPENILLSqDEGTVKLCDFG 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1024 LTKAIETDKEYYTVKDdrdspvFWYAPECLMQ----SKFY--IASDVWSFGVTLHELL-------TYCDSDSSPMALFLK 1090
Cdd:cd13993    154 LATTEKISMDFGVGSE------FYMAPECFDEvgrsLKGYpcAAGDIWSLGIILLNLTfgrnpwkIASESDPIFYDYYLN 227
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1013071061 1091 migpthgQMTVTRLVntlkegkrlpcpPNCPDEVYQLMRKCWEFQPSNRTSFQNL 1145
Cdd:cd13993    228 -------SPNLFDVI------------LPMSDDFYNLLRQIFTVNPNNRILLPEL 263
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
881-1036 6.79e-18

Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GCN2 (or EIF2AK4) is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. Its kinase domain is activated via conformational changes as a result of the binding of uncharged tRNA to the HisRS-like domain. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270948 [Multi-domain]  Cd Length: 278  Bit Score: 85.11  E-value: 6.79e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRydpegdNT--GEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGNGIKliMEF 958
Cdd:cd14046     14 LGKGAFGQVVKVR------NKldGRYYAIKKIKLRSESKNNSRILREVMLLSRLNHQHVVRYYQAWIERANLYIQ--MEY 85
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1013071061  959 LPSGSLKEyLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYT 1036
Cdd:cd14046     86 CEKSTLRD-LIDSGLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLATSNKLNVELAT 162
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
877-1076 6.90e-18

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-1 is expressed ubiquitously and is localized in the cytoplasm. Its kinase activity is cell cycle dependent and peaks at the S and G2 phases. PCTAIRE-1 is highly expressed in the brain and may play a role in regulating neurite outgrowth. It can also associate with Trap (Tudor repeat associator with PCTAIRE-2), a physiological partner of PCTAIRE-2; with p11, a small dimeric protein with similarity to S100; and with 14-3-3 proteins, mediators of phosphorylation-dependent interactions in many different proteins. PCTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270854 [Multi-domain]  Cd Length: 297  Bit Score: 85.82  E-value: 6.90e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  877 RIRDLGEGHFGKVelcrYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDggNGIKLIM 956
Cdd:cd07873      6 KLDKLGEGTYATV----YKGRSKLTDNLVALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIIHTE--KSLTLVF 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  957 EFLPSgSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYt 1036
Cdd:cd07873     80 EYLDK-DLKQYLDDCGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKSIPTKTY- 157
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1013071061 1037 vkdDRDSPVFWY-APECLMQSKFYIAS-DVWSFGVTLHELLT 1076
Cdd:cd07873    158 ---SNEVVTLWYrPPDILLGSTDYSTQiDMWGVGCIFYEMST 196
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
587-836 7.34e-18

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 88.15  E-value: 7.34e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  587 EHLGRGTRTHIYSGTlmdykdDEGTSEEkkikVILKVLDPSHR---DISLAFFEAASMMRQVSHKHIVYLYGVCVRDVEN 663
Cdd:COG0515     13 RLLGRGGMGVVYLAR------DLRLGRP----VALKVLRPELAadpEARERFRREARALARLNHPNIVRVYDVGEEDGRP 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  664 IMVEEFVEGGPLDLFMHRKSdVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGidsecgpFIKLSDPGIp 743
Cdd:COG0515     83 YLVMEYVEGESLADLLRRRG-PLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDG-------RVKLIDFGI- 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  744 ITVLSRQECIER------IPWIAPECVEDSKnLSVAADKWSFGTTLWEICYnGEIPLKDKTLIE-------KERFYESRC 810
Cdd:COG0515    154 ARALGGATLTQTgtvvgtPGYMAPEQARGEP-VDPRSDVYSLGVTLYELLT-GRPPFDGDSPAEllrahlrEPPPPPSEL 231
                          250       260
                   ....*....|....*....|....*.
gi 1013071061  811 RPVTPSckELADLMTRCMNYDPNQRP 836
Cdd:COG0515    232 RPDLPP--ALDAIVLRALAKDPEERY 255
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
880-1078 8.14e-18

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. DAPK2 is also called DAPK-related protein 1 (DRP-1), while DAPK3 has also been named DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk). These proteins are ubiquitously expressed in adult tissues, are capable of cross talk with each other, and may act synergistically in regulating cell death. The DAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 84.85  E-value: 8.14e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  880 DLGEGHFGKVELCRYDpegdNTGEQVAVKSLKPESG-----GNHIADLKKEIEILRNLYHENIVKYKGICteDGGNGIKL 954
Cdd:cd14105     12 ELGSGQFAVVKKCREK----STGLEYAAKFIKKRRSkasrrGVSREDIEREVSILRQVLHPNIITLHDVF--ENKTDVVL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPSGSLKEYLPKnKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLV----ESEHQVKIGDFGLTKAIET 1030
Cdd:cd14105     86 ILELVAGGELFDFLAE-KESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLldknVPIPRIKLIDFGLAHKIED 164
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1013071061 1031 DKEYytvKDDRDSPVFwYAPECLMQSKFYIASDVWSFGVTLHELLTYC 1078
Cdd:cd14105    165 GNEF---KNIFGTPEF-VAPEIVNYEPLGLEADMWSIGVITYILLSGA 208
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
580-841 9.07e-18

Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristylation sites (Srm) and Breast tumor kinase (Brk); PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Srm and Brk (also called protein tyrosine kinase 6) are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Brk has been found to be overexpressed in a majority of breast tumors. Src kinases in general contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr; they are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Srm and Brk however, lack the N-terminal myristylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. The Srm/Brk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133248 [Multi-domain]  Cd Length: 261  Bit Score: 84.41  E-value: 9.07e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  580 KKDLVQGEHLGRGTRTHIYSGTLMDykddegtseekKIKVILKVLDPSHRDISLAFFEAASMMRQVSHKHIVYLYGVCVR 659
Cdd:cd05148      5 REEFTLERKLGSGYFGEVWEGLWKN-----------RVRVAIKILKSDDLLKQQDFQKEVQALKRLRHKHLISLFAVCSV 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  660 DVENIMVEEFVEGGPLDLFMhRKSD--VLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLareGIDSECgpfiKL 737
Cdd:cd05148     74 GEPVYIITELMEKGSLLAFL-RSPEgqVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILV---GEDLVC----KV 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  738 SDPGI------PITVLSRQecieRIP--WIAPECVEDSKnLSVAADKWSFGTTLWEICYNGEIPLKDKTLIEKERFYESR 809
Cdd:cd05148    146 ADFGLarlikeDVYLSSDK----KIPykWTAPEAASHGT-FSTKSDVWSFGILLYEMFTYGQVPYPGMNNHEVYDQITAG 220
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1013071061  810 CR-PVTPSC-KELADLMTRCMNYDPNQRPFFRAI 841
Cdd:cd05148    221 YRmPCPAKCpQEIYKIMLECWAAEPEDRPSFKAL 254
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
881-1075 1.10e-17

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. It slows down cell proliferation, inducing cell cycle arrest and enhancing cell differentiation. PKC-delta is also involved in the regulation of transcription as well as immune and inflammatory responses. It plays a central role in the genotoxic stress response that leads to DNA damaged-induced apoptosis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 85.38  E-value: 1.10e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCrydpEGDNTGEQVAVKSLKPEsggnhIADLKKEIEI------LRNLYHENIVKYKGICTEDGGNGIKL 954
Cdd:cd05620      3 LGKGSFGKVLLA----ELKGKGEYFAVKALKKD-----VVLIDDDVECtmvekrVLALAWENPFLTHLYCTFQTKEHLFF 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPSGSLKEYLpKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAietdkey 1034
Cdd:cd05620     74 VMEFLNGGDLMFHI-QDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKE------- 145
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1013071061 1035 yTVKDDRDSPVF-----WYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd05620    146 -NVFGDNRASTFcgtpdYIAPEILQGLKYTFSVDWWSFGVLLYEML 190
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
875-1124 1.16e-17

Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include human PRKX (X chromosome-encoded protein kinase), Drosophila DC2, and similar proteins. PRKX is present in many tissues including fetal and adult brain, kidney, and lung. The PRKX gene is located in the Xp22.3 subregion and has a homolog called PRKY on the Y chromosome. An abnormal interchange between PRKX aand PRKY leads to the sex reversal disorder of XX males and XY females. PRKX is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PRKX-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270763 [Multi-domain]  Cd Length: 292  Bit Score: 84.79  E-value: 1.16e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  875 LKRIRDLGEGHFGKVELCRydpegDNTGEQ-VAVKSLK-PEsggnhIADLKK------EIEILRNLYHENIVKYkgICTE 946
Cdd:cd05612      3 FERIKTIGTGTFGRVHLVR-----DRISEHyYALKVMAiPE-----VIRLKQeqhvhnEKRVLKEVSHPFIIRL--FWTE 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  947 DGGNGIKLIMEFLPSGSLKEYLpKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTK 1026
Cdd:cd05612     71 HDQRFLYMLMEYVPGGELFSYL-RNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAK 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1027 AIeTDKEyYTVKDDRDspvfWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDS--DSSPMALFLKMIG-----PTHGQM 1099
Cdd:cd05612    150 KL-RDRT-WTLCGTPE----YLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPffDDNPFGIYEKILAgklefPRHLDL 223
                          250       260
                   ....*....|....*....|....*...
gi 1013071061 1100 TVTRLVNTLKE---GKRLPCPPNCPDEV 1124
Cdd:cd05612    224 YAKDLIKKLLVvdrTRRLGNMKNGADDV 251
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
880-1084 1.19e-17

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK2, also called DAPK-related protein 1 (DRP-1), is a Ca2+/calmodulin (CaM)-regulated protein containing an N-terminal kinase domain, a CaM autoinhibitory site and a dimerization module. It lacks the cytoskeletal binding regions of DAPK1 and the exogenous protein has been shown to be soluble and cytoplasmic. FLAG-tagged DAPK2, however, accumulated within membrane-enclosed autophagic vesicles. It is unclear where endogenous DAPK2 is localized. DAPK2 participates in TNF-alpha and FAS-receptor induced cell death and enhances neutrophilic maturation in myeloid leukemic cells. It contributes to the induction of anoikis and its down-regulation is implicated in the beta-catenin induced resistance of malignant epithelial cells to anoikis. The DAPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 84.24  E-value: 1.19e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  880 DLGEGHFGKVELCRYDpegdNTGEQVAVKSLKPESG-----GNHIADLKKEIEILRNLYHENIVKYKGIctEDGGNGIKL 954
Cdd:cd14196     12 ELGSGQFAIVKKCREK----STGLEYAAKFIKKRQSrasrrGVSREEIEREVSILRQVLHPNIITLHDV--YENRTDVVL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPSGSLKEYLPKnKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEH----QVKIGDFGLTKAIET 1030
Cdd:cd14196     86 ILELVSGGELFDFLAQ-KESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIED 164
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1013071061 1031 DKEYytvKDDRDSPVFwYAPECLMQSKFYIASDVWSFGVTLHELLtycdSDSSP 1084
Cdd:cd14196    165 GVEF---KNIFGTPEF-VAPEIVNYEPLGLEADMWSIGVITYILL----SGASP 210
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
911-1149 1.20e-17

Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: GCN2, protein kinase regulated by RNA (PKR), heme-regulated inhibitor kinase (HRI), and PKR-like endoplasmic reticulum kinase (PERK). GCN2 is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kappaB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. The degenerate pseudokinase domain of GCN2 may function as a regulatory domain. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 83.95  E-value: 1.20e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  911 KPESGGNHIADLKKEIEILRNLYHENIVKYKGICTE----DGGNGIKLIMEFLPSGSLKEYLPKNKNkINLKQQLKYAVQ 986
Cdd:cd14012     34 KTSNGKKQIQLLEKELESLKKLRHPNLVSYLAFSIErrgrSDGWKVYLLTEYAPGGSLSELLDSVGS-VPLDTARRWTLQ 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  987 ICKGMDYLGSRQYVHRDLAARNVLVESEHQ---VKIGDFGLTKAIetDKEYYTVKDDRDSPVFWYAPECLMQSKFY-IAS 1062
Cdd:cd14012    113 LLEALEYLHRNGVVHKSLHAGNVLLDRDAGtgiVKLTDYSLGKTL--LDMCSRGSLDEFKQTYWLPPELAQGSKSPtRKT 190
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1063 DVWSFGVtlhelltycdsdsspmaLFLKMIgptHGQMTVTRLvNTLKEgkrLPCPPNCPDEVYQLMRKCWEFQPSNR-TS 1141
Cdd:cd14012    191 DVWDLGL-----------------LFLQML---FGLDVLEKY-TSPNP---VLVSLDLSASLQDFLSKCLSLDPKKRpTA 246

                   ....*...
gi 1013071061 1142 FQNLIEGF 1149
Cdd:cd14012    247 LELLPHEF 254
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
881-1094 1.27e-17

Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mammals have two cGK isoforms from different genes, cGKI and cGKII. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. cGK consists of an N-terminal regulatory domain containing a dimerization and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. cGKII is a membrane-bound protein that is most abundantly expressed in the intestine. It is also present in the brain nuclei, adrenal cortex, kidney, lung, and prostate. cGKI is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. cGKII plays a role in the regulation of secretion, such as renin secretion by the kidney and aldosterone secretion by the adrenal. It also regulates bone growth and the circadian rhythm. The cGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270724 [Multi-domain]  Cd Length: 262  Bit Score: 84.20  E-value: 1.27e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDPegdnTGEQVAVKSLKPesggNHIAD------LKKEIEILRNLYHENIVKYkgICTEDGGNGIKL 954
Cdd:cd05572      1 LGVGGFGRVELVQLKS----KGRTFALKCVKK----RHIVQtrqqehIFSEKEILEECNSPFIVKL--YRTFKDKKYLYM 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPSGSLKEYLpKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEY 1034
Cdd:cd05572     71 LMEYCLGGELWTIL-RDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKKLGSGRKT 149
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1013071061 1035 YTvkddrdspvF-----WYAPECLMQSKFYIASDVWSFGVTLHELLT----YCDSDSSPMALF---LKMIGP 1094
Cdd:cd05572    150 WT---------FcgtpeYVAPEIILNKGYDFSVDYWSLGILLYELLTgrppFGGDDEDPMKIYniiLKGIDK 212
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
882-1089 1.31e-17

N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class III myosins are motor proteins with an N-terminal kinase catalytic domain and a C-terminal actin-binding motor domain. Class III myosins are present in the photoreceptors of invertebrates and vertebrates and in the auditory hair cells of mammals. The kinase domain of myosin III can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, and can autophosphorylate the C-terminal motor domain. Myosin III may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. It may also function as a cargo carrier during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The Drosophila class III myosin, called NinaC (Neither inactivation nor afterpotential protein C), is critical in normal adaptation and termination of photoresponse. Vertebrates contain two isoforms of class III myosin, IIIA and IIIB. This subfamily also includes mammalian NIK-like embryo-specific kinase (NESK), Traf2- and Nck-interacting kinase (TNIK), and mitogen-activated protein kinase (MAPK) kinase kinase kinase 4/6. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The class III myosin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270785 [Multi-domain]  Cd Length: 275  Bit Score: 84.28  E-value: 1.31e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  882 GEGHFGKVelcrYDPEGDNTGEQVAVKSLKPESggNHIADLKKEIEILRNL-YHENIVKYKGICTEDGGNG----IKLIM 956
Cdd:cd06608     15 GEGTYGKV----YKARHKKTGQLAAIKIMDIIE--DEEEEIKLEINILRKFsNHPNIATFYGAFIKKDPPGgddqLWLVM 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  957 EFLPSGSLKEYLpknKNKINLKQQLKYAV------QICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIET 1030
Cdd:cd06608     89 EYCGGGSVTDLV---KGLRKKGKRLKEEWiayilrETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFGVSAQLDS 165
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1013071061 1031 DKEyytvkdDRDSPV---FWYAPECLMQSKFYIA-----SDVWSFGVTLHELltyCD-----SDSSPM-ALFL 1089
Cdd:cd06608    166 TLG------RRNTFIgtpYWMAPEVIACDQQPDAsydarCDVWSLGITAIEL---ADgkpplCDMHPMrALFK 229
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
876-1076 1.33e-17

Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MOK, also called Renal tumor antigen 1 (RAGE-1), is widely expressed and is enriched in testis, kidney, lung, and brain. It is expressed in approximately 50% of renal cell carcinomas (RCC) and is a potential target for immunotherapy. MOK is stabilized by its association with the HSP90 molecular chaperone. It is induced by the transcription factor Cdx2 and may be involved in regulating intestinal epithelial development and differentiation. The MOK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270825 [Multi-domain]  Cd Length: 282  Bit Score: 84.63  E-value: 1.33e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  876 KRIRDLGEGHFGKVELCRYDpegdNTGEQVAVKSLKpesggNHIADLK-----KEIEILRNL-YHENIVKYKGICTEDGG 949
Cdd:cd07831      2 KILGKIGEGTFSEVLKAQSR----KTGKYYAIKCMK-----KHFKSLEqvnnlREIQALRRLsPHPNILRLIEVLFDRKT 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  950 NGIKLIMEfLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHqVKIGDFGLTKAIE 1029
Cdd:cd07831     73 GRLALVFE-LMDMNLYELIKGRKRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDDI-LKLADFGSCRGIY 150
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1013071061 1030 TDKEYYTVKDDRdspvfWY-APECLMQSKFYIAS-DVWSFGVTLHELLT 1076
Cdd:cd07831    151 SKPPYTEYISTR-----WYrAPECLLTDGYYGPKmDIWAVGCVFFEILS 194
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
881-1139 1.44e-17

Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. Vertebrates contain two members, LRRK1 and LRRK2, which show complementary expression in the brain. Mutations in LRRK2 are linked to both familial and sporadic forms of Parkinson's disease. The normal roles of LRRKs are not clearly defined. They may be involved in mitogen-activated protein kinase (MAPK) pathways, protein translation control, programmed cell death pathways, and cytoskeletal dynamics. The LRRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270902 [Multi-domain]  Cd Length: 275  Bit Score: 84.20  E-value: 1.44e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDpegdntGEQVAVKSLKPESGGN--------------------HIADLKKEIEILRNLYHENIVKY 940
Cdd:cd14000      2 LGDGGFGSVYRASYK------GEPVAVKIFNKHTSSNfanvpadtmlrhlratdamkNFRLLRQELTVLSHLHHPSIVYL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  941 KGICTEDggngIKLIMEFLPSGSLKEYLPKN-KNKINLKQQL--KYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQ- 1016
Cdd:cd14000     76 LGIGIHP----LMLVLELAPLGSLDHLLQQDsRSFASLGRTLqqRIALQVADGLRYLHSAMIIYRDLKSHNVLVWTLYPn 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1017 ----VKIGDFGLTKaiETDKEyyTVKDDRDSPVFwYAPECLMQSKFYIAS-DVWSFGVTLHELLtycdSDSSPMALFLKm 1091
Cdd:cd14000    152 saiiIKIADYGISR--QCCRM--GAKGSEGTPGF-RAPEIARGNVIYNEKvDVFSFGMLLYEIL----SGGAPMVGHLK- 221
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1013071061 1092 igpthgqmtvtrLVNTLKEGKRLPCP---PNC--PDEVYQLMRKCWEFQPSNR 1139
Cdd:cd14000    222 ------------FPNEFDIHGGLRPPlkqYECapWPEVEVLMKKCWKENPQQR 262
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
881-1084 1.80e-17

Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and Anti-Muellerian Hormone Type II Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR2 and AMHR2 belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors (GDFs), and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. BMPR2 and AMHR2 act primarily as a receptor for BMPs and AMH, respectively. BMPs induce bone and cartilage formation, as well as regulate tooth, kidney, skin, hair, haematopoietic, and neuronal development. Mutations in BMPR2A is associated with familial pulmonary arterial hypertension. AMH is mainly responsible for the regression of Mullerian ducts during male sex differentiation. It is expressed exclusively by somatic cells of the gonads. Mutations in either AMH or AMHR2 cause persistent Mullerian duct syndrome (PMDS), a rare form of male pseudohermaphroditism characterized by the presence of Mullerian derivatives (ovary and tubes) in otherwise normally masculine males. The BMPR2/AMHR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270956 [Multi-domain]  Cd Length: 300  Bit Score: 84.34  E-value: 1.80e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVelCRydpeGDNTGEQVAVKSLKPESGGNHIADlkKEIEILRNLYHENIVKYKGIC---TEDGGNGIKLIME 957
Cdd:cd14054      3 IGQGRYGTV--WK----GSLDERPVAVKVFPARHRQNFQNE--KDIYELPLMEHSNILRFIGADerpTADGRMEYLLVLE 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  958 FLPSGSLKEYLpkNKNKINLKQQLKYAVQICKGMDYLGS-----RQY----VHRDLAARNVLVESEHQVKIGDFGLTKAI 1028
Cdd:cd14054     75 YAPKGSLCSYL--RENTLDWMSSCRMALSLTRGLAYLHTdlrrgDQYkpaiAHRDLNSRNVLVKADGSCVICDFGLAMVL 152
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1029 ETDKEYYTVKDDRDS-------PVFWYAPECLMQS-------KFYIASDVWSFGVTLHELLTYCdSDSSP 1084
Cdd:cd14054    153 RGSSLVRGRPGAAENasisevgTLRYMAPEVLEGAvnlrdceSALKQVDVYALGLVLWEIAMRC-SDLYP 221
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
878-1093 1.85e-17

Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Rad53 and Cds1 are the checkpoint kinase 2 (Chk2) homologs found in budding and fission yeast, respectively. They play a central role in the cell's response to DNA lesions to prevent genome rearrangements and maintain genome integrity. They are phosphorylated in response to DNA damage and incomplete replication, and are essential for checkpoint control. They help promote DNA repair by stalling the cell cycle prior to mitosis in the presence of DNA damage. The Rad53/Cds1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 83.68  E-value: 1.85e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVELCRydpeGDNTGEQVAVKSL---KPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDggNGIKL 954
Cdd:cd14098      5 IDRLGSGTFAEVKKAV----EVETGKMRAIKQIvkrKVAGNDKNLQLFQREINILKSLEHPGIVRLIDWYEDD--QHIYL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPSGSLKEYLPKNkNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQ--VKIGDFGLTKAIETDk 1032
Cdd:cd14098     79 VMEYVEGGDLMDFIMAW-GAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDPviVKISDFGLAKVIHTG- 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1013071061 1033 eyyTVKDDRDSPVFWYAPECLMQSK------FYIASDVWSFGVTLHELLT-YCDSDSSPMALFLKMIG 1093
Cdd:cd14098    157 ---TFLVTFCGTMAYLAPEILMSKEqnlqggYSNLVDMWSVGCLVYVMLTgALPFDGSSQLPVEKRIR 221
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
878-1076 1.86e-17

Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDK1 carries an N-terminal catalytic domain and a C-terminal pleckstrin homology (PH) domain that binds phosphoinositides. It phosphorylates the activation loop of AGC kinases that are regulated by PI3K such as PKB, SGK, and PKC, among others, and is crucial for their activation. Thus, it contributes in regulating many processes including metabolism, growth, proliferation, and survival. PDK1 also has the ability to autophosphorylate and is constitutively active in mammalian cells. It is essential for normal embryo development and is important in regulating cell volume. The PDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270733 [Multi-domain]  Cd Length: 278  Bit Score: 83.80  E-value: 1.86e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVELCRydpegDN-TGEQVAVKSLKPEsggnHIADLKK------EIEILRNLYHENIVKYkgICT-EDGG 949
Cdd:cd05581      6 GKPLGEGSYSTVVLAK-----EKeTGKEYAIKVLDKR----HIIKEKKvkyvtiEKEVLSRLAHPGIVKL--YYTfQDES 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  950 NgIKLIMEFLPSGSLKEYLPKNKNkINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIE 1029
Cdd:cd05581     75 K-LYFVLEYAPNGDLLEYIRKYGS-LDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGTAKVLG 152
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1013071061 1030 TDKEYYTVKDDRDSPVFWY--------------APECLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd05581    153 PDSSPESTKGDADSQIAYNqaraasfvgtaeyvSPELLNEKPAGKSSDLWALGCIIYQMLT 213
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
881-1141 2.24e-17

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 86.24  E-value: 2.24e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVelcrYDPEGDNTGEQVAVKSL--KPESGgnhiadlKKEIEILRNLYHENIVKYKGI----CTEDGGNGIKL 954
Cdd:PTZ00036    74 IGNGSFGVV----YEAICIDTSEKVAIKKVlqDPQYK-------NRELLIMKNLNHINIIFLKDYyyteCFKKNEKNIFL 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 --IMEFLPSGSLK--EYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVE-SEHQVKIGDFGLTKAIE 1029
Cdd:PTZ00036   143 nvVMEFIPQTVHKymKHYARNNHALPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQNLLIDpNTHTLKLCDFGSAKNLL 222
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1030 TDKEYYTVKDDRdspvFWYAPECLMQSKFYIAS-DVWSFGVTLHEL-LTY----CDSDSSPMALFLKMIG-PTHGQMTV- 1101
Cdd:PTZ00036   223 AGQRSVSYICSR----FYRAPELMLGATNYTTHiDLWSLGCIIAEMiLGYpifsGQSSVDQLVRIIQVLGtPTEDQLKEm 298
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1013071061 1102 ------TRLVNTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTS 1141
Cdd:PTZ00036   299 npnyadIKFPDVKPKDLKKVFPKGTPDDAINFISQFLKYEPLKRLN 344
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
625-848 2.27e-17

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK3 is a mitogen-activated protein kinase kinase kinases (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK3 activates multiple MAPK pathways and plays a role in apoptosis, proliferation, migration, and differentiation, depending on the cellular context. It is highly expressed in breast cancer cells and its signaling through c-Jun N-terminal kinase has been implicated in the migration, invasion, and malignancy of cancer cells. MLK3 also functions as a negative regulator of Inhibitor of Nuclear Factor-KappaB Kinase (IKK) and consequently, it also impacts inflammation and immunity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271049 [Multi-domain]  Cd Length: 267  Bit Score: 83.54  E-value: 2.27e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  625 DPSHrDISL---AFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLD--LFMHRKSDVLTTPWkfkvAKQLA 699
Cdd:cd14147     37 DPDE-DISVtaeSVRQEARLFAMLAHPNIIALKAVCLEEPNLCLVMEYAAGGPLSraLAGRRVPPHVLVNW----AVQIA 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  700 SALSYLEDKDLV---HGNVCTKNLLLAREGIDsEC--GPFIKLSDPGIPIT--VLSRQECIERIPWIAPECVEDSkNLSV 772
Cdd:cd14147    112 RGMHYLHCEALVpviHRDLKSNNILLLQPIEN-DDmeHKTLKITDFGLAREwhKTTQMSAAGTYAWMAPEVIKAS-TFSK 189
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1013071061  773 AADKWSFGTTLWEIcYNGEIPLK--DKTLIEKERFYESRCRPVTPSCKE-LADLMTRCMNYDPNQRPFFRAIMRDINKL 848
Cdd:cd14147    190 GSDVWSFGVLLWEL-LTGEVPYRgiDCLAVAYGVAVNKLTLPIPSTCPEpFAQLMADCWAQDPHRRPDFASILQQLEAL 267
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
879-1075 2.59e-17

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called Doublecortin-like and CAM kinase-like); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL (or DCAMKL) proteins belong to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL proteins contain a C-terminal kinase domain with similarity to CAMKs. They are involved in the regulation of cAMP signaling. Vertebrates contain three DCKL proteins (DCKL1-3); DCKL1 and 2 also contain a serine, threonine, and proline rich domain (SP), while DCKL3 contains only a single DCX domain instead of tandem domains. The DCKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 83.14  E-value: 2.59e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGHFGKVELCRYDpegdNTGEQVAVKSLKPES--GGNHIadLKKEIEILRNLYHENIVK-YKGICTEDGgngIKLI 955
Cdd:cd14095      6 RVIGDGNFAVVKECRDK----ATDKEYALKIIDKAKckGKEHM--IENEVAILRRVKHPNIVQlIEEYDTDTE---LYLV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  956 MEFLPSGSLKEYLpKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVEsEHQ-----VKIGDFGLtkAIET 1030
Cdd:cd14095     77 MELVKGGDLFDAI-TSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVV-EHEdgsksLKLADFGL--ATEV 152
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1013071061 1031 DKEYYTVKddrDSPVFwYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd14095    153 KEPLFTVC---GTPTY-VAPEILAETGYGLKVDIWAAGVITYILL 193
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
589-847 2.62e-17

Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte Tyrosine Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyr residues in protein substrates. ALK and LTK are orphan receptor PTKs (RTKs) whose ligands are not yet well-defined. ALK appears to play an important role in mammalian neural development as well as visceral muscle differentiation in Drosophila. ALK is aberrantly expressed as fusion proteins, due to chromosomal translocations, in about 60% of anaplastic large cell lymphomas (ALCLs). ALK fusion proteins are also found in rare cases of diffuse large B cell lymphomas (DLBCLs). LTK is mainly expressed in B lymphocytes and neuronal tissues. It is important in cell proliferation and survival. Transgenic mice expressing TLK display retarded growth and high mortality rate. In addition, a polymorphism in mouse and human LTK is implicated in the pathogenesis of systemic lupus erythematosus. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. They are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The ALK/LTK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270632 [Multi-domain]  Cd Length: 277  Bit Score: 83.59  E-value: 2.62e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  589 LGRGTRTHIYSGTLMDykddeGTSEEKKIKVILKVL--DPSHRDiSLAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMV 666
Cdd:cd05036     14 LGQGAFGEVYEGTVSG-----MPGDPSPLQVAVKTLpeLCSEQD-EMDFLMEALIMSKFNHPNIVRCIGVCFQRLPRFIL 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  667 EEFVEGGPLDLFMHRKSDVLTTPWKFK------VAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecGPFIKLSDP 740
Cdd:cd05036     88 LELMAGGDLKSFLRENRPRPEQPSSLTmldllqLAQDVAKGCRYLEENHFIHRDIAARNCLLTCKGP----GRVAKIGDF 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  741 GipitvLSRQecIER-------------IPWIAPECVEDSKnLSVAADKWSFGTTLWEICYNGEIPLKDKTLIEKERFYE 807
Cdd:cd05036    164 G-----MARD--IYRadyyrkggkamlpVKWMPPEAFLDGI-FTSKTDVWSFGVLLWEIFSLGYMPYPGKSNQEVMEFVT 235
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1013071061  808 SRCRPVTP-SC-KELADLMTRCMNYDPNQRPFFRAIMRDINK 847
Cdd:cd05036    236 SGGRMDPPkNCpGPVYRIMTQCWQHIPEDRPNFSTILERLNY 277
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
879-1076 2.65e-17

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. It associates with three autophagy-related proteins (Atg13, FIP200 amd Atg101) to form the ULK1 complex. All fours proteins are essential for autophagosome formation. ULK1 is regulated by both mammalian target-of rapamycin complex 1 (mTORC1) and AMP-activated protein kinase (AMPK). mTORC1 negatively regulates the ULK1 complex in a nutrient-dependent manner while AMPK stimulates autophagy by inhibiting mTORC1. ULK1 also plays neuron-specific roles and is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, neurite extension, and axon branching. The ULK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 83.14  E-value: 2.65e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDL-GEGHFGKVELCRYDPEGDntgEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGIctEDGGNGIKLIME 957
Cdd:cd14202      7 KDLiGHGAFAVVFKGRHKEKHD---LEVAVKCINKKNLAKSQTLLGKEIKILKELKHENIVALYDF--QEIANSVYLVME 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  958 FLPSGSLKEYLPK----NKNKINLKQQlkyavQICKGMDYLGSRQYVHRDLAARNVLVESEH---------QVKIGDFGL 1024
Cdd:cd14202     82 YCNGGDLADYLHTmrtlSEDTIRLFLQ-----QIAGAMKMLHSKGIIHRDLKPQNILLSYSGgrksnpnniRIKIADFGF 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1013071061 1025 TKAIETDKEYYTVKddrDSPVFwYAPECLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd14202    157 ARYLQNNMMAATLC---GSPMY-MAPEVIMSQHYDAKADLWSIGTIIYQCLT 204
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
879-1075 2.74e-17

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK2 is ubiquitously expressed and is essential in autophagy induction. It displays partially redundant functions with ULK1 and is able to compensate for the loss of ULK1 in non-selective autophagy. It also displays neuron-specific functions and is important in axon development. The ULK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 83.52  E-value: 2.74e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDL-GEGHFGKVELCRYDPEGDntgEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGIctEDGGNGIKLIME 957
Cdd:cd14201     11 KDLvGHGAFAVVFKGRHRKKTD---WEVAIKSINKKNLSKSQILLGKEIKILKELQHENIVALYDV--QEMPNSVFLVME 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  958 FLPSGSLKEYLpKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVE---------SEHQVKIGDFGLTKAI 1028
Cdd:cd14201     86 YCNGGDLADYL-QAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSyasrkkssvSGIRIKIADFGFARYL 164
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1013071061 1029 ETDKEYYTVKddrDSPVFwYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd14201    165 QSNMMAATLC---GSPMY-MAPEVIMSQHYDAKADLWSIGTVIYQCL 207
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
884-1090 2.97e-17

Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAST kinases, MAST-like (MASTL) kinases (also called greatwall kinase or Gwl), and fungal kinases with similarity to Saccharomyces cerevisiae Rim15 and Schizosaccharomyces pombe cek1. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. MASTL kinases carry only a catalytic domain which contains a long insert relative to other kinases. The fungal kinases in this subfamily harbor other domains in addition to a central catalytic domain, which like in MASTL, also contains an insert relative to MAST kinases. Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MASTL/Gwl is involved in the regulation of mitotic entry, mRNA stabilization, and DNA checkpoint recovery. The fungal proteins Rim15 and cek1 are involved in the regulation of meiosis and mitosis, respectively. The MAST-like kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270731 [Multi-domain]  Cd Length: 272  Bit Score: 83.03  E-value: 2.97e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  884 GHFGKVELCRYDpegdNTGEQVAVKSLKPES--GGNHIADLKKEIEILRNLYHENIVK-YKGICTEdggNGIKLIMEFLP 960
Cdd:cd05579      4 GAYGRVYLAKKK----STGDLYAIKVIKKRDmiRKNQVDSVLAERNILSQAQNPFVVKlYYSFQGK---KNLYLVMEYLP 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  961 SGSLK------EYLPKNKNKInlkqqlkYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKE- 1033
Cdd:cd05579     77 GGDLYsllenvGALDEDVARI-------YIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSKVGLVRRQi 149
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1034 -------YYTVKDDRDSPVF----WYAPECLMQSKFYIASDVWSFGVTLHELLTYCD--SDSSPMALFLK 1090
Cdd:cd05579    150 klsiqkkSNGAPEKEDRRIVgtpdYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPpfHAETPEEIFQN 219
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
879-1139 3.09e-17

Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related kinase 6 and 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 and Nek7 are the shortest Neks, consisting only of the catalytic domain and a very short N-terminal extension. They show distinct expression patterns and both appear to be downstream substrates of Nek9. They are required for mitotic spindle formation and cytokinesis. They may also be regulators of the p70 ribosomal S6 kinase. Nek6/7 is part of a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 83.09  E-value: 3.09e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGHFGKVELCRYDPEGDNtgeqVAVKSLKPESggnhIADLK------KEIEILRNLYHENIVKYKGICTEDggNGI 952
Cdd:cd08224      6 KKIGKGQFSVVYRARCLLDGRL----VALKKVQIFE----MMDAKarqdclKEIDLLQQLNHPNIIKYLASFIEN--NEL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  953 KLIMEFLPSGSLKEYLPKNKNK---INLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTK--A 1027
Cdd:cd08224     76 NIVLELADAGDLSRLIKHFKKQkrlIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGLGRffS 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1028 IETDKEYYTVkddrDSPvFWYAPECLMQSKFYIASDVWSFGVTLHELLTYcdsdSSPmalFLKmigpthGQMTVTRLVNT 1107
Cdd:cd08224    156 SKTTAAHSLV----GTP-YYMSPERIREQGYDFKSDIWSLGCLLYEMAAL----QSP---FYG------EKMNLYSLCKK 217
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1013071061 1108 LKEGKRLPCPPNC-PDEVYQLMRKCWEFQPSNR 1139
Cdd:cd08224    218 IEKCEYPPLPADLySQELRDLVAACIQPDPEKR 250
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
879-1076 3.37e-17

Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase (also called MAK-V); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HUNK/MAK-V was identified from a mammary tumor in an MMTV-neu transgenic mouse. It is required for the metastasis of c-myc-induced mammary tumors, but is not necessary for c-myc-induced primary tumor formation or normal development. It is required for HER2/neu-induced tumor formation and maintenance of the cells' tumorigenic phenotype. It is over-expressed in aggressive subsets of ovary, colon, and breast carcinomas. HUNK interacts with synaptopodin, and may also play a role in synaptic plasticity. The HUNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270972 [Multi-domain]  Cd Length: 262  Bit Score: 82.94  E-value: 3.37e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGHFGKVELCRYDPegdnTGEQVAVKSL---KPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDggNGIKLI 955
Cdd:cd14070      8 RKLGEGSFAKVREGLHAV----TGEKVAIKVIdkkKAKKDSYVTKNLRREGRIQQMIRHPNITQLLDILETE--NSYYLV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  956 MEFLPSGSLKEYLPKnKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLT---KAIETDK 1032
Cdd:cd14070     82 MELCPGGNLMHRIYD-KKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSncaGILGYSD 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1013071061 1033 EYYTvkdDRDSPVFwYAPECLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd14070    161 PFST---QCGSPAY-AAPELLARKKYGPKVDVWSIGVNMYAMLT 200
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
882-1143 3.55e-17

Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. There are two types of TGFbeta receptors included in this subfamily, I and II, that play different roles in signaling. For signaling to occur, the ligand first binds to the high-affinity type II receptor, which is followed by the recruitment of the low-affinity type I receptor to the complex and its activation through trans-phosphorylation by the type II receptor. The active type I receptor kinase starts intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. Different ligands interact with various combinations of types I and II receptors to elicit a specific signaling pathway. Activins primarily signal through combinations of ACVR1b/ALK7 and ACVR2a/b; myostatin and GDF11 through TGFbR1/ALK4 and ACVR2a/b; BMPs through ACVR1/ALK1 and BMPR2; and TGFbeta through TGFbR1 and TGFbR2. The TGFbR-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270900 [Multi-domain]  Cd Length: 289  Bit Score: 83.26  E-value: 3.55e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  882 GEGHFGKVELCRYDpegdntGEQVAVK--SLKPEsggnhiADLKKEIEILR--NLYHENIVKYkgICTEDGGNGIK---- 953
Cdd:cd13998      4 GKGRFGEVWKASLK------NEPVAVKifSSRDK------QSWFREKEIYRtpMLKHENILQF--IAADERDTALRtelw 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  954 LIMEFLPSGSLKEYLpkNKNKINLKQQLKYAVQICKGMDYL-----GSRQY----VHRDLAARNVLVESEHQVKIGDFGL 1024
Cdd:cd13998     70 LVTAFHPNGSL*DYL--SLHTIDWVSLCRLALSVARGLAHLhseipGCTQGkpaiAHRDLKSKNILVKNDGTCCIADFGL 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1025 TKAIETDkeyyTVKDDRDS-----PVFWYAPECL--------MQSkfYIASDVWSFGVTLHELLTYCDSDSSP----MAL 1087
Cdd:cd13998    148 AVRLSPS----TGEEDNANngqvgTKRYMAPEVLegainlrdFES--FKRVDIYAMGLVLWEMASRCTDLFGIveeyKPP 221
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1013071061 1088 FLKMIG--PTHGQMTVTRLVNTLKegkrlpcpPNCPD---------EVYQLMRKCWEFQPSNRTSFQ 1143
Cdd:cd13998    222 FYSEVPnhPSFEDMQEVVVRDKQR--------PNIPNrwlshpglqSLAETIEECWDHDAEARLTAQ 280
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
879-1085 3.98e-17

Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK2 is localized in the sperm neck, equatorial segment, and mid-piece of the sperm tail. Both TSSK1 and TSSK2 phosphorylate their common substrate TSKS (testis-specific-kinase-substrate). TSSK1/TSSK2 double knock-out mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 82.52  E-value: 3.98e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGHFGKVElcryDPEGDNTGEQVAVKSLKPESGGNHIAD--LKKEIEILRNLYHENIVK-YKGICTEDGGngIKLI 955
Cdd:cd14165      7 INLGEGSYAKVK----SAYSERLKCNVAIKIIDKKKAPDDFVEkfLPRELEILARLNHKSIIKtYEIFETSDGK--VYIV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  956 MEFLPSGSLKEYLpKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYY 1035
Cdd:cd14165     81 MELGVQGDLLEFI-KLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRCLRDENGR 159
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1013071061 1036 TVKddrdSPVF-----WYAPEcLMQSKFY--IASDVWSFGVTLHELL----TYCDSDSSPM 1085
Cdd:cd14165    160 IVL----SKTFcgsaaYAAPE-VLQGIPYdpRIYDIWSLGVILYIMVcgsmPYDDSNVKKM 215
PTK_Jak3_rpt1 cd14208
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is ...
875-1146 4.03e-17

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit, common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. Jaks are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271110 [Multi-domain]  Cd Length: 260  Bit Score: 82.64  E-value: 4.03e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  875 LKRIRDLGEGHFGKV-ELCRYDPEGDNTGE-QVAVKSLKPeSGGNHIADLKKEIEILRNLYHENIVKYKGICTedgGNGI 952
Cdd:cd14208      1 LTFMESLGKGSFTKIyRGLRTDEEDDERCEtEVLLKVMDP-THGNCQESFLEAASIMSQISHKHLVLLHGVCV---GKDS 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  953 KLIMEFLPSGSLKEYLPKN--KNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQ------VKIGDFGL 1024
Cdd:cd14208     77 IMVQEFVCHGALDLYLKKQqqKGPVAISWKLQVVKQLAYALNYLEDKQLVHGNVSAKKVLLSREGDkgsppfIKLSDPGV 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1025 TKAIeTDKEYYTvkdDRdspVFWYAPECLMQSK-FYIASDVWSFGVTLHELLtycdsdsspmalflkmigpTHGQMTVTR 1103
Cdd:cd14208    157 SIKV-LDEELLA---ER---IPWVAPECLSDPQnLALEADKWGFGATLWEIF-------------------SGGHMPLSA 210
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1013071061 1104 LVNTLK-----EGKRLPCPPNCpdEVYQLMRKCWEFQPSNRTSFQNLI 1146
Cdd:cd14208    211 LDPSKKlqfynDRKQLPAPHWI--ELASLIQQCMSYNPLLRPSFRAII 256
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
589-846 4.27e-17

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinases 12 and 13; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K12 is also called MAPK upstream kinase (MUK), dual leucine zipper-bearing kinase (DLK) or leucine-zipper protein kinase (ZPK). It is involved in the c-Jun N-terminal kinase (JNK) pathway that directly regulates axonal regulation through the phosphorylation of microtubule-associated protein 1B (MAP1B). It also regulates the differentiation of many cell types including adipocytes and may play a role in adipogenesis. MAP3K13, also called leucine zipper-bearing kinase (LZK), directly phosphorylates and activates MKK7, which in turn activates the JNK pathway. It also activates NF-kB through IKK activation and this activity is enhanced by antioxidant protein-1 (AOP-1). MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAP2Ks (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K12/13 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270961 [Multi-domain]  Cd Length: 237  Bit Score: 81.77  E-value: 4.27e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  589 LGRGTRTHIYSGTLMDykddegtsEEKKIKvilKVLDPSHRDISlaffeaasMMRQVSHKHIVYLYGVCVRDVENIMVEE 668
Cdd:cd14059      1 LGSGAQGAVFLGKFRG--------EEVAVK---KVRDEKETDIK--------HLRKLNHPNIIKFKGVCTQAPCYCILME 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  669 FVEGGPLDLFMHRKSDV---LTTPWkfkvAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGipit 745
Cdd:cd14059     62 YCPYGQLYEVLRAGREItpsLLVDW----SKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDV-------LKISDFG---- 126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  746 vlSRQECIER---------IPWIAPECVEdSKNLSVAADKWSFGTTLWEIcYNGEIPLK--DKTLIEKERFYESRCRPVT 814
Cdd:cd14059    127 --TSKELSEKstkmsfagtVAWMAPEVIR-NEPCSEKVDIWSFGVVLWEL-LTGEIPYKdvDSSAIIWGVGSNSLQLPVP 202
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1013071061  815 PSCKE-LADLMTRCMNYDPNQRPFFRAIMRDIN 846
Cdd:cd14059    203 STCPDgFKLLMKQCWNSKPRNRPSFRQILMHLD 235
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
881-1090 4.60e-17

Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SBK1, also called BSK146, is predominantly expressed in the brain. Its expression is increased in the developing brain during the late embryonic stage, coinciding with dramatic neuronal proliferation, migration, and maturation. SBK1 may play an important role in regulating brain development. The SBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270889 [Multi-domain]  Cd Length: 259  Bit Score: 82.37  E-value: 4.60e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDPegdnTGEQVAVKSLKPESggNHIADLKKEIEILRNL-YHENIVKYKGICTEDGGNGIkLIMEFL 959
Cdd:cd13987      1 LGEGTYGKVLLAVHKG----SGTKMALKFVPKPS--TKLKDFLREYNISLELsVHPHIIKTYDVAFETEDYYV-FAQEYA 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  960 PSGSLKEYLPKNK--NKINLKqqlKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEH--QVKIGDFGLTKAIETdkeyy 1035
Cdd:cd13987     74 PYGDLFSIIPPQVglPEERVK---RCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDcrRVKLCDFGLTRRVGS----- 145
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1013071061 1036 TVKddRDSPVFWY-APE-CLM--QSKFYI--ASDVWSFGVTLHELLTYC------DSDSSPMALFLK 1090
Cdd:cd13987    146 TVK--RVSGTIPYtAPEvCEAkkNEGFVVdpSIDVWAFGVLLFCCLTGNfpwekaDSDDQFYEEFVR 210
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
637-848 4.96e-17

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK4 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The specific function of MLK4 is yet to be determined. Mutations in the kinase domain of MLK4 have been detected in colorectal cancers. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 82.39  E-value: 4.96e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  637 EAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSDVLTTPWKFKV--------AKQLASALSYLEDK 708
Cdd:cd14146     42 QEAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEFARGGTLNRALAAANAAPGPRRARRIpphilvnwAVQIARGMLYLHEE 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  709 DLV---HGNVCTKN-LLLAREGIDSECGPFIKLSDPGIPIT--VLSRQECIERIPWIAPECVEDSKnLSVAADKWSFGTT 782
Cdd:cd14146    122 AVVpilHRDLKSSNiLLLEKIEHDDICNKTLKITDFGLAREwhRTTKMSAAGTYAWMAPEVIKSSL-FSKGSDIWSYGVL 200
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1013071061  783 LWEIcYNGEIPLK--DKTLIEKERFYESRCRPVTPSCKE-LADLMTRCMNYDPNQRPFFRAIMRDINKL 848
Cdd:cd14146    201 LWEL-LTGEVPYRgiDGLAVAYGVAVNKLTLPIPSTCPEpFAKLMKECWEQDPHIRPSFALILEQLTAI 268
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
577-848 6.58e-17

Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER1, ErbB1) is a receptor PTK (RTK) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands for EGFR include EGF, heparin binding EGF-like growth factor (HBEGF), epiregulin, amphiregulin, TGFalpha, and betacellulin. Upon ligand binding, EGFR can form homo- or heterodimers with other EGFR subfamily members. The EGFR signaling pathway is one of the most important pathways regulating cell proliferation, differentiation, survival, and growth. Overexpression and mutation in the kinase domain of EGFR have been implicated in the development and progression of a variety of cancers. A number of monoclonal antibodies and small molecule inhibitors have been developed that target EGFR, including the antibodies Cetuximab and Panitumumab, which are used in combination with other therapies for the treatment of colorectal cancer and non-small cell lung carcinoma (NSCLC). The small molecule inhibitors Gefitinib (Iressa) and Erlotinib (Tarceva), already used for NSCLC, are undergoing clinical trials for other types of cancer including gastrointestinal, breast, head and neck, and bladder. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 83.15  E-value: 6.58e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  577 RILKK-DLVQGEHLGRGTRTHIYSGTLMDykddEGtsEEKKIKVILKVL-DPSHRDISLAFFEAASMMRQVSHKHIVYLY 654
Cdd:cd05108      2 RILKEtEFKKIKVLGSGAFGTVYKGLWIP----EG--EKVKIPVAIKELrEATSPKANKEILDEAYVMASVDNPHVCRLL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  655 GVCVRDVENIMVEEFVEGGPLDlFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAregidsecGP- 733
Cdd:cd05108     76 GICLTSTVQLITQLMPFGCLLD-YVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVK--------TPq 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  734 FIKLSDPGIPITVLSRQECIE----RIP--WIAPECVEdSKNLSVAADKWSFGTTLWEIC------YNGeIPLKD-KTLI 800
Cdd:cd05108    147 HVKITDFGLAKLLGAEEKEYHaeggKVPikWMALESIL-HRIYTHQSDVWSYGVTVWELMtfgskpYDG-IPASEiSSIL 224
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1013071061  801 EK-ERFyesrcrPVTPSCK-ELADLMTRCMNYDPNQRPFFRAIMRDINKL 848
Cdd:cd05108    225 EKgERL------PQPPICTiDVYMIMVKCWMIDADSRPKFRELIIEFSKM 268
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
878-1074 6.83e-17

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO3 is also known as JIK (c-Jun N-terminal kinase inhibitory kinase) or KFC (kinase from chicken). It specifically activates JNK, presumably by phosphorylating and activating MKK4/MKK7. In Saccharomyces cerevisiae, TAO3 is a component of the RAM (regulation of Ace2p activity and cellular morphogenesis) signaling pathway. TAO3 is upregulated in retinal ganglion cells after axotomy, and may play a role in apoptosis. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270803 [Multi-domain]  Cd Length: 313  Bit Score: 83.16  E-value: 6.83e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVelcrYDPEGDNTGEQVAVKSLKPESGGNH--IADLKKEIEILRNLYHENIVKYKGICTEDggNGIKLI 955
Cdd:cd06633     26 LHEIGHGSFGAV----YFATNSHTNEVVAIKKMSYSGKQTNekWQDIIKEVKFLQQLKHPNTIEYKGCYLKD--HTAWLV 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  956 MEFLpSGSLKEYLPKNKNKInlkQQLKYAV---QICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDK 1032
Cdd:cd06633    100 MEYC-LGSASDLLEVHKKPL---QEVEIAAithGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIASPAN 175
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1013071061 1033 EYYtvkddrDSPvFWYAPECLM---QSKFYIASDVWSFGVTLHEL 1074
Cdd:cd06633    176 SFV------GTP-YWMAPEVILamdEGQYDGKVDIWSLGITCIEL 213
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
881-1076 6.85e-17

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK4, also called SAK or STK18, is structurally different from other PLKs in that it contains only one polo box that can form two adjacent polo boxes and a functional PDB by homodimerization. It is required for late mitotic progression, cell survival, and embryonic development. It localizes to centrosomes and is required for centriole duplication and chromosomal stability. Overexpression of PLK4 may be associated with colon tumors. The PLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271088 [Multi-domain]  Cd Length: 256  Bit Score: 81.83  E-value: 6.85e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGkvelCRYDPEGDNTGEQVAVKSL--KPESGGNHIADLKKEIEILRNLYHENIVKYKGIcTEDGgNGIKLIMEF 958
Cdd:cd14186      9 LGKGSFA----CVYRARSLHTGLEVAIKMIdkKAMQKAGMVQRVRNEVEIHCQLKHPSILELYNY-FEDS-NYVYLVLEM 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  959 LPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGL-TKAIETDKEYYTV 1037
Cdd:cd14186     83 CHNGEMSRYLKNRKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLaTQLKMPHEKHFTM 162
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1013071061 1038 KDDRDspvfWYAPECLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd14186    163 CGTPN----YISPEIATRSAHGLESDVWSLGCMFYTLLV 197
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
878-1074 7.29e-17

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIB myosin is expressed highly in retina. It is also present in the brain and testis. The human class IIIB myosin gene maps to a region that overlaps the locus for Bardet-Biedl syndrome, which is characterized by dysmorphic extremities, retinal dystrophy, obesity, male hypogenitalism, and renal abnormalities. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. They may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. They may also function as cargo carriers during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 82.35  E-value: 7.29e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVelcrYDPEGDNTGEQVAVKSLKPesggnhIADLKKEIE----ILRNL-YHENIVKYKGICTEDG---G 949
Cdd:cd06639     27 IETIGKGTYGKV----YKVTNKKDGSLAAVKILDP------ISDVDEEIEaeynILRSLpNHPNVVKFYGMFYKADqyvG 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  950 NGIKLIMEFLPSGSLKEYLpknKNKINLKQQLKYAV------QICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFG 1023
Cdd:cd06639     97 GQLWLVLELCNGGSVTELV---KGLLKCGQRLDEAMisyilyGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFG 173
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1013071061 1024 LTKAIEtdkeyyTVKDDRDSPV---FWYAPECLMQSKFYIAS-----DVWSFGVTLHEL 1074
Cdd:cd06639    174 VSAQLT------SARLRRNTSVgtpFWMAPEVIACEQQYDYSydarcDVWSLGITAIEL 226
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
877-1147 7.83e-17

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL1, also called p42 KKIALRE, is a glial protein that is upregulated in gliosis. It is present in neuroblastoma and A431 human carcinoma cells, and may be implicated in neoplastic transformation. The function of CDKL4 is unknown. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270837 [Multi-domain]  Cd Length: 286  Bit Score: 82.42  E-value: 7.83e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  877 RIRDLGEGHFGKVELCRYDpegdNTGEQVAVKSLKPESGGNHIADLK-KEIEILRNLYHENIVKYKGICTEDggNGIKLI 955
Cdd:cd07847      5 KLSKIGEGSYGVVFKCRNR----ETGQIVAIKKFVESEDDPVIKKIAlREIRMLKQLKHPNLVNLIEVFRRK--RKLHLV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  956 MEFLPSGSLKEyLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYY 1035
Cdd:cd07847     79 FEYCDHTVLNE-LEKNPRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFARILTGPGDDY 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1036 TvkdDRDSPVFWYAPECLMQSKFYIAS-DVWSFGVTLHELLTYC-----DSDSSPMALFLKMIG---PTHGQMTVTrlvN 1106
Cdd:cd07847    158 T---DYVATRWYRAPELLVGDTQYGPPvDVWAIGCVFAELLTGQplwpgKSDVDQLYLIRKTLGdliPRHQQIFST---N 231
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1013071061 1107 TLKEGKRLPCP----------PNCPDEVYQLMRKCWEFQPSNRTSFQNLIE 1147
Cdd:cd07847    232 QFFKGLSIPEPetrepleskfPNISSPALSFLKGCLQMDPTERLSCEELLE 282
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
866-1075 8.33e-17

Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group II PAKs, also called non-conventional PAKs, include PAK4, PAK5, and PAK6. Group II PAKs contain PBD (p21-binding domain) and catalytic domains, but lack other motifs found in group I PAKs, such as an AID (autoinhibitory domain) and SH3 binding sites. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. While group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX, no such binding has been demonstrated for group II PAKs. Some known substrates of group II PAKs are also substrates of group I PAKs such as Raf, BAD, LIMK and GEFH1. Unique group II substrates include MARK/Par-1 and PDZ-RhoGEF. Group II PAKs play important roles in filopodia formation, neuron extension, cytoskeletal organization, and cell survival. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270815 [Multi-domain]  Cd Length: 261  Bit Score: 81.72  E-value: 8.33e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  866 DPTHFEKRFLKrirdLGEGHFGKVELCRydpeGDNTGEQVAVKSLkpesggnhiaDLKK---------EIEILRNLYHEN 936
Cdd:cd06648      4 DPRSDLDNFVK----IGEGSTGIVCIAT----DKSTGRQVAVKKM----------DLRKqqrrellfnEVVIMRDYQHPN 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  937 IVK-YKGICTedgGNGIKLIMEFLPSGSLKEYLpkNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEH 1015
Cdd:cd06648     66 IVEmYSSYLV---GDELWVVMEFLEGGALTDIV--THTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDG 140
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1013071061 1016 QVKIGDFGLTKAIETDKEyytvkdDRDSPV---FWYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd06648    141 RVKLSDFGFCAQVSKEVP------RRKSLVgtpYWMAPEVISRLPYGTEVDIWSLGIMVIEMV 197
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
578-853 1.00e-16

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkC is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkC to its ligand, neurotrophin 3 (NT3), results in receptor oligomerization and activation of the catalytic domain. TrkC is broadly expressed in the nervous system and in some non-neural tissues including the developing heart. NT3/TrkC signaling plays an important role in the innervation of the cardiac conducting system and the development of smooth muscle cells. Mice deficient with NT3 and TrkC have multiple heart defects. NT3/TrkC signaling is also critical for the development and maintenance of enteric neurons that are important for the control of gut peristalsis. The TrkC subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 81.98  E-value: 1.00e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  578 ILKKDLVQGEHLGRGTRTHIYSGTLMDYkddegTSEEKKIKVILKVLDPSHRDISLAFFEAASMMRQVSHKHIVYLYGVC 657
Cdd:cd05094      2 IKRRDIVLKRELGEGAFGKVFLAECYNL-----SPTKDKMLVAVKTLKDPTLAARKDFQREAELLTNLQHDHIVKFYGVC 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  658 VRDVENIMVEEFVEGGPLDLFMH---------------RKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLL 722
Cdd:cd05094     77 GDGDPLIMVFEYMKHGDLNKFLRahgpdamilvdgqprQAKGELGLSQMLHIATQIASGMVYLASQHFVHRDLATRNCLV 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  723 ARegidsecGPFIKLSDPGIPITVLSRQ------ECIERIPWIAPECVEDSKnLSVAADKWSFGTTLWEICYNGEIP--- 793
Cdd:cd05094    157 GA-------NLLVKIGDFGMSRDVYSTDyyrvggHTMLPIRWMPPESIMYRK-FTTESDVWSFGVILWEIFTYGKQPwfq 228
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1013071061  794 LKDKTLIE---KERFYEsrcRP-VTPscKELADLMTRCMNYDPNQRPFFRAIMRDINKLEEQNP 853
Cdd:cd05094    229 LSNTEVIEcitQGRVLE---RPrVCP--KEVYDIMLGCWQREPQQRLNIKEIYKILHALGKATP 287
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
566-848 1.09e-16

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Alternative splicing of FGFR1 transcripts produces a variety of isoforms, which are differentially expressed in cells. FGFR1 binds the ligands, FGF1 and FGF2, with high affinity and has also been reported to bind FGF4, FGF6, and FGF9. FGFR1 signaling is critical in the control of cell migration during embryo development. It promotes cell proliferation in fibroblasts. Nuclear FGFR1 plays a role in the regulation of transcription. Mutations, insertions or deletions of FGFR1 have been identified in patients with Kallman's syndrome (KS), an inherited disorder characterized by hypogonadotropic hypogonadism and loss of olfaction. Aberrant FGFR1 expression has been found in some human cancers including 8P11 myeloproliferative syndrome (EMS), breast cancer, and pancreatic adenocarcinoma. FGFR1 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 82.37  E-value: 1.09e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  566 PVYPMSQLSFDRilkkdLVQGEHLGRGTRTHIYSGTLMDYkDDEGTSEEKKIKVILKVLDPSHRDISLAFFEAASMMRQV 645
Cdd:cd05098      3 PEDPRWELPRDR-----LVLGKPLGEGCFGQVVLAEAIGL-DKDKPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIG 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  646 SHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFM---------------HRKSDVLTTPWKFKVAKQLASALSYLEDKDL 710
Cdd:cd05098     77 KHKNIINLLGACTQDGPLYVIVEYASKGNLREYLqarrppgmeycynpsHNPEEQLSSKDLVSCAYQVARGMEYLASKKC 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  711 VHGNVCTKNLLLAREGIdsecgpfIKLSDPGIPITV----LSRQECIERIP--WIAPECVEDsKNLSVAADKWSFGTTLW 784
Cdd:cd05098    157 IHRDLAARNVLVTEDNV-------MKIADFGLARDIhhidYYKKTTNGRLPvkWMAPEALFD-RIYTHQSDVWSFGVLLW 228
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1013071061  785 EICYNGEIPLKDKTLIEKERFYESRCRPVTPS--CKELADLMTRCMNYDPNQRPFFRAIMRDINKL 848
Cdd:cd05098    229 EIFTLGGSPYPGVPVEELFKLLKEGHRMDKPSncTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRI 294
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
881-1076 1.11e-16

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK3 (or MYLK3) phosphorylates myosin regulatory light chain 2 and controls the contraction of cardiac muscles. It is expressed specifically in both the atrium and ventricle of the heart and its expression is regulated by the cardiac protein Nkx2-5. MLCK3 plays an important role in cardiogenesis by regulating the assembly of cardiac sarcomeres, the repeating contractile unit of striated muscle. MLCK3 contains a single kinase domain near the C-terminus and a unique N-terminal half, and unlike MLCK1/2, it does not appear to be regulated by Ca2+/calmodulin. The MLCK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 81.16  E-value: 1.11e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCrydpEGDNTGEQVAVKSLKPEsGGNHIADLKKEIEILRNLYHENIVK-YKGIcteDGGNGIKLIMEFL 959
Cdd:cd14192     12 LGGGRFGQVHKC----TELSTGLTLAAKIIKVK-GAKEREEVKNEINIMNQLNHVNLIQlYDAF---ESKTNLTLIMEYV 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  960 PSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLV--ESEHQVKIGDFGLTKAIETDKEyytV 1037
Cdd:cd14192     84 DGGELFDRITDESYQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILCvnSTGNQIKIIDFGLARRYKPREK---L 160
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1013071061 1038 KDDRDSPVFwYAPECLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd14192    161 KVNFGTPEF-LAPEVVNYDFVSFPTDMWSVGVITYMLLS 198
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
871-1139 1.12e-16

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and similar MAPKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human MAPK15 is also called Extracellular signal Regulated Kinase 8 (ERK8) while the rat protein is called ERK7. ERK7 and ERK8 display both similar and different biochemical properties. They autophosphorylate and activate themselves and do not require upstream activating kinases. ERK7 is constitutively active and is not affected by extracellular stimuli whereas ERK8 shows low basal activity and is activated by DNA-damaging agents. ERK7 and ERK8 also have different substrate profiles. Genome analysis shows that they are orthologs with similar gene structures. ERK7 and ERK 8 may be involved in the signaling of some nuclear receptor transcription factors. ERK7 regulates hormone-dependent degradation of estrogen receptor alpha while ERK8 down-regulates the transcriptional co-activation androgen and glucocorticoid receptors. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK15 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270841 [Multi-domain]  Cd Length: 337  Bit Score: 82.61  E-value: 1.12e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  871 EKRFLKR---IRDLGEGHFGKVeLCRYDpegDNTGEQVAvkslkpesggnhiadLKK----------------EIEILRN 931
Cdd:cd07852      2 DKHILRRyeiLKKLGKGAYGIV-WKAID---KKTGEVVA---------------LKKifdafrnatdaqrtfrEIMFLQE 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  932 LY-HENIVKYKGICTEDGGNGIKLIMEFLPSgSLKEYLPKNKNKINLKQQLKYavQICKGMDYLGSRQYVHRDLAARNVL 1010
Cdd:cd07852     63 LNdHPNIIKLLNVIRAENDKDIYLVFEYMET-DLHAVIRANILEDIHKQYIMY--QLLKALKYLHSGGVIHRDLKPSNIL 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1011 VESEHQVKIGDFGLTKAIETDkeyytvKDDRDSPVF-------WY-APECLMQSKFYI-ASDVWSFGVTLHELLTycdsd 1081
Cdd:cd07852    140 LNSDCRVKLADFGLARSLSQL------EEDDENPVLtdyvatrWYrAPEILLGSTRYTkGVDMWSVGCILGEMLL----- 208
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1013071061 1082 SSPM----------ALFLKMIGP--------THGQMTVTRLVNT-LKEGKRLP-CPPNCPDEVYQLMRKCWEFQPSNR 1139
Cdd:cd07852    209 GKPLfpgtstlnqlEKIIEVIGRpsaediesIQSPFAATMLESLpPSRPKSLDeLFPKASPDALDLLKKLLVFNPNKR 286
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
920-1139 1.15e-16

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek7 is required for mitotic spindle formation and cytokinesis. It is enriched in the centrosome and is critical for microtubule nucleation. Nek7 is activated by Nek9 during mitosis, and may regulate the p70 ribosomal S6 kinase. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 82.00  E-value: 1.15e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  920 ADLKKEIEILRNLYHENIVKYKGICTEDggNGIKLIMEFLPSGSLKE---YLPKNKNKINLKQQLKYAVQICKGMDYLGS 996
Cdd:cd08229     69 ADCIKEIDLLKQLNHPNVIKYYASFIED--NELNIVLELADAGDLSRmikHFKKQKRLIPEKTVWKYFVQLCSALEHMHS 146
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  997 RQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKeyyTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd08229    147 RRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKT---TAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAA 223
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1013071061 1077 ycdsdsspmalflkMIGPTHG-QMTVTRLVNTLKEGKRLPCPPN-CPDEVYQLMRKCWEFQPSNR 1139
Cdd:cd08229    224 --------------LQSPFYGdKMNLYSLCKKIEQCDYPPLPSDhYSEELRQLVNMCINPDPEKR 274
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
922-1145 1.55e-16

Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270947 [Multi-domain]  Cd Length: 269  Bit Score: 81.06  E-value: 1.55e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  922 LKKEIEILRNLYHENIVKYKGICTEDggNGIKLIMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVH 1001
Cdd:cd14045     49 IRKEVKQVRELDHPNLCKFIGGCIEV--PNVAIITEYCPKGSLNDVLLNEDIPLNWGFRFSFATDIARGMAYLHQHKIYH 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1002 RDLAARNVLVESEHQVKIGDFGLTKaietdkeyYTvKDDRDSPVFWY---------APECLMQSKFYI--ASDVWSFGVT 1070
Cdd:cd14045    127 GRLKSSNCVIDDRWVCKIADYGLTT--------YR-KEDGSENASGYqqrlmqvylPPENHSNTDTEPtqATDVYSYAII 197
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1013071061 1071 LHELLTYCD---SDSSPMALFLKmigPTHGQMTVTRLVNTlkegkrlpCPpnCPDEVYQLMRKCWEFQPSNRTSFQNL 1145
Cdd:cd14045    198 LLEIATRNDpvpEDDYSLDEAWC---PPLPELISGKTENS--------CP--CPADYVELIRRCRKNNPAQRPTFEQI 262
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
874-1074 1.90e-16

Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SIKs are part of a complex network that regulates Na,K-ATPase to maintain sodium homeostasis and blood pressure. Vertebrates contain three forms of SIKs (SIK1-3) from three distinct genes, which display tissue-specific effects. SIK1, also called SNF1LK, controls steroidogenic enzyme production in adrenocortical cells. In the brain, both SIK1 and SIK2 regulate energy metabolism. SIK2, also called QIK or SNF1LK2, is involved in the regulation of gluconeogenesis in the liver and lipogenesis in adipose tissues, where it phosphorylates the insulin receptor substrate-1. In the liver, SIK3 (also called QSK) regulates cholesterol and bile acid metabolism. In addition, SIK2 plays an important role in the initiation of mitosis and regulates the localization of C-Nap1, a centrosome linker protein. The SIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270973 [Multi-domain]  Cd Length: 253  Bit Score: 80.51  E-value: 1.90e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  874 FLKRIRDLGEGHFGKVELCRYDPegdnTGEQVAVKSL-KPESGGNHIADLKKEIEILRNLYHENIVK-YKGICTEDGgng 951
Cdd:cd14071      1 FYDIERTIGKGNFAVVKLARHRI----TKTEVAIKIIdKSQLDEENLKKIYREVQIMKMLNHPHIIKlYQVMETKDM--- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  952 IKLIMEFLPSGSLKEYLPKNkNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETD 1031
Cdd:cd14071     74 LYLVTEYASNGEIFDYLAQH-GRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFSNFFKPG 152
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1013071061 1032 KEYYTVKddrDSPVFwYAPEcLMQSKFYIAS--DVWSFGVTLHEL 1074
Cdd:cd14071    153 ELLKTWC---GSPPY-AAPE-VFEGKEYEGPqlDIWSLGVVLYVL 192
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
876-1080 2.05e-16

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Protein Kinase regulated by RNA; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKR (or EIF2AK2) contains an N-terminal double-stranded RNA (dsRNA) binding domain and a C-terminal catalytic kinase domain. It is activated by dsRNA, which is produced as a replication intermediate in virally infected cells. It plays a key role in mediating innate immune responses to viral infection. PKR is also directly activated by PACT (protein activator of PKR) and heparin, and is inhibited by viral proteins and RNAs. PKR also regulates transcription and signal transduction in diseased cells, playing roles in tumorigenesis and neurodegenerative diseases. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PKR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 80.61  E-value: 2.05e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  876 KRIRDLGEGHFGKVelCRYDPEGDNtgEQVAVKSLKpesggNHIADLKKEIEILRNLYHENIVKYKGiC----------- 944
Cdd:cd14047      9 KEIELIGSGGFGQV--FKAKHRIDG--KTYAIKRVK-----LNNEKAEREVKALAKLDHPNIVRYNG-Cwdgfdydpets 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  945 -TEDGGNGIKLI---MEFLPSGSLKEYLPK-NKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKI 1019
Cdd:cd14047     79 sSNSSRSKTKCLfiqMEFCEKGTLESWIEKrNGEKLDKVLALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGKVKI 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1013071061 1020 GDFGLTKAIETDKEYYTVKDDRDspvfWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDS 1080
Cdd:cd14047    159 GDFGLVTSLKNDGKRTKSKGTLS----YMSPEQISSQDYGKEVDIYALGLILFELLHVCDS 215
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
901-1076 2.15e-16

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK1 is a MAPK kinase kinase (MAPKKK or MKKK) that phosphorylates and activates activates the ERK1/2 and c-Jun N-terminal kinase (JNK) pathways by activating their respective MAPKKs, MEK1/2 and MKK4/MKK7, respectively. MEKK1 is important in regulating cell survival and apoptosis. MEKK1 also plays a role in cell migration, tissue maintenance and homeostasis, and wound healing. The MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270800 [Multi-domain]  Cd Length: 268  Bit Score: 80.55  E-value: 2.15e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  901 TGEQVAVKSLK-----PESGGNHIADLKKEIEILRNLYHENIVKYKGiCTEDGGNgIKLIMEFLPSGS----LKEYLPKN 971
Cdd:cd06630     24 TGTLMAVKQVSfcrnsSSEQEEVVEAIREEIRMMARLNHPNIVRMLG-ATQHKSH-FNIFVEWMAGGSvaslLSKYGAFS 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  972 KNKINlkqqlKYAVQICKGMDYLGSRQYVHRDLAARNVLVESE-HQVKIGDFG--------LTKAIETDKEYYtvkddrd 1042
Cdd:cd06630    102 ENVII-----NYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTgQRLRIADFGaaarlaskGTGAGEFQGQLL------- 169
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1013071061 1043 SPVFWYAPECLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd06630    170 GTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMAT 203
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
633-848 2.16e-16

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphA10, which contains an inactive tyr kinase domain, may function to attenuate signals of co-clustered active receptors. EphA10 is mainly expressed in the testis. Ephrin/EphR interaction results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. EphRs comprise the largest subfamily of receptor tyr kinases (RTKs). In general, class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The EphA10 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133195 [Multi-domain]  Cd Length: 266  Bit Score: 80.74  E-value: 2.16e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  633 LAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVH 712
Cdd:cd05064     51 RGFLAEALTLGQFDHSNIVRLEGVITRGNTMMIVTEYMSNGALDSFLRKHEGQLVAGQLMGMLPGLASGMKYLSEMGYVH 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  713 GNVCTKNLLLAREgIDSECGPFIKLSDPGIPiTVLSRQECIERIPWIAPECVEdSKNLSVAADKWSFGTTLWEICYNGEI 792
Cdd:cd05064    131 KGLAAHKVLVNSD-LVCKISGFRRLQEDKSE-AIYTTMSGKSPVLWAAPEAIQ-YHHFSSASDVWSFGIVMWEVMSYGER 207
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1013071061  793 PLKDKTLIEKERFYESRCR-PVTPSCKE-LADLMTRCMNYDPNQRPFFRAIMRDINKL 848
Cdd:cd05064    208 PYWDMSGQDVIKAVEDGFRlPAPRNCPNlLHQLMLDCWQKERGERPRFSQIHSILSKM 265
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
580-843 2.18e-16

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR2 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR2 results in a slow but sustained receptor activation. DDR2 binds mostly to fibrillar collagens as well as collagen X. DDR2 is widely expressed in many tissues with the highest levels found in skeletal muscle, skin, kidney and lung. It is important in cell proliferation and development. Mice, with a deletion of DDR2, suffer from dwarfism and delayed healing of epidermal wounds. DDR2 also contributes to collagen (type I) regulation by inhibiting fibrillogenesis and altering the morphology of collagen fibers. It is also expressed in immature dendritic cells (DCs), where it plays a role in DC activation and function. The DDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 81.19  E-value: 2.18e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  580 KKDLVQGEHLGRGT--RTHIYSGTLMD-YKDDE---GTSEEKKIKVILKVLDP-SHRDISLAFFEAASMMRQVSHKHIVY 652
Cdd:cd05095      4 RKLLTFKEKLGEGQfgEVHLCEAEGMEkFMDKDfalEVSENQPVLVAVKMLRAdANKNARNDFLKEIKIMSRLKDPNIIR 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  653 LYGVCVRDVENIMVEEFVEGGPLDLFMHRK---------SDVLT---TPWKFkVAKQLASALSYLEDKDLVHGNVCTKNL 720
Cdd:cd05095     84 LLAVCITDDPLCMITEYMENGDLNQFLSRQqpegqlalpSNALTvsySDLRF-MAAQIASGMKYLSSLNFVHRDLATRNC 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  721 LLAREGIdsecgpfIKLSDPGIPITVLS------RQECIERIPWIAPECVEDSKnLSVAADKWSFGTTLWEI-CYNGEIP 793
Cdd:cd05095    163 LVGKNYT-------IKIADFGMSRNLYSgdyyriQGRAVLPIRWMSWESILLGK-FTTASDVWAFGVTLWETlTFCREQP 234
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1013071061  794 ---LKDKTLIEKE-RFYESRCR----PVTPSCKE-LADLMTRCMNYDPNQRPFFRAIMR 843
Cdd:cd05095    235 ysqLSDEQVIENTgEFFRDQGRqtylPQPALCPDsVYKLMLSCWRRDTKDRPSFQEIHT 293
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
881-1143 2.22e-16

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK2 is one of two vertebrate LRRKs which show complementary expression in the brain. Mutations in LRRK2, found in the kinase, ROC-COR, and WD40 domains, are linked to both familial and sporadic forms of Parkinson's disease. The most prevalent mutation, G2019S located in the activation loop of the kinase domain, increases kinase activity. The R1441C/G mutations in the GTPase domain have also been reported to influence kinase activity. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 80.38  E-value: 2.22e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDpegdntGEQVAVKSLKpesggNHIAD--LKKEIEILRNLYHENIVKYKGIctedGGNGIKLIMEF 958
Cdd:cd14068      2 LGDGGFGSVYRAVYR------GEDVAVKIFN-----KHTSFrlLRQELVVLSHLHHPSLVALLAA----GTAPRMLVMEL 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  959 LPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLV-----ESEHQVKIGDFGLTKAIETdke 1033
Cdd:cd14068     67 APKGSLDALLQQDNASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLftlypNCAIIAKIADYGIAQYCCR--- 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1034 yYTVKDDRDSPVFwYAPECLMQSKFY-IASDVWSFGVTLHELLTycdsDSSPMALFLKMIGPTHGQMTVTRLVNTLKEGK 1112
Cdd:cd14068    144 -MGIKTSEGTPGF-RAPEVARGNVIYnQQADVYSFGLLLYDILT----CGERIVEGLKFPNEFDELAIQGKLPDPVKEYG 217
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1013071061 1113 RLPCPpncpdEVYQLMRKCWEFQPSNR-TSFQ 1143
Cdd:cd14068    218 CAPWP-----GVEALIKDCLKENPQCRpTSAQ 244
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
881-1074 2.36e-16

Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNRK is a kinase highly expressed in testis and brain that is found inactive in cells that lack the LKB1 tumour suppressor protein kinase. The regulatory subunits STRAD and MO25 are required for LKB1 to activate SNRK. The SNRK mRNA is increased 3-fold when granule neurons are cultured in low potassium, and may thus play a role in the survival responses in these cells. In some vertebrates, a second SNRK gene (snrkb or snrk-1) has been sequenced and/or identified. Snrk-1 is expressed specifically in embryonic zebrafish vasculature; it plays an essential role in angioblast differentiation, maintenance, and migration. The SNRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 80.15  E-value: 2.36e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDpegdNTGEQVAVKSL-KPESGGNHIADLKKEIEILRNLYHENIVK-YKGICTEdggNGIKLIMEF 958
Cdd:cd14074     11 LGRGHFAVVKLARHV----FTGEKVAVKVIdKTKLDDVSKAHLFQEVRCMKLVQHPNVVRlYEVIDTQ---TKLYLILEL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  959 LPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLV-ESEHQVKIGDFGLTKAIETDKEYYTV 1037
Cdd:cd14074     84 GDGGDMYDYIMKHENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQPGEKLETS 163
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1013071061 1038 KddrdSPVFWYAPECLMqSKFYIAS--DVWSFGVTLHEL 1074
Cdd:cd14074    164 C----GSLAYSAPEILL-GDEYDAPavDIWSLGVILYML 197
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
582-848 2.63e-16

Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The FGFR subfamily consists of FGFR1, FGFR2, FGFR3, FGFR4, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, and to heparin/heparan sulfate (HS) results in the formation of a ternary complex, which leads to receptor dimerization and activation, and intracellular signaling. There are at least 23 FGFs and four types of FGFRs. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. FGF/FGFR signaling is important in the regulation of embryonic development, homeostasis, and regenerative processes. Depending on the cell type and stage, FGFR signaling produces diverse cellular responses including proliferation, growth arrest, differentiation, and apoptosis. Aberrant signaling leads to many human diseases such as skeletal, olfactory, and metabolic disorders, as well as cancer. The FGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 80.92  E-value: 2.63e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  582 DLVQGEHLGRGTRTHIYSGTLMDYKDdegtSEEKKIKVILKVL--DPSHRDISLAFFEAASMMRQVSHKHIVYLYGVCVR 659
Cdd:cd05053     13 RLTLGKPLGEGAFGQVVKAEAVGLDN----KPNEVVTVAVKMLkdDATEKDLSDLVSEMEMMKMIGKHKNIINLLGACTQ 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  660 DVENIMVEEFVEGGPLDLFMHRK---------------SDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAR 724
Cdd:cd05053     89 DGPLYVVVEYASKGNLREFLRARrppgeeaspddprvpEEQLTQKDLVSFAYQVARGMEYLASKKCIHRDLAARNVLVTE 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  725 EGIdsecgpfIKLSDPGipitvLSRQ-ECIE--------RIP--WIAPECVEDsKNLSVAADKWSFGTTLWEIC------ 787
Cdd:cd05053    169 DNV-------MKIADFG-----LARDiHHIDyyrkttngRLPvkWMAPEALFD-RVYTHQSDVWSFGVLLWEIFtlggsp 235
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1013071061  788 YNGeIPLKD--KTLIEKERFYesrcRPvtPSC-KELADLMTRCMNYDPNQRPFFRAIMRDINKL 848
Cdd:cd05053    236 YPG-IPVEElfKLLKEGHRME----KP--QNCtQELYMLMRDCWHEVPSQRPTFKQLVEDLDRI 292
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
580-848 2.73e-16

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Unlike other FGFRs, there is only one splice form of FGFR4. It binds FGF1, FGF2, FGF6, FGF19, and FGF23. FGF19 is a selective ligand for FGFR4. Although disruption of FGFR4 in mice causes no obvious phenotype, in vivo inhibition of FGFR4 in cultured skeletal muscle cells resulted in an arrest of muscle progenitor differentiation. FGF6 and FGFR4 are uniquely expressed in myofibers and satellite cells. FGF6/FGFR4 signaling appears to play a key role in the regulation of muscle regeneration. A polymorphism in FGFR4 is found in head and neck squamous cell carcinoma. FGFR4 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 81.16  E-value: 2.73e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  580 KKDLVQGEHLGRGTRTHIYSGTLMDYKDDEgtsEEKKIKVILKVL--DPSHRDISLAFFEAASMMRQVSHKHIVYLYGVC 657
Cdd:cd05099     11 RDRLVLGKPLGEGCFGQVVRAEAYGIDKSR---PDQTVTVAVKMLkdNATDKDLADLISEMELMKLIGKHKNIINLLGVC 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  658 VRDVENIMVEEFVEGGPLDLFMHRK-----------SDVLTTPWKFK----VAKQLASALSYLEDKDLVHGNVCTKNLLL 722
Cdd:cd05099     88 TQEGPLYVIVEYAAKGNLREFLRARrppgpdytfdiTKVPEEQLSFKdlvsCAYQVARGMEYLESRRCIHRDLAARNVLV 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  723 AREGIdsecgpfIKLSDPGIPITV----LSRQECIERIP--WIAPECVEDsKNLSVAADKWSFGTTLWEIC------YNG 790
Cdd:cd05099    168 TEDNV-------MKIADFGLARGVhdidYYKKTSNGRLPvkWMAPEALFD-RVYTHQSDVWSFGILMWEIFtlggspYPG 239
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1013071061  791 eIPLKD--KTLIEKERFYesrcRPvtPSC-KELADLMTRCMNYDPNQRPFFRAIMRDINKL 848
Cdd:cd05099    240 -IPVEElfKLLREGHRMD----KP--SNCtHELYMLMRECWHAVPTQRPTFKQLVEALDKV 293
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
639-848 2.78e-16

Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated protein Triple Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLTK, also called zipper sterile-alpha-motif kinase (ZAK), contains a catalytic kinase domain and a leucine zipper. There are two alternatively-spliced variants, MLTK-alpha and MLTK-beta. MLTK-alpha contains a sterile-alpha-motif (SAM) at the C-terminus. MLTK regulates the c-Jun N-terminal kinase, extracellular signal-regulated kinase, p38 MAPK, and NF-kB pathways. ZAK is the MAP3K involved in the signaling cascade that leads to the ribotoxic stress response initiated by cellular damage due to Shiga toxins and ricin. It may also play a role in cell transformation and cancer development. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals.The MLTK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 79.62  E-value: 2.78e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  639 ASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPL-DLFMHRKSDVLTTPWKFKVAKQLASALSYLEDK---DLVHGN 714
Cdd:cd14060     33 AEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGSLfDYLNSNESEEMDMDQIMTWATDIAKGMHYLHMEapvKVIHRD 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  715 VCTKNLLLAREGIdsecgpfIKLSDPGIP-----ITVLSrqeCIERIPWIAPECVEdSKNLSVAADKWSFGTTLWEICYN 789
Cdd:cd14060    113 LKSRNVVIAADGV-------LKICDFGASrfhshTTHMS---LVGTFPWMAPEVIQ-SLPVSETCDTYSYGVVLWEMLTR 181
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1013071061  790 gEIPLKD-KTLIEKERFYESRCRPVTPSC--KELADLMTRCMNYDPNQRPFFRAIMRDINKL 848
Cdd:cd14060    182 -EVPFKGlEGLQVAWLVVEKNERPTIPSScpRSFAELMRRCWEADVKERPSFKQIIGILESM 242
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
881-1076 2.90e-16

Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TBK1 is also called T2K and NF-kB-activating kinase. It is widely expressed in most cell types and acts as an IkappaB kinase (IKK)-activating kinase responsible for NF-kB activation in response to growth factors. It plays a role in modulating inflammatory responses through the NF-kB pathway. TKB1 is also a major player in innate immune responses since it functions as a virus-activated kinase necessary for establishing an antiviral state. It phosphorylates IRF-3 and IRF-7, which are important transcription factors for inducing type I interferon during viral infection. In addition, TBK1 may also play roles in cell transformation and oncogenesis. The TBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 81.00  E-value: 2.90e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVelcrYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGNGIKLIMEFLP 960
Cdd:cd13988      1 LGQGATANV----FRGRHKKTGDLYAVKVFNNLSFMRPLDVQMREFEVLKKLNHKNIVKLFAIEEELTTRHKVLVMELCP 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  961 SGSLKEYLPKNKNKINLKQQLKYAV--QICKGMDYLGSRQYVHRDLAARN---VLVESEHQV-KIGDFGLTKAIETDKEY 1034
Cdd:cd13988     77 CGSLYTVLEEPSNAYGLPESEFLIVlrDVVAGMNHLRENGIVHRDIKPGNimrVIGEDGQSVyKLTDFGAARELEDDEQF 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1035 --------YTVKDDRDSPVFWYApeclMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd13988    157 vslygteeYLHPDMYERAVLRKD----HQKKYGATVDLWSIGVTFYHAAT 202
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
876-1076 3.50e-16

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK9, together with a cyclin partner (cyclin T1, T2a, T2b, or K), is the main component of distinct positive transcription elongation factors (P-TEFb), which function as Ser2 C-terminal domain kinases of RNA polymerase II. P-TEFb participates in multiple steps of gene expression including transcription elongation, mRNA synthesis, processing, export, and translation. It also plays a role in mediating cytokine induced transcription networks such as IL6-induced STAT3 signaling. In addition, the CDK9/cyclin T2a complex promotes muscle differentiation and enhances the function of some myogenic regulatory factors. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270848 [Multi-domain]  Cd Length: 310  Bit Score: 80.88  E-value: 3.50e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  876 KRIRDLGEGHFGKVELCRYDpegdNTGEQVAVKS--LKPESGGNHIADLKkEIEILRNLYHENIVKYKGICTED--GGNG 951
Cdd:cd07865     15 EKLAKIGQGTFGEVFKARHR----KTGQIVALKKvlMENEKEGFPITALR-EIKILQLLKHENVVNLIEICRTKatPYNR 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  952 IK----LIMEFLpSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKA 1027
Cdd:cd07865     90 YKgsiyLVFEFC-EHDLAGLLSNKNVKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGVLKLADFGLARA 168
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1013071061 1028 IETDKEYYTVKDDRDSPVFWY-APECLMQSKFY-IASDVWSFGVTLHELLT 1076
Cdd:cd07865    169 FSLAKNSQPNRYTNRVVTLWYrPPELLLGERDYgPPIDMWGAGCIMAEMWT 219
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
876-1074 3.54e-16

Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CdkB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 80.65  E-value: 3.54e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  876 KRIRDLGEGHFGKVelcrYDPEGDNTGEQVAVKSLKPESGGNHIADLK-KEIEILRNLYHEN-IVKYKGI--CTEDGGNG 951
Cdd:cd07837      4 EKLEKIGEGTYGKV----YKARDKNTGKLVALKKTRLEMEEEGVPSTAlREVSLLQMLSQSIyIVRLLDVehVEENGKPL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  952 IKLIMEFLPSgSLKEYLPKNK----NKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQV-KIGDFGLTK 1026
Cdd:cd07837     80 LYLVFEYLDT-DLKKFIDSYGrgphNPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQKGLlKIADLGLGR 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1027 AIETDKEYYTvkddRDSPVFWY-APECLMQSKFY-IASDVWSFGVTLHEL 1074
Cdd:cd07837    159 AFTIPIKSYT----HEIVTLWYrAPEVLLGSTHYsTPVDMWSVGCIFAEM 204
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
577-848 4.22e-16

Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER4 (ErbB4) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands that bind HER4 fall into two groups, the neuregulins (or heregulins) and some EGFR (HER1) ligands including betacellulin, HBEGF, and epiregulin. All four neuregulins (NRG1-4) interact with HER4. Upon ligand binding, HER4 forms homo- or heterodimers with other HER proteins. HER4 is essential in embryonic development. It is implicated in mammary gland, cardiac, and neural development. As a postsynaptic receptor of NRG1, HER4 plays an important role in synaptic plasticity and maturation. The impairment of NRG1/HER4 signaling may contribute to schizophrenia. The HER4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173655 [Multi-domain]  Cd Length: 303  Bit Score: 80.50  E-value: 4.22e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  577 RILKK-DLVQGEHLGRGTRTHIYSGTLMDykddEGtsEEKKIKVILKVLDPSH-RDISLAFFEAASMMRQVSHKHIVYLY 654
Cdd:cd05110      2 RILKEtELKRVKVLGSGAFGTVYKGIWVP----EG--ETVKIPVAIKILNETTgPKANVEFMDEALIMASMDHPHLVRLL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  655 GVCVRDVENiMVEEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGidsecgpF 734
Cdd:cd05110     76 GVCLSPTIQ-LVTQLMPHGCLLDYVHEHKDNIGSQLLLNWCVQIAKGMMYLEERRLVHRDLAARNVLVKSPN-------H 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  735 IKLSDPGIPITVLSRQECIER------IPWIAPECVEDSKnLSVAADKWSFGTTLWEIC------YNGeIPLKD-KTLIE 801
Cdd:cd05110    148 VKITDFGLARLLEGDEKEYNAdggkmpIKWMALECIHYRK-FTHQSDVWSYGVTIWELMtfggkpYDG-IPTREiPDLLE 225
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1013071061  802 K-ERFyesrcrPVTPSCK-ELADLMTRCMNYDPNQRPFFRAIMRDINKL 848
Cdd:cd05110    226 KgERL------PQPPICTiDVYMVMVKCWMIDADSRPKFKELAAEFSRM 268
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
881-1139 4.33e-16

N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), p90-RSKs, or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 80.52  E-value: 4.33e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRyDPEGDNTGEQVAVKSLKPESggNHIAD---LKKEIEILRNLYHENIVK-YKGICTEdggNGIKLIM 956
Cdd:cd05582      3 LGQGSFGKVFLVR-KITGPDAGTLYAMKVLKKAT--LKVRDrvrTKMERDILADVNHPFIVKlHYAFQTE---GKLYLIL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  957 EFLPSGSLKEYLpkNKNKINLKQQLK-YAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTK-AIETDKEY 1034
Cdd:cd05582     77 DFLRGGDLFTRL--SKEVMFTEEDVKfYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKeSIDHEKKA 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1035 Y----TVKddrdspvfWYAPECLMQSKFYIASDVWSFGVTLHELLTycdsdsspMALflkmigPTHGQMTVTRLVNTLKe 1110
Cdd:cd05582    155 YsfcgTVE--------YMAPEVVNRRGHTQSADWWSFGVLMFEMLT--------GSL------PFQGKDRKETMTMILK- 211
                          250       260
                   ....*....|....*....|....*....
gi 1013071061 1111 gKRLPCPPNCPDEVYQLMRKCWEFQPSNR 1139
Cdd:cd05582    212 -AKLGMPQFLSPEAQSLLRALFKRNPANR 239
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
577-848 4.49e-16

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 79.97  E-value: 4.49e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  577 RILKK--DLVQGeHLGRGTrthiysgtLMDYkDDEGTSEEKKIKVilKVLDPSHRDISLA-FFEAASMMRQVSHKHIVYL 653
Cdd:cd05079      4 RFLKRirDLGEG-HFGKVE--------LCRY-DPEGDNTGEQVAV--KSLKPESGGNHIAdLKKEIEILRNLYHENIVKY 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  654 YGVCVRDVEN--IMVEEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIdsec 731
Cdd:cd05079     72 KGICTEDGGNgiKLIMEFLPSGSLKEYLPRNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQ---- 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  732 gpfIKLSDPGIPITVLSRQECI-------ERIPWIAPECVEDSKnLSVAADKWSFGTTLWEI---CYNGEIPLKD----- 796
Cdd:cd05079    148 ---VKIGDFGLTKAIETDKEYYtvkddldSPVFWYAPECLIQSK-FYIASDVWSFGVTLYELltyCDSESSPMTLflkmi 223
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1013071061  797 -------------KTLIEKERFyesrcrPVTPSC-KELADLMTRCMNYDPNQRPFFRAIMRDINKL 848
Cdd:cd05079    224 gpthgqmtvtrlvRVLEEGKRL------PRPPNCpEEVYQLMRKCWEFQPSKRTTFQNLIEGFEAI 283
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
878-1075 4.75e-16

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2, group 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 79.26  E-value: 4.75e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVELCRydpeGDNTGEQVAVKSLkpESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDggNGIKLIME 957
Cdd:cd14665      5 VKDIGSGNFGVARLMR----DKQTKELVAVKYI--ERGEKIDENVQREIINHRSLRHPNIVRFKEVILTP--THLAIVME 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  958 FLPSGSLKEYLPkNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEH--QVKIGDFGLTKAIETDKEyy 1035
Cdd:cd14665     77 YAAGGELFERIC-NAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPapRLKICDFGYSKSSVLHSQ-- 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1013071061 1036 tVKDDRDSPVFwYAPECLMQSKF--YIAsDVWSFGVTLHELL 1075
Cdd:cd14665    154 -PKSTVGTPAY-IAPEVLLKKEYdgKIA-DVWSCGVTLYVML 192
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
879-1139 5.11e-16

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1 functions as a receptor for morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Vertebrates contain two type I BMP receptors, BMPR1a and BMPR1b. BMPR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that also includes TGFbeta, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 79.83  E-value: 5.11e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGHFGKVELCRYdpegdnTGEQVAVKS-LKPESggnhiADLKKEIEILRN--LYHENIVKYkgICTEDGGNG---- 951
Cdd:cd14144      1 RSVGKGRYGEVWKGKW------RGEKVAVKIfFTTEE-----ASWFRETEIYQTvlMRHENILGF--IAADIKGTGswtq 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  952 IKLIMEFLPSGSLKEYLpkNKNKINLKQQLKYAVQICKGMDYL--------GSRQYVHRDLAARNVLVESEHQVKIGDFG 1023
Cdd:cd14144     68 LYLITDYHENGSLYDFL--RGNTLDTQSMLKLAYSAACGLAHLhteifgtqGKPAIAHRDIKSKNILVKKNGTCCIADLG 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1024 L-TKAIETDKEYYTVKDDRDSPVFWYAPECLMQS------KFYIASDVWSFGVTLHELLTYCDSDS--SPMAL-FLKMI- 1092
Cdd:cd14144    146 LaVKFISETNEVDLPPNTRVGTKRYMAPEVLDESlnrnhfDAYKMADMYSFGLVLWEIARRCISGGivEEYQLpYYDAVp 225
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1013071061 1093 -GPTHGQMtvtRLVNTLKegKRLPCPPN------CPDEVYQLMRKCWEFQPSNR 1139
Cdd:cd14144    226 sDPSYEDM---RRVVCVE--RRRPSIPNrwssdeVLRTMSKLMSECWAHNPAAR 274
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
589-835 5.28e-16

Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes yeast ATG1 and metazoan homologs including vertebrate ULK1-3. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. It is involved in nutrient sensing and signaling, the assembly of autophagy factors and the execution of autophagy. In metazoans, ATG1 homologs display additional functions. Unc-51 and ULKs have been implicated in neuronal and axonal development. The ATG1/ULK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270911 [Multi-domain]  Cd Length: 251  Bit Score: 79.19  E-value: 5.28e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  589 LGRGTRTHIYSGTLMDykddegTSEEKKIKVIL------KVLDPSHRDISLaffeaasmMRQVSHKHIVYLYGvCVRDVE 662
Cdd:cd14009      1 IGRGSFATVWKGRHKQ------TGEVVAIKEISrkklnkKLQENLESEIAI--------LKSIKHPNIVRLYD-VQKTED 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  663 NI-MVEEFVEGGPLDLFMHRKSDVlttpwKFKVAK----QLASALSYLEDKDLVHGNVCTKNLLLAREGIDsecgPFIKL 737
Cdd:cd14009     66 FIyLVLEYCAGGDLSQYIRKRGRL-----PEAVARhfmqQLASGLKFLRSKNIIHRDLKPQNLLLSTSGDD----PVLKI 136
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  738 SDPGIP--ITVLSRQECIERIP-WIAPECVEdSKNLSVAADKWSFGTTLWEICYnGEIPLKDKTLIEKERFYES------ 808
Cdd:cd14009    137 ADFGFArsLQPASMAETLCGSPlYMAPEILQ-FQKYDAKADLWSVGAILFEMLV-GKPPFRGSNHVQLLRNIERsdavip 214
                          250       260
                   ....*....|....*....|....*....
gi 1013071061  809 --RCRPVTPSCKelaDLMTRCMNYDPNQR 835
Cdd:cd14009    215 fpIAAQLSPDCK---DLLRRLLRRDPAER 240
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
866-1075 5.83e-16

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK5 is mainly expressed in the brain. It is not required for viability, but together with PAK6, it is required for normal levels of locomotion and activity, and for learning and memory. PAK5 cooperates with Inca (induced in neural crest by AP2) in the regulation of cell adhesion and cytoskeletal organization in the embryo and in neural crest cells during craniofacial development. PAK5 may also play a role in controlling the signaling of Raf-1, an effector of Ras, at the mitochondria. PAK5 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132989 [Multi-domain]  Cd Length: 292  Bit Score: 79.70  E-value: 5.83e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  866 DPTHFEKRFLKrirdLGEGHFGKVELCrydpEGDNTGEQVAVKSLkpesggnhiaDLKK---------EIEILRNLYHEN 936
Cdd:cd06658     19 DPREYLDSFIK----IGEGSTGIVCIA----TEKHTGKQVAVKKM----------DLRKqqrrellfnEVVIMRDYHHEN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  937 IVK-YKGICTedgGNGIKLIMEFLPSGSLKEYLpkNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEH 1015
Cdd:cd06658     81 VVDmYNSYLV---GDELWVVMEFLEGGALTDIV--THTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDG 155
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1016 QVKIGDFGLTKAIEtdKEYYTVKDDRDSPvFWYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd06658    156 RIKLSDFGFCAQVS--KEVPKRKSLVGTP-YWMAPEVISRLPYGTEVDIWSLGIMVIEMI 212
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
866-1075 6.45e-16

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK6 may play a role in stress responses through its activation by the mitogen-activated protein kinase (MAPK) p38 and MAPK kinase 6 (MKK6) pathway. PAK6 is highly expressed in the brain. It is not required for viability, but together with PAK5, it is required for normal levels of locomotion and activity, and for learning and memory. Increased expression of PAK6 is found in primary and metastatic prostate cancer. PAK6 may play a role in the regulation of motility. PAK6 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 79.64  E-value: 6.45e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  866 DPTHFEKRFLKrirdLGEGHFGKVELCRYDpegdNTGEQVAVKSLkpesggnhiaDLKK---------EIEILRNLYHEN 936
Cdd:cd06659     18 DPRQLLENYVK----IGEGSTGVVCIAREK----HSGRQVAVKMM----------DLRKqqrrellfnEVVIMRDYQHPN 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  937 IVK-YKGICTedgGNGIKLIMEFLPSGSLKEYLpkNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEH 1015
Cdd:cd06659     80 VVEmYKSYLV---GEELWVLMEYLQGGALTDIV--SQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDG 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1013071061 1016 QVKIGDFGLTKAIETDKEyytvkdDRDSPV---FWYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd06659    155 RVKLSDFGFCAQISKDVP------KRKSLVgtpYWMAPEVISRCPYGTEVDIWSLGIMVIEMV 211
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
589-850 6.50e-16

Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. InsR is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the insulin ligand to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR signaling plays an important role in many cellular processes including glucose homeostasis, glycogen synthesis, lipid and protein metabolism, ion and amino acid transport, cell cycle and proliferation, cell differentiation, gene transcription, and nitric oxide synthesis. Insulin resistance, caused by abnormalities in InsR signaling, has been described in diabetes, hypertension, cardiovascular disease, metabolic syndrome, heart failure, and female infertility. The InsR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133192 [Multi-domain]  Cd Length: 288  Bit Score: 79.63  E-value: 6.50e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  589 LGRGTRTHIYSGTLMDYkddegTSEEKKIKVILKVLDPSH--RDiSLAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMV 666
Cdd:cd05061     14 LGQGSFGMVYEGNARDI-----IKGEAETRVAVKTVNESAslRE-RIEFLNEASVMKGFTCHHVVRLLGVVSKGQPTLVV 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  667 EEFVEGGPLDLFMHR-KSDVLTTPWK--------FKVAKQLASALSYLEDKDLVHGNVCTKNLLLArEGIDSECGPFIKL 737
Cdd:cd05061     88 MELMAHGDLKSYLRSlRPEAENNPGRppptlqemIQMAAEIADGMAYLNAKKFVHRDLAARNCMVA-HDFTVKIGDFGMT 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  738 SDpgIPITVLSRQECIERIP--WIAPECVEDSKnLSVAADKWSFGTTLWEICYNGEIPLKDKTLIEKERFYESRCRPVTP 815
Cdd:cd05061    167 RD--IYETDYYRKGGKGLLPvrWMAPESLKDGV-FTTSSDMWSFGVVLWEITSLAEQPYQGLSNEQVLKFVMDGGYLDQP 243
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1013071061  816 -SCKE-LADLMTRCMNYDPNQRPFFRAImrdINKLEE 850
Cdd:cd05061    244 dNCPErVTDLMRMCWQFNPKMRPTFLEI---VNLLKD 277
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
881-1075 6.99e-16

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module. MLCK2, MLCK3, and MLCK4 share a simpler domain architecture of a single kinase domain near the C-terminus and the absence of Ig-like or FN3 domains. The MLCK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271005 [Multi-domain]  Cd Length: 250  Bit Score: 78.81  E-value: 6.99e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCrydpEGDNTGEQVAVKSLKPESGGNHiADLKKEIEILRNLYHENIVK-YKGIcteDGGNGIKLIMEFL 959
Cdd:cd14103      1 LGRGKFGTVYRC----VEKATGKELAAKFIKCRKAKDR-EDVRNEIEIMNQLRHPRLLQlYDAF---ETPREMVLVMEYV 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  960 PSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESE--HQVKIGDFGLTKAIETDKEyytV 1037
Cdd:cd14103     73 AGGELFERVVDDDFELTERDCILFMRQICEGVQYMHKQGILHLDLKPENILCVSRtgNQIKIIDFGLARKYDPDKK---L 149
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1013071061 1038 KDDRDSPVFwYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd14103    150 KVLFGTPEF-VAPEVVNYEPISYATDMWSVGVICYVLL 186
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
925-1109 1.06e-15

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 80.31  E-value: 1.06e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  925 EIEILRNLYHENIVKYKGICTEDGGNGIklimeFLP--SGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHR 1002
Cdd:PHA03209   107 EAMLLQNVNHPSVIRMKDTLVSGAITCM-----VLPhySSDLYTYLTKRSRPLPIDQALIIEKQILEGLRYLHAQRIIHR 181
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1003 DLAARNVLVESEHQVKIGDFGLTKAIETDKEYYTVKDDRDSPvfwyAPECLMQSKFYIASDVWSFGVTLHELLTY----- 1077
Cdd:PHA03209   182 DVKTENIFINDVDQVCIGDLGAAQFPVVAPAFLGLAGTVETN----APEVLARDKYNSKADIWSAGIVLFEMLAYpstif 257
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1013071061 1078 CDSDSSPMALFLKmigpthGQMTVTRLVNTLK 1109
Cdd:PHA03209   258 EDPPSTPEEYVKS------CHSHLLKIISTLK 283
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
881-1075 1.10e-15

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-beta is the predominant PKB isoform expressed in insulin-responsive tissues. It plays a critical role in the regulation of glucose homeostasis. It is also implicated in muscle cell differentiation. Mice deficient in PKB-beta display normal growth weights but exhibit severe insulin resistance and diabetes, accompanied by lipoatrophy and B-cell failure. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain.The PKB-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 79.66  E-value: 1.10e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDPegdnTGEQVAVKSLKPES--GGNHIADLKKEIEILRNLYHENIVKYK-GICTEDGgngIKLIME 957
Cdd:cd05595      3 LGKGTFGKVILVREKA----TGRYYAMKILRKEViiAKDEVAHTVTESRVLQNTRHPFLTALKyAFQTHDR---LCFVME 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  958 FLPSGSLKEYLPKNKNKINLKQQLkYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEyyTV 1037
Cdd:cd05595     76 YANGGELFFHLSRERVFTEDRARF-YGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGITDGA--TM 152
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1013071061 1038 KDDRDSPVFwYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd05595    153 KTFCGTPEY-LAPEVLEDNDYGRAVDWWGLGVVMYEMM 189
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
881-1076 1.15e-15

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK2 (or MYLK2) phosphorylates myosin regulatory light chain and controls the contraction of skeletal muscles. MLCK2 contains a single kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site. The MLCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271092 [Multi-domain]  Cd Length: 261  Bit Score: 78.42  E-value: 1.15e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDpegdNTGEQVAVKSLKPESGGNHIADLKkEIEILRNLYHENIVK-YKGICTEdggNGIKLIMEFL 959
Cdd:cd14190     12 LGGGKFGKVHTCTEK----RTGLKLAAKVINKQNSKDKEMVLL-EIQVMNQLNHRNLIQlYEAIETP---NEIVLFMEYV 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  960 PSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLV--ESEHQVKIGDFGLTKAIETDKEyytV 1037
Cdd:cd14190     84 EGGELFERIVDEDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCvnRTGHQVKIIDFGLARRYNPREK---L 160
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1013071061 1038 KDDRDSPVFwYAPECLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd14190    161 KVNFGTPEF-LSPEVVNYDQVSFPTDMWSMGVITYMLLS 198
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
873-1076 1.17e-15

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK4 shows a restricted expression pattern and is usually found in epithelial cells. It is expressed in nephrons and in extrarenal tissues including intestine, eye, mammary glands, and prostate. WNK4 regulates a variety of ion transport proteins including apical or basolateral ion transporters, ion channels in the transcellular pathway, and claudins in the paracellular pathway. Mutations in WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK4 inhibits the activity of the thiazide-sensitive Na-Cl cotransporter (NCC), which is responsible for about 15% of NaCl reabsorption in the kidney. It also inhibits the renal outer medullary potassium channel (ROMK) and decreases its surface expression. Hypertension and hyperkalemia in PHAII patients with WNK4 mutations may be partly due to increased NaCl reabsorption through NCC and impaired renal potassium secretion by ROMK, respectively. The WNK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 78.51  E-value: 1.17e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  873 RFLKRIRDLGEGHFGKVelcrYDPEGDNTGEQVA---VKSLKPESGGNHiaDLKKEIEILRNLYHENIVKY--KGICTED 947
Cdd:cd14033      1 RFLKFNIEIGRGSFKTV----YRGLDTETTVEVAwceLQTRKLSKGERQ--RFSEEVEMLKGLQHPNIVRFydSWKSTVR 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  948 GGNGIKLIMEFLPSGSLKEYLPKNKnKINLKQQLKYAVQICKGMDYLGSR--QYVHRDLAARNVLVESEH-QVKIGDFGL 1024
Cdd:cd14033     75 GHKCIILVTELMTSGTLKTYLKRFR-EMKLKLLQRWSRQILKGLHFLHSRcpPILHRDLKCDNIFITGPTgSVKIGDLGL 153
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1013071061 1025 TkaieTDKEYYTVKDDRDSPVFwYAPEcLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd14033    154 A----TLKRASFAKSVIGTPEF-MAPE-MYEEKYDEAVDVYAFGMCILEMAT 199
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
881-1139 1.21e-15

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mutations in the gene encoding CDKL5, previously called STK9, are associated with early onset epilepsy and severe mental retardation [X-linked infantile spasm syndrome (ISSX) or West syndrome]. In addition, CDKL5 mutations also sometimes cause a phenotype similar to Rett syndrome (RTT), a progressive neurodevelopmental disorder. These pathogenic mutations are located in the N-terminal portion of the protein within the kinase domain. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270838 [Multi-domain]  Cd Length: 287  Bit Score: 78.88  E-value: 1.21e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDpegdNTGEQVAVKSLKPESGGNHIADLK-KEIEILRNLYHENIVKYKGICTEDGGngIKLIMEFL 959
Cdd:cd07848      9 VGEGAYGVVLKCRHK----ETKEIVAIKKFKDSEENEEVKETTlRELKMLRTLKQENIVELKEAFRRRGK--LYLVFEYV 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  960 PSGSLkEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIE--TDKEYYTV 1037
Cdd:cd07848     83 EKNML-ELLEEMPNGVPPEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNLSegSNANYTEY 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1038 KDDRdspvfWY-APECLMQSKFYIASDVWSFGVTLHELltycdSDSSPM--------ALFL--KMIGPTHGQMTVTRLVN 1106
Cdd:cd07848    162 VATR-----WYrSPELLLGAPYGKAVDMWSVGCILGEL-----SDGQPLfpgeseidQLFTiqKVLGPLPAEQMKLFYSN 231
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1013071061 1107 TLKEGKRLPC--PPNCPDEVYQ---------LMRKCWEFQPSNR 1139
Cdd:cd07848    232 PRFHGLRFPAvnHPQSLERRYLgilsgvlldLMKNLLKLNPTDR 275
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
613-848 1.29e-15

Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Mammals have four MLKs (MLK1-4), mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 78.20  E-value: 1.29e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  613 EEKKIKVILKVLDPSHRDISLAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKS---DVLTTp 689
Cdd:cd14061     18 EEVAVKAARQDPDEDISVTLENVRQEARLFWMLRHPNIIALRGVCLQPPNLCLVMEYARGGALNRVLAGRKippHVLVD- 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  690 WkfkvAKQLASALSYLEDKD---LVHGNVCTKNLLLArEGIDSE--CGPFIKLSDPGIP--ITVLSRQECIERIPWIAPE 762
Cdd:cd14061     97 W----AIQIARGMNYLHNEApvpIIHRDLKSSNILIL-EAIENEdlENKTLKITDFGLAreWHKTTRMSAAGTYAWMAPE 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  763 CVEDSKnLSVAADKWSFGTTLWEIcYNGEIPLK--DKTLIEKERFYESRCRPVTPSCKE-LADLMTRCMNYDPNQRPFFR 839
Cdd:cd14061    172 VIKSST-FSKASDVWSYGVLLWEL-LTGEVPYKgiDGLAVAYGVAVNKLTLPIPSTCPEpFAQLMKDCWQPDPHDRPSFA 249

                   ....*....
gi 1013071061  840 AIMRDINKL 848
Cdd:cd14061    250 DILKQLENI 258
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
877-1153 1.35e-15

Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK16 is associated with many names including Myristylated and Palmitylated Serine/threonine Kinase 1 (MPSK1), Kinase related to cerevisiae and thaliana (Krct), and Protein Kinase expressed in day 12 fetal liver (PKL12). It is widely expressed in mammals with highest levels found in liver, testis, and kidney. It is localized in the Golgi but is translocated to the nucleus upon disorganization of the Golgi. STK16 is constitutively active and is capable of phosphorylating itself and other substrates. It may be involved in regulating stromal-epithelial interactions during mammary gland ductal morphogenesis. It may also function as a transcriptional co-activator of type-C natriuretic peptide and VEGF. The STK16 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270888 [Multi-domain]  Cd Length: 282  Bit Score: 78.49  E-value: 1.35e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  877 RIRD-LGEGHFGKVELCrydpEGDNTGEQVAVKSLKPESGgNHIADLKKEIEILRNLYHENIVKYKGICTEDGGNGIKLI 955
Cdd:cd13986      3 RIQRlLGEGGFSFVYLV----EDLSTGRLYALKKILCHSK-EDVKEAMREIENYRLFNHPNILRLLDSQIVKEAGGKKEV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  956 MEFLP---SGSLK---EYLPKNKNKINLKQQLKYAVQICKGMDYL---GSRQYVHRDLAARNVLVESEHQVKIGDFG-LT 1025
Cdd:cd13986     78 YLLLPyykRGSLQdeiERRLVKGTFFPEDRILHIFLGICRGLKAMhepELVPYAHRDIKPGNVLLSEDDEPILMDLGsMN 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1026 KA---IETDKEYYTVKD---DRDSPVfWYAPE-------CLMQSKfyiaSDVWSFGVTLHELLTYcdsdSSPMalflKMI 1092
Cdd:cd13986    158 PArieIEGRREALALQDwaaEHCTMP-YRAPElfdvkshCTIDEK----TDIWSLGCTLYALMYG----ESPF----ERI 224
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1013071061 1093 GPTHGQMTVTRLVNTLKegkrLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALL 1153
Cdd:cd13986    225 FQKGDSLALAVLSGNYS----FPDNSRYSEELHQLVKSMLVVNPAERPSIDDLLSRVHDLI 281
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
881-1076 1.44e-15

Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the mitogen-activated protein kinases (MAPKs) ERK1, ERK2, baker's yeast Fus3, and similar proteins. MAPK pathways are important mediators of cellular responses to extracellular signals. ERK1/2 activation is preferentially by mitogenic factors, differentiation stimuli, and cytokines, through a kinase cascade involving the MAPK kinases MEK1/2 and a MAPK kinase kinase from the Raf family. ERK1/2 have numerous substrates, many of which are nuclear and participate in transcriptional regulation of many cellular processes. They regulate cell growth, cell proliferation, and cell cycle progression from G1 to S phase. Although the distinct roles of ERK1 and ERK2 have not been fully determined, it is known that ERK2 can maintain most functions in the absence of ERK1, and that the deletion of ERK2 is embryonically lethal. The MAPK, Fus3, regulates yeast mating processes including mating-specific gene expression, G1 arrest, mating projection, and cell fusion. This ERK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 79.27  E-value: 1.44e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDPegdnTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGIC---TEDGGNGIKLIME 957
Cdd:cd07849     13 IGEGAYGMVCSAVHKP----TGQKVAIKKISPFEHQTYCLRTLREIKILLRFKHENIIGILDIQrppTFESFKDVYIVQE 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  958 FLPSGSLKeyLPKNKNKINlkQQLKYAV-QICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDK---- 1032
Cdd:cd07849     89 LMETDLYK--LIKTQHLSN--DHIQYFLyQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLARIADPEHdhtg 164
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1013071061 1033 ---EYYTVKddrdspvfWY-APECLMQSKFYIAS-DVWSFGVTLHELLT 1076
Cdd:cd07849    165 fltEYVATR--------WYrAPEIMLNSKGYTKAiDIWSVGCILAEMLS 205
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
881-1076 1.60e-15

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKbeta is involved in the classical pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. It involves NEMO (NF-kB Essential MOdulator)- and IKKbeta-dependent phosphorylation and degradation of the Inhibitor of NF-kB (IkB), which liberates NF-kB dimers (typified by the p50-p65 heterodimer) from an inactive IkB/dimeric NF-kB complex, enabling them to migrate to the nucleus where they regulate gene transcription. The IKKbeta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 78.47  E-value: 1.60e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCrydpEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTED---GGNGIKLI-M 956
Cdd:cd14038      2 LGTGGFGNVLRW----INQETGEQVAIKQCRQELSPKNRERWCLEIQIMKRLNHPNVVAARDVPEGLqklAPNDLPLLaM 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  957 EFLPSGSLKEYLPKNKNKINLKQQ--LKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQV---KIGDFGLTKaiETD 1031
Cdd:cd14038     78 EYCQGGDLRKYLNQFENCCGLREGaiLTLLSDISSALRYLHENRIIHRDLKPENIVLQQGEQRlihKIIDLGYAK--ELD 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1013071061 1032 KEyyTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd14038    156 QG--SLCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECIT 198
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
865-1075 2.27e-15

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. Its localization changes during mitotic progression; associating first with centrosomes in prophase, with kinetochores in prometaphase and metaphase, at the central spindle in anaphase, and in the midbody during telophase. It carries multiple functions throughout the cell cycle through interactions with differrent substrates at these specific subcellular locations. PLK1 is overexpressed in many human cancers and is associated with poor prognosis. The PLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271089 [Multi-domain]  Cd Length: 265  Bit Score: 77.67  E-value: 2.27e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  865 VDPtHFEKRFLkRIRDLGEGHFGKV-ELCRYDPEGDNTGeQVAVKS--LKPesggNHIADLKKEIEILRNLYHENIVKYK 941
Cdd:cd14187      1 VDP-RTRRRYV-RGRFLGKGGFAKCyEITDADTKEVFAG-KIVPKSllLKP----HQKEKMSMEIAIHRSLAHQHVVGFH 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  942 GIcTEDGgNGIKLIMEFLPSGSLKEyLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGD 1021
Cdd:cd14187     74 GF-FEDN-DFVYVVLELCRRRSLLE-LHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGD 150
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1013071061 1022 FGLTKAIETDKEyyTVKDDRDSPVFwYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd14187    151 FGLATKVEYDGE--RKKTLCGTPNY-IAPEVLSKKGHSFEVDIWSIGCIMYTLL 201
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
879-1075 2.41e-15

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called Doublecortin-like and CAM kinase-like 3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL3 (or DCAMKL3) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. DCKL3 contains a single DCX domain (instead of a tandem) and a C-terminal kinase domain with similarity to CAMKs. It has been shown to interact with tubulin and JIP1/2. The DCKL3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271087 [Multi-domain]  Cd Length: 258  Bit Score: 77.30  E-value: 2.41e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGHFGKVELCRYDPEGDNTGEQVAVKS-LKpesGGNHIADlkKEIEILRNLYHENIVKYKGICTEDGGngIKLIME 957
Cdd:cd14185      6 RTIGDGNFAVVKECRHWNENQEYAMKIIDKSkLK---GKEDMIE--SEILIIKSLSHPNIVKLFEVYETEKE--IYLILE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  958 FLPSGSLKEYLPKNKnKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVE----SEHQVKIGDFGLtkAIETDKE 1033
Cdd:cd14185     79 YVRGGDLFDAIIESV-KFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQhnpdKSTTLKLADFGL--AKYVTGP 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1013071061 1034 YYTVKddrDSPVFwYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd14185    156 IFTVC---GTPTY-VAPEILSEKGYGLEVDMWAAGVILYILL 193
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
878-1074 2.41e-15

Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. They activate the MAPKs, p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating the respective MAP/ERK kinases (MEKs, also known as MKKs or MAPKKs), MEK3/MEK6 and MKK4/MKK7. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. Vertebrates contain three TAO subfamily members, named TAO1, TAO2, and TAO3. The TAO subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270784 [Multi-domain]  Cd Length: 258  Bit Score: 77.49  E-value: 2.41e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVelcrYDPEGDNTGEQVAVKSLKpESGGNHIA---DLKKEIEILRNLYHENIVKYKGICTEDggNGIKL 954
Cdd:cd06607      6 LREIGHGSFGAV----YYARNKRTSEVVAIKKMS-YSGKQSTEkwqDIIKEVKFLRQLRHPNTIEYKGCYLRE--HTAWL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLpSGSLKEYLPKNKNKInlkQQLKYAVqICK----GMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTkaiet 1030
Cdd:cd06607     79 VMEYC-LGSASDIVEVHKKPL---QEVEIAA-ICHgalqGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFGSA----- 148
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1031 dkeyyTVKDDRDSPV---FWYAPECLM---QSKFYIASDVWSFGVTLHEL 1074
Cdd:cd06607    149 -----SLVCPANSFVgtpYWMAPEVILamdEGQYDGKVDVWSLGITCIEL 193
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
877-1074 2.56e-15

Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. The PKA subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 77.83  E-value: 2.56e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  877 RIRDLGEGHFGKVELCRYDPegdnTGEQVAVKSLKPESggnhIADLKK------EIEILRNLYHENIVKYKgICTEDGGN 950
Cdd:cd14209      5 RIKTLGTGSFGRVMLVRHKE----TGNYYAMKILDKQK----VVKLKQvehtlnEKRILQAINFPFLVKLE-YSFKDNSN 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  951 gIKLIMEFLPSGSLKEYLPKnKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIET 1030
Cdd:cd14209     76 -LYMVMEYVPGGEMFSHLRR-IGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKRVKG 153
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1013071061 1031 -------DKEYytvkddrdspvfwYAPEcLMQSKFYIAS-DVWSFGVTLHEL 1074
Cdd:cd14209    154 rtwtlcgTPEY-------------LAPE-IILSKGYNKAvDWWALGVLIYEM 191
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
881-1075 2.60e-15

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. Although T-cells also express other PKC isoforms, PKC-theta is unique in that upon antigen stimulation, it is translocated to the plasma membrane at the immunological synapse, where it mediates signals essential for T-cell activation. It is essential for TCR-induced proliferation, cytokine production, T-cell survival, and the differentiation and effector function of T-helper (Th) cells, particularly Th2 and Th17. PKC-theta is being developed as a therapeutic target for Th2-mediated allergic inflammation and Th17-mediated autoimmune diseases. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 78.43  E-value: 2.60e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCrydpEGDNTGEQVAVKSLKPEsggnhIADLKKEIEI------LRNLYHENIVKYKGICTEDGGNGIKL 954
Cdd:cd05619     13 LGKGSFGKVFLA----ELKGTNQFFAIKALKKD-----VVLMDDDVECtmvekrVLSLAWEHPFLTHLFCTFQTKENLFF 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPSGSLKEYLpKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTK-AIETDKE 1033
Cdd:cd05619     84 VMEYLNGGDLMFHI-QSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKeNMLGDAK 162
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1013071061 1034 YYTVKDDRDspvfWYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd05619    163 TSTFCGTPD----YIAPEILLGQKYNTSVDWWSFGVLLYEML 200
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
881-1152 3.64e-15

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK1 plays a role in the activation of IRF3/7, STAT, and NFkB. It mediates IL-6 and IFN-gamma responses following IL-1 and IL-18 stimulation, respectively. It also plays an essential role in IFN-alpha induction downstream of TLR7 and TLR9. The IRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 77.56  E-value: 3.64e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGkvelCRYDPEGDNTgeQVAVKSLKPESGGNHIAdLKK----EIEILRNLYHENIVKYKGICTEDGGngIKLIM 956
Cdd:cd14159      1 IGEGGFG----CVYQAVMRNT--EYAVKRLKEDSELDWSV-VKNsfltEVEKLSRFRHPNIVDLAGYSAQQGN--YCLIY 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  957 EFLPSGSLKEYLPKNKNKINLK--QQLKYAVQICKGMDYLGSRQ--YVHRDLAARNVLVESEHQVKIGDFGLTKAIETDK 1032
Cdd:cd14159     72 VYLPNGSLEDRLHCQVSCPCLSwsQRLHVLLGTARAIQYLHSDSpsLIHGDVKSSNILLDAALNPKLGDFGLARFSRRPK 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1033 E---------YYTVKddrdSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLT---YCDSDSSPMALFLKMI-------G 1093
Cdd:cd14159    152 QpgmsstlarTQTVR----GTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELLTgrrAMEVDSCSPTKYLKDLvkeeeeaQ 227
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1013071061 1094 PTHGQMTVTRLVNTLKEGKRL----------PCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEAL 1152
Cdd:cd14159    228 HTPTTMTHSAEAQAAQLATSIcqkhldpqagPCPPELGIEISQLACRCLHRRAKKRPPMTEVFQELERL 296
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
877-1074 4.62e-15

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK5 is unusual in that it is regulated by non-cyclin proteins, p35 and p39. It is highly expressed in the nervous system and is critical in normal neural development and function. It plays a role in neuronal migration and differentiation, and is also important in synaptic plasticity and learning. CDK5 also participates in protecting against cell death and promoting angiogenesis. Impaired CDK5 activity is implicated in Alzheimer's disease, amyotrophic lateral sclerosis, Parkinson's disease, Huntington's disease and acute neuronal injury. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 77.09  E-value: 4.62e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  877 RIRDLGEGHFGKVelcrYDPEGDNTGEQVAVKSLKPESGGNHI-ADLKKEIEILRNLYHENIVKYKGICTEDggNGIKLI 955
Cdd:cd07839      4 KLEKIGEGTYGTV----FKAKNRETHEIVALKRVRLDDDDEGVpSSALREICLLKELKHKNIVRLYDVLHSD--KKLTLV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  956 MEFLPSgSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYY 1035
Cdd:cd07839     78 FEYCDQ-DLKKYFDSCNGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARAFGIPVRCY 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1013071061 1036 TVkddrDSPVFWY-APECLMQSKFYIAS-DVWSFGVTLHEL 1074
Cdd:cd07839    157 SA----EVVTLWYrPPDVLFGAKLYSTSiDMWSAGCIFAEL 193
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
881-1076 5.36e-15

Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase (also called MAPK14); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38alpha/MAPK14 is expressed in most tissues and is the major isoform involved in the immune and inflammatory response. It is the central p38 MAPK involved in myogenesis. It plays a role in regulating cell cycle check-point transition and promoting cell differentiation. p38alpha also regulates cell proliferation and death through crosstalk with the JNK pathway. Its substrates include MAPK activated protein kinase 2 (MK2), MK5, and the transcription factors ATF2 and Mitf. p38 kinases MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 77.77  E-value: 5.36e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVeLCRYDPEgdnTGEQVAVKSL-KPESGGNHIADLKKEIEILRNLYHENIvkykgictedggngIKLIMEFL 959
Cdd:cd07877     25 VGSGAYGSV-CAAFDTK---TGLRVAVKKLsRPFQSIIHAKRTYRELRLLKHMKHENV--------------IGLLDVFT 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  960 PSGSLKEY---------LPKNKNKINLKQQLK------YAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGL 1024
Cdd:cd07877     87 PARSLEEFndvylvthlMGADLNNIVKCQKLTddhvqfLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGL 166
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1013071061 1025 TKaiETDKEYYTVKDDRdspvfWY-APECLMQSKFY-IASDVWSFGVTLHELLT 1076
Cdd:cd07877    167 AR--HTDDEMTGYVATR-----WYrAPEIMLNWMHYnQTVDIWSVGCIMAELLT 213
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
881-1089 5.69e-15

Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TNIK is an effector of Rap2, a small GTP-binding protein from the Ras family. TNIK specifically activates the c-Jun N-terminal kinase (JNK) pathway and plays a role in regulating the actin cytoskeleton. The TNIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 77.07  E-value: 5.69e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVelcrYDPEGDNTGEQVAVKSLkpESGGNHIADLKKEIEILRNL-YHENIVKYKGICTEDGGNGIK----LI 955
Cdd:cd06637     14 VGNGTYGQV----YKGRHVKTGQLAAIKVM--DVTGDEEEEIKQEINMLKKYsHHRNIATYYGAFIKKNPPGMDdqlwLV 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  956 MEFLPSGSLKEYLPKNKNKINLKQQLKYAV-QICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIetDKEY 1034
Cdd:cd06637     88 MEFCGAGSVTDLIKNTKGNTLKEEWIAYICrEILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL--DRTV 165
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1013071061 1035 YTVKDDRDSPvFWYAPECLM-----QSKFYIASDVWSFGVTLHELLTYCDS--DSSPM-ALFL 1089
Cdd:cd06637    166 GRRNTFIGTP-YWMAPEVIAcdenpDATYDFKSDLWSLGITAIEMAEGAPPlcDMHPMrALFL 227
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
880-1076 6.32e-15

C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), 90 kDa ribosomal protein S6 kinases (p90-RSKs), or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270993 [Multi-domain]  Cd Length: 291  Bit Score: 76.52  E-value: 6.32e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  880 DLGEGHFGKVELCRYDpegdNTGEQVAVKSLKPESggnhiADLKKEIEIL-RNLYHENIVKYKGIcTEDGGNgIKLIMEF 958
Cdd:cd14091      7 EIGKGSYSVCKRCIHK----ATGKEYAVKIIDKSK-----RDPSEEIEILlRYGQHPNIITLRDV-YDDGNS-VYLVTEL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  959 LPSGSLKEYLPKNKNkinLKQQLKYAV--QICKGMDYLGSRQYVHRDLAARNVLVESEHQ----VKIGDFGLTKAIETDK 1032
Cdd:cd14091     76 LRGGELLDRILRQKF---FSEREASAVmkTLTKTVEYLHSQGVVHRDLKPSNILYADESGdpesLRICDFGFAKQLRAEN 152
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1013071061 1033 -----EYYTVKddrdspvfWYAPECLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd14091    153 gllmtPCYTAN--------FVAPEVLKKQGYDAACDIWSLGVLLYTMLA 193
Pkinase pfam00069
Protein kinase domain;
583-844 6.35e-15

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 74.97  E-value: 6.35e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  583 LVQGEHLGRGTRTHIYSGTLMDykddegTSEEKKIKVILKVLDPSHRDISlAFFEAaSMMRQVSHKHIVYLYGVCVRDVE 662
Cdd:pfam00069    1 YEVLRKLGSGSFGTVYKAKHRD------TGKIVAIKKIKKEKIKKKKDKN-ILREI-KILKKLNHPNIVRLYDAFEDKDN 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  663 NIMVEEFVEGGPLDlfmhrksDVLTTPWKF------KVAKQLASALSYLEDKDlvhgnvctknlllaregidSECGpfik 736
Cdd:pfam00069   73 LYLVLEYVEGGSLF-------DLLSEKGAFsereakFIMKQILEGLESGSSLT-------------------TFVG---- 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  737 lsdpgipiTVLsrqecieripWIAPEcVEDSKNLSVAADKWSFGTTLWEIcYNGEIPL---KDKTLIEKERF--YESRCR 811
Cdd:pfam00069  123 --------TPW----------YMAPE-VLGGNPYGPKVDVWSLGCILYEL-LTGKPPFpgiNGNEIYELIIDqpYAFPEL 182
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1013071061  812 PVTPScKELADLMTRCMNYDPNQRPFFRAIMRD 844
Cdd:pfam00069  183 PSNLS-EEAKDLLKKLLKKDPSKRLTATQALQH 214
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
881-1139 6.51e-15

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. No function has yet been ascribed to Nek10. The gene encoding Nek10 is a putative causative gene for breast cancer; it is located within a breast cancer susceptibility loci on chromosome 3p24. Nek10 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270867 [Multi-domain]  Cd Length: 270  Bit Score: 76.39  E-value: 6.51e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRydpEGDNTGEQVAVKSL---KPESGGNH------IADLKKEIEILR-NLYHENIVKYKGICTEdgGN 950
Cdd:cd08528      8 LGSGAFGCVYKVR---KKSNGQTLLALKEInmtNPAFGRTEqerdksVGDIISEVNIIKeQLRHPNIVRYYKTFLE--ND 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  951 GIKLIMEFLPSGSLKEYLP--KNKN-KINLKQQLKYAVQICKGMDYL-GSRQYVHRDLAARNVLVESEHQVKIGDFGLTK 1026
Cdd:cd08528     83 RLYIVMELIEGAPLGEHFSslKEKNeHFTEDRIWNIFVQMVLALRYLhKEKQIVHRDLKPNNIMLGEDDKVTITDFGLAK 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1027 AIETDKEYYTvkdDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYcdsdsSPmalflkmigPTHGQMTVTrLVN 1106
Cdd:cd08528    163 QKGPESSKMT---SVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTL-----QP---------PFYSTNMLT-LAT 224
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1013071061 1107 TLKEGKRLPCPPNC-PDEVYQLMRKCWEFQPSNR 1139
Cdd:cd08528    225 KIVEAEYEPLPEGMySDDITFVIRSCLTPDPEAR 258
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
864-1076 6.76e-15

Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase (also called MAPK12); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38gamma/MAPK12 is predominantly expressed in skeletal muscle. Unlike p38alpha and p38beta, p38gamma is insensitive to pyridinylimidazoles. It displays an antagonizing function compared to p38alpha. p38gamma inhibits, while p38alpha stimulates, c-Jun phosphorylation and AP-1 mediated transcription. p38gamma also plays a role in the signaling between Ras and the estrogen receptor and has been implicated to increase cell invasion and breast cancer progression. In Xenopus, p38gamma is critical in the meiotic maturation of oocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 77.68  E-value: 6.76e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  864 EVDPTHFEKRflKRIRDL---GEGHFGKVelCrYDPEGdNTGEQVAVKSL-KPESGGNHIADLKKEIEILRNLYHENIVK 939
Cdd:cd07880      5 EVNKTIWEVP--DRYRDLkqvGSGAYGTV--C-SALDR-RTGAKVAIKKLyRPFQSELFAKRAYRELRLLKHMKHENVIG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  940 YKGICTEDGG----NGIKLIMEFLPS--GSLKEYLPKNKNKInlkQQLKYavQICKGMDYLGSRQYVHRDLAARNVLVES 1013
Cdd:cd07880     79 LLDVFTPDLSldrfHDFYLVMPFMGTdlGKLMKHEKLSEDRI---QFLVY--QMLKGLKYIHAAGIIHRDLKPGNLAVNE 153
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1013071061 1014 EHQVKIGDFGLTKAIETDKEYYTVKDdrdspvfWY-APECLMQSKFYIAS-DVWSFGVTLHELLT 1076
Cdd:cd07880    154 DCELKILDFGLARQTDSEMTGYVVTR-------WYrAPEVILNWMHYTQTvDIWSVGCIMAEMLT 211
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
878-1154 7.13e-15

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP2, also called RICK or CARDIAK, harbors a C-terminal Caspase Activation and Recruitment domain (CARD) belonging to the Death domain (DD) superfamily. It functions as an effector kinase downstream of the pattern recognition receptors from the Nod-like (NLR) family, Nod1 and Nod2, which recognizes bacterial peptidoglycans released upon infection. RIP2 may also be involved in regulating wound healing and keratinocyte proliferation. RIP kinases serve as essential sensors of cellular stress. The RIP2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270928 [Multi-domain]  Cd Length: 284  Bit Score: 76.50  E-value: 7.13e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVELCRYDpegdNTGEQVAVKSLKPES--GGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGNGIklI 955
Cdd:cd14026      2 LRYLSRGAFGTVSRARHA----DWRVTVAIKCLKLDSpvGDSERNCLLKEAEILHKARFSYILPILGICNEPEFLGI--V 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  956 MEFLPSGSLKEYLPKNKNKINLKQQLKYAV--QICKGMDYLG--SRQYVHRDLAARNVLVESEHQVKIGDFGLTK--AIE 1029
Cdd:cd14026     76 TEYMTNGSLNELLHEKDIYPDVAWPLRLRIlyEIALGVNYLHnmSPPLLHHDLKTQNILLDGEFHVKIADFGLSKwrQLS 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1030 TDKEYYTVKDDRDSPVFWYAPECLMQSKFYIAS---DVWSFGVTLHELLtycdSDSSPmalFLKMIGPTHGQMTVTRLVN 1106
Cdd:cd14026    156 ISQSRSSKSAPEGGTIIYMPPEEYEPSQKRRASvkhDIYSYAIIMWEVL----SRKIP---FEEVTNPLQIMYSVSQGHR 228
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1013071061 1107 TLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALLK 1154
Cdd:cd14026    229 PDTGEDSLPVDIPHRATLINLIESGWAQNPDERPSFLKCLIELEPVLR 276
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
877-1074 7.17e-15

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-2 is specifically expressed in neurons in the central nervous system, mainly in terminally differentiated neurons. It associates with Trap (Tudor repeat associator with PCTAIRE-2) and could play a role in regulating mitochondrial function in neurons. PCTAIRE-2 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 76.95  E-value: 7.17e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  877 RIRDLGEGHFGKVelcrYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDggNGIKLIM 956
Cdd:cd07872     10 KLEKLGEGTYATV----FKGRSKLTENLVALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIVHTD--KSLTLVF 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  957 EFLPSgSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYT 1036
Cdd:cd07872     84 EYLDK-DLKQYMDDCGNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKSVPTKTYS 162
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1013071061 1037 vkddRDSPVFWYAPE--CLMQSKFYIASDVWSFGVTLHEL 1074
Cdd:cd07872    163 ----NEVVTLWYRPPdvLLGSSEYSTQIDMWGVGCIFFEM 198
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
878-1146 7.87e-15

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek4 is highly abundant in the testis. Its specific function is unknown. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. Nek4 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270862 [Multi-domain]  Cd Length: 257  Bit Score: 75.94  E-value: 7.87e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVELCRYDPEGdntgEQVAVK--SLKPESGGNHIAdLKKEIEILRNLYHENIVKYKGiCTEDGGNGIKLI 955
Cdd:cd08223      5 LRVIGKGSYGEVWLVRHKRDR----KQYVIKklNLKNASKRERKA-AEQEAKLLSKLKHPNIVSYKE-SFEGEDGFLYIV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  956 MEFLPSGSLKEYLPKNKNKINLKQQL-KYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEY 1034
Cdd:cd08223     79 MGFCEGGDLYTRLKEQKGVLLEERQVvEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARVLESSSDM 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1035 YTVkddRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTycdsdsspmalfLKMigpTHGQMTVTRLVNTLKEGKRL 1114
Cdd:cd08223    159 ATT---LIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMAT------------LKH---AFNAKDMNSLVYKILEGKLP 220
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1013071061 1115 PCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLI 1146
Cdd:cd08223    221 PMPKQYSPELGELIKAMLHQDPEKRPSVKRIL 252
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
882-1077 7.99e-15

Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK8, CDC2L6, and similar proteins. CDK8 functions as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II-dependent transcription. CDC2L6 also associates with Mediator in complexes lacking CDK8. In VP16-dependent transcriptional activation, CDK8 and CDC2L6 exerts opposing effects by positive and negative regulation, respectively, in similar conditions. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 76.94  E-value: 7.99e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  882 GEGHFGKVELCRYDPEgdNTGEQVAVKSLKPESggNHIADLK----KEIEILRNLYHENIVKYKGICTEDGGNGIKLIME 957
Cdd:cd07842      9 GRGTYGRVYKAKRKNG--KDGKEYAIKKFKGDK--EQYTGISqsacREIALLRELKHENVVSLVEVFLEHADKSVYLLFD 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  958 FLP----------SGSLKEYLPKNKnkinLKQQLKyavQICKGMDYLGSRQYVHRDLAARNVLVESEHQ----VKIGDFG 1023
Cdd:cd07842     85 YAEhdlwqiikfhRQAKRVSIPPSM----VKSLLW---QILNGIHYLHSNWVLHRDLKPANILVMGEGPergvVKIGDLG 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1013071061 1024 LTKAIETD-KEYYTVkddrDSPV--FWY-APECLMQSKFYI-ASDVWSFGVTLHELLTY 1077
Cdd:cd07842    158 LARLFNAPlKPLADL----DPVVvtIWYrAPELLLGARHYTkAIDIWAIGCIFAELLTL 212
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
901-1076 8.24e-15

Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TEY subtype of plant MAPKs and is further subdivided into three groups (A, B, and C). Group A is represented by AtMPK3, AtMPK6, Nicotiana tabacum BTF4 (NtNTF4), among others. They are mostly involved in environmental and hormonal responses. AtMPK3 and AtMPK6 are also key regulators for stomatal development and patterning. Group B is represented by AtMPK4, AtMPK13, and NtNTF6, among others. They may be involved in both cell division and environmental stress response. AtMPK4 also participates in regulating innate immunity. Group C is represented by AtMPK1, AtMPK2, NtNTF3, Oryza sativa MAPK4 (OsMAPK4), among others. They may also be involved in stress responses. AtMPK1 and AtMPK2 are activated following mechanical injury and in the presence of stress chemicals such as jasmonic acid, hydrogen peroxide and abscisic acid. OsMAPK4 is also called OsMSRMK3 for Multiple Stress-Responsive MAPK3. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20. The TEY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 77.03  E-value: 8.24e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  901 TGEQVAVKslKPESGGNHIADLKK---EIEILRNLYHENIVKYKGICT---EDGGNGIKLIMEFLPSgSLKEYLPKNKNK 974
Cdd:cd07858     29 TNEKVAIK--KIANAFDNRIDAKRtlrEIKLLRHLDHENVIAIKDIMPpphREAFNDVYIVYELMDT-DLHQIIRSSQTL 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  975 INlkQQLKYAV-QICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDK----EYYTVKddrdspvfWY- 1048
Cdd:cd07858    106 SD--DHCQYFLyQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLARTTSEKGdfmtEYVVTR--------WYr 175
                          170       180
                   ....*....|....*....|....*....
gi 1013071061 1049 APECLMQSKFYIAS-DVWSFGVTLHELLT 1076
Cdd:cd07858    176 APELLLNCSEYTTAiDVWSVGCIFAELLG 204
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
925-1147 8.63e-15

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek2 subfamily includes Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants prevented from entering mitosis. NIMA is essential for mitotic entry and progression through mitosis, and its degradation is essential for mitotic exit. NIMA is involved in nuclear membrane fission. Vertebrate Nek2 is a cell cycle-regulated STK, localized in centrosomes and kinetochores, that regulates centrosome splitting at the G2/M phase. It also interacts with other mitotic kinases such as Polo-like kinase 1 and may play a role in spindle checkpoint. An increase in the expression of the human NEK2 gene is strongly associated with the progression of non-Hodgkin lymphoma. Nek2 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. It The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270857 [Multi-domain]  Cd Length: 265  Bit Score: 75.66  E-value: 8.63e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  925 EIEILRNLYHENIVKY------KGICTedggngIKLIMEFLPSGSLKEYLPKNKN---KINLKQQLKYAVQICKGMDYLG 995
Cdd:cd08217     49 EVNILRELKHPNIVRYydrivdRANTT------LYIVMEYCEGGDLAQLIKKCKKenqYIPEEFIWKIFTQLLLALYECH 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  996 SRQY-----VHRDLAARNVLVESEHQVKIGDFGLTKAIETDKE---------YYTvkddrdspvfwyAPECLMQSKFYIA 1061
Cdd:cd08217    123 NRSVgggkiLHRDLKPANIFLDSDNNVKLGDFGLARVLSHDSSfaktyvgtpYYM------------SPELLNEQSYDEK 190
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1062 SDVWSFGVTLHELltyCdsdsspmALFLKMIGPTHGQmtvtrLVNTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTS 1141
Cdd:cd08217    191 SDIWSLGCLIYEL---C-------ALHPPFQAANQLE-----LAKKIKEGKFPRIPSRYSSELNEVIKSMLNVDPDKRPS 255

                   ....*.
gi 1013071061 1142 FQNLIE 1147
Cdd:cd08217    256 VEELLQ 261
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
880-1086 8.78e-15

The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. Twitchin and Projectin are both associated with thick filaments. Twitchin is localized in the outer parts of A-bands and is involved in regulating muscle contraction. It interacts with the myofibrillar proteins myosin and actin in a phosphorylation-dependent manner, and may be involved in regulating the myosin cross-bridge cycle. The kinase activity of Twitchen is activated by Ca2+ and the Ca2+ binding protein S100A1. Projectin is associated with the end of thick filaments and is a component of flight muscle connecting filaments. The kinase domain of Projectin may play roles in autophosphorylation and transphosphorylation, which impact the formation of myosin filaments. The Twitchin-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 75.70  E-value: 8.78e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  880 DLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKPESggnhiADLKKEIEILRNLYHENIVKYKGICTEDggNGIKLIMEFL 959
Cdd:cd14114      9 ELGTGAFGVVHRCTERATGNNFAAKFIMTPHESDK-----ETVRKEIQIMNQLHHPKLINLHDAFEDD--NEMVLILEFL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  960 PSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVE--SEHQVKIGDFGLTKAIETDKeyyTV 1037
Cdd:cd14114     82 SGGELFERIAAEHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTtkRSNEVKLIDFGLATHLDPKE---SV 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1013071061 1038 KDDRDSPVFwYAPECLMQSKFYIASDVWSFGVTLHELLtycdSDSSPMA 1086
Cdd:cd14114    159 KVTTGTAEF-AAPEIVEREPVGFYTDMWAVGVLSYVLL----SGLSPFA 202
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
864-1072 9.13e-15

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK2, also called CaMKK beta, is one of the most versatile CaMKs. It is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. CaMKK2 contains unique N- and C-terminal domains and a central catalytic kinase domain that is followed by a regulatory domain that bears overlapping autoinhibitory and CaM-binding regions. It can be activated by signaling through G-coupled receptors, IP3 receptors, plasma membrane ion channels, and Toll-like receptors. Thus, CaMKK2 acts as a molecular hub that is capable of receiving and decoding signals from diverse pathways. The CaMKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 76.16  E-value: 9.13e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  864 EVDPTHFEKRFLKRIRDLGEGHFGKvelcRYDPEGDNTGEQVAVKSLKPesggnhIADLKKEIEILRNLYHENIVKYKGI 943
Cdd:cd14199     24 EDDNTYYAMKVLSKKKLMRQAGFPR----RPPPRGARAAPEGCTQPRGP------IERVYQEIAILKKLDHPNVVKLVEV 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  944 CTEDGGNGIKLIMEFLPSGSLKEyLPKNKnKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFG 1023
Cdd:cd14199     94 LDDPSEDHLYMVFELVKQGPVME-VPTLK-PLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLVGEDGHIKIADFG 171
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1013071061 1024 LTKAIETDKEYYTvkDDRDSPVFwYAPECLMQSKFYI---ASDVWSFGVTLH 1072
Cdd:cd14199    172 VSNEFEGSDALLT--NTVGTPAF-MAPETLSETRKIFsgkALDVWAMGVTLY 220
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
878-1076 9.61e-15

Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include Saccharomyces cerevisiae Rim15, Schizosaccharomyces pombe cek1, and similar fungal proteins. They contain a central catalytic domain, which contains an insert relative to MAST kinases. In addition, Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. Rim15 (or Rim15p) functions as a regulator of meiosis. It acts as a downstream effector of PKA and regulates entry into stationary phase (G0). Thus, it plays a crucial role in regulating yeast proliferation, differentiation, and aging. Cek1 may facilitate progression of mitotic anaphase. The Rim15-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270762 [Multi-domain]  Cd Length: 263  Bit Score: 75.59  E-value: 9.61e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVELCRydpeGDNTGEQVAVKSLKPES--GGNHIADLKKEIEILRNL-YHENIVKYkgICTEDGGNGIKL 954
Cdd:cd05611      1 LKPISKGAFGSVYLAK----KRSTGDYFAIKVLKKSDmiAKNQVTNVKAERAIMMIQgESPYVAKL--YYSFQSKDYLYL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPSGSLkEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEY 1034
Cdd:cd05611     75 VMEYLNGGDC-ASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSRNGLEKRHN 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1013071061 1035 ytvKDDRDSPVFwYAPECLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd05611    154 ---KKFVGTPDY-LAPETILGVGDDKMSDWWSLGCVIFEFLF 191
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
881-1082 9.89e-15

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270985 [Multi-domain]  Cd Length: 259  Bit Score: 75.49  E-value: 9.89e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCrydpEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGIctEDGGNGIKLIMEFLP 960
Cdd:cd14083     11 LGTGAFSEVVLA----EDKATGKLVAIKCIDKKALKGKEDSLENEIAVLRKIKHPNIVQLLDI--YESKSHLYLVMELVT 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  961 SGSLKEYLPKN-----KNKINLKQQLKYAVqickgmDYLGSRQYVHRDLAARNVLV---ESEHQVKIGDFGLTKaIETDK 1032
Cdd:cd14083     85 GGELFDRIVEKgsyteKDASHLIRQVLEAV------DYLHSLGIVHRDLKPENLLYyspDEDSKIMISDFGLSK-MEDSG 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1013071061 1033 EYYTVKddrDSPVFwYAPECLMQSKFYIASDVWSFGVTLHELLT-----YCDSDS 1082
Cdd:cd14083    158 VMSTAC---GTPGY-VAPEVLAQKPYGKAVDCWSIGVISYILLCgyppfYDENDS 208
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
878-1147 1.10e-14

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek9, also called Nercc1, is primarily a cytoplasmic protein but can also localize in the nucleus. It is involved in modulating chromosome alignment and splitting during mitosis. It interacts with the gamma-tubulin ring complex and the Ran GTPase, and is implicated in microtubule organization. Nek9 associates with FACT (FAcilitates Chromatin Transcription) and modulates interphase progression. It also interacts with Nek6, and Nek7, during mitosis, resulting in their activation. Nek9 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 75.16  E-value: 1.10e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVELcrYDPEGDNT---GEQVAVKSLKPesggNHIADLKKEIEILRNLYHENIVKYKGICTEDGGNGIKl 954
Cdd:cd08221      5 VRVLGRGAFGEAVL--YRKTEDNSlvvWKEVNLSRLSE----KERRDALNEIDILSLLNHDNIITYYNHFLDGESLFIE- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 iMEFLPSGSLKEYLPKNKNKINLKQQ-LKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETdkE 1033
Cdd:cd08221     78 -MEYCNGGNLHDKIAQQKNQLFPEEVvLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKVLDS--E 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1034 YYTVKDDRDSPvFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSDSSPMALflkmigpthgqmtvtRLVNTLKEGKR 1113
Cdd:cd08221    155 SSMAESIVGTP-YYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRTFDATNPL---------------RLAVKIVQGEY 218
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1013071061 1114 LPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIE 1147
Cdd:cd08221    219 EDIDEQYSEEIIQLVHDCLHQDPEDRPTAEELLE 252
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
880-1084 1.18e-14

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK3, also called DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk), contains an N-terminal kinase domain and a C-terminal region with nuclear localization signals (NLS) and a leucine zipper motif that mediates homodimerization and interaction with other leucine zipper proteins. It interacts with Par-4, a protein that contains a death domain and interacts with actin filaments. DAPK3 is present in both the cytoplasm and nucleus. Its co-expression with Par-4 results in the co-localization of the two proteins to actin filaments. In addition to cell death, DAPK3 is also implicated in mediating cell motility and the contraction of smooth muscles. The DAPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271097 [Multi-domain]  Cd Length: 271  Bit Score: 75.42  E-value: 1.18e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  880 DLGEGHFGKVELCRYDpegdNTGEQVAVKSLK-----PESGGNHIADLKKEIEILRNLYHENIVKYKGICteDGGNGIKL 954
Cdd:cd14195     12 ELGSGQFAIVRKCREK----GTGKEYAAKFIKkrrlsSSRRGVSREEIEREVNILREIQHPNIITLHDIF--ENKTDVVL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPSGSLKEYLPKnKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEH----QVKIGDFGLTKAIET 1030
Cdd:cd14195     86 ILELVSGGELFDFLAE-KESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNvpnpRIKLIDFGIAHKIEA 164
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1013071061 1031 DKEYytvKDDRDSPVFwYAPECLMQSKFYIASDVWSFGVTLHELLtycdSDSSP 1084
Cdd:cd14195    165 GNEF---KNIFGTPEF-VAPEIVNYEPLGLEADMWSIGVITYILL----SGASP 210
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
876-1076 1.28e-14

Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-like proteins show unusual expression patterns with high levels in post-mitotic tissues, suggesting that they may be involved in regulating post-mitotic cellular events. They share sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The association of PCTAIRE-like proteins with cyclins has not been widely studied, although PFTAIRE-1 has been shown to function as a CDK which is regulated by cyclin D3 as well as the membrane-associated cyclin Y. The PCTAIRE-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 75.88  E-value: 1.28e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  876 KRIRDLGEGHFGKVelcrYDPEGDNTGEQVAVK--SLKPESGGNHIAdlKKEIEILRNLYHENIVKYKGICTEDggNGIK 953
Cdd:cd07844      3 KKLDKLGEGSYATV----YKGRSKLTGQLVALKeiRLEHEEGAPFTA--IREASLLKDLKHANIVTLHDIIHTK--KTLT 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  954 LIMEFLPSgSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKE 1033
Cdd:cd07844     75 LVFEYLDT-DLKQYMDDCGGGLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLARAKSVPSK 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1013071061 1034 YYtvkdDRDSPVFWY-APECLMQSKFYIAS-DVWSFGVTLHELLT 1076
Cdd:cd07844    154 TY----SNEVVTLWYrPPDVLLGSTEYSTSlDMWGVGCIFYEMAT 194
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
613-845 1.34e-14

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK2 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K10. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK2 is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease. MLK2 also binds to normal huntingtin (Htt), which is important in neuronal transcription, development, and survival. MLK2 does not bind to the polyglutamine-expanded Htt, which is implicated in the pathogeneis of Huntington's disease, leading to neuronal toxicity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271050 [Multi-domain]  Cd Length: 258  Bit Score: 75.02  E-value: 1.34e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  613 EEKKIKVILkvLDPShRDISLA---FFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRK---SDVL 686
Cdd:cd14148     18 EEVAVKAAR--QDPD-EDIAVTaenVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVMEYARGGALNRALAGKkvpPHVL 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  687 TTpWkfkvAKQLASALSYLEDKDLV---HGNVCTKNLLLArEGIDSE--CGPFIKLSDPGIPIT--VLSRQECIERIPWI 759
Cdd:cd14148     95 VN-W----AVQIARGMNYLHNEAIVpiiHRDLKSSNILIL-EPIENDdlSGKTLKITDFGLAREwhKTTKMSAAGTYAWM 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  760 APECVEDSKnLSVAADKWSFGTTLWEIcYNGEIPLK--DKTLIEKERFYESRCRPVTPSCKE-LADLMTRCMNYDPNQRP 836
Cdd:cd14148    169 APEVIRLSL-FSKSSDVWSFGVLLWEL-LTGEVPYReiDALAVAYGVAMNKLTLPIPSTCPEpFARLLEECWDPDPHGRP 246

                   ....*....
gi 1013071061  837 FFRAIMRDI 845
Cdd:cd14148    247 DFGSILKRL 255
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
878-1074 1.45e-14

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIA myosin is highly expressed in retina and in inner ear hair cells. It is localized to the distal ends of actin-bundled structures. Mutations in human myosin IIIA are responsible for progressive nonsyndromic hearing loss. Human myosin IIIA possesses ATPase and kinase activities, and the ability to move actin filaments in a motility assay. It may function as a cellular transporter capable of moving along actin bundles in sensory cells. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. Class III myosins may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. In photoreceptor cells, they may also function as cargo carriers during light-dependent translocation of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 75.43  E-value: 1.45e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVelcrYDPEGDNTGEQVAVKSLKPesggnhIADLKKEIE----ILRNLY-HENIVKYKGIC-TEDGGNG 951
Cdd:cd06638     23 IETIGKGTYGKV----FKVLNKKNGSKAAVKILDP------IHDIDEEIEaeynILKALSdHPNVVKFYGMYyKKDVKNG 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  952 IKL--IMEFLPSGSLKEYLP---KNKNKINlKQQLKYAV-QICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLT 1025
Cdd:cd06638     93 DQLwlVLELCNGGSVTDLVKgflKRGERME-EPIIAYILhEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFGVS 171
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1013071061 1026 KAIEtdkeyyTVKDDRDSPV---FWYAPECL-----MQSKFYIASDVWSFGVTLHEL 1074
Cdd:cd06638    172 AQLT------STRLRRNTSVgtpFWMAPEVIaceqqLDSTYDARCDVWSLGITAIEL 222
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
872-1074 1.52e-14

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO1 is sometimes referred to as prostate-derived sterile 20-like kinase 2 (PSK2). TAO1 activates the p38 MAPK through direct interaction with and activation of MEK3. TAO1 is highly expressed in the brain and may play a role in neuronal apoptosis. TAO1 interacts with the checkpoint proteins BubR1 and Mad2, and plays an important role in regulating mitotic progression, which is required for both chromosome congression and checkpoint-induced anaphase delay. TAO1 may play a role in protecting genomic stability. TAO proteins possess MAPK kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 76.24  E-value: 1.52e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  872 KRFLKRIRDLGEGHFGKVELCRydpeGDNTGEQVAVK--SLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDgg 949
Cdd:cd06635     24 EKLFSDLREIGHGSFGAVYFAR----DVRTSEVVAIKkmSYSGKQSNEKWQDIIKEVKFLQRIKHPNSIEYKGCYLRE-- 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  950 NGIKLIMEFLpSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIE 1029
Cdd:cd06635     98 HTAWLVMEYC-LGSASDLLEVHKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIAS 176
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1013071061 1030 TDKEYYTVKddrdspvFWYAPECLM---QSKFYIASDVWSFGVTLHEL 1074
Cdd:cd06635    177 PANSFVGTP-------YWMAPEVILamdEGQYDGKVDVWSLGITCIEL 217
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
634-848 1.57e-14

Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. The KSR subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 75.08  E-value: 1.57e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  634 AFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHG 713
Cdd:cd14063     42 AFKEEVAAYKNTRHDNLVLFMGACMDPPHLAIVTSLCKGRTLYSLIHERKEKFDFNKTVQIAQQICQGMGYLHAKGIIHK 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  714 NVCTKNLLLAREGI---DSECGPFIKLSDPGipitvlsRQECIERIP--WI---APECV---------EDSKNLSVAADK 776
Cdd:cd14063    122 DLKSKNIFLENGRVvitDFGLFSLSGLLQPG-------RREDTLVIPngWLcylAPEIIralspdldfEESLPFTKASDV 194
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1013071061  777 WSFGTTLWEIcYNGEIPLKD---KTLIEKERFYESRCRPVTPSCKELADLMTRCMNYDPNQRPFFRAIMRDINKL 848
Cdd:cd14063    195 YAFGTVWYEL-LAGRWPFKEqpaESIIWQVGCGKKQSLSQLDIGREVKDILMQCWAYDPEKRPTFSDLLRMLERL 268
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
641-849 1.67e-14

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak2 is widely expressed in many tissues and is essential for the signaling of hormone-like cytokines such as growth hormone, erythropoietin, thrombopoietin, and prolactin, as well as some IFNs and cytokines that signal through the IL-3 and gp130 receptors. Disruption of Jak2 in mice results in an embryonic lethal phenotype with multiple defects including erythropoietic and cardiac abnormalities. It is the only Jak gene that results in a lethal phenotype when disrupted in mice. A mutation in the pseudokinase domain of Jak2, V617F, is present in many myeloproliferative diseases, including almost all patients with polycythemia vera, and 50% of patients with essential thrombocytosis and myelofibrosis. Jak2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 75.44  E-value: 1.67e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  641 MMRQVSHKHIVYLYGVCV----RDVENIMveEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVC 716
Cdd:cd14205     58 ILKSLQHDNIVKYKGVCYsagrRNLRLIM--EYLPYGSLRDYLQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLA 135
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  717 TKNLLLAREGidsecgpFIKLSDPGIPITVLSRQECIE-------RIPWIAPECVEDSKnLSVAADKWSFGTTLWEICYN 789
Cdd:cd14205    136 TRNILVENEN-------RVKIGDFGLTKVLPQDKEYYKvkepgesPIFWYAPESLTESK-FSVASDVWSFGVVLYELFTY 207
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  790 GEIPL-----------KDKT-------LIEkerFYESRCR-PVTPSC-KELADLMTRCMNYDPNQRPFFRAIMRDINKLE 849
Cdd:cd14205    208 IEKSKsppaefmrmigNDKQgqmivfhLIE---LLKNNGRlPRPDGCpDEIYMIMTECWNNNVNQRPSFRDLALRVDQIR 284
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
566-848 1.70e-14

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Many FGFR3 splice variants have been reported with the IIIb and IIIc isoforms being the predominant forms. FGFR3 IIIc is the isoform expressed in chondrocytes, the cells affected in dwarfism, while IIIb is expressed in epithelial cells. FGFR3 ligands include FGF1, FGF2, FGF4, FGF8, FGF9, and FGF23. It is a negative regulator of long bone growth. In the cochlear duct and in the lens, FGFR3 is involved in differentiation while it appears to have a role in cell proliferation in epithelial cells. Germline mutations in FGFR3 are associated with skeletal disorders including several forms of dwarfism. Some missense mutations are associated with multiple myeloma and carcinomas of the bladder and cervix. Overexpression of FGFR3 is found in thyroid carcinoma. FGFR3 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 76.21  E-value: 1.70e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  566 PVYPMSQLSFDRilkkdLVQGEHLGRGTRTHIYSGTLMDYKDDEgtsEEKKIKVILKVL--DPSHRDISLAFFEAASMMR 643
Cdd:cd05100      2 PADPKWELSRTR-----LTLGKPLGEGCFGQVVMAEAIGIDKDK---PNKPVTVAVKMLkdDATDKDLSDLVSEMEMMKM 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  644 QVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRK---------------SDVLTTPWKFKVAKQLASALSYLEDK 708
Cdd:cd05100     74 IGKHKNIINLLGACTQDGPLYVLVEYASKGNLREYLRARrppgmdysfdtcklpEEQLTFKDLVSCAYQVARGMEYLASQ 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  709 DLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGIPITVLS----RQECIERIP--WIAPECVEDsKNLSVAADKWSFGTT 782
Cdd:cd05100    154 KCIHRDLAARNVLVTEDNV-------MKIADFGLARDVHNidyyKKTTNGRLPvkWMAPEALFD-RVYTHQSDVWSFGVL 225
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1013071061  783 LWEICYNGEIPLKDKTLIEKERFYESRCRPVTP-SCK-ELADLMTRCMNYDPNQRPFFRAIMRDINKL 848
Cdd:cd05100    226 LWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPaNCThELYMIMRECWHAVPSQRPTFKQLVEDLDRV 293
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
923-1147 1.70e-14

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 77.36  E-value: 1.70e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  923 KKEIEILRNLYHENIVK-YKGICTEDGgngIKLIMEFLPSGSL--------KEYLPKNKNKINLkqqLKYavQICKGMDY 993
Cdd:PTZ00267   113 RSELHCLAACDHFGIVKhFDDFKSDDK---LLLIMEYGSGGDLnkqikqrlKEHLPFQEYEVGL---LFY--QIVLALDE 184
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  994 LGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIeTDKEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHE 1073
Cdd:PTZ00267   185 VHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQY-SDSVSLDVASSFCGTPYYLAPELWERKRYSKKADMWSLGVILYE 263
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1013071061 1074 LLTycdsdsspmaLFLKMIGPTHGQMTVTRLVntlkeGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIE 1147
Cdd:PTZ00267   264 LLT----------LHRPFKGPSQREIMQQVLY-----GKYDPFPCPVSSGMKALLDPLLSKNPALRPTTQQLLH 322
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
878-1075 1.87e-14

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 74.81  E-value: 1.87e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVELCRydpeGDNTGEQVAVKSLkpESGGNHIADLKKEIEILRNLYHENIVKYKGICTEdgGNGIKLIME 957
Cdd:cd14662      5 VKDIGSGNFGVARLMR----NKETKELVAVKYI--ERGLKIDENVQREIINHRSLRHPNIIRFKEVVLT--PTHLAIVME 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  958 FLPSGSLKEYLPkNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESE--HQVKIGDFGLTK-AIETDKEY 1034
Cdd:cd14662     77 YAAGGELFERIC-NAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGSpaPRLKICDFGYSKsSVLHSQPK 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1013071061 1035 YTVkddrDSPVFwYAPECLMQSKF--YIAsDVWSFGVTLHELL 1075
Cdd:cd14662    156 STV----GTPAY-IAPEVLSRKEYdgKVA-DVWSCGVTLYVML 192
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
875-1104 1.89e-14

Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase (also called MAPK11); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38beta/MAPK11 is widely expressed in tissues and shows more similarity with p38alpha than with the other isoforms. Both are sensitive to pyridinylimidazoles and share some common substrates such as MAPK activated protein kinase 2 (MK2) and the transcription factors ATF2, c-Fos and, ELK-1. p38beta is involved in regulating the activation of the cyclooxygenase-2 promoter and the expression of TGFbeta-induced alpha-smooth muscle cell actin. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 76.24  E-value: 1.89e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  875 LKRIRDLGEGHFGKVelCR-YDPEgdnTGEQVAVKSL-KPESGGNHIADLKKEIEILRNLYHENIvkykgictedggngI 952
Cdd:cd07878     17 YQNLTPVGSGAYGSV--CSaYDTR---LRQKVAVKKLsRPFQSLIHARRTYRELRLLKHMKHENV--------------I 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  953 KLIMEFLPSGSLKE----YLPKNKNKINLKQQLKYA-----------VQICKGMDYLGSRQYVHRDLAARNVLVESEHQV 1017
Cdd:cd07878     78 GLLDVFTPATSIENfnevYLVTNLMGADLNNIVKCQklsdehvqfliYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCEL 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1018 KIGDFGLTKaiETDKEYYTVKDDRdspvfWY-APECLMQSKFYIAS-DVWSFGVTLHELLT---------YCDS------ 1080
Cdd:cd07878    158 RILDFGLAR--QADDEMTGYVATR-----WYrAPEIMLNWMHYNQTvDIWSVGCIMAELLKgkalfpgndYIDQlkrime 230
                          250       260
                   ....*....|....*....|....*
gi 1013071061 1081 -DSSPMALFLKMIGPTHGQMTVTRL 1104
Cdd:cd07878    231 vVGTPSPEVLKKISSEHARKYIQSL 255
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
872-1075 1.91e-14

Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group I PAKs, also called conventional PAKs, include PAK1, PAK2, and PAK3. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). They interact with the SH3 domain containing proteins Nck, Grb2 and PIX. Binding of group I PAKs to activated GTPases leads to conformational changes that destabilize the AID, allowing autophosphorylation and full activation of the kinase domain. Known group I PAK substrates include MLCK, Bad, Raf, MEK1, LIMK, Merlin, Vimentin, Myc, Stat5a, and Aurora A, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270814 [Multi-domain]  Cd Length: 261  Bit Score: 74.58  E-value: 1.91e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  872 KRFLKRIRDLGEGHFGKVelcrYDPEGDNTGEQVAVK--SLKPESGGNHIADlkkEIEILRNLYHENIVKYkgICTEDGG 949
Cdd:cd06647      6 KKKYTRFEKIGQGASGTV----YTAIDVATGQEVAIKqmNLQQQPKKELIIN---EILVMRENKNPNIVNY--LDSYLVG 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  950 NGIKLIMEFLPSGSLKEYLpkNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAI- 1028
Cdd:cd06647     77 DELWVVMEYLAGGSLTDVV--TETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQIt 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1013071061 1029 -ETDKEYYTVkddrDSPvFWYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd06647    155 pEQSKRSTMV----GTP-YWMAPEVVTRKAYGPKVDIWSLGIMAIEMV 197
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
587-841 2.01e-14

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror kinases are expressed in many tissues during development. Avian Ror1 was found to be involved in late limb development. Studies in mice reveal that Ror1 is important in the regulation of neurite growth in central neurons, as well as in respiratory development. Loss of Ror1 also enhances the heart and skeletal abnormalities found in Ror2-deficient mice. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 75.05  E-value: 2.01e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  587 EHLGRGTRTHIYSGTLmdYKDDEGTSEEKKIKVILKVLDPSHRDislAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMV 666
Cdd:cd05090     11 EELGECAFGKIYKGHL--YLPGMDHAQLVAIKTLKDYNNPQQWN---EFQQEASLMTELHHPNIVCLLGVVTQEQPVCML 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  667 EEFVEGGPLDLFMHRKS---DVLTTPWK-------------FKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREgidse 730
Cdd:cd05090     86 FEFMNQGDLHEFLIMRSphsDVGCSSDEdgtvkssldhgdfLHIAIQIAAGMEYLSSHFFVHKDLAARNILVGEQ----- 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  731 cgPFIKLSDPGIPITVLS------RQECIERIPWIAPECVEDSKnLSVAADKWSFGTTLWEICYNGEIP---LKDKTLIE 801
Cdd:cd05090    161 --LHVKISDLGLSREIYSsdyyrvQNKSLLPIRWMPPEAIMYGK-FSSDSDIWSFGVVLWEIFSFGLQPyygFSNQEVIE 237
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1013071061  802 KERfyESRCRPVTPSC-KELADLMTRCMNYDPNQRPFFRAI 841
Cdd:cd05090    238 MVR--KRQLLPCSEDCpPRMYSLMTECWQEIPSRRPRFKDI 276
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
879-1075 2.07e-14

Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2, which also localizes the kinase to spindle microtubules. Aurora-A is overexpressed in many cancer types such as prostate, ovarian, breast, bladder, gastric, and pancreatic. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 74.61  E-value: 2.07e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKPESGGNHiaDLKKEIEILRNLYHENIVKYKGICTEdgGNGIKLIMEF 958
Cdd:cd14116     11 RPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVEH--QLRREVEIQSHLRHPNILRLYGYFHD--ATRVYLILEY 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  959 LPSGSLKEYLPKnKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEyYTVK 1038
Cdd:cd14116     87 APLGTVYRELQK-LSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSRR-TTLC 164
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1013071061 1039 DDRDspvfwYAPECLMQSKFYIAS-DVWSFGVTLHELL 1075
Cdd:cd14116    165 GTLD-----YLPPEMIEGRMHDEKvDLWSLGVLCYEFL 197
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
881-1075 2.34e-14

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271069 [Multi-domain]  Cd Length: 263  Bit Score: 74.68  E-value: 2.34e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCrydpEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGIcTEDGGNgIKLIMEFLP 960
Cdd:cd14167     11 LGTGAFSEVVLA----EEKRTQKLVAIKCIAKKALEGKETSIENEIAVLHKIKHPNIVALDDI-YESGGH-LYLIMQLVS 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  961 SGSLKEYLPKnKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVL---VESEHQVKIGDFGLTKaIETDKeyyTV 1037
Cdd:cd14167     85 GGELFDRIVE-KGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGLSK-IEGSG---SV 159
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1013071061 1038 KDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd14167    160 MSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILL 197
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
872-1074 2.43e-14

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human TAO2 is also known as prostate-derived Ste20-like kinase (PSK) and was identified in a screen for overexpressed RNAs in prostate cancer. TAO2 possesses mitogen-activated protein kinase (MAPK) kinase kinase activity and activates both p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating their respective MAP/ERK kinases, MEK3/MEK6 and MKK4/MKK7. It contains a long C-terminal extension with autoinhibitory segments, and is activated by the release of this inhibition and the phosphorylation of its activation loop serine. TAO2 functions as a regulator of actin cytoskeletal and microtubule organization. In addition, it regulates the transforming growth factor-activated kinase 1 (TAK1), which is a MAPKKK that plays an essential role in the signaling pathways of tumor necrosis factor, interleukin 1, and Toll-like receptor. The TAO2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 75.44  E-value: 2.43e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  872 KRFLKRIRDLGEGHFGKVELCRydpeGDNTGEQVAVK--SLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDgg 949
Cdd:cd06634     14 EKLFSDLREIGHGSFGAVYFAR----DVRNNEVVAIKkmSYSGKQSNEKWQDIIKEVKFLQKLRHPNTIEYRGCYLRE-- 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  950 NGIKLIMEFLpSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIE 1029
Cdd:cd06634     88 HTAWLVMEYC-LGSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFGSASIMA 166
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1013071061 1030 TDKEYYTVKddrdspvFWYAPECLM---QSKFYIASDVWSFGVTLHEL 1074
Cdd:cd06634    167 PANSFVGTP-------YWMAPEVILamdEGQYDGKVDVWSLGITCIEL 207
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
876-1076 2.44e-14

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 74.85  E-value: 2.44e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  876 KRIRDLGEGHFGKVelcrYDPEGDNTGEQVAVKSLKPESGGNHIADLK-KEIEILRNLYHENIVKYKGICTEDggNGIKL 954
Cdd:PLN00009     5 EKVEKIGEGTYGVV----YKARDRVTNETIALKKIRLEQEDEGVPSTAiREISLLKEMQHGNIVRLQDVVHSE--KRLYL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLpSGSLKEYLPKNKNKINLKQQLK-YAVQICKGMDYLGSRQYVHRDLAARNVLVE-SEHQVKIGDFGLTKAIETDK 1032
Cdd:PLN00009    79 VFEYL-DLDLKKHMDSSPDFAKNPRLIKtYLYQILRGIAYCHSHRVLHRDLKPQNLLIDrRTNALKLADFGLARAFGIPV 157
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1013071061 1033 EYYTvkddRDSPVFWY-APECLMQSKFY-IASDVWSFGVTLHELLT 1076
Cdd:PLN00009   158 RTFT----HEVVTLWYrAPEILLGSRHYsTPVDIWSVGCIFAEMVN 199
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
881-1076 2.60e-14

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. MLCK4 (or MYLK4 or SgK085) contains a single kinase domain near the C-terminus. The MLCK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 74.18  E-value: 2.60e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCrydpEGDNTGEQVAVKSLKPESGGNHiADLKKEIEILRNLYHENIVK-YKGIcteDGGNGIKLIMEFL 959
Cdd:cd14193     12 LGGGRFGQVHKC----EEKSSGLKLAAKIIKARSQKEK-EEVKNEIEVMNQLNHANLIQlYDAF---ESRNDIVLVMEYV 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  960 PSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESE--HQVKIGDFGLTKAIetdKEYYTV 1037
Cdd:cd14193     84 DGGELFDRIIDENYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCVSReaNQVKIIDFGLARRY---KPREKL 160
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1013071061 1038 KDDRDSPVFwYAPECLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd14193    161 RVNFGTPEF-LAPEVVNYEFVSFPTDMWSLGVIAYMLLS 198
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
873-1073 2.74e-14

Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of fungal Wee1 proteins, also called Swe1 in budding yeast and Mik1 in fission yeast. Yeast Wee1 is required to control cell size. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The fungal Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 74.77  E-value: 2.74e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  873 RFlKRIRDLGEGHFGKVELCRydpEGDNTGEQVAVKSLKPESGG-NHIADLKKEIEILRNLY---HENIVKYKGICtEDG 948
Cdd:cd14052      1 RF-ANVELIGSGEFSQVYKVS---ERVPTGKVYAVKKLKPNYAGaKDRLRRLEEVSILRELTldgHDNIVQLIDSW-EYH 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  949 GNgIKLIMEFLPSGSLKEYLPKNknkiNLKQQL------KYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDF 1022
Cdd:cd14052     76 GH-LYIQTELCENGSLDVFLSEL----GLLGRLdefrvwKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDF 150
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1013071061 1023 GLTKA--------IETDKEYytvkddrdspvfwYAPECLMQSKFYIASDVWSFGVTLHE 1073
Cdd:cd14052    151 GMATVwplirgieREGDREY-------------IAPEILSEHMYDKPADIFSLGLILLE 196
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
881-1089 2.75e-14

N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinase Kinase 4 and 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K4 is also called Nck Interacting kinase (NIK). It facilitates the activation of the MAPKs, extracellular signal-regulated kinase (ERK) 1, ERK2, and c-Jun N-terminal kinase (JNK), by phosphorylating and activating MEKK1. MAP4K4 plays a role in tumor necrosis factor (TNF) alpha-induced insulin resistance. MAP4K4 silencing in skeletal muscle cells from type II diabetic patients restores insulin-mediated glucose uptake. MAP4K4, through JNK, also plays a broad role in cell motility, which impacts inflammation, homeostasis, as well as the invasion and spread of cancer. MAP4K4 is found to be highly expressed in most tumor cell lines relative to normal tissue. MAP4K6 (also called MINK for Misshapen/NIKs-related kinase) is activated after Ras induction and mediates activation of p38 MAPK. MAP4K6 plays a role in cell cycle arrest, cytoskeleton organization, cell adhesion, and cell motility. The MAP4K4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 74.66  E-value: 2.75e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVelcrYDPEGDNTGEQVAVKSLKPESggNHIADLKKEIEILRNL-YHENIVKYKGICTEDGGNG----IKLI 955
Cdd:cd06636     24 VGNGTYGQV----YKGRHVKTGQLAAIKVMDVTE--DEEEEIKLEINMLKKYsHHRNIATYYGAFIKKSPPGhddqLWLV 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  956 MEFLPSGSLKEYLPKNKNKINLKQQLKYAV-QICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIetDKEY 1034
Cdd:cd06636     98 MEFCGAGSVTDLVKNTKGNALKEDWIAYICrEILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL--DRTV 175
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1013071061 1035 YTVKDDRDSPvFWYAPECLM-----QSKFYIASDVWSFGVTLHELLT----YCdsDSSPM-ALFL 1089
Cdd:cd06636    176 GRRNTFIGTP-YWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEgappLC--DMHPMrALFL 237
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
901-1076 3.66e-14

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ULK4 is a functionally uncharacterized kinase that shows similarity to ATG1/ULKs. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. The ULK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270912 [Multi-domain]  Cd Length: 269  Bit Score: 73.87  E-value: 3.66e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  901 TGEQVAVKSL----KPEsggnhiadLKKEIEILRNLYHENIVK-YKGICTEdggNGIKLIMEFLPSGSLKEYLPKNKNki 975
Cdd:cd14010     24 TIEFVAIKCVdkskRPE--------VLNEVRLTHELKHPNVLKfYEWYETS---NHLWLVVEYCTGGDLETLLRQDGN-- 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  976 nLKQQ--LKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAI-ETDKEYYTVKDDRD---------- 1042
Cdd:cd14010     91 -LPESsvRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLARREgEILKELFGQFSDEGnvnkvskkqa 169
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1013071061 1043 ---SPVFwYAPECLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd14010    170 krgTPYY-MAPELFQGGVHSFASDLWALGCVLYEMFT 205
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
868-1075 4.01e-14

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-gamma is predominantly expressed in neuronal tissues. Mice deficient in PKB-gamma show a reduction in brain weight due to the decreases in cell size and cell number. PKB-gamma has also been shown to be upregulated in estrogen-deficient breast cancer cells, androgen-independent prostate cancer cells, and primary ovarian tumors. It acts as a key mediator in the genesis of ovarian cancer. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 75.12  E-value: 4.01e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  868 THFEKRFLKR---IRDLGEGHFGKVELCRYDPegdnTGEQVAVKSLKPES--GGNHIADLKKEIEILRNLYHENIVKYK- 941
Cdd:cd05593      7 THHKRKTMNDfdyLKLLGKGTFGKVILVREKA----SGKYYAMKILKKEViiAKDEVAHTLTESRVLKNTRHPFLTSLKy 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  942 GICTEDGgngIKLIMEFLPSGSLKEYLPKNKNKINLKQQLkYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGD 1021
Cdd:cd05593     83 SFQTKDR---LCFVMEYVNGGELFFHLSRERVFSEDRTRF-YGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITD 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1013071061 1022 FGLTKAIETDKEyyTVKDDRDSPVFwYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd05593    159 FGLCKEGITDAA--TMKTFCGTPEY-LAPEVLEDNDYGRAVDWWGLGVVMYEMM 209
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
864-1078 4.19e-14

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK1, also called CaMKK alpha, is involved in the regulation of glucose uptake in skeletal muscles, independently of AMPK and PKB activation. It also play roles in learning and memory. Studies on CaMKK1 knockout mice reveal deficits in fear conditioning. The CaMKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 74.22  E-value: 4.19e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  864 EVDPTHFEKRFLKRIRDLGEGHFGKvelcRYDPEGDNTGEQVAVKSLKPesggnhIADLKKEIEILRNLYHENIVKYKGI 943
Cdd:cd14200     22 ESDDKYYAMKVLSKKKLLKQYGFPR----RPPPRGSKAAQGEQAKPLAP------LERVYQEIAILKKLDHVNIVKLIEV 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  944 CTEDGGNGIKLIMEFLPSGSLKEyLPKNKnKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFG 1023
Cdd:cd14200     92 LDDPAEDNLYMVFDLLRKGPVME-VPSDK-PFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGDDGHVKIADFG 169
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1013071061 1024 LTKAIETDKEyyTVKDDRDSPVFwYAPECLM---QSKFYIASDVWSFGVTLhelltYC 1078
Cdd:cd14200    170 VSNQFEGNDA--LLSSTAGTPAF-MAPETLSdsgQSFSGKALDVWAMGVTL-----YC 219
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
577-842 4.96e-14

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Tyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 73.78  E-value: 4.96e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  577 RILKKDLVQGE-HLGRgTRTHIYSGTlmdykdDEGTSEEKKIKVILKVLDPSHRDislAFFEAASMMRQVSHKHIVYLYG 655
Cdd:cd05080      4 RYLKKIRDLGEgHFGK-VSLYCYDPT------NDGTGEMVAVKALKADCGPQHRS---GWKQEIDILKTLYHENIVKYKG 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  656 VCVRDVENI--MVEEFVEGGPLDLFMHRKSDVLTTPWKFkvAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgp 733
Cdd:cd05080     74 CCSEQGGKSlqLIMEYVPLGSLRDYLPKHSIGLAQLLLF--AQQICEGMAYLHSQHYIHRDLAARNVLLDNDRL------ 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  734 fIKLSDPGIPITVLS-------RQECIERIPWIAPECVEDSKnLSVAADKWSFGTTLWEI---CYNGEIPLKD------- 796
Cdd:cd05080    146 -VKIGDFGLAKAVPEgheyyrvREDGDSPVFWYAPECLKEYK-FYYASDVWSFGVTLYELlthCDSSQSPPTKflemigi 223
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1013071061  797 -KTLIEKERFYESRCR----PVTPSC-KELADLMTRCMNYDPNQRPFFRAIM 842
Cdd:cd05080    224 aQGQMTVVRLIELLERgerlPCPDKCpQEVYHLMKNCWETEASFRPTFENLI 275
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
874-1151 5.00e-14

Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer T-cell-originated protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TOPK, also called PDZ-binding kinase (PBK), is activated at the early stage of mitosis and plays a critical role in cytokinesis. It partly functions as a mitogen-activated protein kinase (MAPK) kinase and is capable of phosphorylating p38, JNK1, and ERK2. TOPK also plays a role in DNA damage sensing and repair through its phosphorylation of histone H2AX. It contributes to cancer development and progression by downregulating the function of tumor suppressor p53 and reducing cell-cycle regulatory proteins. TOPK is found highly expressed in breast and skin cancer cells. The TOPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 73.97  E-value: 5.00e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  874 FLKRirdLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKPESGGNHIAD----LKKEIEILRNLYHENIVKYKGICTEDGG 949
Cdd:cd14001      3 FMKK---LGYGTGVNVYLMKRSPRGGSSRSPWAVKKINSKCDKGQRSLyqerLKEEAKILKSLNHPNIVGFRAFTKSEDG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  950 NgIKLIMEFLPS---GSLKEYLPKNKNKINLKQQLKYAVQICKGMDYL-GSRQYVHRDLAARNVLVESEHQ-VKIGDFGL 1024
Cdd:cd14001     80 S-LCLAMEYGGKslnDLIEERYEAGLGPFPAATILKVALSIARALEYLhNEKKILHGDIKSGNVLIKGDFEsVKLCDFGV 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1025 tkAIETDKEYYTVKDDRDSPV---FWYAPECLMQ-----SKfyiaSDVWSFGVTLHELLTYcdsdsSPMALFLKMIGPTH 1096
Cdd:cd14001    159 --SLPLTENLEVDSDPKAQYVgtePWKAKEALEEggvitDK----ADIFAYGLVLWEMMTL-----SVPHLNLLDIEDDD 227
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1013071061 1097 GQMTVTR--LVNTLKEGKRLPCPP---NCPDEVYQ----LMRKCWEFQPSNRTSFQNLIEGFEA 1151
Cdd:cd14001    228 EDESFDEdeEDEEAYYGTLGTRPAlnlGELDDSYQkvieLFYACTQEDPKDRPSAAHIVEALEA 291
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
620-850 5.19e-14

Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A-Raf cooperates with C-Raf in regulating ERK transient phosphorylation that is associated with cyclin D expression and cell cycle progression. Mice deficient in A-Raf are born alive but show neurological and intestinal defects. A-Raf demonstrates low kinase activity to MEK, compared with B- and C-Raf, and may also have alternative functions other than in the ERK signaling cascade. It regulates the M2 type pyruvate kinase, a key glycolytic enzyme. It also plays a role in endocytic membrane trafficking. A-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The A-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271052 [Multi-domain]  Cd Length: 265  Bit Score: 73.51  E-value: 5.19e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  620 ILKVLDPSHRDISlAFFEAASMMRQVSHKHIVYLYGVCVRDVENImVEEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLA 699
Cdd:cd14150     29 ILKVTEPTPEQLQ-AFKNEMQVLRKTRHVNILLFMGFMTRPNFAI-ITQWCEGSSLYRHLHVTETRFDTMQLIDVARQTA 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  700 SALSYLEDKDLVHGNVCTKNLLLaREGIDsecgpfIKLSDPGIPiTVLSR---QECIER----IPWIAPECV--EDSKNL 770
Cdd:cd14150    107 QGMDYLHAKNIIHRDLKSNNIFL-HEGLT------VKIGDFGLA-TVKTRwsgSQQVEQpsgsILWMAPEVIrmQDTNPY 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  771 SVAADKWSFGTTLWEIcYNGEIPL-----KDKTLIEKERFYES-RCRPVTPSC-KELADLMTRCMNYDPNQRPFFRAIMR 843
Cdd:cd14150    179 SFQSDVYAYGVVLYEL-MSGTLPYsninnRDQIIFMVGRGYLSpDLSKLSSNCpKAMKRLLIDCLKFKREERPLFPQILV 257

                   ....*..
gi 1013071061  844 DINKLEE 850
Cdd:cd14150    258 SIELLQR 264
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
878-1089 5.75e-14

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). MAP4K5 also facilitates Wnt signaling in B cells, and may therefore be implicated in the control of cell fate, proliferation, and polarity. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 73.52  E-value: 5.75e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVelcrYDPEGDNTGEQVAVKSLKPESGgNHIADLKKEIEILRNLYHENIVKYKG--ICTEDggngIKLI 955
Cdd:cd06646     14 IQRVGSGTYGDV----YKARNLHTGELAAVKIIKLEPG-DDFSLIQQEIFMVKECKHCNIVAYFGsyLSREK----LWIC 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  956 MEFLPSGSLKEYLPKNKNKINLkqQLKYAV-QICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFG----LTKAIET 1030
Cdd:cd06646     85 MEYCGGGSLQDIYHVTGPLSEL--QIAYVCrETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGvaakITATIAK 162
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1013071061 1031 DKEYYtvkddrDSPvFWYAPECLMQSK---FYIASDVWSFGVTLHEL--LTYCDSDSSPM-ALFL 1089
Cdd:cd06646    163 RKSFI------GTP-YWMAPEVAAVEKnggYNQLCDIWAVGITAIELaeLQPPMFDLHPMrALFL 220
PTK_Jak1_rpt1 cd05077
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely ...
928-1146 6.97e-14

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits, common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270662 [Multi-domain]  Cd Length: 266  Bit Score: 73.05  E-value: 6.97e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  928 ILRNLYHENIVKYKGICTEDGGNgiKLIMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAAR 1007
Cdd:cd05077     61 MMRQVSHKHIVLLYGVCVRDVEN--IMVEEFVEFGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTK 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1008 NVLVESEHQ-------VKIGDFGLTKAIETDKEyytvkddRDSPVFWYAPECLMQSK-FYIASDVWSFGVTLHELltyCD 1079
Cdd:cd05077    139 NILLAREGIdgecgpfIKLSDPGIPITVLSRQE-------CVERIPWIAPECVEDSKnLSIAADKWSFGTTLWEI---CY 208
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1013071061 1080 SDSSPMAlflkmigpthgqmtvtrlVNTLKEGKR------LPCPPNCpDEVYQLMRKCWEFQPSNRTSFQNLI 1146
Cdd:cd05077    209 NGEIPLK------------------DKTLAEKERfyegqcMLVTPSC-KELADLMTHCMNYDPNQRPFFRAIM 262
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
870-1075 7.53e-14

Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR kinases regulate mitosis, cell growth, embryonic development, and neurological processes. They are also required for proper centrosome duplication. Higher eukaryotes contain two NDR isoforms, NDR1 and NDR2. This subfamily also contains fungal NDR-like kinases. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270750 [Multi-domain]  Cd Length: 324  Bit Score: 74.19  E-value: 7.53e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  870 FEkrFLKRIrdlGEGHFGKVELCRYDpegdNTGEQVAVKSLKPES--GGNHIADLKKEIEILRNLYHENIVKYKgiCTED 947
Cdd:cd05599      3 FE--PLKVI---GRGAFGEVRLVRKK----DTGHVYAMKKLRKSEmlEKEQVAHVRAERDILAEADNPWVVKLY--YSFQ 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  948 GGNGIKLIMEFLPSGSLKEYLPKnKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKA 1027
Cdd:cd05599     72 DEENLYLIMEFLPGGDMMTLLMK-KDTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGLCTG 150
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1013071061 1028 IETD-KEYYTVkddrDSPVFwYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd05599    151 LKKShLAYSTV----GTPDY-IAPEVFLQKGYGKECDWWSLGVIMYEML 194
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
881-1092 8.45e-14

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 74.08  E-value: 8.45e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDpegdNTGEQVAVKSLKPES-----GGNHIAdlkKEIEILRNLYHENIVK-YKGICTEdggNGIKL 954
Cdd:PTZ00263    26 LGTGSFGRVRIAKHK----GTGEYYAIKCLKKREilkmkQVQHVA---QEKSILMELSHPFIVNmMCSFQDE---NRVYF 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPSGSLKEYLPKNKNKINLKQQLkYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIeTDKEY 1034
Cdd:PTZ00263    96 LLEFVVGGELFTHLRKAGRFPNDVAKF-YHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKV-PDRTF 173
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1013071061 1035 YTVkddrDSPVFwYAPEcLMQSKFY-IASDVWSFGVTLHELLTYCDS--DSSPMALFLKMI 1092
Cdd:PTZ00263   174 TLC----GTPEY-LAPE-VIQSKGHgKAVDWWTMGVLLYEFIAGYPPffDDTPFRIYEKIL 228
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
881-1076 8.87e-14

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The IKK complex functions as a master regulator of Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. It is composed of two kinases, IKKalpha and IKKbeta, and the regulatory subunit IKKgamma or NEMO (NF-kB Essential MOdulator). IKKs facilitate the release of NF-kB dimers from an inactive state, allowing them to migrate to the nucleus where they regulate gene transcription. There are two IKK pathways that regulate NF-kB signaling, called the classical (involving IKKbeta and NEMO) and non-canonical (involving IKKalpha) pathways. The classical pathway regulates the majority of genes activated by NF-kB. The IKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270891 [Multi-domain]  Cd Length: 289  Bit Score: 73.25  E-value: 8.87e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDpegdNTGEQVAVKSLKPESGGN--HIADLKKEIEILRNLYHENIVKYKGICTEDGGNGIK----L 954
Cdd:cd13989      1 LGSGGFGYVTLWKHQ----DTGEYVAIKKCRQELSPSdkNRERWCLEVQIMKKLNHPNVVSARDVPPELEKLSPNdlplL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPSGSLKEYLPKNKNKINLKQ-QLKYAVQ-ICKGMDYLGSRQYVHRDLAARN-VLVESEHQV--KIGDFGLTKAIe 1029
Cdd:cd13989     77 AMEYCSGGDLRKVLNQPENCCGLKEsEVRTLLSdISSAISYLHENRIIHRDLKPENiVLQQGGGRViyKLIDLGYAKEL- 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1013071061 1030 tdkeyytvkDDRDS------PVFWYAPEcLMQSKFYIAS-DVWSFGVTLHELLT 1076
Cdd:cd13989    156 ---------DQGSLctsfvgTLQYLAPE-LFESKKYTCTvDYWSFGTLAFECIT 199
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
875-1074 9.23e-14

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 2; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK2 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 73.93  E-value: 9.23e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  875 LKRIRDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKPESGGNHIadlkKEIEILRNLYHENIVKYKGICTEDGGngIKL 954
Cdd:cd06649      7 FERISELGAGNGGVVTKVQHKPSGLIMARKLIHLEIKPAIRNQII----RELQVLHECNSPYIVGFYGAFYSDGE--ISI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPSGSLKEYLpKNKNKINLKQQLKYAVQICKGMDYLGSR-QYVHRDLAARNVLVESEHQVKIGDFGLTKAIeTDKE 1033
Cdd:cd06649     81 CMEHMDGGSLDQVL-KEAKRIPEEILGKVSIAVLRGLAYLREKhQIMHRDVKPSNILVNSRGEIKLCDFGVSGQL-IDSM 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1013071061 1034 YYTVKDDRDspvfWYAPECLMQSKFYIASDVWSFGVTLHEL 1074
Cdd:cd06649    159 ANSFVGTRS----YMSPERLQGTHYSVQSDIWSMGLSLVEL 195
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
880-1091 9.97e-14

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271020 [Multi-domain]  Cd Length: 275  Bit Score: 72.78  E-value: 9.97e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  880 DLGEGHFGKVELCrYDpEGDNTGEQVAVKSLK------------PESGGNH--------IADLKKEIEILRNLYHENIVK 939
Cdd:cd14118      1 EIGKGSYGIVKLA-YN-EEDNTLYAMKILSKKkllkqagffrrpPPRRKPGalgkpldpLDRVYREIAILKKLDHPNVVK 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  940 YKGICTEDGGNGIKLIMEFLPSGSLKEYLPKNKnkINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKI 1019
Cdd:cd14118     79 LVEVLDDPNEDNLYMVFELVDKGAVMEVPTDNP--LSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKI 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1020 GDFGLTKAIETDKEYYTvkDDRDSPVFwYAPECLMQSKFYI---ASDVWSFGVTLhelltYC-------DSDSSPMALFL 1089
Cdd:cd14118    157 ADFGVSNEFEGDDALLS--STAGTPAF-MAPEALSESRKKFsgkALDIWAMGVTL-----YCfvfgrcpFEDDHILGLHE 228

                   ..
gi 1013071061 1090 KM 1091
Cdd:cd14118    229 KI 230
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
577-848 1.01e-13

Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER2 (ErbB2, HER2/neu) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER2 does not bind to any known EGFR subfamily ligands, but contributes to the kinase activity of all possible heterodimers. It acts as the preferred partner of other ligand-bound EGFR proteins and functions as a signal amplifier, with the HER2-HER3 heterodimer being the most potent pair in mitogenic signaling. HER2 plays an important role in cell development, proliferation, survival and motility. Overexpression of HER2 results in its activation and downstream signaling, even in the absence of ligand. HER2 overexpression, mainly due to gene amplification, has been shown in a variety of human cancers. Its role in breast cancer is especially well-documented. HER2 is up-regulated in about 25% of breast tumors and is associated with increases in tumor aggressiveness, recurrence and mortality. HER2 is a target for monoclonal antibodies and small molecule inhibitors, which are being developed as treatments for cancer. The first humanized antibody approved for clinical use is Trastuzumab (Herceptin), which is being used in combination with other therapies to improve the survival rates of patients with HER2-overexpressing breast cancer. The HER2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270684 [Multi-domain]  Cd Length: 279  Bit Score: 72.75  E-value: 1.01e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  577 RILKK-DLVQGEHLGRGTRTHIYSGTLMDykddegTSEEKKIKVILKVL-DPSHRDISLAFFEAASMMRQVSHKHIVYLY 654
Cdd:cd05109      2 RILKEtELKKVKVLGSGAFGTVYKGIWIP------DGENVKIPVAIKVLrENTSPKANKEILDEAYVMAGVGSPYVCRLL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  655 GVCVRDVENIMVEEFVEGGPLDlFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGidsecgpF 734
Cdd:cd05109     76 GICLTSTVQLVTQLMPYGCLLD-YVRENKDRIGSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPN-------H 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  735 IKLSDPGipitvLSRQECIER-----------IPWIAPECVEDSKnLSVAADKWSFGTTLWEIC------YNGeIPLKD- 796
Cdd:cd05109    148 VKITDFG-----LARLLDIDEteyhadggkvpIKWMALESILHRR-FTHQSDVWSYGVTVWELMtfgakpYDG-IPAREi 220
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1013071061  797 KTLIEK-ERFyesrcrPVTPSC-KELADLMTRCMNYDPNQRPFFRAIMRDINKL 848
Cdd:cd05109    221 PDLLEKgERL------PQPPICtIDVYMIMVKCWMIDSECRPRFRELVDEFSRM 268
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
587-835 1.01e-13

Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Nak1, Saccharomyces cerevisiae Kic1p (kinase that interacts with Cdc31p) and related proteins. Nak1 (also called N-rich kinase 1), is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Kic1p is required by budding yeast for cell integrity and morphogenesis. Kic1p interacts with Cdc31p, the yeast homologue of centrin, and phosphorylates substrates in a Cdc31p-dependent manner. The Nak1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 72.89  E-value: 1.01e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  587 EHLGRGTRTHIYSGTLMDykddegTSEEKKIKVIlkVLDPSHRDISLAFFEAA--SMMRQVSHKHIVYLYGVCVRDVENI 664
Cdd:cd06917      7 ELVGRGSYGAVYRGYHVK------TGRVVALKVL--NLDTDDDDVSDIQKEVAllSQLKLGQPKNIIKYYGSYLKGPSLW 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  665 MVEEFVEGGPLDLFMhrKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGidsecgpFIKLSDPGIP- 743
Cdd:cd06917     79 IIMDYCEGGSIRTLM--RAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTG-------NVKLCDFGVAa 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  744 ---ITVLSRQECIERIPWIAPECVEDSKNLSVAADKWSFGTTLWEICYnGEIPLKDK------TLIEKERfyesrcRPVT 814
Cdd:cd06917    150 slnQNSSKRSTFVGTPYWMAPEVITEGKYYDTKADIWSLGITTYEMAT-GNPPYSDVdalravMLIPKSK------PPRL 222
                          250       260
                   ....*....|....*....|....
gi 1013071061  815 PS---CKELADLMTRCMNYDPNQR 835
Cdd:cd06917    223 EGngySPLLKEFVAACLDEEPKDR 246
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
647-844 1.02e-13

Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the subfamily include SLK, STK10 (also called LOK for Lymphocyte-Oriented Kinase), SmSLK (Schistosoma mansoni SLK), and related proteins. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It also plays a role in mediating actin reorganization. STK10 is responsible in regulating the CD28 responsive element in T cells, as well as leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. SmSLK is capable of activating the MAPK Jun N-terminal kinase (JNK) pathway in human embryonic kidney cells as well as in Xenopus oocytes. It may participate in regulating MAPK cascades during host-parasite interactions. The SLK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 72.85  E-value: 1.02e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  647 HKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREG 726
Cdd:cd06611     61 HPNIVGLYEAYFYENKLWILIEFCDGGALDSIMLELERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDG 140
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  727 IdsecgpfIKLSDPGIPITVLS----RQECIERIPWIAPECV--EDSKN--LSVAADKWSFGTTLWEICyNGEIPLKDKT 798
Cdd:cd06611    141 D-------VKLADFGVSAKNKStlqkRDTFIGTPYWMAPEVVacETFKDnpYDYKADIWSLGITLIELA-QMEPPHHELN 212
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1013071061  799 LIeKERFYESRCRPVT---PS--CKELADLMTRCMNYDPNQRPFFRAIMRD 844
Cdd:cd06611    213 PM-RVLLKILKSEPPTldqPSkwSSSFNDFLKSCLVKDPDDRPTAAELLKH 262
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
879-1145 1.02e-13

Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of RIP4, ankyrin (ANK) repeat and kinase domain containing 1 (ANKK1), and similar proteins, all of which harbor C-terminal ANK repeats. RIP4, also called Protein Kinase C-associated kinase (PKK), regulates keratinocyte differentiation and cutaneous inflammation. It activates NF-kappaB and is important in the survival of diffuse large B-cell lymphoma cells. The ANKK1 protein, also called PKK2, has not been studied extensively. The ANKK1 gene, located less than 10kb downstream of the D2 dopamine receptor (DRD2) locus, is altered in the Taq1 A1 polymorphism, which is related to a reduced DRD2 binding affinity and consequently, to mental disorders. The RIP4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 72.53  E-value: 1.02e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGHFGKVelcrYDPEGDNTGEQVAVK---SLKP-ESGGNHIADLKKEIEILRNLYhenIVKYKGICTEDGGngikL 954
Cdd:cd14025      2 EKVGSGGFGQV----YKVRHKHWKTWLAIKcppSLHVdDSERMELLEEAKKMEMAKFRH---ILPVYGICSEPVG----L 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPSGSLKEYLPKNKNKINLKQQLKYavQICKGMDYLGSRQ--YVHRDLAARNVLVESEHQVKIGDFGLTKAIETDK 1032
Cdd:cd14025     71 VMEYMETGSLEKLLASEPLPWELRFRIIH--ETAVGMNFLHCMKppLLHLDLKPANILLDAHYHVKISDFGLAKWNGLSH 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1033 EYYTVKDDRDSPVFWYAPECLMQSK--FYIASDVWSFGVTLHELLTycdsDSSPMALFLKMIgpthgqMTVTRLVNTLKE 1110
Cdd:cd14025    149 SHDLSRDGLRGTIAYLPPERFKEKNrcPDTKHDVYSFAIVIWGILT----QKKPFAGENNIL------HIMVKVVKGHRP 218
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1013071061 1111 GKRLPC---PPNCpDEVYQLMRKCWEFQPSNRTSFQNL 1145
Cdd:cd14025    219 SLSPIPrqrPSEC-QQMICLMKRCWDQDPRKRPTFQDI 255
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
566-848 1.05e-13

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. There are many splice variants of FGFR2 which show differential expression and binding to FGF ligands. Disruption of either FGFR2 or FGFR2b is lethal in mice, due to defects in the placenta or severe impairment of tissue development including lung, limb, and thyroid, respectively. Disruption of FGFR2c in mice results in defective bone and skull development. Genetic alterations of FGFR2 are associated with many human skeletal disorders including Apert syndrome, Crouzon syndrome, Jackson-Weiss syndrome, and Pfeiffer syndrome. FGFR2 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 73.51  E-value: 1.05e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  566 PVYPMSQLSFDRilkkdLVQGEHLGRGTRTHIYSGTLMDYKDDEgtsEEKKIKVILKVL--DPSHRDISLAFFEAASMMR 643
Cdd:cd05101     14 PEDPKWEFPRDK-----LTLGKPLGEGCFGQVVMAEAVGIDKDK---PKEAVTVAVKMLkdDATEKDLSDLVSEMEMMKM 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  644 QVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRK-----------SDVLTTPWKFK----VAKQLASALSYLEDK 708
Cdd:cd05101     86 IGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRARrppgmeysydiNRVPEEQMTFKdlvsCTYQLARGMEYLASQ 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  709 DLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGIPITVLS----RQECIERIP--WIAPECVEDsKNLSVAADKWSFGTT 782
Cdd:cd05101    166 KCIHRDLAARNVLVTENNV-------MKIADFGLARDINNidyyKKTTNGRLPvkWMAPEALFD-RVYTHQSDVWSFGVL 237
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1013071061  783 LWEICYNGEIPLKDKTLIEKERFYESRCRPVTPS--CKELADLMTRCMNYDPNQRPFFRAIMRDINKL 848
Cdd:cd05101    238 MWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPAncTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRI 305
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
875-1074 1.29e-13

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 1; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. MEK1 also plays a role in cell cycle control. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 73.17  E-value: 1.29e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  875 LKRIRDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKPESGGNHIadlkKEIEILRNLYHENIVKYKGICTEDGGngIKL 954
Cdd:cd06650      7 FEKISELGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPAIRNQII----RELQVLHECNSPYIVGFYGAFYSDGE--ISI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPSGSLKEYLpKNKNKINLKQQLKYAVQICKGMDYLGSRQYV-HRDLAARNVLVESEHQVKIGDFGLTKAIeTDKE 1033
Cdd:cd06650     81 CMEHMDGGSLDQVL-KKAGRIPEQILGKVSIAVIKGLTYLREKHKImHRDVKPSNILVNSRGEIKLCDFGVSGQL-IDSM 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1013071061 1034 YYTVKDDRDspvfWYAPECLMQSKFYIASDVWSFGVTLHEL 1074
Cdd:cd06650    159 ANSFVGTRS----YMSPERLQGTHYSVQSDIWSMGLSLVEM 195
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
639-851 1.44e-13

Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TESK proteins phosphorylate cofilin and induce actin cytoskeletal reorganization. In the Drosphila eye, TESK is required for epithelial cell organization. Mammals contain two TESK proteins, TESK1 and TESK2, which are highly expressed in testis and play roles in spermatogenesis. TESK1 is found in testicular germ cells while TESK2 is expressed mainly in nongerminal Sertoli cells. TESK1 is stimulated by integrin-mediated signaling pathways. It regulates cell spreading and focal adhesion formation. The TESK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 72.12  E-value: 1.44e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  639 ASMMRQV------SHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKsDVLTTPWKFKVAKQLASALSYLEDKDLVH 712
Cdd:cd14155     33 ANMLREVqlmnrlSHPNILRFMGVCVHQGQLHALTEYINGGNLEQLLDSN-EPLSWTVRVKLALDIARGLSYLHSKGIFH 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  713 GNVCTKNLLLAREgidsECGPFIKLSDPGIPITVLSRQECIERIP------WIAPECVEDSKnLSVAADKWSFGTTLWEI 786
Cdd:cd14155    112 RDLTSKNCLIKRD----ENGYTAVVGDFGLAEKIPDYSDGKEKLAvvgspyWMAPEVLRGEP-YNEKADVFSYGIILCEI 186
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1013071061  787 CynGEIPLKDKTLIEKERF------YESRCRPVTPSCKELAdlmTRCMNYDPNQRPFFRAIMRDINKLEEQ 851
Cdd:cd14155    187 I--ARIQADPDYLPRTEDFgldydaFQHMVGDCPPDFLQLA---FNCCNMDPKSRPSFHDIVKTLEEILEK 252
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
873-1139 1.47e-13

Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin receptor-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR1, also called Activin receptor-Like Kinase 2 (ALK2), and ALK1 act as receptors for bone morphogenetic proteins (BMPs) and they activate SMAD1/5/8. ACVR1 is widely expressed while ALK1 is limited mainly to endothelial cells. The specificity of BMP binding to type I receptors is affected by type II receptors. ACVR1 binds BMP6/7/9/10 and can also bind anti-Mullerian hormone (AMH) in the presence of AMHR2. ALK1 binds BMP9/10 as well as TGFbeta in endothelial cells. A missense mutation in the GS domain of ACVR1 causes fibrodysplasia ossificans progressiva, a complex and disabling disease characterized by congenital skeletal malformations and extraskeletal bone formation. ACVR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like ACVR1 and ALK1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The ACVR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271044 [Multi-domain]  Cd Length: 298  Bit Score: 72.86  E-value: 1.47e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  873 RFLKRIRDLGEGHFGKVElcrydpEGDNTGEQVAVK--SLKPEsggnhiADLKKEIEILRN--LYHENIVKY-------K 941
Cdd:cd14142      5 RQITLVECIGKGRYGEVW------RGQWQGESVAVKifSSRDE------KSWFRETEIYNTvlLRHENILGFiasdmtsR 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  942 GICTEdggngIKLIMEFLPSGSLKEYLpkNKNKINLKQQLKYAVQICKGMDYL--------GSRQYVHRDLAARNVLVES 1013
Cdd:cd14142     73 NSCTQ-----LWLITHYHENGSLYDYL--QRTTLDHQEMLRLALSAASGLVHLhteifgtqGKPAIAHRDLKSKNILVKS 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1014 EHQVKIGDFGLTKAIETDKEYYTVKDDRDSPVFWY-APECLMQS------KFYIASDVWSFGVTLHELLTYCDSD---SS 1083
Cdd:cd14142    146 NGQCCIADLGLAVTHSQETNQLDVGNNPRVGTKRYmAPEVLDETintdcfESYKRVDIYAFGLVLWEVARRCVSGgivEE 225
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1013071061 1084 PMALFLKMIG--PTHGQMTVTRLVNTLKegkrlPCPPN--CPDEVY----QLMRKCWEFQPSNR 1139
Cdd:cd14142    226 YKPPFYDVVPsdPSFEDMRKVVCVDQQR-----PNIPNrwSSDPTLtamaKLMKECWYQNPSAR 284
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
881-1075 1.47e-13

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I gamma; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 72.72  E-value: 1.47e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDpegdNTGEQVAVKSLKpESGGNHIADLKKEIEILRNLYHENIVKYKGIctEDGGNGIKLIMEFLP 960
Cdd:cd14166     11 LGSGAFSEVYLVKQR----STGKLYALKCIK-KSPLSRDSSLENEIAVLKRIKHENIVTLEDI--YESTTHYYLVMQLVS 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  961 SGSLKEYLPK-----NKNKINLKQQLKYAVQickgmdYLGSRQYVHRDLAARNVLV---ESEHQVKIGDFGLTKAietdk 1032
Cdd:cd14166     84 GGELFDRILErgvytEKDASRVINQVLSAVK------YLHENGIVHRDLKPENLLYltpDENSKIMITDFGLSKM----- 152
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1013071061 1033 EYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd14166    153 EQNGIMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILL 195
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
876-1079 1.52e-13

Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Myt1 is a cytoplasmic cell cycle checkpoint kinase that can keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of N-terminal thr (T14) and tyr (Y15) residues, leading to the delay of meiosis I entry. Meiotic progression is ensured by a two-step inhibition and downregulation of Myt1 by CDK1/XRINGO and p90Rsk during oocyte maturation. In addition, Myt1 targets cyclin B1/B2 and is essential for Golgi and ER assembly during telophase. In Drosophila, Myt1 may be a downstream target of Notch during eye development. The Myt1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270952 [Multi-domain]  Cd Length: 249  Bit Score: 71.96  E-value: 1.52e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  876 KRIRDLGEGHFGKV--ELCRYDpegdntGEQVAVK-SLKPESGGNHIADLKKEIEILRNLY-HENIVKYKGICTEdggNG 951
Cdd:cd14050      4 TILSKLGEGSFGEVfkVRSRED------GKLYAVKrSRSRFRGEKDRKRKLEEVERHEKLGeHPNCVRFIKAWEE---KG 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  952 IKLIMEFLPSGSLKEYLPKNkNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTkaIETD 1031
Cdd:cd14050     75 ILYIQTELCDTSLQQYCEET-HSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLV--VELD 151
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1013071061 1032 KEYYTVKDDRDSPvfWYAPEcLMQSKFYIASDVWSFGVTLHELLTYCD 1079
Cdd:cd14050    152 KEDIHDAQEGDPR--YMAPE-LLQGSFTKAADIFSLGITILELACNLE 196
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
628-850 1.52e-13

Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie proteins, consisting of Tie1 and Tie2, are receptor PTKs (RTKs) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2, while no specific ligand has been identified for Tie1. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. In vivo studies of Tie1 show that it is critical in vascular development. The Tie subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 72.38  E-value: 1.52e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  628 HRDISlafFEAASMMRQVSHKHIVYLYGVCV-RDVENIMVEEFVEGGPLDLFmhRKSDVLTTPWKFKVAKQLASALS--- 703
Cdd:cd05047     39 HRDFA---GELEVLCKLGHHPNIINLLGACEhRGYLYLAIEYAPHGNLLDFL--RKSRVLETDPAFAIANSTASTLSsqq 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  704 -------------YLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGipitvLSRQE------CIERIP--WIAPE 762
Cdd:cd05047    114 llhfaadvargmdYLSQKQFIHRDLAARNILVGENYV-------AKIADFG-----LSRGQevyvkkTMGRLPvrWMAIE 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  763 cvedSKNLSV---AADKWSFGTTLWEICYNGEIPLKDKTLIEKERFYESRCRPVTP-SCK-ELADLMTRCMNYDPNQRPF 837
Cdd:cd05047    182 ----SLNYSVyttNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPlNCDdEVYDLMRQCWREKPYERPS 257
                          250
                   ....*....|...
gi 1013071061  838 FRAIMRDINKLEE 850
Cdd:cd05047    258 FAQILVSLNRMLE 270
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
875-1076 1.84e-13

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 and MEK2 are MAPK kinases (MAPKKs or MKKs), and are dual-specificity PKs that phosphorylate and activate the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1/2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. This cascade has also been implicated in synaptic plasticity, migration, morphological determination, and stress response immunological reactions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1/2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 72.47  E-value: 1.84e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  875 LKRIRDLGEGHFGKVELCRYDPegdnTGEQVAVKSLKPEsggnhiadLKKEI--EILRNL--YHE----NIVKYKGICTE 946
Cdd:cd06615      3 FEKLGELGAGNGGVVTKVLHRP----SGLIMARKLIHLE--------IKPAIrnQIIRELkvLHEcnspYIVGFYGAFYS 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  947 DGGngIKLIMEFLPSGSLKEYLpKNKNKINLKQQLKYAVQICKGMDYL-GSRQYVHRDLAARNVLVESEHQVKIGDFGLT 1025
Cdd:cd06615     71 DGE--ISICMEHMDGGSLDQVL-KKAGRIPENILGKISIAVLRGLTYLrEKHKIMHRDVKPSNILVNSRGEIKLCDFGVS 147
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1013071061 1026 KAIeTDKEYYTVKDDRDspvfWYAPECLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd06615    148 GQL-IDSMANSFVGTRS----YMSPERLQGTHYTVQSDIWSLGLSLVEMAI 193
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
878-1115 1.96e-13

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 75.16  E-value: 1.96e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVELCRYDpegdNTGE-----QVAVKSLKPESGgnhiADLKKEIEILRNLYHENIVKYKGICTEDGGNGI 952
Cdd:PTZ00266    18 IKKIGNGRFGEVFLVKHK----RTQEffcwkAISYRGLKEREK----SQLVIEVNVMRELKHKNIVRYIDRFLNKANQKL 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  953 KLIMEFLPSGSLKEYLPK---------NKNKINLKQQLKYAVQICKGM-DYLGSRQYVHRDLAARNVLVESEHQ------ 1016
Cdd:PTZ00266    90 YILMEFCDAGDLSRNIQKcykmfgkieEHAIVDITRQLLHALAYCHNLkDGPNGERVLHRDLKPQNIFLSTGIRhigkit 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1017 -----------VKIGDFGLTKAIETDKEYYTVKddrDSPVFWyAPECLM-QSKFY-IASDVWSFGVTLHELltyCDSDSs 1083
Cdd:PTZ00266   170 aqannlngrpiAKIGDFGLSKNIGIESMAHSCV---GTPYYW-SPELLLhETKSYdDKSDMWALGCIIYEL---CSGKT- 241
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1013071061 1084 pmalflkmigPTHGQMTVTRLVNTLKEGKRLP 1115
Cdd:PTZ00266   242 ----------PFHKANNFSQLISELKRGPDLP 263
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
605-838 2.24e-13

Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. Members of this subfamily include LIMK, Testicular or testis-specific protein kinase (TESK), and similar proteins. LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270967 [Multi-domain]  Cd Length: 252  Bit Score: 71.37  E-value: 2.24e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  605 YKDDEGTSeeKKIKVILKVLDPSHRDislAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSD 684
Cdd:cd14065     10 YKVTHRET--GKVMVMKELKRFDEQR---SFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGTLEELLKSMDE 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  685 VLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLL-----AREGIDSECG-----PFIKLSDP--GIPITVLSRQEc 752
Cdd:cd14065     85 QLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVreanrGRNAVVADFGlaremPDEKTKKPdrKKRLTVVGSPY- 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  753 ieripWIAPECVE----DSKnlsvaADKWSFGTTLWEICynGEIPLKDKTLIEKERF---YESRCRPVTPSC-KELADLM 824
Cdd:cd14065    164 -----WMAPEMLRgesyDEK-----VDVFSFGIVLCEII--GRVPADPDYLPRTMDFgldVRAFRTLYVPDCpPSFLPLA 231
                          250
                   ....*....|....
gi 1013071061  825 TRCMNYDPNQRPFF 838
Cdd:cd14065    232 IRCCQLDPEKRPSF 245
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
578-847 2.45e-13

Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. IGF-1R is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the ligand (IGF-1 or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, which stimulates downstream kinase activities and biological function. IGF-1R signaling is important in the differentiation, growth, and survival of normal cells. In cancer cells, where it is frequently overexpressed, IGF-1R is implicated in proliferation, the suppression of apoptosis, invasion, and metastasis. IGF-1R is being developed as a therapeutic target in cancer treatment. The IGF-1R subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133193 [Multi-domain]  Cd Length: 277  Bit Score: 71.60  E-value: 2.45e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  578 ILKKDLVQGEHLGRGTRTHIYSGTLMDYKDDEgtseeKKIKVILKVLD--PSHRDiSLAFFEAASMMRQVSHKHIVYLYG 655
Cdd:cd05062      3 VAREKITMSRELGQGSFGMVYEGIAKGVVKDE-----PETRVAIKTVNeaASMRE-RIEFLNEASVMKEFNCHHVVRLLG 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  656 VCVRDVENIMVEEFVEGGPLDLFMHR-KSDVLTTPWK--------FKVAKQLASALSYLEDKDLVHGNVCTKNLLLArEG 726
Cdd:cd05062     77 VVSQGQPTLVIMELMTRGDLKSYLRSlRPEMENNPVQappslkkmIQMAGEIADGMAYLNANKFVHRDLAARNCMVA-ED 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  727 IDSECGPFIKLSDpgIPITVLSRQECIERIP--WIAPECVEDSKnLSVAADKWSFGTTLWEICYNGEIPLKDKTLIEKER 804
Cdd:cd05062    156 FTVKIGDFGMTRD--IYETDYYRKGGKGLLPvrWMSPESLKDGV-FTTYSDVWSFGVVLWEIATLAEQPYQGMSNEQVLR 232
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1013071061  805 F-YESRCRPVTPSCKE-LADLMTRCMNYDPNQRPFFRAIMRDINK 847
Cdd:cd05062    233 FvMEGGLLDKPDNCPDmLFELMRMCWQYNPKMRPSFLEIISSIKE 277
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
697-848 2.49e-13

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR alpha is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR alpha forms homodimers or heterodimers with PDGFR beta, depending on the nature of the PDGF ligand. PDGF-AA, PDGF-AB, and PDGF-CC induce PDGFR alpha homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR alpha signaling is important in the formation of lung alveoli, intestinal villi, mesenchymal dermis, and hair follicles, as well as in the development of oligodendrocytes, retinal astrocytes, neural crest cells, and testicular cells. Aberrant PDGFR alpha expression is associated with some human cancers. Mutations in PDGFR alpha have been found within a subset of gastrointestinal stromal tumors (GISTs). An active fusion protein FIP1L1-PDGFR alpha, derived from interstitial deletion, is associated with idiopathic hypereosinophilic syndrome and chronic eosinophilic leukemia. The PDGFR alpha subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173653 [Multi-domain]  Cd Length: 400  Bit Score: 73.13  E-value: 2.49e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  697 QLASALSYLEDKDLVHGNVCTKNLLLARegidsecGPFIKLSDPGIPITVLSRQECIER------IPWIAPECVEDskNL 770
Cdd:cd05105    245 QVARGMEFLASKNCVHRDLAARNVLLAQ-------GKIVKICDFGLARDIMHDSNYVSKgstflpVKWMAPESIFD--NL 315
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  771 -SVAADKWSFGTTLWEICYNGEIPLKDktLIEKERFY---ESRCRPVTP--SCKELADLMTRCMNYDPNQRPFFRAIMRD 844
Cdd:cd05105    316 yTTLSDVWSYGILLWEIFSLGGTPYPG--MIVDSTFYnkiKSGYRMAKPdhATQEVYDIMVKCWNSEPEKRPSFLHLSDI 393

                   ....
gi 1013071061  845 INKL 848
Cdd:cd05105    394 VESL 397
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
866-1075 2.69e-13

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK4 regulates cell morphology and cytoskeletal organization. It is essential for embryonic viability and proper neural development. Mice lacking PAK4 die due to defects in the fetal heart. In addition, their spinal cord motor neurons showed failure to differentiate and migrate. PAK4 also plays a role in cell survival and tumorigenesis. It is overexpressed in many primary tumors including colon, esophageal, and mammary tumors. PAK4 has also been implicated in viral and bacterial infection pathways. PAK4 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 71.98  E-value: 2.69e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  866 DPTHFEKRFLKrirdLGEGHFGKVELCRYDpegdNTGEQVAVKSLkpesggnhiaDLKK---------EIEILRNLYHEN 936
Cdd:cd06657     17 DPRTYLDNFIK----IGEGSTGIVCIATVK----SSGKLVAVKKM----------DLRKqqrrellfnEVVIMRDYQHEN 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  937 IVK-YKGICTedgGNGIKLIMEFLPSGSLKEYLpkNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEH 1015
Cdd:cd06657     79 VVEmYNSYLV---GDELWVVMEFLEGGALTDIV--THTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDG 153
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1016 QVKIGDFGLTKaiETDKEYYTVKDDRDSPvFWYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd06657    154 RVKLSDFGFCA--QVSKEVPRRKSLVGTP-YWMAPELISRLPYGPEVDIWSLGIMVIEMV 210
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
899-1075 3.09e-13

Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK2 is a tetrameric protein with two catalytic (alpha) and two regulatory (beta) subunits. It is constitutively active and ubiquitously expressed, and is found in the cytoplasm, nucleus, as well as in the plasma membrane. It phosphorylates a wide variety of substrates including gylcogen synthase, cell cycle proteins, nuclear proteins (e.g. DNA topoisomerase II), and ion channels (e.g. ENaC), among others. It may be considered a master kinase controlling the activity or lifespan of many other kinases and exerting its effect over cell fate, gene expression, protein synthesis and degradation, and viral infection. CK2 is implicated in every stage of the cell cycle and is required for cell cycle progression. It plays crucial roles in cell differentiation, proliferation, and survival, and is thus implicated in cancer. CK2 is not an oncogene by itself but elevated CK2 levels create an environment that enhances the survival of tumor cells. The CK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 71.80  E-value: 3.09e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  899 DNTGEQVAVKSLKPEsggnHIADLKKEIEILRNLY-HENIVKYKGICTEDGGNGIKLIMEFLPSGSLKEYLPK-NKNKIN 976
Cdd:cd14132     40 IGNNEKVVIKVLKPV----KKKKIKREIKILQNLRgGPNIVKLLDVVKDPQSKTPSLIFEYVNNTDFKTLYPTlTDYDIR 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  977 LkqqlkYAVQICKGMDYLGSRQYVHRDLAARNVLVESEH-QVKIGDFGLTkaietdkEYYTVKDDRDSPV---FWYAPEC 1052
Cdd:cd14132    116 Y-----YMYELLKALDYCHSKGIMHRDVKPHNIMIDHEKrKLRLIDWGLA-------EFYHPGQEYNVRVasrYYKGPEL 183
                          170       180
                   ....*....|....*....|....
gi 1013071061 1053 LMQSKFYIAS-DVWSFGVTLHELL 1075
Cdd:cd14132    184 LVDYQYYDYSlDMWSLGCMLASMI 207
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
881-1147 3.67e-13

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Heme-Regulated Inhibitor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HRI (or EIF2AK1) contains an N-terminal regulatory heme-binding domain and a C-terminal catalytic kinase domain. It is suppressed under normal conditions by binding of the heme iron, and is activated during heme deficiency. It functions as a critical regulator that ensures balanced synthesis of globins and heme, in order to form stable hemoglobin during erythroid differentiation and maturation. HRI also protects cells and enhances survival under iron-deficient conditions. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The HRI subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270951 [Multi-domain]  Cd Length: 284  Bit Score: 71.38  E-value: 3.67e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVelcrYDPEGDNTGEQVAVKSL--KPESGGNHIADLKkEIEILRNLYHENIVKYKGICTEDGGNGIKLIMEf 958
Cdd:cd14049     14 LGKGGYGKV----YKVRNKLDGQYYAIKKIliKKVTKRDCMKVLR-EVKVLAGLQHPNIVGYHTAWMEHVQLMLYIQMQ- 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  959 LPSGSLKEYLPKNKNKINLKQQ-------------LKYAVQICKGMDYLGSRQYVHRDLAARNVLVE-SEHQVKIGDFGL 1024
Cdd:cd14049     88 LCELSLWDWIVERNKRPCEEEFksapytpvdvdvtTKILQQLLEGVTYIHSMGIVHRDLKPRNIFLHgSDIHVRIGDFGL 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1025 T-KAIETDKEYYTVKDDRDSP--------VFWYAPECLMQSKFYIASDVWSFGVTLHELLTycdsdsspmalflkmigPT 1095
Cdd:cd14049    168 AcPDILQDGNDSTTMSRLNGLthtsgvgtCLYAAPEQLEGSHYDFKSDMYSIGVILLELFQ-----------------PF 230
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1013071061 1096 HGQMTVTRLVNTLKEGKrLPCP--PNCPDEVyQLMRKCWEFQPSNRTSFQNLIE 1147
Cdd:cd14049    231 GTEMERAEVLTQLRNGQ-IPKSlcKRWPVQA-KYIKLLTSTEPSERPSASQLLE 282
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
611-836 3.77e-13

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270687 [Multi-domain]  Cd Length: 258  Bit Score: 70.58  E-value: 3.77e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  611 TSEEKKIKVILKVLDPSHRDisLAFFEAASMMRQVSHKHIVYLYGVCVrDVENI-MVEEFVEGGplDLFmhrksDVLTTP 689
Cdd:cd05117     24 TGEEYAVKIIDKKKLKSEDE--EMLRREIEILKRLDHPNIVKLYEVFE-DDKNLyLVMELCTGG--ELF-----DRIVKK 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  690 WKF------KVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIDSEcgpfIKLSDPGIPITVLSRQECIERI--P-WIA 760
Cdd:cd05117     94 GSFsereaaKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDSP----IKIIDFGLAKIFEEGEKLKTVCgtPyYVA 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  761 PECVEDSK-NLSVaaDKWSFGTTLWeICYNGEIPLKDKTLIEKER--------FYESRCRPVTPSCKelaDLMTRCMNYD 831
Cdd:cd05117    170 PEVLKGKGyGKKC--DIWSLGVILY-ILLCGYPPFYGETEQELFEkilkgkysFDSPEWKNVSEEAK---DLIKRLLVVD 243

                   ....*
gi 1013071061  832 PNQRP 836
Cdd:cd05117    244 PKKRL 248
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
881-1075 3.79e-13

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKN has a C-terminal catalytic domain that is highly homologous to PKCs. Its unique N-terminal regulatory region contains antiparallel coiled-coil (ACC) domains. In mammals, there are three PKN isoforms from different genes (designated PKN-alpha, beta, and gamma), which show different enzymatic properties, tissue distribution, and varied functions. PKN can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytokeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. The PKN subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 71.95  E-value: 3.79e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDPegdnTGEQVAVKSLKPesgGNHIAdlKKEIEIL---RNLY-------HENIVKYKGiC--TEDG 948
Cdd:cd05589      7 LGRGHFGKVLLAEYKP----TGELFAIKALKK---GDIIA--RDEVESLmceKRIFetvnsarHPFLVNLFA-CfqTPEH 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  949 gngIKLIMEFLPSGSLKEYLpkNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKai 1028
Cdd:cd05589     77 ---VCFVMEYAAGGDLMMHI--HEDVFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCK-- 149
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1013071061 1029 etDKEYYTvkdDRDS-----PVFwYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd05589    150 --EGMGFG---DRTStfcgtPEF-LAPEVLTDTSYTRAVDWWGLGVLIYEML 195
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
897-1079 3.88e-13

Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), is an ER-localized type I transmembrane protein with kinase and endoribonuclease domains in the cytoplasmic side. It acts as an ER stress sensor and is the oldest and most conserved component of the unfolded protein response (UPR) in eukaryotes. The UPR is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. During ER stress, IRE1 dimerizes and forms oligomers, allowing the kinase domain to undergo trans-autophosphorylation. This leads to a conformational change that stimulates its endoribonuclease activity and results in the cleavage of its mRNA substrate, HAC1 in yeast and XBP1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. Mammals contain two IRE1 proteins, IRE1alpha (or ERN1) and IRE1beta (or ERN2). The Ire1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 71.15  E-value: 3.88e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  897 EGDNTGEQVAVKSLKPESggNHIADlkKEIEILRNL-YHENIVKYkgICTEDGGNGIKLIMEFLPSgSLKEYLpKNKNKI 975
Cdd:cd13982     20 RGTFDGRPVAVKRLLPEF--FDFAD--REVQLLRESdEHPNVIRY--FCTEKDRQFLYIALELCAA-SLQDLV-ESPRES 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  976 NLKQQ-----LKYAVQICKGMDYLGSRQYVHRDLAARNVLV--ESEH---QVKIGDFGLTKAIETDKEYYTVKDDRDSPV 1045
Cdd:cd13982     92 KLFLRpglepVRLLRQIASGLAHLHSLNIVHRDLKPQNILIstPNAHgnvRAMISDFGLCKKLDVGRSSFSRRSGVAGTS 171
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1013071061 1046 FWYAPECLMQSKFYIAS---DVWSFGVTLHELLTYCD 1079
Cdd:cd13982    172 GWIAPEMLSGSTKRRQTravDIFSLGCVFYYVLSGGS 208
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
587-841 4.96e-13

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror2 plays important roles in skeletal and heart formation. Ror2-deficient mice show widespread bone abnormalities, ventricular defects in the heart, and respiratory dysfunction. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Ror2 is also implicated in neural development. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 70.82  E-value: 4.96e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  587 EHLGRGTRTHIYSGTLMdykddeGTS--EEKKIKVILKVLDPSHRDISLAFFEAASMMRQVSHKHIVYLYGVCVRDVENI 664
Cdd:cd05091     12 EELGEDRFGKVYKGHLF------GTApgEQTQAVAIKTLKDKAEGPLREEFRHEAMLRSRLQHPNIVCLLGVVTKEQPMS 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  665 MVEEFVEGGPLDLFMHRKS---DV------------LTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLaregids 729
Cdd:cd05091     86 MIFSYCSHGDLHEFLVMRSphsDVgstdddktvkstLEPADFLHIVTQIAAGMEYLSSHHVVHKDLATRNVLV------- 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  730 eCGPF-IKLSDPGIPITVLSRQ------ECIERIPWIAPECVEDSKnLSVAADKWSFGTTLWEICYNGEIP---LKDKTL 799
Cdd:cd05091    159 -FDKLnVKISDLGLFREVYAADyyklmgNSLLPIRWMSPEAIMYGK-FSIDSDIWSYGVVLWEVFSYGLQPycgYSNQDV 236
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1013071061  800 IEKERfyESRCRPVTPSCKE-LADLMTRCMNYDPNQRPFFRAI 841
Cdd:cd05091    237 IEMIR--NRQVLPCPDDCPAwVYTLMLECWNEFPSRRPRFKDI 277
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
878-1147 5.06e-13

Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs MPK1 from Saccharomyces cerevisiae, Pmk1 from Schizosaccharomyces pombe, and similar proteins. MPK1 (also called Slt2) and Pmk1 (also called Spm1) are stress-activated MAPKs that regulate the cell wall integrity pathway, and are therefore important in the maintainance of cell shape, cell wall construction, morphogenesis, and ion homeostasis. MPK1 is activated in response to cell wall stress including heat stimulation, osmotic shock, UV irradiation, and any agents that interfere with cell wall biogenesis such as chitin antagonists, caffeine, or zymolase. MPK1 is regulated by the MAP2Ks Mkk1/2, which are regulated by the MAP3K Bck1. Pmk1 is also activated by multiple stresses including elevated temperatures, hyper- or hypotonic stress, glucose deprivation, exposure to cell-wall damaging compounds, and oxidative stress. It is regulated by the MAP2K Pek1, which is regulated by the MAP3K Mkh1. MAPKs are important mediators of cellular responses to extracellular signals. The MPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173750 [Multi-domain]  Cd Length: 332  Bit Score: 71.67  E-value: 5.06e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVelCRYDPEGDNTGEQVAVKSLkPESGGNHIADLK--KEIEILRNLY-HENIVKY--KGICTEDGGNGI 952
Cdd:cd07857      5 IKELGQGAYGIV--CSARNAETSEEETVAIKKI-TNVFSKKILAKRalRELKLLRHFRgHKNITCLydMDIVFPGNFNEL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  953 KLIMEflpsgsLKEYlpkNKNK-INLKQQLKYA------VQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLT 1025
Cdd:cd07857     82 YLYEE------LMEA---DLHQiIRSGQPLTDAhfqsfiYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLA 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1026 KAIETD--------KEYYTVKddrdspvfWY-APECLMQSKFYIAS-DVWSFGVTLHELL---------TYCDSdsspMA 1086
Cdd:cd07857    153 RGFSENpgenagfmTEYVATR--------WYrAPEIMLSFQSYTKAiDVWSVGCILAELLgrkpvfkgkDYVDQ----LN 220
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1013071061 1087 LFLKMIG-PTHGQMTVTRLVNTLKEGKRLPCPPNCP---------DEVYQLMRKCWEFQPSNRTSFQNLIE 1147
Cdd:cd07857    221 QILQVLGtPDEETLSRIGSPKAQNYIRSLPNIPKKPfesifpnanPLALDLLEKLLAFDPTKRISVEEALE 291
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
880-1075 5.24e-13

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called Ribosomal protein S6 kinase alpha-2 or 90kDa ribosomal protein S6 kinase 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK3 is also called S6K-alpha-2, RPS6KA2, p90RSK2 or MAPK-activated protein kinase 1c (MAPKAPK-1c). RSK3 binds muscle A-kinase anchoring protein (mAKAP)-b directly and regulates concentric cardiac myocyte growth. The RSK3 gene, RPS6KA2, is a putative tumor suppressor gene in sporadic epithelial ovarian cancer and variations to the gene may be associated with rectal cancer risk. RSK3 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 71.20  E-value: 5.24e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  880 DLGEGHFGKVELCRYDPegdnTGEQVAVKSLKPESggnhiADLKKEIEIL-RNLYHENIVKYKGIctEDGGNGIKLIMEF 958
Cdd:cd14178     10 DIGIGSYSVCKRCVHKA----TSTEYAVKIIDKSK-----RDPSEEIEILlRYGQHPNIITLKDV--YDDGKFVYLVMEL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  959 LPSGSLKEYLPKNKNkINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESE----HQVKIGDFGLTKAIETDKEY 1034
Cdd:cd14178     79 MRGGELLDRILRQKC-FSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYMDEsgnpESIRICDFGFAKQLRAENGL 157
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1013071061 1035 YTvkddrdSPVF---WYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd14178    158 LM------TPCYtanFVAPEVLKRQGYDAACDIWSLGILLYTML 195
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
642-848 5.36e-13

Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 70.50  E-value: 5.36e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  642 MRQVSHKHIVYLYGVCVrDVENIM-VEEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDL-VHGNVCTKN 719
Cdd:cd13992     50 LKELVHDNLNKFIGICI-NPPNIAvVTEYCTRGSLQDVLLNREIKMDWMFKSSFIKDIVKGMNYLHSSSIgYHGRLKSSN 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  720 LLlaregIDSECgpFIKLSDPGIPiTVLSRQECI--------ERIPWIAPECV---EDSKNLSVAADKWSFGTTLWEI-C 787
Cdd:cd13992    129 CL-----VDSRW--VVKLTDFGLR-NLLEEQTNHqldedaqhKKLLWTAPELLrgsLLEVRGTQKGDVYSFAIILYEIlF 200
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1013071061  788 YNGEIPLKD-KTLIEKERFYES---RCRPVTPSCK---ELADLMTRCMNYDPNQRPFFRAIMRDINKL 848
Cdd:cd13992    201 RSDPFALEReVAIVEKVISGGNkpfRPELAVLLDEfppRLVLLVKQCWAENPEKRPSFKQIKKTLTEN 268
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
880-1078 5.40e-13

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called Ribosomal protein S6 kinase alpha-1 or 90kDa ribosomal protein S6 kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK1 is also called S6K-alpha-1, RPS6KA1, p90RSK1 or MAPK-activated protein kinase 1a (MAPKAPK-1a). It is a component of the insulin transduction pathway, regulating the function of IRS1. It also interacts with PKA and promotes its inactivation. RSK1 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271077 [Multi-domain]  Cd Length: 291  Bit Score: 70.83  E-value: 5.40e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  880 DLGEGHFGKVELCRYDpegdNTGEQVAVKSLKPESggnhiADLKKEIEILRNL-YHENIVKYKGIctEDGGNGIKLIMEF 958
Cdd:cd14175      8 TIGVGSYSVCKRCVHK----ATNMEYAVKVIDKSK-----RDPSEEIEILLRYgQHPNIITLKDV--YDDGKHVYLVTEL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  959 LPSGSLKEYLPKNKNkINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESE----HQVKIGDFGLTKAIETDKEY 1034
Cdd:cd14175     77 MRGGELLDKILRQKF-FSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYVDEsgnpESLRICDFGFAKQLRAENGL 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1013071061 1035 YTvkddrdSPVF---WYAPECLMQSKFYIASDVWSFGVTLHELLTYC 1078
Cdd:cd14175    156 LM------TPCYtanFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGY 196
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
867-1075 5.40e-13

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called Doublecortin-like and CAM kinase-like 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL1 (or DCAMKL1) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL1 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL1 interacts with tubulin, glucocorticoid receptor, dynein, JIP1/2, caspases (3 and 8), and calpain, among others. It plays roles in neurogenesis, neuronal migration, retrograde transport, and neuronal apoptosis. The DCKL1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271085 [Multi-domain]  Cd Length: 268  Bit Score: 70.41  E-value: 5.40e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  867 PTHFEKRFlKRIRDLGEGHFGKVELCRYDpegdNTGEQVAVKSLKPES--GGNHIadLKKEIEILRNLYHENIVKYkgIC 944
Cdd:cd14183      1 PASISERY-KVGRTIGDGNFAVVKECVER----STGREYALKIINKSKcrGKEHM--IQNEVSILRRVKHPNIVLL--IE 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  945 TEDGGNGIKLIMEFLPSGSLKEYLpKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVeSEHQ-----VKI 1019
Cdd:cd14183     72 EMDMPTELYLVMELVKGGDLFDAI-TSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLV-YEHQdgsksLKL 149
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1013071061 1020 GDFGLTKAIetDKEYYTVKDdrdSPVFwYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd14183    150 GDFGLATVV--DGPLYTVCG---TPTY-VAPEIIAETGYGLKVDIWAAGVITYILL 199
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
879-1076 6.11e-13

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called 90kDa ribosomal protein S6 kinase 3 or Ribosomal protein S6 kinase alpha-3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK2 is also called p90RSK3, RPS6KA3, S6K-alpha-3, or MAPK-activated protein kinase 1b (MAPKAPK-1b). RSK2 is expressed highly in the regions of the brain with high synaptic activity. It plays a role in the maintenance and consolidation of excitatory synapses. It is a specific modulator of phospholipase D in calcium-regulated exocytosis. Mutations in the RSK2 gene, RPS6KA3, cause Coffin-Lowry syndrome (CLS), a rare syndromic form of X-linked mental retardation characterized by growth and psychomotor retardation and skeletal abnormalities. RSK2 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 71.59  E-value: 6.11e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGHFGKVELCRYDpegdNTGEQVAVKSLKPESggnhiADLKKEIEIL-RNLYHENIVKYKGIctEDGGNGIKLIME 957
Cdd:cd14176     25 EDIGVGSYSVCKRCIHK----ATNMEFAVKIIDKSK-----RDPTEEIEILlRYGQHPNIITLKDV--YDDGKYVYVVTE 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  958 FLPSGSLKEYLPKNKNkINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESE----HQVKIGDFGLTKAIETDKE 1033
Cdd:cd14176     94 LMKGGELLDKILRQKF-FSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDEsgnpESIRICDFGFAKQLRAENG 172
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1013071061 1034 YYTvkddrdSPVF---WYAPECLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd14176    173 LLM------TPCYtanFVAPEVLERQGYDAACDIWSLGVLLYTMLT 212
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
587-835 6.39e-13

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK3 mRNA is up-regulated in fibroblasts after Ras-induced senescence, and its overexpression induces both autophagy and senescence in a fibroblast cell line. ULK3, through its kinase activity, positively regulates Gli proteins, mediators of the Sonic hedgehog (Shh) signaling pathway that is implicated in tissue homeostasis maintenance and neurogenesis. It is inhibited by binding to Suppressor of Fused (Sufu). The ULK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271023 [Multi-domain]  Cd Length: 252  Bit Score: 70.01  E-value: 6.39e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  587 EHLGRGTRTHIYSGtlmdYKDDeGTSEEKKIKVILK-VLDPSHRDISLAFFEaasMMRQVSHKHIVYLYGVcVRDVENI- 664
Cdd:cd14121      1 EKLGSGTYATVYKA----YRKS-GAREVVAVKCVSKsSLNKASTENLLTEIE---LLKKLKHPHIVELKDF-QWDEEHIy 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  665 MVEEFVEGGPLDLFMHRKSDVlttpwKFKVAK----QLASALSYLEDKDLVHGNVCTKNLLLAREGidsecGPFIKLSDP 740
Cdd:cd14121     72 LIMEYCSGGDLSRFIRSRRTL-----PESTVRrflqQLASALQFLREHNISHMDLKPQNLLLSSRY-----NPVLKLADF 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  741 GIPITVLSRQE--CIERIP-WIAPECVEdSKNLSVAADKWSFGTTLWEiCYNGEIPLKDKTL------IEKERFYESRCR 811
Cdd:cd14121    142 GFAQHLKPNDEahSLRGSPlYMAPEMIL-KKKYDARVDLWSVGVILYE-CLFGRAPFASRSFeeleekIRSSKPIEIPTR 219
                          250       260
                   ....*....|....*....|....*
gi 1013071061  812 P-VTPSCKelaDLMTRCMNYDPNQR 835
Cdd:cd14121    220 PeLSADCR---DLLLRLLQRDPDRR 241
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
881-1073 7.77e-13

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKalpha is involved in the non-canonical or alternative pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The non-canonical pathway functions in cells lacking NEMO (NF-kB Essential MOdulator) and IKKbeta. It is induced by a subset of TNFR family members including CD40, RANK, and B cell-activating factor receptor. IKKalpha processes the Inhibitor of NF-kB (IkB)-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus. This pathway is dependent on NIK (NF-kB Inducing Kinase) which phosphorylates and activates IKKalpha. The IKKalpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 70.33  E-value: 7.77e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVelCRYdpEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGG--NGIKLI-ME 957
Cdd:cd14039      1 LGTGGFGNV--CLY--QNQETGEKIAIKSCRLELSVKNKDRWCHEIQIMKKLNHPNVVKACDVPEEMNFlvNDVPLLaME 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  958 FLPSGSLKEYLPKNKNKINLK--QQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQV---KIGDFGLTKaietDK 1032
Cdd:cd14039     77 YCSGGDLRKLLNKPENCCGLKesQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEINGKivhKIIDLGYAK----DL 152
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1013071061 1033 EYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHE 1073
Cdd:cd14039    153 DQGSLCTSFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFE 193
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
881-1152 8.57e-13

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as TGFbR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. TGFbR2 acts as the receptor for TGFbeta, which is crucial in growth control and homeostasis in many different tissues. It plays roles in regulating apoptosis and in maintaining the balance between self renewal and cell loss. It also plays a key role in maintaining vascular integrity and in regulating responses to genotoxic stress. Mutations in TGFbR2 can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. The TGFbR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270957 [Multi-domain]  Cd Length: 295  Bit Score: 70.48  E-value: 8.57e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKV---ELcRYDPEGDNtgEQVAVKSLKPEsggnHIADLKKEIEILR--NLYHENIVKYkgICTEDGGNGIK-- 953
Cdd:cd14055      3 VGKGRFAEVwkaKL-KQNASGQY--ETVAVKIFPYE----EYASWKNEKDIFTdaSLKHENILQF--LTAEERGVGLDrq 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  954 --LIMEFLPSGSLKEYLpkNKNKINLKQQLKYAVQICKGMDYLGSRQY---------VHRDLAARNVLVESEHQVKIGDF 1022
Cdd:cd14055     74 ywLITAYHENGSLQDYL--TRHILSWEDLCKMAGSLARGLAHLHSDRTpcgrpkipiAHRDLKSSNILVKNDGTCVLADF 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1023 GLtkAIETDKEyYTVKDDRDS---PVFWY-APECLmQSKFYIAS-------DVWSFGVTLHELLTYCD--SDSSPMAL-F 1088
Cdd:cd14055    152 GL--ALRLDPS-LSVDELANSgqvGTARYmAPEAL-ESRVNLEDlesfkqiDVYSMALVLWEMASRCEasGEVKPYELpF 227
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1013071061 1089 LKMIG--PTHGQMtvtrLVNTLKEGKRlpcpPNCPDE--VYQLMR-------KCWEFQPSNRTSFQNLIEGFEAL 1152
Cdd:cd14055    228 GSKVRerPCVESM----KDLVLRDRGR----PEIPDSwlTHQGMCvlcdtitECWDHDPEARLTASCVAERFNEL 294
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
878-1075 8.67e-13

Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear Dbf2-Related (NDR)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include ROCK and ROCK-like proteins such as DMPK, MRCK, and CRIK, as well as NDR and NDR-like proteins such as LATS, CBK1 and Sid2p. ROCK and CRIK are effectors of the small GTPase Rho, while MRCK is an effector of the small GTPase Cdc42. NDR and NDR-like kinases contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Proteins in this subfamily are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. The ROCK/NDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 71.16  E-value: 8.67e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVELCRyDPEgdnTGEQVAVKSLKPES--GGNHIADLKKEIEILRNLYHENIVKYKgiCTEDGGNGIKLI 955
Cdd:cd05573      6 IKVIGRGAFGEVWLVR-DKD---TGQVYAMKILRKSDmlKREQIAHVRAERDILADADSPWIVRLH--YAFQDEDHLYLV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  956 MEFLPSGSLKEYLPKnKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYY 1035
Cdd:cd05573     80 MEYMPGGDLMNLLIK-YDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCTKMNKSGDRE 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1013071061 1036 TVKDDRDSPVFW-------------------------Y-APECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd05573    159 SYLNDSVNTLFQdnvlarrrphkqrrvraysavgtpdYiAPEVLRGTGYGPECDWWSLGVILYEML 224
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
585-836 9.37e-13

Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of plant MAPK kinase kinases (MAPKKKs) including Arabidopsis thaliana MEKK1 and MAPKKK3. Arabidopsis thaliana MEKK1 activates MPK4, a MAPK that regulates systemic acquired resistance. MEKK1 also participates in the regulation of temperature-sensitive and tissue-specific cell death. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The plant MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270802 [Multi-domain]  Cd Length: 259  Bit Score: 69.74  E-value: 9.37e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  585 QGEHLGRGTRTHIYSGtlmdYKDDEGTSeeKKIKVILKVLDPSHRDISLAFFEA-ASMMRQVSHKHIVYLYGVcVRDVEN 663
Cdd:cd06632      4 KGQLLGSGSFGSVYEG----FNGDTGDF--FAVKEVSLVDDDKKSRESVKQLEQeIALLSKLRHPNIVQYYGT-EREEDN 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  664 IMVE-EFVEGGPLDLFMHRkSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGI 742
Cdd:cd06632     77 LYIFlEYVPGGSIHKLLQR-YGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGV-------VKLADFGM 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  743 ------PITVLSrqeCIERIPWIAPEcVEDSKNLS--VAADKWSFGTTLWEICyNGEIPLKDKTLIEKE-RFYESRCRPV 813
Cdd:cd06632    149 akhveaFSFAKS---FKGSPYWMAPE-VIMQKNSGygLAVDIWSLGCTVLEMA-TGKPPWSQYEGVAAIfKIGNSGELPP 223
                          250       260
                   ....*....|....*....|....*
gi 1013071061  814 TPS--CKELADLMTRCMNYDPNQRP 836
Cdd:cd06632    224 IPDhlSPDAKDFIRLCLQRDPEDRP 248
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
924-1076 9.48e-13

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also called ERK4) and 6 (also called ERK3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK4 (also called ERK4 or p63MAPK) and MAPK6 (also called ERK3 or p97MAPK) are atypical MAPKs that are not regulated by MAPK kinases. MAPK6 is expressed ubiquitously with highest amounts in brain and skeletal muscle. It may be involved in the control of cell differentiation by negatively regulating cell cycle progression in certain conditions. It may also play a role in glucose-induced insulin secretion. MAPK6 and MAPK4 cooperate to regulate the activity of MAPK-activated protein kinase 5 (MK5), leading to its relocation to the cytoplasm and exclusion from the nucleus. The MAPK6/MK5 and MAPK4/MK5 pathways may play critical roles in embryonic and post-natal development. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143359 [Multi-domain]  Cd Length: 342  Bit Score: 70.96  E-value: 9.48e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  924 KEIEILRNLYHENIVK-YK--GICTEDGGNGIKLIMEFLPSGSLKEYLPKNKNKINLKQQLK------YAVQICKGMDYL 994
Cdd:cd07854     51 REIKIIRRLDHDNIVKvYEvlGPSGSDLTEDVGSLTELNSVYIVQEYMETDLANVLEQGPLSeeharlFMYQLLRGLKYI 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  995 GSRQYVHRDLAARNVLVESEHQV-KIGDFGLTKAIETDKEYYTVKDDRDSPVFWYAPECLMQSKFYI-ASDVWSFGVTLH 1072
Cdd:cd07854    131 HSANVLHRDLKPANVFINTEDLVlKIGDFGLARIVDPHYSHKGYLSEGLVTKWYRSPRLLLSPNNYTkAIDMWAAGCIFA 210

                   ....
gi 1013071061 1073 ELLT 1076
Cdd:cd07854    211 EMLT 214
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
856-1075 1.05e-12

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-alpha is predominantly expressed in endothelial cells. It is critical for the regulation of angiogenesis and the maintenance of vascular integrity. It also plays a role in adipocyte differentiation. Mice deficient in PKB-alpha exhibit perinatal morbidity, growth retardation, reduction in body weight accompanied by reduced sizes of multiple organs, and enhanced apoptosis in some cell types. PKB-alpha activity has been reported to be frequently elevated in breast and prostate cancers. In some cancer cells, PKB-alpha may act as a suppressor of metastasis. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 70.83  E-value: 1.05e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  856 VSEKKPATEVDPTHFEkrFLKRirdLGEGHFGKVELCRYDPegdnTGEQVAVKSLKPES--GGNHIADLKKEIEILRNLY 933
Cdd:cd05594     13 VSLTKPKHKVTMNDFE--YLKL---LGKGTFGKVILVKEKA----TGRYYAMKILKKEVivAKDEVAHTLTENRVLQNSR 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  934 HENIVKYK-GICTEDGgngIKLIMEFLPSGSLKEYLPKNKNKINLKQQLkYAVQICKGMDYLGS-RQYVHRDLAARNVLV 1011
Cdd:cd05594     84 HPFLTALKySFQTHDR---LCFVMEYANGGELFFHLSRERVFSEDRARF-YGAEIVSALDYLHSeKNVVYRDLKLENLML 159
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1013071061 1012 ESEHQVKIGDFGLTKaiETDKEYYTVKDDRDSPVFwYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd05594    160 DKDGHIKITDFGLCK--EGIKDGATMKTFCGTPEY-LAPEVLEDNDYGRAVDWWGLGVVMYEMM 220
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
620-855 1.19e-12

Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. C-Raf, also known as Raf-1 or c-Raf-1, is ubiquitously expressed and was the first Raf identified. It was characterized as the acquired oncogene from an acutely transforming murine sarcoma virus (3611-MSV) and the transforming agent from the avian retrovirus MH2. C-Raf-deficient mice embryos die around midgestation with increased apoptosis of embryonic tissues, especially in the fetal liver. One of the main functions of C-Raf is restricting caspase activation to promote survival in response to specific stimuli such as Fas stimulation, macrophage apoptosis, and erythroid differentiation. C-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The C-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 69.67  E-value: 1.19e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  620 ILKVLDPSHRDISlAFFEAASMMRQVSHKHIVYLYGVCVRDVENImVEEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLA 699
Cdd:cd14149     41 ILKVVDPTPEQFQ-AFRNEVAVLRKTRHVNILLFMGYMTKDNLAI-VTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTA 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  700 SALSYLEDKDLVHGNVCTKNLLLaREGIDsecgpfIKLSDPGIPiTVLSR-------QECIERIPWIAPECV--EDSKNL 770
Cdd:cd14149    119 QGMDYLHAKNIIHRDMKSNNIFL-HEGLT------VKIGDFGLA-TVKSRwsgsqqvEQPTGSILWMAPEVIrmQDNNPF 190
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  771 SVAADKWSFGTTLWEIcYNGEIPL-----KDKTLIEKERFYES-RCRPVTPSC-KELADLMTRCMNYDPNQRPFFRAIMR 843
Cdd:cd14149    191 SFQSDVYSYGIVLYEL-MTGELPYshinnRDQIIFMVGRGYASpDLSKLYKNCpKAMKRLVADCIKKVKEERPLFPQILS 269
                          250
                   ....*....|..
gi 1013071061  844 DINKLEEQNPDI 855
Cdd:cd14149    270 SIELLQHSLPKI 281
PTK_Tyk2_rpt1 cd05076
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; Tyk2 is ...
899-1146 1.26e-12

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. The Tyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270661 [Multi-domain]  Cd Length: 273  Bit Score: 69.55  E-value: 1.26e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  899 DNTGEQVAVKSLKPESGGNHIAdLKKEIEILRNLYHENIVKYKGICTEDGGNgiKLIMEFLPSGSLKEYLPKNKNKINLK 978
Cdd:cd05076     40 RGQELRVVLKVLDPSHHDIALA-FFETASLMSQVSHTHLVFVHGVCVRGSEN--IMVEEFVEHGPLDVWLRKEKGHVPMA 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  979 QQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVES---EHQ----VKIGDFGLTKAIETdkeyytvKDDRDSPVFWYAPE 1051
Cdd:cd05076    117 WKFVVARQLASALSYLENKNLVHGNVCAKNILLARlglEEGtspfIKLSDPGVGLGVLS-------REERVERIPWIAPE 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1052 CLMQ-SKFYIASDVWSFGVTLHELltyCDSDSSPMAlflkmigpthgQMTVTRLVNTLKEGKRLPcPPNCPdEVYQLMRK 1130
Cdd:cd05076    190 CVPGgNSLSTAADKWGFGATLLEI---CFNGEAPLQ-----------SRTPSEKERFYQRQHRLP-EPSCP-ELATLISQ 253
                          250
                   ....*....|....*.
gi 1013071061 1131 CWEFQPSNRTSFQNLI 1146
Cdd:cd05076    254 CLTYEPTQRPSFRTIL 269
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
881-1075 1.33e-12

Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. There are four nPKC isoforms, delta, epsilon, eta, and theta. The nPKC-theta-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270744 [Multi-domain]  Cd Length: 320  Bit Score: 70.11  E-value: 1.33e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCrydpEGDNTGEQVAVKSLKPESG-----------GNHIADLKKEIEILRNLYhenivkykgiCTEDGG 949
Cdd:cd05592      3 LGKGSFGKVMLA----ELKGTNQYFAIKALKKDVVledddvectmiERRVLALASQHPFLTHLF----------CTFQTE 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  950 NGIKLIMEFLPSGSLKEYLpKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAie 1029
Cdd:cd05592     69 SHLFFVMEYLNGGDLMFHI-QQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMCKE-- 145
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1013071061 1030 tdkeyyTVKDDRDSPVF-----WYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd05592    146 ------NIYGENKASTFcgtpdYIAPEILKGQKYNQSVDWWSFGVLLYEML 190
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
635-838 1.46e-12

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. Vertebrate have two members, LIMK1 and LIMK2. The LIMK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 69.46  E-value: 1.46e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  635 FFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGN 714
Cdd:cd14154     37 FLKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGGTLKDVLKDMARPLPWAQRVRFAKDIASGMAYLHSMNIIHRD 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  715 VCTKNLL-------------LAREgIDSECGPFIKLSDPGIPITVLSRQE-----CIERIPWIAPECVeDSKNLSVAADK 776
Cdd:cd14154    117 LNSHNCLvredktvvvadfgLARL-IVEERLPSGNMSPSETLRHLKSPDRkkrytVVGNPYWMAPEML-NGRSYDEKVDI 194
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1013071061  777 WSFGTTLWEICYNGE-----IPLKDKTLIEKERFYESRCRPVTPSCKELAdlmTRCMNYDPNQRPFF 838
Cdd:cd14154    195 FSFGIVLCEIIGRVEadpdyLPRTKDFGLNVDSFREKFCAGCPPPFFKLA---FLCCDLDPEKRPPF 258
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
872-1075 1.50e-12

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine/threonine kinases (STKs), p21-activated kinase (PAK) 3, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. PAK3 belongs to group I. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAK3 is highly expressed in the brain. It is implicated in neuronal plasticity, synapse formation, dendritic spine morphogenesis, cell cycle progression, neuronal migration, and apoptosis. Inactivating mutations in the PAK3 gene cause X-linked non-syndromic mental retardation, the severity of which depends on the site of the mutation.


Pssm-ID: 132987 [Multi-domain]  Cd Length: 297  Bit Score: 69.75  E-value: 1.50e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  872 KRFLKRIRDLGEGHFGKVelcrYDPEGDNTGEQVAVKSLKPESGGNHiADLKKEIEILRNLYHENIVKYkgICTEDGGNG 951
Cdd:cd06656     18 KKKYTRFEKIGQGASGTV----YTAIDIATGQEVAIKQMNLQQQPKK-ELIINEILVMRENKNPNIVNY--LDSYLVGDE 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  952 IKLIMEFLPSGSLKEYLpkNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETD 1031
Cdd:cd06656     91 LWVVMEYLAGGSLTDVV--TETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPE 168
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1013071061 1032 KeyyTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd06656    169 Q---SKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMV 209
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
577-853 1.50e-12

Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER3 contains an impaired tyr kinase domain, which lacks crucial residues for catalytic activity against exogenous substrates but is still able to bind ATP and autophosphorylate. HER3 binds the neuregulin ligands, NRG1 and NRG2, and it relies on its heterodimerization partners for activity following ligand binding. The HER2-HER3 heterodimer constitutes a high affinity co-receptor capable of potent mitogenic signaling. HER3 participates in a signaling pathway involved in the proliferation, survival, adhesion, and motility of tumor cells. The HER3 subfamily is part of a larger superfamily that includes other pseudokinases and the the catalytic domains of active kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173656 [Multi-domain]  Cd Length: 279  Bit Score: 69.60  E-value: 1.50e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  577 RILKK-DLVQGEHLGRGTRTHIYSGTLMDykddEGTSeeKKIKVILKVL-DPSHRDISLAFFEAASMMRQVSHKHIVYLY 654
Cdd:cd05111      2 RIFKEtELRKLKVLGSGVFGTVHKGIWIP----EGDS--IKIPVAIKVIqDRSGRQSFQAVTDHMLAIGSLDHAYIVRLL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  655 GVCVRDVENIMVEEFVEGGPLDLFMHRKsDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpf 734
Cdd:cd05111     76 GICPGASLQLVTQLLPLGSLLDHVRQHR-GSLGPQLLLNWCVQIAKGMYYLEEHRMVHRNLAARNVLLKSPSQ------- 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  735 IKLSDPGIPITV------LSRQECIERIPWIAPECVEDSKnLSVAADKWSFGTTLWEICYNGEIPLKDKTLIEKERFYES 808
Cdd:cd05111    148 VQVADFGVADLLypddkkYFYSEAKTPIKWMALESIHFGK-YTHQSDVWSYGVTVWEMMTFGAEPYAGMRLAEVPDLLEK 226
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1013071061  809 RCRPVTPS-CK-ELADLMTRCMNYDPNQRPFFRAIMRDINKLEEQNP 853
Cdd:cd05111    227 GERLAQPQiCTiDVYMVMVKCWMIDENIRPTFKELANEFTRMARDPP 273
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
881-1023 1.66e-12

Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 65.93  E-value: 1.66e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCrydpEGDNTGEQVAVKSLKPESGGNHIaDLKKEIEILR-NLYHE-NIVKYKGICTEDGGNgiKLIMEF 958
Cdd:cd13968      1 MGEGASAKVFWA----EGECTTIGVAVKIGDDVNNEEGE-DLESEMDILRrLKGLElNIPKVLVTEDVDGPN--ILLMEL 73
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1013071061  959 LPSGSLKEYLPKNKNKinlKQQLKYAVQIC-KGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFG 1023
Cdd:cd13968     74 VKGGTLIAYTQEEELD---EKDVESIMYQLaECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
879-1147 1.66e-12

Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). This subfamily includes Aurora-B and Aurora-C. Aurora-B is most active at the transition during metaphase to the end of mitosis. It associates with centromeres, relocates to the midzone of the central spindle, and concentrates at the midbody during cell division. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. INCENP participates in the activation of Aurora-B in a two-step process: first by binding to form an intermediate state of activation and the phosphorylation of its C-terminal TSS motif to generate the fully active kinase. The Aurora-B subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271019 [Multi-domain]  Cd Length: 270  Bit Score: 69.12  E-value: 1.66e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKPESGGNHiaDLKKEIEILRNLYHENIVKYKGICTEDggNGIKLIMEF 958
Cdd:cd14117     12 RPLGKGKFGNVYLAREKQSKFIVALKVLFKSQIEKEGVEH--QLRREIEIQSHLRHPNILRLYNYFHDR--KRIYLILEY 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  959 LPSGSLKEYLPKNKnKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEyYTVK 1038
Cdd:cd14117     88 APRGELYKELQKHG-RFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWSVHAPSLRR-RTMC 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1039 DDRDspvfwYAPECLMQSKFYIAS-DVWSFGVTLHELLTycdsDSSPMAlflkmiGPTHGQmTVTRLVNTlkegkRLPCP 1117
Cdd:cd14117    166 GTLD-----YLPPEMIEGRTHDEKvDLWCIGVLCYELLV----GMPPFE------SASHTE-TYRRIVKV-----DLKFP 224
                          250       260       270
                   ....*....|....*....|....*....|
gi 1013071061 1118 PNCPDEVYQLMRKCWEFQPSNRTSFQNLIE 1147
Cdd:cd14117    225 PFLSDGSRDLISKLLRYHPSERLPLKGVME 254
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
881-1075 1.70e-12

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called Doublecortin-like and CAM kinase-like 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL2 (or DCAMKL2) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL2 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL2 has been shown to interact with tubulin, JIP1/2, JNK, neurabin 2, and actin. It is associated with the terminal segments of axons and dendrites, and may function as a phosphorylation-dependent switch to control microtubule dynamics in neuronal growth cones. The DCKL2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 68.91  E-value: 1.70e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRydpeGDNTGEQVAVKSLKPES--GGNHIadLKKEIEILRNLYHENIVKYkgICTEDGGNGIKLIMEF 958
Cdd:cd14184      9 IGDGNFAVVKECV----ERSTGKEFALKIIDKAKccGKEHL--IENEVSILRRVKHPNIIML--IEEMDTPAELYLVMEL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  959 LPSGSLKEYLpKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLV----ESEHQVKIGDFGLTKAIEtdKEY 1034
Cdd:cd14184     81 VKGGDLFDAI-TSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVceypDGTKSLKLGDFGLATVVE--GPL 157
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1013071061 1035 YTVKDdrdSPVFwYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd14184    158 YTVCG---TPTY-VAPEIIAETGYGLKVDIWAAGVITYILL 194
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
878-1026 1.93e-12

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. Some isoforms have several splice variants such as the long (L) and short (S) variants of CK1alpha. CK1 proteins are involved in the regulation of many cellular processes including membrane transport processes, circadian rhythm, cell division, apoptosis, and the development of cancer and neurodegenerative diseases. The CK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 68.64  E-value: 1.93e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVELCRyDPEgdnTGEQVAVKSLKPESGGNHiadLKKEIEILRNL-YHENI--VKYKGictEDGGNGIkL 954
Cdd:cd14016      5 VKKIGSGSFGEVYLGI-DLK---TGEEVAIKIEKKDSKHPQ---LEYEAKVYKLLqGGPGIprLYWFG---QEGDYNV-M 73
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1013071061  955 IMEFLpsG-SLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLV---ESEHQVKIGDFGLTK 1026
Cdd:cd14016     74 VMDLL--GpSLEDLFNKCGRKFSLKTVLMLADQMISRLEYLHSKGYIHRDIKPENFLMglgKNSNKVYLIDFGLAK 147
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
901-1075 1.99e-12

Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases Sty1 and Hog1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs Sty1 from Schizosaccharomyces pombe, Hog1 from Saccharomyces cerevisiae, and similar proteins. Sty1 and Hog1 are stress-activated MAPKs that partipate in transcriptional regulation in response to stress. Sty1 is activated in response to oxidative stress, osmotic stress, and UV radiation. It is regulated by the MAP2K Wis1, which is activated by the MAP3Ks Wis4 and Win1, which receive signals of the stress condition from membrane-spanning histidine kinases Mak1-3. Activated Sty1 stabilizes the Atf1 transcription factor and induces transcription of Atf1-dependent genes of the core environmetal stress response. Hog1 is the key element in the high osmolarity glycerol (HOG) pathway and is activated upon hyperosmotic stress. Activated Hog1 accumulates in the nucleus and regulates stress-induced transcription. The HOG pathway is mediated by two transmembrane osmosensors, Sln1 and Sho1. MAPKs are important mediators of cellular responses to extracellular signals. The Sty1/Hog1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270843 [Multi-domain]  Cd Length: 328  Bit Score: 69.91  E-value: 1.99e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  901 TGEQVAVKSL-KPESGGNHIADLKKEIEILRNLYHENIVKYKGIC---TEDggngIKLIMEFLPSgSLKEYLPKNKNKIN 976
Cdd:cd07856     34 TGQNVAVKKImKPFSTPVLAKRTYRELKLLKHLRHENIISLSDIFispLED----IYFVTELLGT-DLHRLLTSRPLEKQ 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  977 LKQQLKYavQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYTvkddrdSPVFWYAPECLMQ- 1055
Cdd:cd07856    109 FIQYFLY--QILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLARIQDPQMTGYV------STRYYRAPEIMLTw 180
                          170       180
                   ....*....|....*....|
gi 1013071061 1056 SKFYIASDVWSFGVTLHELL 1075
Cdd:cd07856    181 QKYDVEVDIWSAGCIFAEML 200
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
589-845 2.04e-12

Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Met and Ron are receptor PTKs (RTKs) composed of an alpha-beta heterodimer. The extracellular alpha chain is disulfide linked to the beta chain, which contains an extracellular ligand-binding region with a sema domain, a PSI domain and four IPT repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. Met binds to the ligand, hepatocyte growth factor/scatter factor (HGF/SF), and is also called the HGF receptor. HGF/Met signaling plays a role in growth, transformation, cell motility, invasion, metastasis, angiogenesis, wound healing, and tissue regeneration. Aberrant expression of Met through mutations or gene amplification is associated with many human cancers including hereditary papillary renal and gastric carcinomas. The ligand for Ron is macrophage stimulating protein (MSP). Ron signaling is important in regulating cell motility, adhesion, proliferation, and apoptosis. Aberrant Ron expression is implicated in tumorigenesis and metastasis. The Met/Ron subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270649 [Multi-domain]  Cd Length: 262  Bit Score: 68.65  E-value: 2.04e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  589 LGRGTRTHIYSGTLMDykddegtSEEKKIKVILKVLD--PSHRDISlAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMV 666
Cdd:cd05058      3 IGKGHFGCVYHGTLID-------SDGQKIHCAVKSLNriTDIEEVE-QFLKEGIIMKDFSHPNVLSLLGICLPSEGSPLV 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  667 E-EFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGIPIT 745
Cdd:cd05058     75 VlPYMKHGDLRNFIRSETHNPTVKDLIGFGLQVAKGMEYLASKKFVHRDLAARNCMLDESFT-------VKVADFGLARD 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  746 VLSR------QECIERIP--WIAPECVEDSKnLSVAADKWSFGTTLWEICYNGEIPLKDKTLIEKERFYESRCRPVTPS- 816
Cdd:cd05058    148 IYDKeyysvhNHTGAKLPvkWMALESLQTQK-FTTKSDVWSFGVLLWELMTRGAPPYPDVDSFDITVYLLQGRRLLQPEy 226
                          250       260       270
                   ....*....|....*....|....*....|
gi 1013071061  817 CKE-LADLMTRCMNYDPNQRPFFRAIMRDI 845
Cdd:cd05058    227 CPDpLYEVMLSCWHPKPEMRPTFSELVSRI 256
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
871-1147 2.05e-12

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 3 or PKR-like Endoplasmic Reticulum Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PERK (or EIF2AK3) is a type-I ER transmembrane protein containing a luminal domain bound with the chaperone BiP under unstressed conditions and a cytoplasmic catalytic kinase domain. In response to the accumulation of misfolded or unfolded proteins in the ER, PERK is activated through the release of BiP, allowing it to dimerize and autophosphorylate. It functions as the central regulator of translational control during the Unfolded Protein Response (UPR) pathway. In addition to the eIF-2 alpha subunit, PERK also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PERK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270950 [Multi-domain]  Cd Length: 281  Bit Score: 69.13  E-value: 2.05e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  871 EKRFL---KRIRDLGEGHFG-------KVELCRYdpegdntgeqvAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKY 940
Cdd:cd14048      1 TSRFLtdfEPIQCLGRGGFGvvfeaknKVDDCNY-----------AVKRIRLPNNELAREKVLREVRALAKLDHPGIVRY 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  941 KGICTEDGGNG---------IKLIMEFLPSGSLKEYLPKNKN--KINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNV 1009
Cdd:cd14048     70 FNAWLERPPEGwqekmdevyLYIQMQLCRKENLKDWMNRRCTmeSRELFVCLNIFKQIASAVEYLHSKGLIHRDLKPSNV 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1010 LVESEHQVKIGDFGLTKAIETDKEYYTVKDDRDSPV---------FWYAPECLMQSKFYIASDVWSFGVTLHELLtycds 1080
Cdd:cd14048    150 FFSLDDVVKVGDFGLVTAMDQGEPEQTVLTPMPAYAkhtgqvgtrLYMSPEQIHGNQYSEKVDIFALGLILFELI----- 224
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1013071061 1081 dsspmalflkmigptHGQMTVTRLVNTLKEGKRLPCPP----NCPDEvYQLMRKCWEFQPSNRTSFQNLIE 1147
Cdd:cd14048    225 ---------------YSFSTQMERIRTLTDVRKLKFPAlftnKYPEE-RDMVQQMLSPSPSERPEAHEVIE 279
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
881-1078 2.15e-12

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). Each subunit has tissue-specific isoforms or splice variants. Vertebrates contain two isoforms of the gamma subunit (gamma 1 and gamma 2). The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270995 [Multi-domain]  Cd Length: 272  Bit Score: 68.92  E-value: 2.15e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDpegdNTGEQVAVK-------SLKPESGGNHIADLKKEIEILRNLY-HENIVKYKGICTEDggNGI 952
Cdd:cd14093     11 LGRGVSSTVRRCIEK----ETGQEFAVKiiditgeKSSENEAEELREATRREIEILRQVSgHPNIIELHDVFESP--TFI 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  953 KLIMEFLPSGSLKEYLPKnKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDK 1032
Cdd:cd14093     85 FLVFELCRKGELFDYLTE-VVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFATRLDEGE 163
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1013071061 1033 EyytVKDDRDSPVFwYAPECLMQSKFYIAS------DVWSFGVTLHELLTYC 1078
Cdd:cd14093    164 K---LRELCGTPGY-LAPEVLKCSMYDNAPgygkevDMWACGVIMYTLLAGC 211
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
881-1072 2.20e-12

Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They contain N-terminal cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. The PKD subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 68.59  E-value: 2.20e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVelcrYDPEGDNTGEQVAVKSL-KPESGGNHIADLKKEIEILRNLYHENIVKYKGIC-TEDGgngIKLIMEF 958
Cdd:cd14082     11 LGSGQFGIV----YGGKHRKTGRDVAIKVIdKLRFPTKQESQLRNEVAILQQLSHPGVVNLECMFeTPER---VFVVMEK 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  959 LPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEH---QVKIGDFGLTKAIETdkeyy 1035
Cdd:cd14082     84 LHGDMLEMILSSEKGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEpfpQVKLCDFGFARIIGE----- 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1013071061 1036 tvKDDRDSPV---FWYAPECLMQSKFYIASDVWSFGVTLH 1072
Cdd:cd14082    159 --KSFRRSVVgtpAYLAPEVLRNKGYNRSLDMWSVGVIIY 196
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
878-1076 2.29e-12

Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily contains uncharacterized STKs with similarity to the human protein designated as Yank1 or STK32A. The Yank1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270730 [Multi-domain]  Cd Length: 257  Bit Score: 68.44  E-value: 2.29e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVELCRYDpegdNTGEQVAVKSLKPES--GGNHIADLKKEIEILRNLYHENIVK-YKGICTEDGgngIKL 954
Cdd:cd05578      5 LRVIGKGSFGKVCIVQKK----DTKKMFAMKYMNKQKciEKDSVRNVLNELEILQELEHPFLVNlWYSFQDEED---MYM 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPSGSLKEYLPKNKnKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGltkaIETDKEY 1034
Cdd:cd05578     78 VVDLLLGGDLRYHLQQKV-KFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFN----IATKLTD 152
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1013071061 1035 YTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd05578    153 GTLATSTSGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLR 194
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
876-1075 2.48e-12

Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ERK5 (also called Big MAPK1 (BMK1) or MAPK7) has a unique C-terminal extension, making it approximately twice as big as other MAPKs. This extension contains transcriptional activation capability which is inhibited by the N-terminal half. ERK5 is activated in response to growth factors and stress by a cascade that leads to its phosphorylation by the MAP2K MEK5, which in turn is regulated by the MAP3Ks MEKK2 and MEKK3. Activated ERK5 phosphorylates its targets including myocyte enhancer factor 2 (MEF2), Sap1a, c-Myc, and RSK. It plays a role in EGF-induced cell proliferation during the G1/S phase transition. Studies on knockout mice revealed that ERK5 is essential for cardiovascular development and plays an important role in angiogenesis. It is also critical for neural differentiation and survival. The ERK5 pathway has been implicated in the pathogenesis of many diseases including cancer, cardiac hypertrophy, and atherosclerosis. MAPKs are important mediators of cellular responses to extracellular signals. The ERK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270842 [Multi-domain]  Cd Length: 336  Bit Score: 69.70  E-value: 2.48e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  876 KRIRDLGEGHFGKVelCryDPEGDNTGEQVAVKSLkpesgGNHIADLK------KEIEILRNLYHENIVKYKGI-----C 944
Cdd:cd07855      8 EPIETIGSGAYGVV--C--SAIDTKSGQKVAIKKI-----PNAFDVVTtakrtlRELKILRHFKHDNIIAIRDIlrpkvP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  945 TEDGGNgIKLIMEFLPSgslkeylpkNKNKINLKQQ------LKYAV-QICKGMDYLGSRQYVHRDLAARNVLVESEHQV 1017
Cdd:cd07855     79 YADFKD-VYVVLDLMES---------DLHHIIHSDQpltlehIRYFLyQLLRGLKYIHSANVIHRDLKPSNLLVNENCEL 148
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1018 KIGDFGLTKAIETDKEYYTVKDDRDSPVFWY-APECLMQSKFY-IASDVWSFGVTLHELL 1075
Cdd:cd07855    149 KIGDFGMARGLCTSPEEHKYFMTEYVATRWYrAPELMLSLPEYtQAIDMWSVGCIFAEML 208
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
878-1092 2.67e-12

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 69.62  E-value: 2.67e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVELCRYDPEgdnTGEQVAVKSLKPES--GGNHIADLKKEIEILRNLYHENIVKYKGICTEDggNGIKLI 955
Cdd:PTZ00426    35 IRTLGTGSFGRVILATYKNE---DFPPVAIKRFEKSKiiKQKQVDHVFSERKILNYINHPFCVNLYGSFKDE--SYLYLV 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  956 MEFLPSGSLKEYLPKNKNKINlKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETdkEYY 1035
Cdd:PTZ00426   110 LEFVIGGEFFTFLRRNKRFPN-DVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGFAKVVDT--RTY 186
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1013071061 1036 TVKDDRDspvfWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDS--DSSPMALFLKMI 1092
Cdd:PTZ00426   187 TLCGTPE----YIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPfyANEPLLIYQKIL 241
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
879-1075 2.67e-12

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK3, also called Prk or Fnk (FGF-inducible kinase), regulates angiogenesis and responses to DNA damage. Activated PLK3 mediates Chk2 phosphorylation by ATM and the resulting checkpoint activation. PLK3 phosphorylates DNA polymerase delta and may be involved in DNA repair. It also inhibits Cdc25c, thereby regulating the onset of mitosis. The PLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271091 [Multi-domain]  Cd Length: 255  Bit Score: 68.42  E-value: 2.67e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGHFGKVelcrYDPEGDNTGEQVAVKSLkPESGGNHIADLKK---EIEILRNLYHENIVKYKGIcTEDGGNgIKLI 955
Cdd:cd14189      7 RLLGKGGFARC----YEMTDLATNKTYAVKVI-PHSRVAKPHQREKivnEIELHRDLHHKHVVKFSHH-FEDAEN-IYIF 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  956 MEFLPSGSLKeYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIET-DKEY 1034
Cdd:cd14189     80 LELCSRKSLA-HIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAARLEPpEQRK 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1013071061 1035 YTVKDDRDspvfWYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd14189    159 KTICGTPN----YLAPEVLLRQGHGPESDVWSLGCVMYTLL 195
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
881-1090 3.00e-12

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271071 [Multi-domain]  Cd Length: 277  Bit Score: 68.38  E-value: 3.00e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDpegdNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGIctEDGGNGIKLIMEFLP 960
Cdd:cd14169     11 LGEGAFSEVVLAQER----GSQRLVALKCIPKKALRGKEAMVENEIAVLRRINHENIVSLEDI--YESPTHLYLAMELVT 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  961 SGSLKEYLPKnKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVES---EHQVKIGDFGLTKaIETDKEYYTV 1037
Cdd:cd14169     85 GGELFDRIIE-RGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYATpfeDSKIMISDFGLSK-IEAQGMLSTA 162
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1013071061 1038 KddrDSPVFwYAPECLMQSKFYIASDVWSFGVTLHELLT-----YCDSDSSPMALFLK 1090
Cdd:cd14169    163 C---GTPGY-VAPELLEQKPYGKAVDVWAIGVISYILLCgyppfYDENDSELFNQILK 216
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
879-1075 3.23e-12

Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK33 is highly expressed in the testis and is present in low levels in most tissues. It may be involved in spermatogenesis and organ ontogenesis. It interacts with and phosphorylates vimentin and may be involved in regulating intermediate filament cytoskeletal dynamics. Its role in promoting the cell viability of KRAS-dependent cancer cells is under debate; some studies have found STK33 to promote cancer cell viability, while other studies have found it to be non-essential. KRAS is the most commonly mutated human oncogene, thus, studies on the role of STK33 in KRAS mutant cancer cells are important. The STK33 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 68.34  E-value: 3.23e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGHFGKVelcrYDPEGDNTGEQVAVKSL-KPESGGNHIADLKKEIEILRNLYHENIVKYKGICteDGGNGIKLIME 957
Cdd:cd14097      7 RKLGQGSFGVV----IEATHKETQTKWAIKKInREKAGSSAVKLLEREVDILKHVNHAHIIHLEEVF--ETPKRMYLVME 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  958 FLPSGSLKEYLpkNKNKINLKQQLKYAVQ-ICKGMDYLGSRQYVHRDLAARNVLVES-------EHQVKIGDFGLtkAIE 1029
Cdd:cd14097     81 LCEDGELKELL--LRKGFFSENETRHIIQsLASAVAYLHKNDIVHRDLKLENILVKSsiidnndKLNIKVTDFGL--SVQ 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1013071061 1030 TdkeyYTVKDDR-----DSPVFwYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd14097    157 K----YGLGEDMlqetcGTPIY-MAPEVISAHGYSQQCDIWSIGVIMYMLL 202
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
646-787 3.23e-12

Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SBK1, also called BSK146, is predominantly expressed in the brain. Its expression is increased in the developing brain during the late embryonic stage, coinciding with dramatic neuronal proliferation, migration, and maturation. SBK1 may play an important role in regulating brain development. The SBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270889 [Multi-domain]  Cd Length: 259  Bit Score: 68.12  E-value: 3.23e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  646 SHKHIVYLYGVCVRDVEN-IMVEEFVEGGplDLFMHRKSDV-LTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLa 723
Cdd:cd13987     48 VHPHIIKTYDVAFETEDYyVFAQEYAPYG--DLFSIIPPQVgLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLL- 124
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1013071061  724 regIDSECgPFIKLSDPGIPITVLSRQECIER-IPWIAPECVEDSKNLSVAADK----WSFGTTL---------WEIC 787
Cdd:cd13987    125 ---FDKDC-RRVKLCDFGLTRRVGSTVKRVSGtIPYTAPEVCEAKKNEGFVVDPsidvWAFGVLLfccltgnfpWEKA 198
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
880-1075 3.31e-12

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called Ribosomal protein S6 kinase alpha-6 or 90kDa ribosomal protein S6 kinase 6); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK4 is also called S6K-alpha-6, RPS6KA6, p90RSK6 or pp90RSK4. RSK4 is a substrate of ERK and is a modulator of p53-dependent proliferation arrest in human cells. Deletion of the RSK4 gene, RPS6KA6, frequently occurs in patients of X-linked deafness type 3, mental retardation and choroideremia. Studies of RSK4 in cancer cells and tissues suggest that it may be oncogenic or tumor suppressive depending on many factors. RSK4 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 68.50  E-value: 3.31e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  880 DLGEGHFGKVELCRYDpegdNTGEQVAVKSLKPESggnhiADLKKEIEIL-RNLYHENIVKYKGIctEDGGNGIKLIMEF 958
Cdd:cd14177     11 DIGVGSYSVCKRCIHR----ATNMEFAVKIIDKSK-----RDPSEEIEILmRYGQHPNIITLKDV--YDDGRYVYLVTEL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  959 LPSGSLKEYLPKNKNkINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEH----QVKIGDFGLTKAIETDKEY 1034
Cdd:cd14177     80 MKGGELLDRILRQKF-FSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDDSanadSIRICDFGFAKQLRGENGL 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1013071061 1035 YTvkddrdSPVF---WYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd14177    159 LL------TPCYtanFVAPEVLMRQGYDAACDIWSLGVLLYTML 196
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
881-1076 3.39e-12

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, classical PKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. Novel PKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. Also included in this subfamily are the PKC-like proteins, called PKNs. The PKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 68.78  E-value: 3.39e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCrydpEGDNTGEQVAVKSLKPESggnhiadlkkeieILRNLYHENIVKYKGI--------------CTE 946
Cdd:cd05570      3 LGKGSFGKVMLA----ERKKTDELYAIKVLKKEV-------------IIEDDDVECTMTEKRVlalanrhpfltglhACF 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  947 DGGNGIKLIMEFLPSGSLKEYLPKNKnKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTK 1026
Cdd:cd05570     66 QTEDRLYFVMEYVNGGDLMFHIQRAR-RFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMCK 144
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1013071061 1027 AietdkeyyTVKDDRDSPVF-----WYAPECLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd05570    145 E--------GIWGGNTTSTFcgtpdYIAPEILREQDYGFSVDWWALGVLLYEMLA 191
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
878-1151 3.43e-12

Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Drosophila melanogaster NAK, human BMP-2-inducible protein kinase (BMP2K or BIKe) and similar vertebrate proteins, as well as the Saccharomyces cerevisiae proteins Prk1, Actin-regulating kinase 1 (Ark1), and Akl1. NAK was the first characterized member of this subfamily. It plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. BMP2K contains a nuclear localization signal and a kinase domain that is capable of phosphorylating itself and myelin basic protein. The expression of the BMP2K gene is increase during BMP-2-induced osteoblast differentiation. It may function to control the rate of differentiation. Prk1, Ark1, and Akl1 comprise a subfamily of yeast proteins that are important regulators of the actin cytoskeleton and endocytosis. They share an N-terminal kinase domain but no significant homology in other regions of their sequences. The NAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 68.46  E-value: 3.43e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVELCRydpeGDNTGEQVAVK--SLKPESGGNhiaDLKKEIEILRNLY-HENIVKY---KGICTEDGGNG 951
Cdd:cd14037      8 EKYLAEGGFAHVYLVK----TSNGGNRAALKrvYVNDEHDLN---VCKREIEIMKRLSgHKNIVGYidsSANRSGNGVYE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  952 IKLIMEFLPSGSLKEYLPKN-KNKINLKQQLKYAVQICKGMDYLGSRQ--YVHRDLAARNVLVESEHQVKIGDFGLTKAI 1028
Cdd:cd14037     81 VLLLMEYCKGGGVIDLMNQRlQTGLTESEILKIFCDVCEAVAAMHYLKppLIHRDLKVENVLISDSGNYKLCDFGSATTK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1029 ----ETDKEYYTVKDD--RDSPVFWYAPEC--LMQSK-FYIASDVWSFGVTLHELLTYCD--SDSSPMALflkmigpTHG 1097
Cdd:cd14037    161 ilppQTKQGVTYVEEDikKYTTLQYRAPEMidLYRGKpITEKSDIWALGCLLYKLCFYTTpfEESGQLAI-------LNG 233
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1013071061 1098 QMTVtrlvntlkegkrlpcPPNCP--DEVYQLMRKCWEFQPSNRTS-FQNLIEGFEA 1151
Cdd:cd14037    234 NFTF---------------PDNSRysKRLHKLIRYMLEEDPEKRPNiYQVSYEAFEL 275
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
880-1075 3.56e-12

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type II; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. In addition, CaMKII contains a C-terminal association domain that facilitates oligomerization. There are four CaMKII proteins (alpha, beta, gamma, delta) encoded by different genes; each gene undergoes alternative splicing to produce more than 30 isoforms. CaMKII-alpha and -beta are enriched in neurons while CaMKII-gamma and -delta are predominant in myocardium. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. It is a major component of the postsynaptic density and is critical in regulating synaptic plasticity including long-term potentiation. It is critical in regulating ion channels and proteins involved in myocardial excitation-contraction and excitation-transcription coupling. Excessive CaMKII activity promotes processes that contribute to heart failure and arrhythmias. The CaMKII subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 68.60  E-value: 3.56e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  880 DLGEGHFGKVELCRYDPegdnTGEQVAVK--SLKPESGGNHiADLKKEIEILRNLYHENIVKYKGICTEDGGNgiKLIME 957
Cdd:cd14086      8 ELGKGAFSVVRRCVQKS----TGQEFAAKiiNTKKLSARDH-QKLEREARICRLLKHPNIVRLHDSISEEGFH--YLVFD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  958 FLPSGSL------KEYLPKnKNKINLKQQLKYAVQICKgmdylgSRQYVHRDLAARNVLVESEHQ---VKIGDFGLtkAI 1028
Cdd:cd14086     81 LVTGGELfedivaREFYSE-ADASHCIQQILESVNHCH------QNGIVHRDLKPENLLLASKSKgaaVKLADFGL--AI 151
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1013071061 1029 ETDKEYYTVKDDRDSPVFwYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd14086    152 EVQGDQQAWFGFAGTPGY-LSPEVLRKDPYGKPVDIWACGVILYILL 197
PK_GC-C cd14044
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain ...
888-1145 3.82e-12

Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-C binds and is activated by the intestinal hormones, guanylin (GN) and uroguanylin (UGN), which are secreted after salty meals to inhibit sodium absorption and induce the secretion of chloride, bicarbonate, and water. GN and UGN are also present in the kidney, where they induce increased salt and water secretion. This prevents the development of hypernatremia and hypervolemia after ingestion of high amounts of salt. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-C subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270946 [Multi-domain]  Cd Length: 271  Bit Score: 67.99  E-value: 3.82e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  888 KVELCRYDPEgdntgeQVAVKSLKpESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDggNGIKLIMEFLPSGSLKEY 967
Cdd:cd14044     23 RLRQGKYDKK------VVILKDLK-NNEGNFTEKQKIELNKLLQIDYYNLTKFYGTVKLD--TMIFGVIEYCERGSLRDV 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  968 LPKN---KNKINLKQQLKYAV--QICKGMDYL-GSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEyytvkddr 1041
Cdd:cd14044     94 LNDKisyPDGTFMDWEFKISVmyDIAKGMSYLhSSKTEVHGRLKSTNCVVDSRMVVKITDFGCNSILPPSKD-------- 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1042 dspvFWYAPECLMQSKFYIASDVWSFGVTLHELL----TYCDSDSSPMALFLKMIGPTHGQMTVTRLVNTLKEGKRlpcp 1117
Cdd:cd14044    166 ----LWTAPEHLRQAGTSQKGDVYSYGIIAQEIIlrkeTFYTAACSDRKEKIYRVQNPKGMKPFRPDLNLESAGER---- 237
                          250       260
                   ....*....|....*....|....*...
gi 1013071061 1118 pncPDEVYQLMRKCWEFQPSNRTSFQNL 1145
Cdd:cd14044    238 ---EREVYGLVKNCWEEDPEKRPDFKKI 262
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
881-1076 3.99e-12

Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TDY subtype and is composed of Group D plant MAPKs including Arabidopsis thaliana MPK18 (AtMPK18), Oryza sativa Blast- and Wound-induced MAPK1 (OsBWMK1), OsWJUMK1 (Wound- and JA-Uninducible MAPK1), Zea mays MPK6, and the Medicago sativa TDY1 gene product. OsBWMK1 enhances resistance to pathogenic infections. It mediates stress-activated defense responses by activating a transcription factor that affects the expression of stress-related genes. AtMPK18 is involved in microtubule-related functions. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20 while Oryza sativa contains at least 17 MAPKs. Arabidopsis thaliana contains more TEY-type MAPKs than TDY-type, whereas the reverse is true for Oryza sativa. The TDY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 69.04  E-value: 3.99e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVelCR-YDPEgdnTGEQVAVKslKPESGGNHIAD---LKKEIEILRNLYHENIVKYKGICTEDGGNGIK--- 953
Cdd:cd07859      8 IGKGSYGVV--CSaIDTH---TGEKVAIK--KINDVFEHVSDatrILREIKLLRLLRHPDIVEIKHIMLPPSRREFKdiy 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  954 LIMEFLPSgSLKEYLPKNKNKINLKQQLkYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKE 1033
Cdd:cd07859     81 VVFELMES-DLHQVIKANDDLTPEHHQF-FLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGLARVAFNDTP 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1013071061 1034 YYTVKDDRDSPVFWYAPE-C-LMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd07859    159 TAIFWTDYVATRWYRAPElCgSFFSKYTPAIDIWSIGCIFAEVLT 203
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
642-844 4.01e-12

Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AMPK-like subfamily is composed of AMPK, MARK, BRSK, NUAK, MELK, SNRK, TSSK, and SIK, among others. LKB1 serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. BRSKs play important roles in establishing neuronal polarity. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. The AMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270905 [Multi-domain]  Cd Length: 252  Bit Score: 67.54  E-value: 4.01e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  642 MRQVSHKHIVYLYGVcVRDVENI-MVEEFVEGGplDLF----MHRKSDVLTTPWKFkvaKQLASALSYLEDKDLVHGNVC 716
Cdd:cd14003     53 MKLLNHPNIIKLYEV-IETENKIyLVMEYASGG--ELFdyivNNGRLSEDEARRFF---QQLISAVDYCHSNGIVHRDLK 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  717 TKNLLLaregiDSECGpfIKLSDPGIPITVLSRQECIER---IPWIAPECVEDSKNLSVAADKWSFGTTLWeICYNGEIP 793
Cdd:cd14003    127 LENILL-----DKNGN--LKIIDFGLSNEFRGGSLLKTFcgtPAYAAPEVLLGRKYDGPKADVWSLGVILY-AMLTGYLP 198
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1013071061  794 LKD------KTLIEKERFYESrcRPVTPSCKelaDLMTRCMNYDPNQRPFFRAIMRD 844
Cdd:cd14003    199 FDDdndsklFRKILKGKYPIP--SHLSPDAR---DLIRRMLVVDPSKRITIEEILNH 250
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
881-1076 4.59e-12

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase; Protein Kinases (PKs), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK) subfamily, catalytic (c) domain. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. The DYRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein S/T PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. Vertebrates contain multiple DYRKs (DYRK1-4) and mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A is involved in neuronal differentiation and is implicated in the pathogenesis of DS (Down syndrome). DYRK1B plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRK2 promotes apoptosis in response to DNA damage by phosphorylating the tumor suppressor p53, while DYRK3 promotes cell survival by phosphorylating SIRT1 and promoting p53 deacetylation. DYRK4 is a testis-specific kinase that may function during spermiogenesis.


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 68.34  E-value: 4.59e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCrYDPEgdnTGEQVAVKSLKpesggNHIADLKK---EIEILRNL------YHENIVKYKG-------IC 944
Cdd:cd14210     21 LGKGSFGQVVKC-LDHK---TGQLVAIKIIR-----NKKRFHQQalvEVKILKHLndndpdDKHNIVRYKDsfifrghLC 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  945 tedggngikLIMEFLpSGSLKEYLPKNKNK-INLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEH--QVKIGD 1021
Cdd:cd14210     92 ---------IVFELL-SINLYELLKSNNFQgLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPSksSIKVID 161
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1013071061 1022 FGlTKAIETDKeYYTVKDDRdspvFWYAPECLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd14210    162 FG-SSCFEGEK-VYTYIQSR----FYRAPEVILGLPYDTAIDMWSLGCILAELYT 210
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
879-1086 4.67e-12

The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2 (also called STK17B). Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. DRAK2 has been implicated in inducing or enhancing apoptosis in beta cells, fibroblasts, and lymphoid cells, where it is highly expressed. It is involved in regulating many immune processes including the germinal center (GC) reaction, responses to thymus-dependent antigens, activated T cell survival, memory T cell responses. It may be involved in the development of autoimmunity. The DRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271100 [Multi-domain]  Cd Length: 270  Bit Score: 67.64  E-value: 4.67e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGHFGKVELCRydpeGDNTGEQVAVKSLKPESGGNHI-ADLKKEIEILRnLYHEN--IVKYKGICTEDggNGIKLI 955
Cdd:cd14198     14 KELGRGKFAVVRQCI----SKSTGQEYAAKFLKKRRRGQDCrAEILHEIAVLE-LAKSNprVVNLHEVYETT--SEIILI 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  956 MEFLPSGSLKEY-LPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEH---QVKIGDFGLTKAIETD 1031
Cdd:cd14198     87 LEYAAGGEIFNLcVPDLAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIYplgDIKIVDFGMSRKIGHA 166
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1013071061 1032 KEYYTVKDDRDspvfWYAPECLMQSKFYIASDVWSFGVTLHELLTYcdsdSSPMA 1086
Cdd:cd14198    167 CELREIMGTPE----YLAPEILNYDPITTATDMWNIGVIAYMLLTH----ESPFV 213
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
878-1089 4.97e-12

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. MAP4K3 is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. mTOR regulates ribosome biogenesis and protein translation, and is frequently deregulated in cancer. MAP4Ks are involved in MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 67.76  E-value: 4.97e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVelcrYDPEGDNTGEQVAVKSLKPESGGNhIADLKKEIEILRNLYHENIVKYKGICTEDggNGIKLIME 957
Cdd:cd06645     16 IQRIGSGTYGDV----YKARNVNTGELAAIKVIKLEPGED-FAVVQQEIIMMKDCKHSNIVAYFGSYLRR--DKLWICME 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  958 FLPSGSLKEyLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETdkEYYTV 1037
Cdd:cd06645     89 FCGGGSLQD-IYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQITA--TIAKR 165
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1013071061 1038 KDDRDSPvFWYAPECLMQSK---FYIASDVWSFGVTLHEL--LTYCDSDSSPM-ALFL 1089
Cdd:cd06645    166 KSFIGTP-YWMAPEVAAVERkggYNQLCDIWAVGITAIELaeLQPPMFDLHPMrALFL 222
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
864-1076 5.25e-12

Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase (also called MAPK13); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38delta/MAPK13 is found in skeletal muscle, heart, lung, testis, pancreas, and small intestine. It regulates microtubule function by phosphorylating Tau. It activates the c-jun promoter and plays a role in G2 cell cycle arrest. It also controls the degration of c-Myb, which is associated with myeloid leukemia and poor prognosis in colorectal cancer. p38delta is the main isoform involved in regulating the differentiation and apoptosis of keratinocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 68.78  E-value: 5.25e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  864 EVDPTHFE--KRFLkRIRDLGEGHFGKVelCRYDPEgdNTGEQVAVKSL-KPESGGNHIADLKKEIEILRNLYHENIVKY 940
Cdd:cd07879      5 EVNKTVWElpERYT-SLKQVGSGAYGSV--CSAIDK--RTGEKVAIKKLsRPFQSEIFAKRAYRELTLLKHMQHENVIGL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  941 KGICTE----DGGNGIKLIMEFLPSGSLKEY-LPKNKNKInlkQQLKYavQICKGMDYLGSRQYVHRDLAARNVLVESEH 1015
Cdd:cd07879     80 LDVFTSavsgDEFQDFYLVMPYMQTDLQKIMgHPLSEDKV---QYLVY--QMLCGLKYIHSAGIIHRDLKPGNLAVNEDC 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1013071061 1016 QVKIGDFGLTKAIETDKEYYTVKDdrdspvfWY-APECLMQSKFYIAS-DVWSFGVTLHELLT 1076
Cdd:cd07879    155 ELKILDFGLARHADAEMTGYVVTR-------WYrAPEVILNWMHYNQTvDIWSVGCIMAEMLT 210
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
881-1075 5.42e-12

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. There are three PKB isoforms from different genes, PKB-alpha (or Akt1), PKB-beta (or Akt2), and PKB-gamma (or Akt3). PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. It is activated downstream of phosphoinositide 3-kinase (PI3K) and plays important roles in diverse cellular functions including cell survival, growth, proliferation, angiogenesis, motility, and migration. PKB also has a central role in a variety of human cancers, having been implicated in tumor initiation, progression, and metastasis. The PKB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 68.54  E-value: 5.42e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDpegdNTGEQVAVKSLKPES--GGNHIADLKKEIEILRNLYHENIVKYK-GICTEDGgngIKLIME 957
Cdd:cd05571      3 LGKGTFGKVILCREK----ATGELYAIKILKKEViiAKDEVAHTLTENRVLQNTRHPFLTSLKySFQTNDR---LCFVME 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  958 FLPSGSLKEYLPKNKnKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEyyTV 1037
Cdd:cd05571     76 YVNGGELFFHLSRER-VFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLCKEEISYGA--TT 152
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1013071061 1038 KDDRDSPVFwYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd05571    153 KTFCGTPEY-LAPEVLEDNDYGRAVDWWGLGVVMYEMM 189
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
879-1139 6.01e-12

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1a, also called Activin receptor-Like Kinase 3 (ALK3), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Germline mutations in BMPR1a are associated with an increased risk to Juvenile Polyposis Syndrome, a hamartomatous disorder that may lead to gastrointestinal cancer. BMPR1a may also play an indirect role in the development of hematopoietic stem cells (HSCs) as osteoblasts are a major component of the HSC niche within the bone marrow. BMPR1a belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1a, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271122 [Multi-domain]  Cd Length: 287  Bit Score: 67.76  E-value: 6.01e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGHFGKVELCRYdpegdnTGEQVAVKSLKPESGgnhiADLKKEIEILRN--LYHENIVKYkgICTEDGGNG----I 952
Cdd:cd14220      1 RQIGKGRYGEVWMGKW------RGEKVAVKVFFTTEE----ASWFRETEIYQTvlMRHENILGF--IAADIKGTGswtqL 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  953 KLIMEFLPSGSLKEYLpkNKNKINLKQQLKYAVQICKGMDYLGSRQY--------VHRDLAARNVLVESEHQVKIGDFGL 1024
Cdd:cd14220     69 YLITDYHENGSLYDFL--KCTTLDTRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGTCCIADLGL 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1025 TKAIETDKEYYTVK-DDRDSPVFWYAPECLMQS------KFYIASDVWSFGVTLHELLTYCDSD---SSPMALFLKMI-- 1092
Cdd:cd14220    147 AVKFNSDTNEVDVPlNTRVGTKRYMAPEVLDESlnknhfQAYIMADIYSFGLIIWEMARRCVTGgivEEYQLPYYDMVps 226
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1013071061 1093 GPTHGQMTVTRLVNTLKegkrlPCPPN------CPDEVYQLMRKCWEFQPSNR 1139
Cdd:cd14220    227 DPSYEDMREVVCVKRLR-----PTVSNrwnsdeCLRAVLKLMSECWAHNPASR 274
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
879-1086 6.16e-12

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs, also called STK17, were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. They may play a role in apoptotic signaling. The DRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271008 [Multi-domain]  Cd Length: 268  Bit Score: 67.38  E-value: 6.16e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGHFGKVELCRYDpegdNTGEQVAVKSLKPESGGnhiADLKKEI--EIL---RNLYHENIVKYKGIctEDGGNGIK 953
Cdd:cd14106     14 TPLGRGKFAVVRKCIHK----ETGKEYAAKFLRKRRRG---QDCRNEIlhEIAvleLCKDCPRVVNLHEV--YETRSELI 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  954 LIMEFLPSGSL------KEYLPKNKNKINLKQqlkyavqICKGMDYLGSRQYVHRDLAARNVLVESEH---QVKIGDFGL 1024
Cdd:cd14106     85 LILELAAGGELqtlldeEECLTEADVRRLMRQ-------ILEGVQYLHERNIVHLDLKPQNILLTSEFplgDIKLCDFGI 157
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1013071061 1025 TKAIETDKEYYTVKDDRDspvfWYAPECLMQSKFYIASDVWSFGVTLHELLTYCdsdsSPMA 1086
Cdd:cd14106    158 SRVIGEGEEIREILGTPD----YVAPEILSYEPISLATDMWSIGVLTYVLLTGH----SPFG 211
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
881-1076 6.38e-12

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK1 (or MYLK1) phosphorylates myosin regulatory light chain and controls the contraction of smooth muscles. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module which results in the expression of telokin in phasic smooth muscles, leading to Ca2+ desensitization by cyclic nucleotides of smooth muscle force. MLCK1 is also responsible for myosin regulatory light chain phosphorylation in nonmuscle cells and may play a role in regulating myosin II ATPase activity. The MLCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271093 [Multi-domain]  Cd Length: 259  Bit Score: 67.34  E-value: 6.38e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVelcrYDPEGDNTGEQVAVKSLKPESGGNHiADLKKEIEILRNLYHENIVKykgiCTE--DGGNGIKLIMEF 958
Cdd:cd14191     10 LGSGKFGQV----FRLVEKKTKKVWAGKFFKAYSAKEK-ENIRQEISIMNCLHHPKLVQ----CVDafEEKANIVMVLEM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  959 LPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLV--ESEHQVKIGDFGLTKAIETDKeyyT 1036
Cdd:cd14191     81 VSGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCvnKTGTKIKLIDFGLARRLENAG---S 157
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1013071061 1037 VKDDRDSPVFwYAPECLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd14191    158 LKVLFGTPEF-VAPEVINYEPIGYATDMWSIGVICYILVS 196
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
873-1076 6.48e-12

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on S/T residues. In Drosophila, the CLK homolog DOA (Darkener of apricot) is essential for embryogenesis and its mutation leads to defects in sexual differentiation, eye formation, and neuronal development. In fission yeast, the CLK homolog Lkh1 is a negative regulator of filamentous growth and asexual flocculation, and is also involved in oxidative stress response. Vertebrates contain mutliple CLK proteins and mammals have four (CLK1-4). The CLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 68.36  E-value: 6.48e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  873 RFlKRIRDLGEGHFGKVELCrYDpegDNTGEQVAVKSLKPESggNHIADLKKEIEILRNLYHE------NIVK------Y 940
Cdd:cd14134     13 RY-KILRLLGEGTFGKVLEC-WD---RKRKRYVAVKIIRNVE--KYREAAKIEIDVLETLAEKdpngksHCVQlrdwfdY 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  941 KG-ICtedggngikLIMEFLPSgSLKEYLPKNKNK-INLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESehqvk 1018
Cdd:cd14134     86 RGhMC---------IVFELLGP-SLYDFLKKNNYGpFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLVD----- 150
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1013071061 1019 iGDFGLTKAIETDKEYYTVKDDR----D--SPVFWY-------------APECLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd14134    151 -SDYVKVYNPKKKRQIRVPKSTDikliDfgSATFDDeyhssivstrhyrAPEVILGLGWSYPCDVWSIGCILVELYT 226
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
636-839 6.56e-12

Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group II PAKs, also called non-conventional PAKs, include PAK4, PAK5, and PAK6. Group II PAKs contain PBD (p21-binding domain) and catalytic domains, but lack other motifs found in group I PAKs, such as an AID (autoinhibitory domain) and SH3 binding sites. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. While group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX, no such binding has been demonstrated for group II PAKs. Some known substrates of group II PAKs are also substrates of group I PAKs such as Raf, BAD, LIMK and GEFH1. Unique group II substrates include MARK/Par-1 and PDZ-RhoGEF. Group II PAKs play important roles in filopodia formation, neuron extension, cytoskeletal organization, and cell survival. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270815 [Multi-domain]  Cd Length: 261  Bit Score: 67.08  E-value: 6.56e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  636 FEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPL-DLFMHRKsdvLTTPWKFKVAKQLASALSYLEDKDLVHGN 714
Cdd:cd06648     52 FNEVVIMRDYQHPNIVEMYSSYLVGDELWVVMEFLEGGALtDIVTHTR---MNEEQIATVCRAVLKALSFLHSQGVIHRD 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  715 VCTKNLLLAREGIdsecgpfIKLSDPG----IPITVLSRQECIERIPWIAPEcVEDSKNLSVAADKWSFGTTLWEIC--- 787
Cdd:cd06648    129 IKSDSILLTSDGR-------VKLSDFGfcaqVSKEVPRRKSLVGTPYWMAPE-VISRLPYGTEVDIWSLGIMVIEMVdge 200
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1013071061  788 --YNGEIPLKDKTLIEKERFYESR-CRPVTPsckELADLMTRCMNYDPNQR---------PFFR 839
Cdd:cd06648    201 ppYFNEPPLQAMKRIRDNEPPKLKnLHKVSP---RLRSFLDRMLVRDPAQRataaellnhPFLA 261
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
879-1075 6.61e-12

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK1 (also called rhodopsin kinase) belongs to the visual group of GRKs and is expressed in retinal cells. It phosphorylates rhodopsin in rod cells, which leads to termination of the phototransduction cascade. Mutations in GRK1 are associated to a recessively inherited form of stationary nightblindness called Oguchi disease. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 67.60  E-value: 6.61e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGHFGKVELCRYDPegdnTGEQVAVKSLKPESggnhiadLKK---------EIEILRNLYHENIVKYKgiCTEDGG 949
Cdd:cd05608      7 RVLGKGGFGEVSACQMRA----TGKLYACKKLNKKR-------LKKrkgyegamvEKRILAKVHSRFIVSLA--YAFQTK 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  950 NGIKLIMEFLPSGSLKEY---LPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLtk 1026
Cdd:cd05608     74 TDLCLVMTIMNGGDLRYHiynVDEENPGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGL-- 151
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1013071061 1027 AIETDKEYYTVKDDRDSPVFwYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd05608    152 AVELKDGQTKTKGYAGTPGF-MAPELLLGEEYDYSVDYFTLGVTLYEMI 199
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
881-1090 6.89e-12

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-delta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271070 [Multi-domain]  Cd Length: 301  Bit Score: 67.77  E-value: 6.89e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCrydpEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGIctEDGGNGIKLIMEFLP 960
Cdd:cd14168     18 LGTGAFSEVVLA----EERATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDI--YESPNHLYLVMQLVS 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  961 SGSLKEYLPKnKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLV---ESEHQVKIGDFGLTKAIETDKEYYTV 1037
Cdd:cd14168     92 GGELFDRIVE-KGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYfsqDEESKIMISDFGLSKMEGKGDVMSTA 170
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1013071061 1038 KddrDSPVFwYAPECLMQSKFYIASDVWSFGVTLHELLT-----YCDSDSSPMALFLK 1090
Cdd:cd14168    171 C---GTPGY-VAPEVLAQKPYSKAVDCWSIGVIAYILLCgyppfYDENDSKLFEQILK 224
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
878-1075 7.80e-12

Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PASK (or PASKIN) is a nutrient and energy sensor and thus, plays an important role in maintaining cellular energy homeostasis. It coordinates the utilization of glucose in response to metabolic demand. It contains an N-terminal PAS domain which directly interacts and inhibits a C-terminal catalytic kinase domain. The PAS domain serves as a sensory module for different environmental signals such as light, redox state, and various metabolites. Binding of ligands to the PAS domain causes structural changes which leads to kinase activation and the phosphorylation of substrates to trigger the appropriate cellular response. The PASK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270906 [Multi-domain]  Cd Length: 256  Bit Score: 67.03  E-value: 7.80e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVELCRYDPEGDntgeQVAVKSLKPEsggnHI--------ADLKK---EIEI---LRNLYHENIVK---- 939
Cdd:cd14004      5 LKEMGEGAYGQVNLAIYKSKGK----EVVIKFIFKE----RIlvdtwvrdRKLGTvplEIHIldtLNKRSHPNIVKlldf 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  940 -----YKGICTEDGGNGIKL--IMEFLPSgsLKEYLPKNknkinLKQQLKYAVQickgmdYLGSRQYVHRDLAARNVLVE 1012
Cdd:cd14004     77 feddeFYYLVMEKHGSGMDLfdFIERKPN--MDEKEAKY-----IFRQVADAVK------HLHDQGIVHRDIKDENVILD 143
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1013071061 1013 SEHQVKIGDFGLTKAIETDKeYYTVKDDRDspvfWYAPECLMQSKfYIAS--DVWSFGVTLHELL 1075
Cdd:cd14004    144 GNGTIKLIDFGSAAYIKSGP-FDTFVGTID----YAAPEVLRGNP-YGGKeqDIWALGVLLYTLV 202
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
635-836 7.85e-12

Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. Vertebrates contain two members, LRRK1 and LRRK2, which show complementary expression in the brain. Mutations in LRRK2 are linked to both familial and sporadic forms of Parkinson's disease. The normal roles of LRRKs are not clearly defined. They may be involved in mitogen-activated protein kinase (MAPK) pathways, protein translation control, programmed cell death pathways, and cytoskeletal dynamics. The LRRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270902 [Multi-domain]  Cd Length: 275  Bit Score: 67.25  E-value: 7.85e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  635 FFEAASMMRQVSHKHIVYLYGVCVRDVenIMVEEFVEGGPLD--LFMHRKSDVLTTPWKF-KVAKQLASALSYLEDKDLV 711
Cdd:cd14000     57 LRQELTVLSHLHHPSIVYLLGIGIHPL--MLVLELAPLGSLDhlLQQDSRSFASLGRTLQqRIALQVADGLRYLHSAMII 134
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  712 HGNVCTKNLLLARegIDSECGPFIKLSDPGIpitvlSRQECIERIP-------WIAPECVEDSKNLSVAADKWSFGTTLW 784
Cdd:cd14000    135 YRDLKSHNVLVWT--LYPNSAIIIKIADYGI-----SRQCCRMGAKgsegtpgFRAPEIARGNVIYNEKVDVFSFGMLLY 207
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1013071061  785 EIcYNGEIPLKDKTLIEKERFYESRCRPV--TPSC---KELADLMTRCMNYDPNQRP 836
Cdd:cd14000    208 EI-LSGGAPMVGHLKFPNEFDIHGGLRPPlkQYECapwPEVEVLMKKCWKENPQQRP 263
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
872-1075 7.85e-12

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK1 is important in the regulation of many cellular processes including cytoskeletal dynamics, cell motility, growth, and proliferation. Although PAK1 has been regarded mainly as a cytosolic protein, recent reports indicate that PAK1 also exists in significant amounts in the nucleus, where it is involved in transcription modulation and in cell cycle regulatory events. PAK1 is also involved in transformation and tumorigenesis. Its overexpression, hyperactivation and increased nuclear accumulation is correlated to breast cancer invasiveness and progression. Nuclear accumulation is also linked to tamoxifen resistance in breast cancer cells. PAK1 belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270820 [Multi-domain]  Cd Length: 296  Bit Score: 67.44  E-value: 7.85e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  872 KRFLKRIRDLGEGHFGKVelcrYDPEGDNTGEQVAVKSLKPESGGNHiADLKKEIEILRNLYHENIVKYkgICTEDGGNG 951
Cdd:cd06654     19 KKKYTRFEKIGQGASGTV----YTAMDVATGQEVAIRQMNLQQQPKK-ELIINEILVMRENKNPNIVNY--LDSYLVGDE 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  952 IKLIMEFLPSGSLKEYLpkNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETD 1031
Cdd:cd06654     92 LWVVMEYLAGGSLTDVV--TETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPE 169
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1013071061 1032 KeyyTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd06654    170 Q---SKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMI 210
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
879-1143 8.37e-12

Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK6, also called SSTK, is expressed at the head of elongated sperm. It can phosphorylate histones and associate with heat shock protens HSP90 and HSC70. Male mice deficient in TSSK6 are infertile, showing spermatogenic impairment including reduced sperm counts, impaired DNA condensation, abnormal morphology and decreased motility rates. The TSSK6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 66.81  E-value: 8.37e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGHFGKVELCrydPEGDNTGeQVAVKSLKPESGGNHIAD--LKKEIEILRNLYHENIVKYKGiCTEDGGNGIKLIM 956
Cdd:cd14164      6 TTIGEGSFSKVKLA---TSQKYCC-KVAIKIVDRRRASPDFVQkfLPRELSILRRVNHPNIVQMFE-CIEVANGRLYIVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  957 EfLPSGSLKEYLPKNKnKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVES-EHQVKIGDFGLTKAIETDKEYY 1035
Cdd:cd14164     81 E-AAATDLLQKIQEVH-HIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSAdDRKIKIADFGFARFVEDYPELS 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1036 TVKDDRDSpvfWYAPECLM----QSKFYiasDVWSFGVTLHELLTYCdsdsspmalflkmiGPTHGqmTVTRLVNTLKEG 1111
Cdd:cd14164    159 TTFCGSRA---YTPPEVILgtpyDPKKY---DVWSLGVVLYVMVTGT--------------MPFDE--TNVRRLRLQQRG 216
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1013071061 1112 KRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQ 1143
Cdd:cd14164    217 VLYPSGVALEEPCRALIRTLLQFNPSTRPSIQ 248
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
697-848 9.23e-12

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR1 (or Flt1) binds VEGFA, VEGFB, and placenta growth factor (PLGF). It regulates monocyte and macrophage migration, vascular permeability, haematopoiesis, and the recruitment of haematopietic progenitor cells from the bone marrow. VEGFR1 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 67.72  E-value: 9.23e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  697 QLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGIPITVLSRQECIE----RIP--WIAPECVEDsKNL 770
Cdd:cd14207    188 QVARGMEFLSSRKCIHRDLAARNILLSENNV-------VKICDFGLARDIYKNPDYVRkgdaRLPlkWMAPESIFD-KIY 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  771 SVAADKWSFGTTLWEICYNGEIPLKDKTLIEK--ERFYES-RCRPVTPSCKELADLMTRCMNYDPNQRPFFRAIMRDINK 847
Cdd:cd14207    260 STKSDVWSYGVLLWEIFSLGASPYPGVQIDEDfcSKLKEGiRMRAPEFATSEIYQIMLDCWQGDPNERPRFSELVERLGD 339

                   .
gi 1013071061  848 L 848
Cdd:cd14207    340 L 340
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
615-836 9.61e-12

Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and Ste20-related proline alanine-rich kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SPAK is also referred to as STK39 or PASK (proline-alanine-rich STE20-related kinase). OSR1 and SPAK regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. They are also implicated in cytoskeletal rearrangement, cell differentiation, transformation and proliferation. OSR1 and SPAK contain a conserved C-terminal (CCT) domain, which recognizes a unique motif ([RK]FX[VI]) present in their activating kinases (WNK1/WNK4) and their substrates. The OSR1 and SPAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270787 [Multi-domain]  Cd Length: 267  Bit Score: 66.61  E-value: 9.61e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  615 KKIKVILKVLDPSHRDISLAFF-EAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGP-LDLFMHR-KSDVLTTPWK 691
Cdd:cd06610     25 KKEKVAIKRIDLEKCQTSMDELrKEIQAMSQCNHPNVVSYYTSFVVGDELWLVMPLLSGGSlLDIMKSSyPRGGLDEAII 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  692 FKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGIPITVLSRQECIERI-------P-WIAPEC 763
Cdd:cd06610    105 ATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGS-------VKIADFGVSASLATGGDRTRKVrktfvgtPcWMAPEV 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  764 VEDSKNLSVAADKWSFGTTLWEICyNGEIPLKD--------KTLIEKERFYESrCRPVTPSCKELADLMTRCMNYDPNQR 835
Cdd:cd06610    178 MEQVRGYDFKADIWSFGITAIELA-TGAAPYSKyppmkvlmLTLQNDPPSLET-GADYKKYSKSFRKMISLCLQKDPSKR 255

                   .
gi 1013071061  836 P 836
Cdd:cd06610    256 P 256
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
875-1076 1.03e-11

Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase Kinases 3 and 6; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK3 and MKK6 are dual-specificity PKs that phosphorylate and activate their downstream target, p38 MAPK, on specific threonine and tyrosine residues. MKK3/6 play roles in the regulation of cell cycle progression, cytokine- and stress-induced apoptosis, oncogenic transformation, and adult tissue regeneration. In addition, MKK6 plays a critical role in osteoclast survival in inflammatory disease while MKK3 is associated with tumor invasion, progression, and poor patient survival in glioma. The MKK3/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 67.06  E-value: 1.03e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  875 LKRIRDLGEGHFGKVELCRYDPegdnTGEQVAVKSLKPESGGNHIADLKKEIEI-LRNLYHENIVKYKGICTEDGGNGIk 953
Cdd:cd06617      3 LEVIEELGRGAYGVVDKMRHVP----TGTIMAVKRIRATVNSQEQKRLLMDLDIsMRSVDCPYTVTFYGALFREGDVWI- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  954 lIMEFLPSGSLKEYLPKNKNKINLKQQL--KYAVQICKGMDYLGSRQYV-HRDLAARNVLVESEHQVKIGDFGLTKAIeT 1030
Cdd:cd06617     78 -CMEVMDTSLDKFYKKVYDKGLTIPEDIlgKIAVSIVKALEYLHSKLSViHRDVKPSNVLINRNGQVKLCDFGISGYL-V 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1031 DKEYYTVkDDRDSPvfWYAPE----CLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd06617    156 DSVAKTI-DAGCKP--YMAPErinpELNQKGYDVKSDVWSLGITMIELAT 202
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
881-1147 1.08e-11

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 5; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK5 (also called MEK5) is a dual-specificity PK that phosphorylates its downstream target, extracellular signal-regulated kinase 5 (ERK5), on specific threonine and tyrosine residues. MKK5 is activated by MEKK2 and MEKK3 in response to mitogenic and stress stimuli. The ERK5 cascade promotes cell proliferation, differentiation, neuronal survival, and neuroprotection. This cascade plays an essential role in heart development. Mice deficient in either ERK5 or MKK5 die around embryonic day 10 due to cardiovascular defects including underdevelopment of the myocardium. In addition, MKK5 is associated with metastasis and unfavorable prognosis in prostate cancer. The MKK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 66.83  E-value: 1.08e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVelcrYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDggNGIKLIMEFLP 960
Cdd:cd06619      9 LGHGNGGTV----YKAYHLLTRRILAVKVIPLDITVELQKQIMSELEILYKCDSPYIIGFYGAFFVE--NRISICTEFMD 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  961 SGSLKEYlpknkNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGL-TKAIETDKEYYTVKD 1039
Cdd:cd06619     83 GGSLDVY-----RKIPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVsTQLVNSIAKTYVGTN 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1040 DrdspvfWYAPECLMQSKFYIASDVWSFGVTLHELLtycdSDSSPMALFLKmigpTHGQMTVTRLVNTL--KEGKRLPC- 1116
Cdd:cd06619    158 A------YMAPERISGEQYGIHSDVWSLGISFMELA----LGRFPYPQIQK----NQGSLMPLQLLQCIvdEDPPVLPVg 223
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1013071061 1117 --PPNCPDEVYQLMRKcwefQPSNRTSFQNLIE 1147
Cdd:cd06619    224 qfSEKFVHFITQCMRK----QPKERPAPENLMD 252
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
878-1075 1.14e-11

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-2 is also referred to as ALS2CR7 (amyotrophic lateral sclerosis 2 (juvenile) chromosome region candidate 7). It may be associated with amyotrophic lateral sclerosis 2 (ALS2), an autosomal recessive form of juvenile ALS. The function of PFTAIRE-2 is not yet known. It shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270852 [Multi-domain]  Cd Length: 286  Bit Score: 66.91  E-value: 1.14e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVelcrYDPEGDNTGEQVAVK--SLKPESGGNHIAdlKKEIEILRNLYHENIVKYKGICTEDggNGIKLI 955
Cdd:cd07870      5 LEKLGEGSYATV----YKGISRINGQLVALKviSMKTEEGVPFTA--IREASLLKGLKHANIVLLHDIIHTK--ETLTFV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  956 MEFLPSgSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYY 1035
Cdd:cd07870     77 FEYMHT-DLAQYMIQHPGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLARAKSIPSQTY 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1013071061 1036 TvkddRDSPVFWY-APECLMQSKFYIAS-DVWSFGVTLHELL 1075
Cdd:cd07870    156 S----SEVVTLWYrPPDVLLGATDYSSAlDIWGAGCIFIEML 193
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
876-1075 1.26e-11

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-1 is widely expressed except in the spleen and thymus. It is highly expressed in the brain, heart, pancreas, testis, and ovary, and is localized in the cytoplasm. It is regulated by cyclin D3 and is inhibited by the p21 cell cycle inhibitor. It has also been shown to interact with the membrane-associated cyclin Y, which recruits the protein to the plasma membrane. PFTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143374 [Multi-domain]  Cd Length: 303  Bit Score: 67.03  E-value: 1.26e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  876 KRIRDLGEGHFGKVelcrYDPEGDNTGEQVAVK--SLKPESGGNHIAdlKKEIEILRNLYHENIVKYKGICTEDggNGIK 953
Cdd:cd07869      8 EKLEKLGEGSYATV----YKGKSKVNGKLVALKviRLQEEEGTPFTA--IREASLLKGLKHANIVLLHDIIHTK--ETLT 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  954 LIMEFLPSgSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKE 1033
Cdd:cd07869     80 LVFEYVHT-DLCQYMDKHPGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARAKSVPSH 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1013071061 1034 YYTvkddRDSPVFWYAPE--CLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd07869    159 TYS----NEVVTLWYRPPdvLLGSTEYSTCLDMWGVGCIFVEMI 198
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
586-836 1.26e-11

Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase kinase kinase (MAPKKK) epsilon, and related proteins. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Cdc7 is essential for cell division by playing a key role in the initiation of septum formation and cytokinesis. Budding yeast Cdc15 functions to coordinate mitotic exit with cytokinesis. Arabidopsis MAPKKK epsilon is required for pollen development in the plasma membrane. The Cdc7-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270797 [Multi-domain]  Cd Length: 254  Bit Score: 66.09  E-value: 1.26e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  586 GEHLGRGTRTHIYSGTlmdykdDEGTSEEKKIKVIlKVLDPSHRDISLAFFEAAsMMRQVSHKHIVYLYGvCVRDVENI- 664
Cdd:cd06627      5 GDLIGRGAFGSVYKGL------NLNTGEFVAIKQI-SLEKIPKSDLKSVMGEID-LLKKLNHPNIVKYIG-SVKTKDSLy 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  665 MVEEFVEGGPLdlfmhrkSDVLTTPWKFK---VAK---QLASALSYLEDKDLVHGNVCTKNLLLAREGidsecgpFIKLS 738
Cdd:cd06627     76 IILEYVENGSL-------ASIIKKFGKFPeslVAVyiyQVLEGLAYLHEQGVIHRDIKGANILTTKDG-------LVKLA 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  739 DPGIPITVLSRQECIERI---P-WIAPECVEDSkNLSVAADKWSFGTTLWEIcYNGEIPLKDKT----LIekeRFYESRC 810
Cdd:cd06627    142 DFGVATKLNEVEKDENSVvgtPyWMAPEVIEMS-GVTTASDIWSVGCTVIEL-LTGNPPYYDLQpmaaLF---RIVQDDH 216
                          250       260
                   ....*....|....*....|....*..
gi 1013071061  811 RPVTPSC-KELADLMTRCMNYDPNQRP 836
Cdd:cd06627    217 PPLPENIsPELRDFLLQCFQKDPTLRP 243
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
881-1154 1.32e-11

Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR2 interacts with the protein phosphatase calcineurin and functions in calcium-mediated ERK signaling. It also functions in energy metabolism by regulating AMP kinase and AMPK-dependent processes such as glucose uptake and fatty acid oxidation. KSR proteins act as scaffold proteins that function downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases. The KSR2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 66.57  E-value: 1.32e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDPEgdntgeqVAVKSLKPESGG-NHIADLKKEIEILRNLYHENIVKYKGICTEDggNGIKLIMEFL 959
Cdd:cd14153      8 IGKGRFGQVYHGRWHGE-------VAIRLIDIERDNeEQLKAFKREVMAYRQTRHENVVLFMGACMSP--PHLAIITSLC 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  960 PSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESeHQVKIGDFGLTkAIETDKEYYTVKD 1039
Cdd:cd14153     79 KGRTLYSVVRDAKVVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGLF-TISGVLQAGRRED 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1040 DRDSPVFW---YAPECLMQSK---------FYIASDVWSFGVTLHELLTY-CDSDSSPMALFLKMIGpthgqMTVTRLVN 1106
Cdd:cd14153    157 KLRIQSGWlchLAPEIIRQLSpeteedklpFSKHSDVFAFGTIWYELHAReWPFKTQPAEAIIWQVG-----SGMKPNLS 231
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1013071061 1107 TLKEGKrlpcppncpdEVYQLMRKCWEFQPSNRTSFQNLIEGFEALLK 1154
Cdd:cd14153    232 QIGMGK----------EISDILLFCWAYEQEERPTFSKLMEMLEKLPK 269
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
878-1076 1.33e-11

Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They function in the regulation of the cell cycle, cell development, cell differentiation, senescence, tumorigenesis, apoptosis, pain development and pain progression, and immune responses. p38 kinases are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. p38 substrates include other protein kinases and factors that regulate transcription, nuclear export, mRNA stability and translation. p38 kinases are drug targets for the inflammatory diseases psoriasis, rheumatoid arthritis, and chronic pulmonary disease. Vertebrates contain four isoforms of p38, named alpha, beta, gamma, and delta, which show varying substrate specificity and expression patterns. p38alpha and p38beta are ubiquitously expressed, p38gamma is predominantly found in skeletal muscle, and p38delta is found in the heart, lung, testis, pancreas, and small intestine. The p38 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143356 [Multi-domain]  Cd Length: 343  Bit Score: 67.32  E-value: 1.33e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVelCR-YDPEgdnTGEQVAVKSL-KPESGGNHIADLKKEIEILRNLYHENIvkykgictedggngIKLI 955
Cdd:cd07851     20 LSPVGSGAYGQV--CSaFDTK---TGRKVAIKKLsRPFQSAIHAKRTYRELRLLKHMKHENV--------------IGLL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  956 MEFLPSGSLKE----YL-----PKNKNKInLKQQ------LKYAV-QICKGMDYLGSRQYVHRDLAARNVLVESEHQVKI 1019
Cdd:cd07851     81 DVFTPASSLEDfqdvYLvthlmGADLNNI-VKCQklsddhIQFLVyQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKI 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1013071061 1020 GDFGLtkAIETDKEYYTVKDDRdspvfWY-APECLMQSKFYI-ASDVWSFGVTLHELLT 1076
Cdd:cd07851    160 LDFGL--ARHTDDEMTGYVATR-----WYrAPEIMLNWMHYNqTVDIWSVGCIMAELLT 211
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
881-1075 1.42e-11

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG, and in most cases, phosphatidylserine (PS) for activation. The cPKC-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 66.95  E-value: 1.42e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCrydpEGDNTGEQVAVKSLKPEsggnhIADLKKEIEIlrNLYHENIVKYKG---------ICTEDGgNG 951
Cdd:cd05616      8 LGKGSFGKVMLA----ERKGTDELYAVKILKKD-----VVIQDDDVEC--TMVEKRVLALSGkppfltqlhSCFQTM-DR 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  952 IKLIMEFLPSGSLKeYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKaiETD 1031
Cdd:cd05616     76 LYFVMEYVNGGDLM-YHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCK--ENI 152
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1013071061 1032 KEYYTVKDDRDSPVFwYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd05616    153 WDGVTTKTFCGTPDY-IAPEIIAYQPYGKSVDWWAFGVLLYEML 195
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
881-1139 1.60e-11

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I Receptor and Activin Type IB/IC Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR1, also called Activin receptor-Like Kinase 5 (ALK5), functions as a receptor for TGFbeta and phoshorylates SMAD2/3. TGFbeta proteins are cytokines that regulate cell growth, differentiation, and survival, and are critical in the development and progression of many human cancers. Mutations in TGFbR1 (and TGFbR2) can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. ACVR1b (also called ALK4) and ACVR1c (also called ALK7) act as receptors for activin A and B, respectively. TGFbR1, ACVR1b, and ACVR1c belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like TGFbR1, ACVR1b, and ACVR1c, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The TGFbR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271045 [Multi-domain]  Cd Length: 288  Bit Score: 66.31  E-value: 1.60e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYdpegdnTGEQVAVK--SLKPESGGNHIADLKKEIeILRnlyHENIVKYkgICTEDGGNG----IKL 954
Cdd:cd14143      3 IGKGRFGEVWRGRW------RGEDVAVKifSSREERSWFREAEIYQTV-MLR---HENILGF--IAADNKDNGtwtqLWL 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPSGSLKEYLpkNKNKINLKQQLKYAVQICKG-----MDYLGSR---QYVHRDLAARNVLVESEHQVKIGDFGLtk 1026
Cdd:cd14143     71 VSDYHEHGSLFDYL--NRYTVTVEGMIKLALSIASGlahlhMEIVGTQgkpAIAHRDLKSKNILVKKNGTCCIADLGL-- 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1027 AIETDKEYYTVK---DDRDSPVFWYAPECL-----MQS-KFYIASDVWSFGVTLHELLTYCDSDSspmalflkmiGPTHG 1097
Cdd:cd14143    147 AVRHDSATDTIDiapNHRVGTKRYMAPEVLddtinMKHfESFKRADIYALGLVFWEIARRCSIGG----------IHEDY 216
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1013071061 1098 QMTVTRLVN---TLKEGKRLPCP----PNCPDE---------VYQLMRKCWEFQPSNR 1139
Cdd:cd14143    217 QLPYYDLVPsdpSIEEMRKVVCEqklrPNIPNRwqscealrvMAKIMRECWYANGAAR 274
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
873-1075 1.73e-11

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK7 (also called iodopsin kinase) belongs to the visual group of GRKs. It is primarily found in the retina and plays a role in the regulation of opsin light receptors. GRK7 is located in retinal cone outer segments and plays an important role in regulating photoresponse of the cones. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270758 [Multi-domain]  Cd Length: 286  Bit Score: 66.47  E-value: 1.73e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  873 RFLKRIRDLGEGHFGkvELCRYDPEgdNTGEQVAVKSLKPE----SGGNHIADLKKEI-EILRNLYHENIVKykgicTED 947
Cdd:cd05607      2 KYFYEFRVLGKGGFG--EVCAVQVK--NTGQMYACKKLDKKrlkkKSGEKMALLEKEIlEKVNSPFIVSLAY-----AFE 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  948 GGNGIKLIMEFLPSGSLKEYLPKNKNK-INLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTK 1026
Cdd:cd05607     73 TKTHLCLVMSLMNGGDLKYHIYNVGERgIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAV 152
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1013071061 1027 AIETDKEYytvkDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd05607    153 EVKEGKPI----TQRAGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMV 197
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
582-857 1.90e-11

Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase Kinases 3 and 6; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK3 and MKK6 are dual-specificity PKs that phosphorylate and activate their downstream target, p38 MAPK, on specific threonine and tyrosine residues. MKK3/6 play roles in the regulation of cell cycle progression, cytokine- and stress-induced apoptosis, oncogenic transformation, and adult tissue regeneration. In addition, MKK6 plays a critical role in osteoclast survival in inflammatory disease while MKK3 is associated with tumor invasion, progression, and poor patient survival in glioma. The MKK3/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 66.29  E-value: 1.90e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  582 DLVQGEHLGRG-------TRtHIYSGTLMDYKDDEGTSEEKKIKVILKVLDPShrdislaffeaasmMRQVSHKHIVYLY 654
Cdd:cd06617      2 DLEVIEELGRGaygvvdkMR-HVPTGTIMAVKRIRATVNSQEQKRLLMDLDIS--------------MRSVDCPYTVTFY 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  655 GVCVR--DVENIMveEFVEGGPLDLFMHRKSDVLTTPWKF--KVAKQLASALSYLEDK-DLVHGNVCTKNLLLAREGIds 729
Cdd:cd06617     67 GALFRegDVWICM--EVMDTSLDKFYKKVYDKGLTIPEDIlgKIAVSIVKALEYLHSKlSVIHRDVKPSNVLINRNGQ-- 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  730 ecgpfIKLSDPGIP---ITVLSRQECIERIPWIAPECVE---DSKNLSVAADKWSFGTTLWEICyNGEIPLKD-KTLIEK 802
Cdd:cd06617    143 -----VKLCDFGISgylVDSVAKTIDAGCKPYMAPERINpelNQKGYDVKSDVWSLGITMIELA-TGRFPYDSwKTPFQQ 216
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  803 ERFYESRCRPVTPSCK---ELADLMTRCMNYDPNQRPFFRAIMRD--INKLEEQNPDIVS 857
Cdd:cd06617    217 LKQVVEEPSPQLPAEKfspEFQDFVNKCLKKNYKERPNYPELLQHpfFELHLSKNTDVAS 276
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
875-1141 1.91e-11

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1b, also called Activin receptor-Like Kinase 6 (ALK6), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Mutations in BMPR1b that led to inhibition of chondrogenesis can cause Brachydactyly (BD) type A2, a dominant hand malformation characterized by shortening and lateral deviation of the index fingers. A point mutation in the BMPR1b kinase domain is also associated with the Booroola phenotype, characterized by precocious differentiation of ovarian follicles. BMPR1b belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1b, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1b subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271121 [Multi-domain]  Cd Length: 305  Bit Score: 66.61  E-value: 1.91e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  875 LKRIRDLGEGHFGKVELCRYdpegdnTGEQVAVKSLKPESGgnhiADLKKEIEILRN--LYHENIVKYkgICTEDGGNG- 951
Cdd:cd14219      7 IQMVKQIGKGRYGEVWMGKW------RGEKVAVKVFFTTEE----ASWFRETEIYQTvlMRHENILGF--IAADIKGTGs 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  952 ---IKLIMEFLPSGSLKEYLpkNKNKINLKQQLKYAVQICKGMDYL--------GSRQYVHRDLAARNVLVESEHQVKIG 1020
Cdd:cd14219     75 wtqLYLITDYHENGSLYDYL--KSTTLDTKAMLKLAYSSVSGLCHLhteifstqGKPAIAHRDLKSKNILVKKNGTCCIA 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1021 DFGL-TKAIETDKEYYTVKDDRDSPVFWYAPECLMQS------KFYIASDVWSFGVTLHELLTYCDSDSSPMALFLkmig 1093
Cdd:cd14219    153 DLGLaVKFISDTNEVDIPPNTRVGTKRYMPPEVLDESlnrnhfQSYIMADMYSFGLILWEVARRCVSGGIVEEYQL---- 228
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1013071061 1094 PTHGQMTVTRLVNTLKEG---KRL-PCPPN------CPDEVYQLMRKCWEFQPSNRTS 1141
Cdd:cd14219    229 PYHDLVPSDPSYEDMREIvciKRLrPSFPNrwssdeCLRQMGKLMTECWAHNPASRLT 286
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
902-1146 2.35e-11

Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. ILK contains N-terminal ankyrin repeats, a Pleckstrin Homology (PH) domain, and a C-terminal pseudokinase domain. It is a component of the IPP (ILK/PINCH/Parvin) complex that couples beta integrins to the actin cytoskeleton, and plays important roles in cell adhesion, spreading, invasion, and migration. ILK was initially thought to be an active kinase despite the lack of key conserved residues because of in vitro studies showing that it can phosphorylate certain protein substrates. However, in vivo experiments in Caenorhabditis elegans, Drosophila melanogaster, and mice (ILK-null and knock-in) proved that ILK is not an active kinase. In addition to actin cytoskeleton regulation, ILK also influences the microtubule network and mitotic spindle orientation. The pseudokinase domain of ILK binds several adaptor proteins including the parvins and paxillin. The ILK subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270959 [Multi-domain]  Cd Length: 251  Bit Score: 65.20  E-value: 2.35e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  902 GEQVAVKSLKPESGGNHIA-DLKKEIEILRNLYHENIVKYKGICTEdgGNGIKLIMEFLPSGSLKEYLPKNKN-KINLKQ 979
Cdd:cd14057     18 GNDIVAKILKVRDVTTRISrDFNEEYPRLRIFSHPNVLPVLGACNS--PPNLVVISQYMPYGSLYNVLHEGTGvVVDQSQ 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  980 QLKYAVQICKGMDYLGS------RQYvhrdLAARNVLVESEHQVKI--GDFGLTKAiETDKEYytvkddrdSPVfWYAPE 1051
Cdd:cd14057     96 AVKFALDIARGMAFLHTleplipRHH----LNSKHVMIDEDMTARInmADVKFSFQ-EPGKMY--------NPA-WMAPE 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1052 CLMQSKFYI---ASDVWSFGVTLHELLT--YCDSDSSPMALFLKMIGpthgqmtvtrlvntlkEGKRLPCPPNCPDEVYQ 1126
Cdd:cd14057    162 ALQKKPEDInrrSADMWSFAILLWELVTreVPFADLSNMEIGMKIAL----------------EGLRVTIPPGISPHMCK 225
                          250       260
                   ....*....|....*....|
gi 1013071061 1127 LMRKCWEFQPSNRTSFQNLI 1146
Cdd:cd14057    226 LMKICMNEDPGKRPKFDMIV 245
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
873-1076 2.47e-11

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK3 shows a restricted expression pattern; it is found at high levels in the pituary glands and is also expressed in the kidney and brain. It has been shown to regulate many ion transporters including members of the SLC12A family of cation-chloride cotransporters such as NCC and NKCC2, the renal potassium channel ROMK, and the epithelial calcium channels TRPV5 and TRPV6. WNK3 appears to sense low-chloride hypotonic stress and under these conditions, it activates SPAK, which directly interacts and phosphorylates cation-chloride cotransporters. WNK3 has also been shown to promote cell survival, possibly through interaction with procaspase-3 and HSP70. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 65.90  E-value: 2.47e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  873 RFLKRIRDLGEGHFGKVelcrYDPEGDNTGEQVAVKSLKPES-GGNHIADLKKEIEILRNLYHENIVKYKGICTE--DGG 949
Cdd:cd14031     10 RFLKFDIELGRGAFKTV----YKGLDTETWVEVAWCELQDRKlTKAEQQRFKEEAEMLKGLQHPNIVRFYDSWESvlKGK 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  950 NGIKLIMEFLPSGSLKEYLPKNKnKINLKQQLKYAVQICKGMDYLGSRQ--YVHRDLAARNVLVESEH-QVKIGDFGLTK 1026
Cdd:cd14031     86 KCIVLVTELMTSGTLKTYLKRFK-VMKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGPTgSVKIGDLGLAT 164
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1027 AIETDkeyyTVKDDRDSPVFwYAPEcLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd14031    165 LMRTS----FAKSVIGTPEF-MAPE-MYEEHYDESVDVYAFGMCMLEMAT 208
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
879-1075 2.81e-11

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-eta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 66.08  E-value: 2.81e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGHFGKVELCRYDpegdNTGEQVAVKSLKPES--GGNHIADLKKEIEILrNLYHENIVKYKGICTEDGGNGIKLIM 956
Cdd:cd05590      1 RVLGKGSFGKVMLARLK----ESGRLYAVKVLKKDVilQDDDVECTMTEKRIL-SLARNHPFLTQLYCCFQTPDRLFFVM 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  957 EFLPSGSLKEYLPKNKNKINLKQQLkYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTK-AIETDKEYY 1035
Cdd:cd05590     76 EFVNGGDLMFHIQKSRRFDEARARF-YAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKeGIFNGKTTS 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1013071061 1036 TVKDDRDspvfWYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd05590    155 TFCGTPD----YIAPEILQEMLYGPSVDWWAMGVLLYEML 190
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
875-1152 2.86e-11

Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GAK, also called auxilin-2, contains an N-terminal kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2. In addition, it contains an auxilin-1-like domain structure consisting of PTEN-like, clathrin-binding, and J domains. Like auxilin-1, GAK facilitates Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, unlike auxilin-1 which is nerve-specific. GAK also plays regulatory roles outside of clathrin-mediated membrane traffic including the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses through interaction with the interleukin 12 receptor. It also interacts with the androgen receptor, acting as a transcriptional coactivator, and its expression is significantly increased with the progression of prostate cancer. The GAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 65.61  E-value: 2.86e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  875 LKRIRDLGEGHFGKVelcrYDPEGDNTGEQVAVKSL--KPESGGNHIAdlkKEIEILRNLY-HENIVKYKG---ICTEDG 948
Cdd:cd14036      2 LRIKRVIAEGGFAFV----YEAQDVGTGKEYALKRLlsNEEEKNKAII---QEINFMKKLSgHPNIVQFCSaasIGKEES 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  949 GNGIK--LIMEFLPSGSLKEYLPKNKNK--INLKQQLKYAVQICKGMDYLGSRQ--YVHRDLAARNVLVESEHQVKIGDF 1022
Cdd:cd14036     75 DQGQAeyLLLTELCKGQLVDFVKKVEAPgpFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIGNQGQIKLCDF 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1023 G--LTKAIETDKEYYT-----VKDD--RDSPVFWYAPECL-MQSKFYIA--SDVWSFGVTLHELLTYcdsdSSPMALFLK 1090
Cdd:cd14036    155 GsaTTEAHYPDYSWSAqkrslVEDEitRNTTPMYRTPEMIdLYSNYPIGekQDIWALGCILYLLCFR----KHPFEDGAK 230
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1013071061 1091 MigpthgqmtvtRLVNTlkegkRLPCPPNcpDEVYQ----LMRKCWEFQPSNRTSFQNLIEGFEAL 1152
Cdd:cd14036    231 L-----------RIINA-----KYTIPPN--DTQYTvfhdLIRSTLKVNPEERLSITEIVEQLQEL 278
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
697-852 3.01e-11

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR2 (or Flk1) binds the ligands VEGFA, VEGFC, VEGFD and VEGFE. VEGFR2 signaling is implicated in all aspects of normal and pathological vascular endothelial cell biology. It induces a variety of cellular effects including migration, survival, and proliferation. It is critical in regulating embryonic vascular development and angiogenesis. VEGFR2 is the major signal transducer in pathological angiogenesis including cancer and diabetic retinopathy, and is a target for inhibition in cancer therapy. The carboxyl terminus of VEGFR2 plays an important role in its autophosphorylation and activation. VEGFR2 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 66.16  E-value: 3.01e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  697 QLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGIPITVLSRQECIE----RIP--WIAPECVEDsKNL 770
Cdd:cd05103    187 QVAKGMEFLASRKCIHRDLAARNILLSENNV-------VKICDFGLARDIYKDPDYVRkgdaRLPlkWMAPETIFD-RVY 258
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  771 SVAADKWSFGTTLWEICYNGEIPLKDKTLIEK--ERFYE-SRCRPVTPSCKELADLMTRCMNYDPNQRPFFRAIMRDINK 847
Cdd:cd05103    259 TIQSDVWSFGVLLWEIFSLGASPYPGVKIDEEfcRRLKEgTRMRAPDYTTPEMYQTMLDCWHGEPSQRPTFSELVEHLGN 338

                   ....*
gi 1013071061  848 LEEQN 852
Cdd:cd05103    339 LLQAN 343
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
888-1146 3.09e-11

Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity.STRAD-beta is also referred to as ALS2CR2 (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 2 protein), since the human gene encoding it is located within the juvenile ALS2 critical region on chromosome 2q33-q34. It is not linked to the development of ALS2. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. The STRAD-beta subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270864 [Multi-domain]  Cd Length: 328  Bit Score: 66.05  E-value: 3.09e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  888 KVELCRYDPegdnTGEQVAVKSLKPES-GGNHIADLKKEIEILRNLYHENIVKYKGICTEdgGNGIKLIMEFLPSGS--- 963
Cdd:cd08226     15 SVYLARHTP----TGTLVTVKITNLDNcSEEHLKALQNEVVLSHFFRHPNIMTHWTVFTE--GSWLWVISPFMAYGSarg 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  964 -LKEYLPKNKNKINLKQQLKYAVqicKGMDYLGSRQYVHRDLAARNVLVESEHQVKI----GDFGLTKAIETDKEYYTVK 1038
Cdd:cd08226     89 lLKTYFPEGMNEALIGNILYGAI---KALNYLHQNGCIHRSVKASHILISGDGLVSLsglsHLYSMVTNGQRSKVVYDFP 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1039 DDRDSPVFWYAPECLMQ--SKFYIASDVWSFGVTLHELLT----YCDSDSSPMaLFLKMIGPTHG--------------- 1097
Cdd:cd08226    166 QFSTSVLPWLSPELLRQdlHGYNVKSDIYSVGITACELARgqvpFQDMRRTQM-LLQKLKGPPYSpldifpfpelesrmk 244
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1013071061 1098 ------------QMTVTRLVNTL-KEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLI 1146
Cdd:cd08226    245 nsqsgmdsgigeSVATSSMTRTMtSERLQTPSSKTFSPAFHNLVELCLQQDPEKRPSASSLL 306
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
875-1110 3.20e-11

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK6 is widely expressed in many tissues and is expressed as multiple splice variants with different domain architectures. It is post-translationally palmitoylated and localized in the membrane. GRK6 plays important roles in the regulation of dopamine, M3 muscarinic, opioid, and chemokine receptor signaling. It also plays maladaptive roles in addiction and Parkinson's disease. GRK6-deficient mice exhibit altered dopamine receptor regulation, decreased lymphocyte chemotaxis, and increased acute inflammation and neutrophil chemotaxis. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 65.43  E-value: 3.20e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  875 LKRIRDLGEGHFGKVELCRYDPegdnTGEQVAVKSLKPES----GGNHIAdlKKEIEILRNLYHENIVKYK-GICTEDGg 949
Cdd:cd05630      2 FRQYRVLGKGGFGEVCACQVRA----TGKMYACKKLEKKRikkrKGEAMA--LNEKQILEKVNSRFVVSLAyAYETKDA- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  950 ngIKLIMEFLPSGSLKEYL-PKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAI 1028
Cdd:cd05630     75 --LCLVLTLMNGGDLKFHIyHMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHV 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1029 ETDKeyyTVKdDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLtycdSDSSPMALFLKMIgpthGQMTVTRLVNTL 1108
Cdd:cd05630    153 PEGQ---TIK-GRVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMI----AGQSPFQQRKKKI----KREEVERLVKEV 220

                   ..
gi 1013071061 1109 KE 1110
Cdd:cd05630    221 PE 222
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
585-836 3.47e-11

Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. YSK4 is a putative MAPKKK, whose mammalian gene has been isolated. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The YSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 65.15  E-value: 3.47e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  585 QGEHLGRGTRTHIYSGTlmdykddegTSEEKKIKVILKVLDPSHRDIS----LAFFEAASMMRQVSHKHIVYLYGVCVRD 660
Cdd:cd06631      5 KGNVLGKGAYGTVYCGL---------TSTGQLIAVKQVELDTSDKEKAekeyEKLQEEVDLLKTLKHVNIVGYLGTCLED 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  661 -VENIMVEeFVEGGPLDLFMHRKSdVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSD 739
Cdd:cd06631     76 nVVSIFME-FVPGGSIASILARFG-ALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGV-------IKLID 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  740 PG------IPITVLSRQECIERI---P-WIAPECVEDSKNlSVAADKWSFGTTLWEICyNGEIPLKDKTLIEKERFYESR 809
Cdd:cd06631    147 FGcakrlcINLSSGSQSQLLKSMrgtPyWMAPEVINETGH-GRKSDIWSIGCTVFEMA-TGKPPWADMNPMAAIFAIGSG 224
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1013071061  810 CRPVtPS-----CKELADLMTRCMNYDPNQRP 836
Cdd:cd06631    225 RKPV-PRlpdkfSPEARDFVHACLTRDQDERP 255
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
878-1076 3.63e-11

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. They play important roles in mediating pre-mRNA processing and mRNA maturation, as well as other cellular functions such as chromatin reorganization, cell cycle and p53 regulation, and metabolic signaling. Vertebrates contain three distinct SRPKs, called SRPK1-3. The SRPK homolog in budding yeast, Sky1p, recognizes and phosphorylates its substrate Npl3p, which lacks a classic RS domain but contains a single RS dipeptide at the C-terminus of its RGG domain. Npl3p is a shuttling heterogeneous nuclear ribonucleoprotein (hnRNP) that exports a distinct class of mRNA from the nucleus to the cytoplasm. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 65.68  E-value: 3.63e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVELCrYDPEGDntgEQVAVKSLKpesGGNHIADL-KKEIEILR--------NLYHENIVKYKGICTEDG 948
Cdd:cd14136     15 VRKLGWGHFSTVWLC-WDLQNK---RFVALKVVK---SAQHYTEAaLDEIKLLKcvreadpkDPGREHVVQLLDDFKHTG 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  949 GNG--IKLIMEFLPSGSLKeyLPKNKN----KINLKQQLkyAVQICKGMDYLGSR-QYVHRDLAARNVLVE-SEHQVKIG 1020
Cdd:cd14136     88 PNGthVCMVFEVLGPNLLK--LIKRYNyrgiPLPLVKKI--ARQVLQGLDYLHTKcGIIHTDIKPENVLLCiSKIEVKIA 163
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1013071061 1021 DFGltKAIETDKEYYTVKDDRDspvfwY-APECLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd14136    164 DLG--NACWTDKHFTEDIQTRQ-----YrSPEVILGAGYGTPADIWSTACMAFELAT 213
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
874-1076 4.16e-11

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Triple functional domain protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Triple functional domain protein (Trio), also called PTPRF-interacting protein, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. Trio plays important roles in neuronal cell migration and axon guidance. It was originally identified as an interacting partner of the of the receptor-like tyrosine phosphatase (RPTP) LAR (leukocyte-antigen-related protein), a family of receptors that function in the signaling to the actin cytoskeleton during development. Trio functions as a GEF for Rac1, RhoG, and RhoA, and is involved in the regulation of lamellipodia formation, mediating Rac1-dependent cell spreading and migration. The Trio subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 65.00  E-value: 4.16e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  874 FLKRIRDLGEGHFGKVELCryDPEGdnTGEQVAVK----SLKPESGGNHiadlkkEIEILRNLYHENIVKYkgICTEDGG 949
Cdd:cd14113      8 FYSEVAELGRGRFSVVKKC--DQRG--TKRAVATKfvnkKLMKRDQVTH------ELGVLQSLQHPQLVGL--LDTFETP 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  950 NGIKLIMEFLPSGSLKEYLPKNKNKINLKQQLkYAVQICKGMDYLGSRQYVHRDLAARNVLVE---SEHQVKIGDFGltK 1026
Cdd:cd14113     76 TSYILVLEMADQGRLLDYVVRWGNLTEEKIRF-YLREILEALQYLHNCRIAHLDLKPENILVDqslSKPTIKLADFG--D 152
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1027 AIETDKEYYtVKDDRDSPVFwYAPECLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd14113    153 AVQLNTTYY-IHQLLGSPEF-AAPEIILGNPVSLTSDLWSIGVLTYVLLS 200
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
872-1075 5.08e-11

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK2 plays a role in pro-apoptotic signaling. It is cleaved and activated by caspases leading to morphological changes during apoptosis. PAK2 is also activated in response to a variety of stresses including DNA damage, hyperosmolarity, serum starvation, and contact inhibition, and may play a role in coordinating the stress response. PAK2 also contributes to cancer cell invasion through a mechanism distinct from that of PAK1. It belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132986 [Multi-domain]  Cd Length: 296  Bit Score: 65.13  E-value: 5.08e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  872 KRFLKRIRDLGEGHFGKVelcrYDPEGDNTGEQVAVK--SLKPESGGNHIADlkkEIEILRNLYHENIVKYkgICTEDGG 949
Cdd:cd06655     18 KKKYTRYEKIGQGASGTV----FTAIDVATGQEVAIKqiNLQKQPKKELIIN---EILVMKELKNPNIVNF--LDSFLVG 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  950 NGIKLIMEFLPSGSLKEYLpkNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIE 1029
Cdd:cd06655     89 DELFVVMEYLAGGSLTDVV--TETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCAQIT 166
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1013071061 1030 TDKeyyTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd06655    167 PEQ---SKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMV 209
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
881-1076 5.56e-11

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 65.05  E-value: 5.56e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCrydpEGDNTGEQVAVKSLKPESGGNHiADLKKEIEILRNLY-HENIVKYKGICTEDggNGIKLIMEFL 959
Cdd:cd14174     10 LGEGAYAKVQGC----VSLQNGKEYAVKIIEKNAGHSR-SRVFREVETLYQCQgNKNILELIEFFEDD--TRFYLVFEKL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  960 PSGSLKEYLPKNKNkINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQ---VKIGDFGLTKAIETDKEYYT 1036
Cdd:cd14174     83 RGGSILAHIQKRKH-FNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESPDKvspVKICDFDLGSGVKLNSACTP 161
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1013071061 1037 VKD-DRDSP---VFWYAPECLM----QSKFYIAS-DVWSFGVTLHELLT 1076
Cdd:cd14174    162 ITTpELTTPcgsAEYMAPEVVEvftdEATFYDKRcDLWSLGVILYIMLS 210
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
881-1076 8.02e-11

Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p70S6K (or S6K) contains only one catalytic kinase domain, unlike p90 ribosomal S6 kinases (RSKs). It acts as a downstream effector of the STK mTOR (mammalian Target of Rapamycin) and plays a role in the regulation of the translation machinery during protein synthesis. p70S6K also plays a pivotal role in regulating cell size and glucose homeostasis. Its targets include S6, the translation initiation factor eIF3, and the insulin receptor substrate IRS-1, among others. Mammals contain two isoforms of p70S6K, named S6K1 and S6K2 (or S6K-beta). The p70S6K subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 64.73  E-value: 8.02e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRyDPEGDNTGEQVAVKSLKPES---GGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGngIKLIME 957
Cdd:cd05584      4 LGKGGYGKVFQVR-KTTGSDKGKIFAMKVLKKASivrNQKDTAHTKAERNILEAVKHPFIVDLHYAFQTGGK--LYLILE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  958 FLPSGSLKEYLpkNKNKINLKQQLK-YAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTK-AIETDKEYY 1035
Cdd:cd05584     81 YLSGGELFMHL--EREGIFMEDTACfYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLCKeSIHDGTVTH 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1013071061 1036 TVKddrdSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd05584    159 TFC----GTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLT 195
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
628-872 8.40e-11

Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie2 is a receptor PTK (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie2 is expressed mainly in endothelial cells and hematopoietic stem cells. It is also found in a subset of tumor-associated monocytes and eosinophils. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. Tie2 signaling plays key regulatory roles in vascular integrity and quiescence, and in inflammation. The Tie2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133219 [Multi-domain]  Cd Length: 303  Bit Score: 64.63  E-value: 8.40e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  628 HRDISlafFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMhRKSDVLTTPWKFKVAKQLASALS---- 703
Cdd:cd05088     51 HRDFA---GELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPHGNLLDFL-RKSRVLETDPAFAIANSTASTLSsqql 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  704 ------------YLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGipitvLSR------QECIERIP--WIAPEC 763
Cdd:cd05088    127 lhfaadvargmdYLSQKQFIHRDLAARNILVGENYV-------AKIADFG-----LSRgqevyvKKTMGRLPvrWMAIES 194
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  764 VEDSKnLSVAADKWSFGTTLWEICYNGEIPLKDKTLIEKERFYESRCRPVTP-SCK-ELADLMTRCMNYDPNQRPFFRAI 841
Cdd:cd05088    195 LNYSV-YTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPlNCDdEVYDLMRQCWREKPYERPSFAQI 273
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1013071061  842 MRDINKLEEqnpdivsEKKpaTEVDPTHFEK 872
Cdd:cd05088    274 LVSLNRMLE-------ERK--TYVNTTLYEK 295
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
870-1076 8.82e-11

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 4; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK4 is a dual-specificity PK that phosphorylates and activates the downstream targets, c-Jun N-terminal kinase (JNK) and p38 MAPK, on specific threonine and tyrosine residues. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. Their activation is associated with the induction of cell death. Mice deficient in MKK4 die during embryogenesis and display anemia, severe liver hemorrhage, and abnormal hepatogenesis. MKK4 may also play roles in the immune system and in cardiac hypertrophy. It plays a major role in cancer as a tumor and metastasis suppressor. Under certain conditions, MKK4 is pro-oncogenic. The MKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 64.31  E-value: 8.82e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  870 FEKRFLKRIRDLGEGHFGKVELCRYDPegdnTGEQVAVKSLKPESGGNHIADLKKEIE-ILRNLYHENIVKYKGICTEDG 948
Cdd:cd06616      3 FTAEDLKDLGEIGRGAFGTVNKMLHKP----SGTIMAVKRIRSTVDEKEQKRLLMDLDvVMRSSDCPYIVKFYGALFREG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  949 GNGIklIMEFLPSGSLKEY-LPKNKNKINLKQQL--KYAVQICKGMDYLGSR-QYVHRDLAARNVLVESEHQVKIGDFGL 1024
Cdd:cd06616     79 DCWI--CMELMDISLDKFYkYVYEVLDSVIPEEIlgKIAVATVKALNYLKEElKIIHRDVKPSNILLDRNGNIKLCDFGI 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1013071061 1025 TKAIETdkeyyTVKDDRDSPVFWY-APECLMQS----KFYIASDVWSFGVTLHELLT 1076
Cdd:cd06616    157 SGQLVD-----SIAKTRDAGCRPYmAPERIDPSasrdGYDVRSDVWSLGITLYEVAT 208
pknD PRK13184
serine/threonine-protein kinase PknD;
878-1076 1.05e-10

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 66.33  E-value: 1.05e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVELCrYDPEgdnTGEQVAVKSLKPESGGNHIadLKK----EIEILRNLYHENIVKYKGICTEdgGNGIK 953
Cdd:PRK13184     7 IRLIGKGGMGEVYLA-YDPV---CSRRVALKKIREDLSENPL--LKKrflrEAKIAADLIHPGIVPVYSICSD--GDPVY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  954 LIMEFLPSGSLKEYLPKNKNKINLKQQL--KYAV--------QICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFG 1023
Cdd:PRK13184    79 YTMPYIEGYTLKSLLKSVWQKESLSKELaeKTSVgaflsifhKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWG 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1013071061 1024 LTKAIETDKEYYTVKDDRDSPVF---------------WYAPECLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:PRK13184   159 AAIFKKLEEEDLLDIDVDERNICyssmtipgkivgtpdYMAPERLLGVPASESTDIYALGVILYQMLT 226
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
881-1075 1.18e-10

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. GRKs play important roles in the cardiovascular, immune, respiratory, skeletal, and nervous systems. They contain a central catalytic domain, flanked by N- and C-terminal extensions. The N-terminus contains an RGS (regulator of G protein signaling) homology (RH) domain and several motifs. The C-terminus diverges among different groups of GRKs. There are seven types of GRKs, named GRK1 to GRK7, which are subdivided into three main groups: visual (GRK1/7); beta-adrenergic receptor kinases (GRK2/3); and GRK4-like (GRK4/5/6). Expression of GRK2/3/5/6 is widespread while GRK1/4/7 show a limited tissue distribution. The substrate spectrum of the widely expressed GRKs partially overlaps. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 63.70  E-value: 1.18e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDpegdNTGEQVAVKSLKPE----SGGNHIADLKKEIeiLRNLYHENIVKYK-GICTEDGgngIKLI 955
Cdd:cd05577      1 LGRGGFGEVCACQVK----ATGKMYACKKLDKKrikkKKGETMALNEKII--LEKVSSPFIVSLAyAFETKDK---LCLV 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  956 MEFLPSGSLKEYLPK-NKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLtkAIETdKEY 1034
Cdd:cd05577     72 LTLMNGGDLKYHIYNvGTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGL--AVEF-KGG 148
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1013071061 1035 YTVKDDRDSPVFwYAPECLMQSKFYIAS-DVWSFGVTLHELL 1075
Cdd:cd05577    149 KKIKGRVGTHGY-MAPEVLQKEVAYDFSvDWFALGCMLYEMI 189
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
637-841 1.51e-10

Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of RIP4, ankyrin (ANK) repeat and kinase domain containing 1 (ANKK1), and similar proteins, all of which harbor C-terminal ANK repeats. RIP4, also called Protein Kinase C-associated kinase (PKK), regulates keratinocyte differentiation and cutaneous inflammation. It activates NF-kappaB and is important in the survival of diffuse large B-cell lymphoma cells. The ANKK1 protein, also called PKK2, has not been studied extensively. The ANKK1 gene, located less than 10kb downstream of the D2 dopamine receptor (DRD2) locus, is altered in the Taq1 A1 polymorphism, which is related to a reduced DRD2 binding affinity and consequently, to mental disorders. The RIP4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 63.28  E-value: 1.51e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  637 EAASMMRQVSHKHIVYLYGVCVRDVENIMveEFVEGGPLDLFMhrKSDVLTTPWKFKVAKQLASALSYLE--DKDLVHGN 714
Cdd:cd14025     44 EEAKKMEMAKFRHILPVYGICSEPVGLVM--EYMETGSLEKLL--ASEPLPWELRFRIIHETAVGMNFLHcmKPPLLHLD 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  715 VCTKNLLLaregiDSECgpFIKLSDPG-IPITVLSRQECIER------IPWIAPECV-EDSKNLSVAADKWSFGTTLWEI 786
Cdd:cd14025    120 LKPANILL-----DAHY--HVKISDFGlAKWNGLSHSHDLSRdglrgtIAYLPPERFkEKNRCPDTKHDVYSFAIVIWGI 192
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1013071061  787 C-----YNGE-----IPLKDKTLIEKERFYESRCRPvtPSCKELADLMTRCMNYDPNQRPFFRAI 841
Cdd:cd14025    193 LtqkkpFAGEnnilhIMVKVVKGHRPSLSPIPRQRP--SECQQMICLMKRCWDQDPRKRPTFQDI 255
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
875-1075 1.54e-10

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK4 has a limited tissue distribution. It is mainly found in the testis, but is also present in the cerebellum and kidney. It is expressed as multiple splice variants with different domain architectures and is post-translationally palmitoylated and localized in the membrane. GRK4 polymorphisms are associated with hypertension and salt sensitivity, as they cause hyperphosphorylation, desensitization, and internalization of the dopamine 1 (D1) receptor while increasing the expression of the angiotensin II type 1 receptor. GRK4 plays a crucial role in the D1 receptor regulation of sodium excretion and blood pressure. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 63.47  E-value: 1.54e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  875 LKRIRDLGEGHFGKVELCRYDPegdnTGEQVAVKSLKPES----GGNHIAdlKKEIEILRNLYHENIVKYKgiCTEDGGN 950
Cdd:cd05631      2 FRHYRVLGKGGFGEVCACQVRA----TGKMYACKKLEKKRikkrKGEAMA--LNEKRILEKVNSRFVVSLA--YAYETKD 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  951 GIKLIMEFLPSGSLKEYLPKNKNK-INLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIe 1029
Cdd:cd05631     74 ALCLVLTIMNGGDLKFHIYNMGNPgFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVQI- 152
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1013071061 1030 tdKEYYTVKdDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd05631    153 --PEGETVR-GRVGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMI 195
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
635-845 1.56e-10

Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TNNI3K, also called cardiac ankyrin repeat kinase (CARK), is a cardiac-specific troponin I-interacting kinase that promotes cardiac myogenesis, improves cardiac performance, and protects the myocardium from ischemic injury. It contains N-terminal ankyrin repeats, a catalytic kinase domain, and a C-terminal serine-rich domain. TNNI3K exerts a disease-accelerating effect on cardiac dysfunction and reduced survival in mouse models of cardiomyopathy. The TNNI3K subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270966 [Multi-domain]  Cd Length: 254  Bit Score: 62.93  E-value: 1.56e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  635 FFEAASMMRQVSHKHIVYLYGVCVRDVENI-MVEEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLED--KDLV 711
Cdd:cd14064     38 FCREVSILCRLNHPCVIQFVGACLDDPSQFaIVTQYVSGGSLFSLLHEQKRVIDLQSKLIIAVDVAKGMEYLHNltQPII 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  712 HGNVCTKNLLLAREGidsecgpFIKLSDPGIPITVLSRQE-CIERIP----WIAPECVEDSKNLSVAADKWSFGTTLWEI 786
Cdd:cd14064    118 HRDLNSHNILLYEDG-------HAVVADFGESRFLQSLDEdNMTKQPgnlrWMAPEVFTQCTRYSIKADVFSYALCLWEL 190
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1013071061  787 cYNGEIPLKD-KTLIEKERFYESRCRPVTPSC--KELADLMTRCMNYDPNQRPFFRAIMRDI 845
Cdd:cd14064    191 -LTGEIPFAHlKPAAAAADMAYHHIRPPIGYSipKPISSLLMRGWNAEPESRPSFVEIVALL 251
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
922-1075 1.68e-10

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK2, also called Snk (serum-inducible kinase), functions in G1 progression, S-phase arrest, and centriole duplication. Its gene is responsive to both growth factors and cellular stress, is a transcriptional target of p53, and activates a G2-M checkpoint. The PLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271090 [Multi-domain]  Cd Length: 255  Bit Score: 62.72  E-value: 1.68e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  922 LKKEIEILRNLYHENIVKYKGIcTEDGGNgIKLIMEFLPSGSLKEYLpKNKNKINLKQQLKYAVQICKGMDYLGSRQYVH 1001
Cdd:cd14188     48 IDKEIELHRILHHKHVVQFYHY-FEDKEN-IYILLEYCSRRSMAHIL-KARKVLTEPEVRYYLRQIVSGLKYLHEQEILH 124
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1013071061 1002 RDLAARNVLVESEHQVKIGDFGLTKAIE-TDKEYYTVKDDRDspvfWYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd14188    125 RDLKLGNFFINENMELKVGDFGLAARLEpLEHRRRTICGTPN----YLSPEVLNKQGHGCESDIWALGCVMYTML 195
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
629-836 1.72e-10

Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: GCN2, protein kinase regulated by RNA (PKR), heme-regulated inhibitor kinase (HRI), and PKR-like endoplasmic reticulum kinase (PERK). GCN2 is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kappaB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. The degenerate pseudokinase domain of GCN2 may function as a regulatory domain. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 62.76  E-value: 1.72e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  629 RDISLAFFEAASMMrQVSHKHIVYLYGVCVRDVENI------MVEEFVEGGPLdlfmhrkSDVLTTPWKFKVAK------ 696
Cdd:cd14012     40 KQIQLLEKELESLK-KLRHPNLVSYLAFSIERRGRSdgwkvyLLTEYAPGGSL-------SELLDSVGSVPLDTarrwtl 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  697 QLASALSYLEDKDLVHGNVCTKNLLLAREGIDSECgpfiKLSDPGIPITVLS-----RQECIERIPWIAPECVEDSKNLS 771
Cdd:cd14012    112 QLLEALEYLHRNGVVHKSLHAGNVLLDRDAGTGIV----KLTDYSLGKTLLDmcsrgSLDEFKQTYWLPPELAQGSKSPT 187
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1013071061  772 VAADKWSFGTTLWEICYNGEIPLKDKTLIEkerFYESRCRPvtpscKELADLMTRCMNYDPNQRP 836
Cdd:cd14012    188 RKTDVWDLGLLFLQMLFGLDVLEKYTSPNP---VLVSLDLS-----ASLQDFLSKCLSLDPKKRP 244
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
986-1075 1.81e-10

Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NLK is an atypical mitogen-activated protein kinase (MAPK) that is not regulated by a MAPK kinase. It functions downstream of the MAPK kinase kinase Tak1, which also plays a role in activating the JNK and p38 MAPKs. The Tak1/NLK pathways are regulated by Wnts, a family of secreted proteins that is critical in the control of asymmetric division and cell polarity. NLK can phosphorylate transcription factors from the TCF/LEF family, inhibiting their ability to activate the transcription of target genes. In prostate cancer cells, NLK is involved in regulating androgen receptor-mediated transcription and its expression is altered during cancer progression. MAPKs are important mediators of cellular responses to extracellular signals. The NLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 63.99  E-value: 1.81e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  986 QICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYTVKDDRDSpvFWYAPECLMQSKFYI-ASDV 1064
Cdd:cd07853    111 QILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLARVEEPDESKHMTQEVVTQ--YYRAPEILMGSRHYTsAVDI 188
                           90
                   ....*....|.
gi 1013071061 1065 WSFGVTLHELL 1075
Cdd:cd07853    189 WSVGCIFAELL 199
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
642-848 1.91e-10

Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. CSF-1R, also called c-Fms, is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of CSF-1R to its ligand, CSF-1, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. It leads to increases in gene transcription and protein translation, and induces cytoskeletal remodeling. CSF-1R signaling leads to a variety of cellular responses including survival, proliferation, and differentiation of target cells. It plays an important role in innate immunity, tissue development and function, and the pathogenesis of some diseases including atherosclerosis and cancer. CSF-1R signaling is also implicated in mammary gland development during pregnancy and lactation. Aberrant CSF-1/CSF-1R expression correlates with tumor cell invasiveness, poor clinical prognosis, and bone metastasis in breast cancer. Although the structure of the human CSF-1R catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. The CSF-1R subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133237 [Multi-domain]  Cd Length: 374  Bit Score: 64.10  E-value: 1.91e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  642 MRQVSHKHIVYLYGVCVRDVENIMveefveggPLDLfmhrkSDVLttpwkfKVAKQLASALSYLEDKDLVHGNVCTKNLL 721
Cdd:cd05106    184 MRPVSSSSSQSSDSKDEEDTEDSW--------PLDL-----DDLL------RFSSQVAQGMDFLASKNCIHRDVAARNVL 244
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  722 LARegidsecGPFIKLSDPGIPITVLSRQECI----ERIP--WIAPECVEDSKnLSVAADKWSFGTTLWEICYNGEIPLk 795
Cdd:cd05106    245 LTD-------GRVAKICDFGLARDIMNDSNYVvkgnARLPvkWMAPESIFDCV-YTVQSDVWSYGILLWEIFSLGKSPY- 315
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1013071061  796 dKTLIEKERFYESRCRPVTPSC-----KELADLMTRCMNYDPNQRPFFRAIMRDINKL 848
Cdd:cd05106    316 -PGILVNSKFYKMVKRGYQMSRpdfapPEIYSIMKMCWNLEPTERPTFSQISQLIQRQ 372
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
586-848 2.11e-10

Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. B-Raf activates ERK with the strongest magnitude, compared with other Raf kinases. Mice embryos deficient in B-Raf die around midgestation due to vascular hemorrhage caused by apoptotic endothelial cells. Mutations in B-Raf have been implicated in initiating tumorigenesis and tumor progression, and are found in malignant cutaneous melanoma, papillary thyroid cancer, as well as in ovarian and colorectal carcinomas. Most oncogenic B-Raf mutations are located at the activation loop of the kinase and surrounding regions; the V600E mutation accounts for around 90% of oncogenic mutations. The V600E mutant constitutively activates MEK, resulting in sustained activation of ERK. B-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The B-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 62.77  E-value: 2.11e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  586 GEHLGRGTRTHIYSGTlmdYKDDEGTSeekkikvILKVLDPSHRDISlAFFEAASMMRQVSHKHIVYLYGVCVRDvENIM 665
Cdd:cd14151     13 GQRIGSGSFGTVYKGK---WHGDVAVK-------MLNVTAPTPQQLQ-AFKNEVGVLRKTRHVNILLFMGYSTKP-QLAI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  666 VEEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGIPiT 745
Cdd:cd14151     81 VTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLT-------VKIGDFGLA-T 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  746 VLSR-------QECIERIPWIAPECV--EDSKNLSVAADKWSFGTTLWEIcYNGEIPL-----KDKTLIEKERFYES-RC 810
Cdd:cd14151    153 VKSRwsgshqfEQLSGSILWMAPEVIrmQDKNPYSFQSDVYAFGIVLYEL-MTGQLPYsninnRDQIIFMVGRGYLSpDL 231
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1013071061  811 RPVTPSC-KELADLMTRCMNYDPNQRPFFRAIMRDINKL 848
Cdd:cd14151    232 SKVRSNCpKAMKRLMAECLKKKRDERPLFPQILASIELL 270
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
618-843 2.16e-10

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek family is composed of 11 different mammalian members (Nek1-11) with similarity to the catalytic domain of Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants that were prevented from entering mitosis. Neks contain a conserved N-terminal catalytic domain and a more divergent C-terminal regulatory region of various sizes and structures. They are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270855 [Multi-domain]  Cd Length: 258  Bit Score: 62.48  E-value: 2.16e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  618 KVILKVLDPSH---RDISLAFFEAaSMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGplDLFMH----RKSDVLTTP- 689
Cdd:cd08215     27 LYVLKEIDLSNmseKEREEALNEV-KLLSKLKHPNIVKYYESFEENGKLCIVMEYADGG--DLAQKikkqKKKGQPFPEe 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  690 --WKFKVakQLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGIPITVLSRQECIERI---P-WIAPEC 763
Cdd:cd08215    104 qiLDWFV--QICLALKYLHSRKILHRDLKTQNIFLTKDGV-------VKLGDFGISKVLESTTDLAKTVvgtPyYLSPEL 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  764 VEDsKNLSVAADKWSFGTTLWEICyNGEIPLKDKTL------IEKERFyesrcRPVtPSC--KELADLMTRCMNYDPNQR 835
Cdd:cd08215    175 CEN-KPYNYKSDIWALGCVLYELC-TLKHPFEANNLpalvykIVKGQY-----PPI-PSQysSELRDLVNSMLQKDPEKR 246

                   ....*...
gi 1013071061  836 PFFRAIMR 843
Cdd:cd08215    247 PSANEILS 254
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
697-852 2.18e-10

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR3 (or Flt4) preferentially binds the ligands VEGFC and VEGFD. VEGFR3 is essential for lymphatic endothelial cell (EC) development and function. It has been shown to regulate adaptive immunity during corneal transplantation. VEGFR3 is upregulated on blood vascular ECs in pathological conditions such as vascular tumors and the periphery of solid tumors. It plays a role in cancer progression and lymph node metastasis. Missense mutations in the VEGFR3 gene are associated with primary human lymphedema. VEGFR3 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 63.46  E-value: 2.18e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  697 QLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGIPITVLSRQECIE----RIP--WIAPECVEDsKNL 770
Cdd:cd05102    180 QVARGMEFLASRKCIHRDLAARNILLSENNV-------VKICDFGLARDIYKDPDYVRkgsaRLPlkWMAPESIFD-KVY 251
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  771 SVAADKWSFGTTLWEICYNGEIPLKDKTLIEK--ERFYE-SRCRPVTPSCKELADLMTRCMNYDPNQRPFFRAIMRDINK 847
Cdd:cd05102    252 TTQSDVWSFGVLLWEIFSLGASPYPGVQINEEfcQRLKDgTRMRAPEYATPEIYRIMLSCWHGDPKERPTFSDLVEILGD 331

                   ....*
gi 1013071061  848 LEEQN 852
Cdd:cd05102    332 LLQEN 336
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
879-1076 2.37e-10

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 (also called STK17A) and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. Rabbit DRAK1 has been shown to induce apoptosis in osteoclasts and overexpressio of human DRAK1 induces apoptosis in cultured fibroblast cells. DRAK1 may be involved in apoptotic signaling. The DRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 62.65  E-value: 2.37e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGHFGKVELCRYDpegdNTGEQVAVKSL-KPESGGNHIADLKKEIEILR----NLYHENIVKYKGICTEdggngIK 953
Cdd:cd14197     15 RELGRGKFAVVRKCVEK----DSGKEFAAKFMrKRRKGQDCRMEIIHEIAVLElaqaNPWVINLHEVYETASE-----MI 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  954 LIMEFLPSGSLKEYLPKNKNKINLKQQLKYAV-QICKGMDYLGSRQYVHRDLAARNVLVESEH---QVKIGDFGLTKAIE 1029
Cdd:cd14197     86 LVLEYAAGGEIFNQCVADREEAFKEKDVKRLMkQILEGVSFLHNNNVVHLDLKPQNILLTSESplgDIKIVDFGLSRILK 165
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1013071061 1030 TDKEyytVKDDRDSPVFwYAPECLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd14197    166 NSEE---LREIMGTPEY-VAPEILSYEPISTATDMWSIGVLAYVMLT 208
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
586-844 2.41e-10

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK3 is represented in this cd. The SnRK3 group contains members also known as CBL-interacting protein kinase, salt overly sensitive 2, SOS3-interacting proteins and protein kinase S. These kinases interact with calcium-binding proteins such as SOS3, SCaBPs, and CBL proteins, and are involved in responses to salt stress and in sugar and ABA signaling. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271133 [Multi-domain]  Cd Length: 256  Bit Score: 62.42  E-value: 2.41e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  586 GEHLGRGTRTHIYSGtlmdyKDDEgTSEEKKIKVILKVLDPSHRdISLAFFEAASMMRQVSHKHIVYLYGVCVRDVENIM 665
Cdd:cd14663      5 GRTLGEGTFAKVKFA-----RNTK-TGESVAIKIIDKEQVAREG-MVEQIKREIAIMKLLRHPNIVELHEVMATKTKIFF 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  666 VEEFVEGGplDLFmhrksDVLTTPWKFK--VAK----QLASALSYLEDKDLVHGNVCTKNLLLAREGidsecgpFIKLSD 739
Cdd:cd14663     78 VMELVTGG--ELF-----SKIAKNGRLKedKARkyfqQLIDAVDYCHSRGVFHRDLKPENLLLDEDG-------NLKISD 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  740 PGIPITVLSRQE-------CieRIP-WIAPECVEDSKNLSVAADKWSFGTTLWeICYNGEIPLKDKTL------IEKERF 805
Cdd:cd14663    144 FGLSALSEQFRQdgllhttC--GTPnYVAPEVLARRGYDGAKADIWSCGVILF-VLLAGYLPFDDENLmalyrkIMKGEF 220
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1013071061  806 yesRCRPVTPscKELADLMTRCMNYDPNQRPFFRAIMRD 844
Cdd:cd14663    221 ---EYPRWFS--PGAKSLIKRILDPNPSTRITVEQIMAS 254
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
882-1077 2.41e-10

Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 62.53  E-value: 2.41e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  882 GEGHFGKVELCRydpeGDNTGEQVAVKSLKPESGGNHiaDLKKEIEILRNLYHENIVK-YKGICTEdggNGIKLIMEFLp 960
Cdd:cd14111     12 ARGRFGVIRRCR----ENATGKNFPAKIVPYQAEEKQ--GVLQEYEILKSLHHERIMAlHEAYITP---RYLVLIAEFC- 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  961 sgSLKEYLPKNKNKINLKQQ--LKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGltKAIETDKEYYTVK 1038
Cdd:cd14111     82 --SGKELLHSLIDRFRYSEDdvVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFG--SAQSFNPLSLRQL 157
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1013071061 1039 DDRDSPVFWYAPECLMQSKFYIASDVWSFGVtlhelLTY 1077
Cdd:cd14111    158 GRRTGTLEYMAPEMVKGEPVGPPADIWSIGV-----LTY 191
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
619-841 2.52e-10

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP1 harbors a C-terminal Death domain (DD), which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 can also recruit other kinases including MEKK1, MEKK3, and RIP3 through an intermediate domain (ID) that bears a RIP homotypic interaction motif (RHIM). RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accummulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. RIP kinases serve as essential sensors of cellular stress. The RIP1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 62.52  E-value: 2.52e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  619 VILKVL--DPSHRDISLAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSDVLTTpwKFKVAK 696
Cdd:cd14027     20 VVLKTVytGPNCIEHNEALLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKGNLMHVLKKVSVPLSV--KGRIIL 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  697 QLASALSYLEDKDLVHGNVCTKNLLLAREGidsecgpFIKLSDPGIPI----TVLSRQE-CIER------------IPWI 759
Cdd:cd14027     98 EIIEGMAYLHGKGVIHKDLKPENILVDNDF-------HIKIADLGLASfkmwSKLTKEEhNEQRevdgtakknagtLYYM 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  760 APECVEDSKNLSV-AADKWSFGTTLWEICYNGEiPLKDKtlIEKERFYESRC---RP----VTPSC-KELADLMTRCMNY 830
Cdd:cd14027    171 APEHLNDVNAKPTeKSDVYSFAIVLWAIFANKE-PYENA--INEDQIIMCIKsgnRPdvddITEYCpREIIDLMKLCWEA 247
                          250
                   ....*....|.
gi 1013071061  831 DPNQRPFFRAI 841
Cdd:cd14027    248 NPEARPTFPGI 258
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
639-843 2.54e-10

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii FA2 was discovered in a genetic screen for deflagellation-defective mutants. It is essential for basal-body/centriole-associated microtubule severing, and plays a role in cell cycle progression. No cellular function has yet been ascribed to CNK4. The Chlamydomonas reinhardtii FA2-like subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily contains FA2 and CNK4. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 62.43  E-value: 2.54e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  639 ASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKsdvLTTP------WKFKVakQLASALSYLEDKDLVH 712
Cdd:cd08529     50 ARVLSKLNSPYVIKYYDSFVDKGKLNIVMEYAENGDLHSLIKSQ---RGRPlpedqiWKFFI--QTLLGLSHLHSKKILH 124
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  713 GNVCTKNLLLAREGIdsecgpfIKLSDPGIPiTVLSRQ----ECIERIP-WIAPECVEDsKNLSVAADKWSFGTTLWEIC 787
Cdd:cd08529    125 RDIKSMNIFLDKGDN-------VKIGDLGVA-KILSDTtnfaQTIVGTPyYLSPELCED-KPYNEKSDVWALGCVLYELC 195
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  788 yNGEIPLKDKT---LIEKerFYESRCRPV-TPSCKELADLMTRCMNYDPNQRPFFRAIMR 843
Cdd:cd08529    196 -TGKHPFEAQNqgaLILK--IVRGKYPPIsASYSQDLSQLIDSCLTKDYRQRPDTTELLR 252
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
615-836 2.60e-10

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. PAK deregulation is associated with tumor development. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). Group II PAKs contain a PBD and a catalytic domain, but lack other motifs found in group I PAKs. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. Group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX; no such binding has been demonstrated for group II PAKs. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270789 [Multi-domain]  Cd Length: 255  Bit Score: 62.23  E-value: 2.60e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  615 KKIKVILKVLDPSHRDISLAFFEAaSMMRQVSHKHIVYLYGvCVRDVENI-MVEEFVEGGPLdlfmhrkSDVLT-TPWKF 692
Cdd:cd06614     24 TGKEVAIKKMRLRKQNKELIINEI-LIMKECKHPNIVDYYD-SYLVGDELwVVMEYMDGGSL-------TDIITqNPVRM 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  693 K------VAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGIPITVLSRQEciER-----IP-WIA 760
Cdd:cd06614     95 NesqiayVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGS-------VKLADFGFAAQLTKEKS--KRnsvvgTPyWMA 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  761 PECVEdSKNLSVAADKWSFGTTLWEIC-----YNGEIPLKDKTLIEKE---RFYESRcrpvtPSCKELADLMTRCMNYDP 832
Cdd:cd06614    166 PEVIK-RKDYGPKVDIWSLGIMCIEMAegeppYLEEPPLRALFLITTKgipPLKNPE-----KWSPEFKDFLNKCLVKDP 239

                   ....
gi 1013071061  833 NQRP 836
Cdd:cd06614    240 EKRP 243
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
635-836 2.80e-10

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK1 is one of two vertebrate LRRKs which show complementary expression in the brain. It can form heterodimers with LRRK2, and may influence the age of onset of LRRK2-associated Parkinson's disease. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 62.67  E-value: 2.80e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  635 FFEAASMMRQVSHKHIVYLYGVCVRDV-----------ENIMVEEFVEGGPLDLFMHrksdVLTtpwkFKVAKQLASALS 703
Cdd:cd14067     57 FRQEASMLHSLQHPCIVYLIGISIHPLcfalelaplgsLNTVLEENHKGSSFMPLGH----MLT----FKIAYQIAAGLA 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  704 YLEDKDLVHGNVCTKNLLL----AREGIDsecgpfIKLSDPGIpitvlSRQECIE-----------RIPWIAPECVEDSK 768
Cdd:cd14067    129 YLHKKNIIFCDLKSDNILVwsldVQEHIN------IKLSDYGI-----SRQSFHEgalgvegtpgyQAPEIRPRIVYDEK 197
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1013071061  769 nlsvaADKWSFGTTLWEIcYNGEIPLKDKTLIEKERFYESRCRPVTPSCKE-----LADLMTRCMNYDPNQRP 836
Cdd:cd14067    198 -----VDMFSYGMVLYEL-LSGQRPSLGHHQLQIAKKLSKGIRPVLGQPEEvqffrLQALMMECWDTKPEKRP 264
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
640-850 2.81e-10

Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This group is composed of uncharacterized proteins with similarity to LIMK and Testicular or testis-specific protein kinase (TESK). LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 62.15  E-value: 2.81e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  640 SMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKN 719
Cdd:cd14156     40 SLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGCLEELLAREELPLSWREKVELACDISRGMVYLHSKNIYHRDLNSKN 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  720 LLL-----AREGIDSECGPFIKLSDpgIPITVLSRQ-ECIERIPWIAPECVEdSKNLSVAADKWSFGTTLWEICynGEIP 793
Cdd:cd14156    120 CLIrvtprGREAVVTDFGLAREVGE--MPANDPERKlSLVGSAFWMAPEMLR-GEPYDRKVDVFSFGIVLCEIL--ARIP 194
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1013071061  794 LKDKTLIEKERF------YESRCrpvtPSCKE-LADLMTRCMNYDPNQRPFFRAIMRDINKLEE 850
Cdd:cd14156    195 ADPEVLPRTGDFgldvqaFKEMV----PGCPEpFLDLAASCCRMDAFKRPSFAELLDELEDIAE 254
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
875-1147 2.84e-10

Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Polymyxin B resistance protein 2 (PBS2) from Saccharomyces cerevisiae, Wis1 from Schizosaccharomyces pombe, and related proteins. PBS2 and Wis1 are components of stress-activated MAPK cascades in budding and fission yeast, respectively. PBS2 is the specific activator of the MAPK Hog1, which plays a central role in the response of budding yeast to stress including exposure to arsenite and hyperosmotic environments. Wis1 phosphorylates and activates the MAPK Sty1 (also called Spc1 or Phh1), which stimulates a transcriptional response to a wide range of cellular insults through the bZip transcription factors Atf1, Pcr1, and Pap1. The PBS2 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 62.56  E-value: 2.84e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  875 LKRIRDLGEGHFGKVELCRYDPegdnTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGngIKL 954
Cdd:cd06622      3 IEVLDELGKGNYGSVYKVLHRP----TGVTMAMKEIRLELDESKFNQIIMELDILHKAVSPYIVDFYGAFFIEGA--VYM 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPSGSL-KEYLPKNKNKINLKQQL-KYAVQICKGMDYLGSR-QYVHRDLAARNVLVESEHQVKIGDFGLTKAIETd 1031
Cdd:cd06622     77 CMEYMDAGSLdKLYAGGVATEGIPEDVLrRITYAVVKGLKFLKEEhNIIHRDVKPTNVLVNGNGQVKLCDFGVSGNLVA- 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1032 keyyTVKDDRDSPVFWYAPECLM------QSKFYIASDVWSFGVTLHELLTYCdsdsSPMalflkmigPTHGQMTVTRLV 1105
Cdd:cd06622    156 ----SLAKTNIGCQSYMAPERIKsggpnqNPTYTVQSDVWSLGLSILEMALGR----YPY--------PPETYANIFAQL 219
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1013071061 1106 NTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIE 1147
Cdd:cd06622    220 SAIVDGDPPTLPSGYSDDAQDFVAKCLNKIPNRRPTYAQLLE 261
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
878-1076 2.88e-10

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Cdc7 kinase (or Hsk1 in fission yeast) is a critical regulator in the initiation of DNA replication. It forms a complex with a Dbf4-related regulatory subunit, a cyclin-like molecule that activates the kinase in late G1 phase, and is also referred to as Dbf4-dependent kinase (DDK). Its main targets are mini-chromosome maintenance (MCM) proteins. Cdc7 kinase may also have additional roles in meiosis, checkpoint responses, the maintenance and repair of chromosome structures, and cancer progression. The Cdc7 kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 62.24  E-value: 2.88e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKV---ELCRYDPEGDNTGEQVAVKSLKPESGGNHIADlkkEIEILRNLY-HENIVKYKGiCTEDGGNgIK 953
Cdd:cd14019      6 IEKIGEGTFSSVykaEDKLHDLYDRNKGRLVALKHIYPTSSPSRILN---ELECLERLGgSNNVSGLIT-AFRNEDQ-VV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  954 LIMEFLPSGSLKEYLpknkNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVL--VESEHQVKIgDFGLTKAIETD 1031
Cdd:cd14019     81 AVLPYIEHDDFRDFY----RKMSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLynRETGKGVLV-DFGLAQREEDR 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1013071061 1032 KEyytVKDDRDSPVFWYAPECLM----QSkfyIASDVWSFGVTLHELLT 1076
Cdd:cd14019    156 PE---QRAPRAGTRGFRAPEVLFkcphQT---TAIDIWSAGVILLSILS 198
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
881-1139 3.10e-10

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270892 [Multi-domain]  Cd Length: 279  Bit Score: 62.34  E-value: 3.10e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVelcrYDPEGDNTGEQVAVK------SLKPESGGNHIADLKKEIEILRNLYHENIVK-YKgiCTEDGGNGIK 953
Cdd:cd13990      8 LGKGGFSEV----YKAFDLVEQRYVACKihqlnkDWSEEKKQNYIKHALREYEIHKSLDHPRIVKlYD--VFEIDTDSFC 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  954 LIMEFLPSGSLKEYLPKNKNkINLKQQLKYAVQICKGMDYLGSRQ--YVHRDLAARNVLVESEHQ---VKIGDFGLTKAI 1028
Cdd:cd13990     82 TVLEYCDGNDLDFYLKQHKS-IPEREARSIIMQVVSALKYLNEIKppIIHYDLKPGNILLHSGNVsgeIKITDFGLSKIM 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1029 EtDKEYYTVKDDRDSP---VFWY-APECLMQSKFY--IAS--DVWSFGVTLHELltycdsdsspmaLFLKMigP-THGQM 1099
Cdd:cd13990    161 D-DESYNSDGMELTSQgagTYWYlPPECFVVGKTPpkISSkvDVWSVGVIFYQM------------LYGRK--PfGHNQS 225
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1013071061 1100 TVTRL-VNTLKEGKRL--PCPPNCPDEVYQLMRKCWEFQPSNR 1139
Cdd:cd13990    226 QEAILeENTILKATEVefPSKPVVSSEAKDFIRRCLTYRKEDR 268
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
879-1075 3.13e-10

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type IV; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKIV is found predominantly in neurons and immune cells. It is activated by the binding of calcium/CaM and phosphorylation by CaMKK (alpha or beta). The CaMKK-CaMKIV cascade participates in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors. It also is implicated in T-cell development and signaling, cytokine secretion, and signaling through Toll-like receptors, and is thus, pivotal in immune response and inflammation. The CaMKIV subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270987 [Multi-domain]  Cd Length: 294  Bit Score: 62.54  E-value: 3.13e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGHFGKVELCRYDpegdNTGEQVAVKSLKpesggnHIADLK---KEIEILRNLYHENIVKYKGICTEDggNGIKLI 955
Cdd:cd14085      9 SELGRGATSVVYRCRQK----GTQKPYAVKKLK------KTVDKKivrTEIGVLLRLSHPNIIKLKEIFETP--TEISLV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  956 MEFLPSGSLKEYLPKnKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQ---VKIGDFGLTKAIETDK 1032
Cdd:cd14085     77 LELVTGGELFDRIVE-KGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPdapLKIADFGLSKIVDQQV 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1013071061 1033 EYYTVKddrDSPVFWyAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd14085    156 TMKTVC---GTPGYC-APEILRGCAYGPEVDMWSVGVITYILL 194
PK_STRAD_alpha cd08227
Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain ...
889-1074 3.18e-10

Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha, stabilized through ATP and MO25, may be needed to activate LKB1. A mutation which results in a truncation of a C-terminal part of the human STRAD-alpha pseudokinase domain and disrupts its association with LKB1, leads to PMSE (polyhydramnios, megalencephaly, symptomatic epilepsy) syndrome. Several splice variants of STRAD-alpha exist which exhibit different effects on the localization and activation of LKB1. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. The STRAD alpha subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173767 [Multi-domain]  Cd Length: 327  Bit Score: 63.04  E-value: 3.18e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  889 VELCRYDPegdnTGEQVAVKSLKPESGGNHIAD-LKKEIEILRNLYHENIVKYKGICTEDggNGIKLIMEFLPSGSLKEY 967
Cdd:cd08227     16 VNLARYKP----TGEYVTVRRINLEACTNEMVTfLQGELHVSKLFNHPNIVPYRATFIAD--NELWVVTSFMAYGSAKDL 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  968 LPKNKNKINLKQQLKYAVQ-ICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGdfGLTKAIETDKEYYTVKDDRDSPVF 1046
Cdd:cd08227     90 ICTHFMDGMSELAIAYILQgVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNLSMINHGQRLRVVHDFPKY 167
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1013071061 1047 ------WYAPECLMQS-KFYIA-SDVWSFGVTLHEL 1074
Cdd:cd08227    168 svkvlpWLSPEVLQQNlQGYDAkSDIYSVGITACEL 203
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
881-1075 3.20e-10

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK2 shows a more restricted distribution than SGK1 and is most abundantly expressed in epithelial tissues including kidney, liver, pancreas, and the choroid plexus of the brain. In vitro cellular assays show that SGK2 can stimulate the activity of ion channels, the glutamate transporter EEAT4, and the glutamate receptors, GluR6 and GLUR1. The SGK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270754 [Multi-domain]  Cd Length: 321  Bit Score: 63.06  E-value: 3.20e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYdpEGDNTGEQVAV---KSLKPESGGNHIadLKKEIEILRNLYHENIV--KYKGICTEDggngIKLI 955
Cdd:cd05603      3 IGKGSFGKVLLAKR--KCDGKFYAVKVlqkKTILKKKEQNHI--MAERNVLLKNLKHPFLVglHYSFQTSEK----LYFV 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  956 MEFLPSGSLKEYLPKNKNKINLKQQLkYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTK-AIETDKEY 1034
Cdd:cd05603     75 LDYVNGGELFFHLQRERCFLEPRARF-YAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKeGMEPEETT 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1013071061 1035 YTVKDDRDspvfWYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd05603    154 STFCGTPE----YLAPEVLRKEPYDRTVDWWCLGAVLYEML 190
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
863-1076 3.35e-10

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 64.12  E-value: 3.35e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  863 TEVDPTHFEKRFLKRIrdLGEGHFGKVeLCrydPEGDNTGEQVAVKSLKPEsgGNHIADLKK---EIEILRNLYHENIVK 939
Cdd:PTZ00283    24 EATAKEQAKKYWISRV--LGSGATGTV-LC---AKRVSDGEPFAVKVVDME--GMSEADKNRaqaEVCCLLNCDFFSIVK 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  940 ------YKGICTEDGGNGIKLIMEFLPSGSLKEYLpKNKNKINLKQQLKYA----VQICKGMDYLGSRQYVHRDLAARNV 1009
Cdd:PTZ00283    96 chedfaKKDPRNPENVLMIALVLDYANAGDLRQEI-KSRAKTNRTFREHEAgllfIQVLLAVHHVHSKHMIHRDIKSANI 174
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1013071061 1010 LVESEHQVKIGDFGLTKAIETdkeyyTVKDDR-----DSPvFWYAPECLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:PTZ00283   175 LLCSNGLVKLGDFGFSKMYAA-----TVSDDVgrtfcGTP-YYVAPEIWRRKPYSKKADMFSLGVLLYELLT 240
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
609-808 3.38e-10

Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK33 is highly expressed in the testis and is present in low levels in most tissues. It may be involved in spermatogenesis and organ ontogenesis. It interacts with and phosphorylates vimentin and may be involved in regulating intermediate filament cytoskeletal dynamics. Its role in promoting the cell viability of KRAS-dependent cancer cells is under debate; some studies have found STK33 to promote cancer cell viability, while other studies have found it to be non-essential. KRAS is the most commonly mutated human oncogene, thus, studies on the role of STK33 in KRAS mutant cancer cells are important. The STK33 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 62.18  E-value: 3.38e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  609 EGTSEEKKIK-VILKVLDPSHRDISLAFFE-AASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSdVL 686
Cdd:cd14097     19 EATHKETQTKwAIKKINREKAGSSAVKLLErEVDILKHVNHAHIIHLEEVFETPKRMYLVMELCEDGELKELLLRKG-FF 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  687 TTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIDSECGPFIKLSDPGIPITVLSR-----QECIERIPWIAP 761
Cdd:cd14097     98 SENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSIIDNNDKLNIKVTDFGLSVQKYGLgedmlQETCGTPIYMAP 177
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1013071061  762 EcVEDSKNLSVAADKWSFGTTLWeICYNGEIPLKDKTlieKERFYES 808
Cdd:cd14097    178 E-VISAHGYSQQCDIWSIGVIMY-MLLCGEPPFVAKS---EEKLFEE 219
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
874-1092 3.77e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 63.94  E-value: 3.77e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  874 FLKRIR---DLGEGHFGKVELC---RYDPEGDNTGEQVAVKSLKPES----------GGNHIADLKKEIEILRNLYHENI 937
Cdd:PHA03210   146 FLAHFRvidDLPAGAFGKIFICalrASTEEAEARRGVNSTNQGKPKCerliakrvkaGSRAAIQLENEILALGRLNHENI 225
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  938 VKYKGIC-TEDGGNGIKLIMEFlpsgSLKEYLPKN----KNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVE 1012
Cdd:PHA03210   226 LKIEEILrSEANTYMITQKYDF----DLYSFMYDEafdwKDRPLLKQTRAIMKQLLCAVEYIHDKKLIHRDIKLENIFLN 301
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1013 SEHQVKIGDFGLTKAIETDKEYY------TVKDDrdspvfwyAPECLMQSKFYIASDVWSFGVTL-----HELLTYCDSD 1081
Cdd:PHA03210   302 CDGKIVLGDFGTAMPFEKEREAFdygwvgTVATN--------SPEILAGDGYCEITDIWSCGLILldmlsHDFCPIGDGG 373
                          250
                   ....*....|.
gi 1013071061 1082 SSPMALFLKMI 1092
Cdd:PHA03210   374 GKPGKQLLKII 384
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
901-1095 3.83e-10

Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. There are two forms of STRAD, alpha and beta, that complex with LKB1 and MO25. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha stabilized through ATP and MO25 may be needed to activate LKB1. The STRAD subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 62.70  E-value: 3.83e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  901 TGEQVAVKSLKPESGGNhiADLK---KEIEILRNLYHENIVKYkgICTEDGGNGIKLIMEFLPSGS----LKEYLPKNKN 973
Cdd:cd08216     24 TNTLVAVKKINLESDSK--EDLKflqQEILTSRQLQHPNILPY--VTSFVVDNDLYVVTPLMAYGScrdlLKTHFPEGLP 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  974 KINLKQQLKYAVQickGMDYLGSRQYVHRDLAARNVLVESEHQVKIGdfGLTKAIETDKEYYTVKDDRDSPVF------W 1047
Cdd:cd08216    100 ELAIAFILRDVLN---ALEYIHSKGYIHRSVKASHILISGDGKVVLS--GLRYAYSMVKHGKRQRVVHDFPKSseknlpW 174
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1013071061 1048 YAPECLMQS-KFYIA-SDVWSFGVTLHEL----LTYCDSDSSPMaLFLKMIGPT 1095
Cdd:cd08216    175 LSPEVLQQNlLGYNEkSDIYSVGITACELangvVPFSDMPATQM-LLEKVRGTT 227
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
867-1075 4.13e-10

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK1 is ubiquitously expressed and is under transcriptional control of numerous stimuli including cell stress (cell shrinkage), serum, hormones (gluco- and mineralocorticoids), gonadotropins, growth factors, interleukin-6, and other cytokines. It plays roles in sodium retention and potassium elimination in the kidney, nutrient transport, salt sensitivity, memory consolidation, and cardiac repolarization. A common SGK1 variant is associated with increased blood pressure and body weight. SGK1 may also contribute to tumor growth, neurodegeneration, fibrosing disease, and ischemia. The SGK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270753 [Multi-domain]  Cd Length: 339  Bit Score: 62.73  E-value: 4.13e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  867 PTHFEkrFLKRIrdlGEGHFGKVELCRYDPEGdntgEQVAVKSLKPEsggnhiADLKKEIE---------ILRNLYHENI 937
Cdd:cd05602      6 PSDFH--FLKVI---GKGSFGKVLLARHKSDE----KFYAVKVLQKK------AILKKKEEkhimsernvLLKNVKHPFL 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  938 VK-YKGICTEDGgngIKLIMEFLPSGSLKEYLPKNKNKINLKQQLkYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQ 1016
Cdd:cd05602     71 VGlHFSFQTTDK---LYFVLDYINGGELFYHLQRERCFLEPRARF-YAAEIASALGYLHSLNIVYRDLKPENILLDSQGH 146
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1013071061 1017 VKIGDFGLTKaiETDKEYYTVKDDRDSPVFwYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd05602    147 IVLTDFGLCK--ENIEPNGTTSTFCGTPEY-LAPEVLHKQPYDRTVDWWCLGAVLYEML 202
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
881-1078 4.17e-10

Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CASK belongs to the MAGUK (membrane-associated guanylate kinase) protein family, which functions as multiple domain adaptor proteins and is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The enzymatically inactive GuK domain in MAGUK proteins mediates protein-protein interactions and associates intramolecularly with the SH3 domain. In addition, CASK contains a catalytic kinase and two L27 domains. It is highly expressed in the nervous system and plays roles in synaptic protein targeting, neural development, and regulation of gene expression. Binding partners include parkin (a Parkinson's disease molecule), neurexin (adhesion molecule), syndecans, calcium channel proteins, CINAP (nucleosome assembly protein), transcription factor Tbr-1, and the cytoplasmic adaptor proteins Mint1, Veli/mLIN-7/MALS, SAP97, caskin, and CIP98. Deletion or mutations in the CASK gene have been implicated in X-linked mental retardation. The CASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 62.17  E-value: 4.17e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDPegdnTGEQVAVKSLK----PESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGngIKLIM 956
Cdd:cd14094     11 IGKGPFSVVRRCIHRE----TGQQFAVKIVDvakfTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGM--LYMVF 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  957 EFLPSGSLK-EYLPKNKNKINLKQQL--KYAVQICKGMDYLGSRQYVHRDLAARNVL---VESEHQVKIGDFGLTKAIet 1030
Cdd:cd14094     85 EFMDGADLCfEIVKRADAGFVYSEAVasHYMRQILEALRYCHDNNIIHRDVKPHCVLlasKENSAPVKLGGFGVAIQL-- 162
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1013071061 1031 dKEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYC 1078
Cdd:cd14094    163 -GESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGC 209
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
954-1093 4.42e-10

Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine/threonine kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. There are four mammalian MAST kinases, named MAST1-MAST4. MAST1 is also called syntrophin-associated STK (SAST) while MAST2 is also called MAST205. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MAST1, MAST2, and MAST3 bind and phosphorylate the tumor suppressor PTEN, and may contribute to the regulation and stabilization of PTEN. MAST2 is involved in the regulation of the Fc-gamma receptor of the innate immune response in macrophages, and may also be involved in the regulation of the Na+/H+ exchanger NHE3. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 62.04  E-value: 4.42e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  954 LIMEFLPSGSLKEYLpKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKA--IETD 1031
Cdd:cd05609     77 MVMEYVEGGDCATLL-KNIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLSKIglMSLT 155
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1013071061 1032 KEYYTVKDDRDSPVF----------WYAPECLMQSKFYIASDVWSFGVTLHELLTYCDS--DSSPMALFLKMIG 1093
Cdd:cd05609    156 TNLYEGHIEKDTREFldkqvcgtpeYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPffGDTPEELFGQVIS 229
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
611-844 4.53e-10

Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MARKs, also called Partitioning-defective 1 (Par1) proteins, function as regulators of diverse cellular processes in nematodes, Drosophila, yeast, and vertebrates. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. Vertebrates contain four isoforms, namely MARK1 (or Par1c), MARK2 (or Par1b), MARK3 (Par1a), and MARK4 (or MARKL1). Known substrates of MARKs include the cell cycle-regulating phosphatase Cdc25, tyrosine phosphatase PTPH1, MAPK scaffolding protein KSR1, class IIa histone deacetylases, and plakophilin 2. The MARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270974 [Multi-domain]  Cd Length: 253  Bit Score: 61.38  E-value: 4.53e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  611 TSEEKKIKVILKV-LDPSHRDislAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPL--DLFMHRKSDVLT 687
Cdd:cd14072     24 TGREVAIKIIDKTqLNPSSLQ---KLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEYASGGEVfdYLVAHGRMKEKE 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  688 TPWKFKvakQLASALSYLEDKDLVHGNVCTKNLLLaregiDSECGpfIKLSDPGIPITVLSRQE----CiERIPWIAPEC 763
Cdd:cd14072    101 ARAKFR---QIVSAVQYCHQKRIVHRDLKAENLLL-----DADMN--IKIADFGFSNEFTPGNKldtfC-GSPPYAAPEL 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  764 VEDSKNLSVAADKWSFGTTLWEICyNGEIPLKDKTLIE-KERFYESRCRPVTPSCKELADLMTRCMNYDPNQRPFFRAIM 842
Cdd:cd14072    170 FQGKKYDGPEVDVWSLGVILYTLV-SGSLPFDGQNLKElRERVLRGKYRIPFYMSTDCENLLKKFLVLNPSKRGTLEQIM 248

                   ..
gi 1013071061  843 RD 844
Cdd:cd14072    249 KD 250
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
620-848 5.00e-10

Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. ILK contains N-terminal ankyrin repeats, a Pleckstrin Homology (PH) domain, and a C-terminal pseudokinase domain. It is a component of the IPP (ILK/PINCH/Parvin) complex that couples beta integrins to the actin cytoskeleton, and plays important roles in cell adhesion, spreading, invasion, and migration. ILK was initially thought to be an active kinase despite the lack of key conserved residues because of in vitro studies showing that it can phosphorylate certain protein substrates. However, in vivo experiments in Caenorhabditis elegans, Drosophila melanogaster, and mice (ILK-null and knock-in) proved that ILK is not an active kinase. In addition to actin cytoskeleton regulation, ILK also influences the microtubule network and mitotic spindle orientation. The pseudokinase domain of ILK binds several adaptor proteins including the parvins and paxillin. The ILK subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270959 [Multi-domain]  Cd Length: 251  Bit Score: 61.35  E-value: 5.00e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  620 ILKVLDPSHRdISLAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSD-VLTTPWKFKVAKQL 698
Cdd:cd14057     25 ILKVRDVTTR-ISRDFNEEYPRLRIFSHPNVLPVLGACNSPPNLVVISQYMPYGSLYNVLHEGTGvVVDQSQAVKFALDI 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  699 ASALSYLEDKD--LVHGNVCTKNLLlaregIDSECGPFIKLSDpgipiTVLSRQeCIERI---PWIAPECVE---DSKNL 770
Cdd:cd14057    104 ARGMAFLHTLEplIPRHHLNSKHVM-----IDEDMTARINMAD-----VKFSFQ-EPGKMynpAWMAPEALQkkpEDINR 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  771 SvAADKWSFGTTLWEICYNgEIPLKDKTLIE-KERFYESRCRPVTP--SCKELADLMTRCMNYDPNQRPFFRAIMRDINK 847
Cdd:cd14057    173 R-SADMWSFAILLWELVTR-EVPFADLSNMEiGMKIALEGLRVTIPpgISPHMCKLMKICMNEDPGKRPKFDMIVPILEK 250

                   .
gi 1013071061  848 L 848
Cdd:cd14057    251 M 251
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
586-836 5.04e-10

Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. TSSK6, also called SSTK, is expressed at the head of elongated sperm. TSSK1/TSSK2 double knock-out and TSSK6 null mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270982 [Multi-domain]  Cd Length: 262  Bit Score: 61.43  E-value: 5.04e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  586 GEHLGRGTrthiYSGTLMDYKDDEGTSEEKKIKVILKVLDPSH-------RDISlaffeaasMMRQVSHKHIVYLYGVCV 658
Cdd:cd14080      5 GKTIGEGS----YSKVKLAEYTKSGLKEKVACKIIDKKKAPKDflekflpRELE--------ILRKLRHPNIIQVYSIFE 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  659 RDVENIMVEEFVEGGplDLFMH-RKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLaregidseCGPF-IK 736
Cdd:cd14080     73 RGSKVFIFMEYAEHG--DLLEYiQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILL--------DSNNnVK 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  737 LSDPGI-------PITVLSRQECiERIPWIAPECVEDSKNLSVAADKWSFGTTLWeICYNGEIPLKD---KTLIEKE--- 803
Cdd:cd14080    143 LSDFGFarlcpddDGDVLSKTFC-GSAAYAAPEILQGIPYDPKKYDIWSLGVILY-IMLCGSMPFDDsniKKMLKDQqnr 220
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1013071061  804 --RFYESRcRPVTPSCKelaDLMTRCMNYDPNQRP 836
Cdd:cd14080    221 kvRFPSSV-KKLSPECK---DLIDQLLEPDPTKRA 251
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
584-836 5.24e-10

Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Saccharomyces cerevisiae Bck1 and Schizosaccharomyces pombe Mkh1, and related proteins. Budding yeast Bck1 is part of the cell integrity MAPK pathway, which is activated by stresses and aggressions to the cell wall. The MAPKKK Bck1, MAPKKs Mkk1 and Mkk2, and the MAPK Slt2 make up the cascade that is important in the maintenance of cell wall homeostasis. Fission yeast Mkh1 is involved in MAPK cascades regulating cell morphology, cell wall integrity, salt resistance, and filamentous growth in response to stress. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The Bck1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270799 [Multi-domain]  Cd Length: 270  Bit Score: 61.63  E-value: 5.24e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  584 VQGEHLGRGTRTHIY------SGTLMDYKDDE--GTSEEKKikvilkvlDPSHRDISLAFFEAASMMRQVSHKHIV-YLY 654
Cdd:cd06629      4 VKGELIGKGTYGRVYlamnatTGEMLAVKQVElpKTSSDRA--------DSRQKTVVDALKSEIDTLKDLDHPNIVqYLG 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  655 GVCVRDVENIMVEeFVEGGPLdlfmhrkSDVLTTPWKFK------VAKQLASALSYLEDKDLVHGNVCTKNLLLAREGId 728
Cdd:cd06629     76 FEETEDYFSIFLE-YVPGGSI-------GSCLRKYGKFEedlvrfFTRQILDGLAYLHSKGILHRDLKADNILVDLEGI- 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  729 seCgpfiKLSDPGIpitvlSRQE-----------CIERIPWIAPECVE-DSKNLSVAADKWSFGTTLWEICyNGEIPLKD 796
Cdd:cd06629    147 --C----KISDFGI-----SKKSddiygnngatsMQGSVFWMAPEVIHsQGQGYSAKVDIWSLGCVVLEML-AGRRPWSD 214
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1013071061  797 KTLIEK--ERFYESRCRPVTPS---CKELADLMTRCMNYDPNQRP 836
Cdd:cd06629    215 DEAIAAmfKLGNKRSAPPVPEDvnlSPEALDFLNACFAIDPRDRP 259
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
875-1075 5.33e-10

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR2 (also called STK38-like) plays a role in proper centrosome duplication. In addition, it is involved in regulating neuronal growth and differentiation, as well as in facilitating neurite outgrowth. NDR2 is also implicated in fear conditioning as it contributes to the coupling of neuronal morphological changes with fear-memory consolidation. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 62.77  E-value: 5.33e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  875 LKRIRDLGEGHFGKVELCrydpEGDNTGEQVAVKSLKPES--GGNHIADLKKEIEILRNLYHENIVKYKgICTEDGGNgI 952
Cdd:cd05627      4 FESLKVIGRGAFGEVRLV----QKKDTGHIYAMKILRKADmlEKEQVAHIRAERDILVEADGAWVVKMF-YSFQDKRN-L 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  953 KLIMEFLPSGSLKEYLPKnKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIET-- 1030
Cdd:cd05627     78 YLIMEFLPGGDMMTLLMK-KDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLCTGLKKah 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1013071061 1031 DKEYY-----------------------TVKDDRDSPVF-------WYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd05627    157 RTEFYrnlthnppsdfsfqnmnskrkaeTWKKNRRQLAYstvgtpdYIAPEVFMQTGYNKLCDWWSLGVIMYEML 231
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
881-1075 5.76e-10

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. The cPKC-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270766 [Multi-domain]  Cd Length: 341  Bit Score: 62.32  E-value: 5.76e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCrydpEGDNTGEQVAVKSLKpesggnhiadlkKEIEILRNLYHENIVKYKGICTEDGG----------- 949
Cdd:cd05615     18 LGKGSFGKVMLA----ERKGSDELYAIKILK------------KDVVIQDDDVECTMVEKRVLALQDKPpfltqlhscfq 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  950 --NGIKLIMEFLPSGSLKeYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKa 1027
Cdd:cd05615     82 tvDRLYFVMEYVNGGDLM-YHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCK- 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1013071061 1028 iETDKEYYTVKDDRDSPVFwYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd05615    160 -EHMVEGVTTRTFCGTPDY-IAPEIIAYQPYGRSVDWWAYGVLLYEML 205
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
635-838 6.55e-10

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK2 activation is induced by transforming growth factor-beta l (TGFb-l) and shares the same subcellular location as the cofilin family member twinfilin, which may be its biological substrate. LIMK2 plays a role in spermatogenesis, and may contribute to tumor progression and metastasis formation in some cancer cells. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 61.50  E-value: 6.55e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  635 FFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHrksDVLTTPWKFKV--AKQLASALSYLEDKDLVH 712
Cdd:cd14222     37 FLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGTLKDFLR---ADDPFPWQQKVsfAKGIASGMAYLHSMSIIH 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  713 GNVCTKNLLLAREGI----DSECGPFI----KLSDPGIPIT---VLSRQECIERIP------WIAPECVeDSKNLSVAAD 775
Cdd:cd14222    114 RDLNSHNCLIKLDKTvvvaDFGLSRLIveekKKPPPDKPTTkkrTLRKNDRKKRYTvvgnpyWMAPEML-NGKSYDEKVD 192
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1013071061  776 KWSFGTTLWEICynGEI-------------PLKDKTLIEKerFYESRCRPVtpsckeLADLMTRCMNYDPNQRPFF 838
Cdd:cd14222    193 IFSFGIVLCEII--GQVyadpdclprtldfGLNVRLFWEK--FVPKDCPPA------FFPLAAICCRLEPDSRPAF 258
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
881-1152 6.63e-10

Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK3 (or IRAK-M) is the only IRAK that does not show kinase activity. It is found only in monocytes and macrophages in humans, and functions as a negative regulator of TLR signaling including TLR-2 induced p38 activation. It also negatively regulates the alternative NFkB pathway in a TLR-2 specific manner. IRAK3 is downregulated in the monocytes of obese people, and is associated with high SOD2, a marker of mitochondrial oxidative stress. It is an important inhibitor of inflammation in association with obesity and metabolic syndrome. The IRAK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271062 [Multi-domain]  Cd Length: 276  Bit Score: 61.44  E-value: 6.63e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVElcrydpEGDNTGEQVAVKSLKPESGGN---HIADLKKEIEILRNLYHENIVKYKGICTEDggNGIKLIME 957
Cdd:cd14160      1 IGEGEIFEVY------RVRIGNRSYAVKLFKQEKKMQwkkHWKRFLSELEVLLLFQHPNILELAAYFTET--EKFCLVYP 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  958 FLPSGSLKEYLPKNKNKINLKQQLKYAV--QICKGMDYLGSRQ---YVHRDLAARNVLVESEHQVKIGDFGLT--KAIET 1030
Cdd:cd14160     73 YMQNGTLFDRLQCHGVTKPLSWHERINIliGIAKAIHYLHNSQpctVICGNISSANILLDDQMQPKLTDFALAhfRPHLE 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1031 DKEYYTVKDDRDSPVFWYAPE-CLMQSKFYIASDVWSFGVTLHELLTYCD-SDSSPMALFLKmiGPTHGQMTVTRLVNTL 1108
Cdd:cd14160    153 DQSCTINMTTALHKHLWYMPEeYIRQGKLSVKTDVYSFGIVIMEVLTGCKvVLDDPKHLQLR--DLLHELMEKRGLDSCL 230
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1013071061 1109 K--EGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEAL 1152
Cdd:cd14160    231 SflDLKFPPCPRNFSAKLFRLAGRCTATKAKLRPDMDEVLQRLEST 276
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
581-836 7.25e-10

Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDK1 carries an N-terminal catalytic domain and a C-terminal pleckstrin homology (PH) domain that binds phosphoinositides. It phosphorylates the activation loop of AGC kinases that are regulated by PI3K such as PKB, SGK, and PKC, among others, and is crucial for their activation. Thus, it contributes in regulating many processes including metabolism, growth, proliferation, and survival. PDK1 also has the ability to autophosphorylate and is constitutively active in mammalian cells. It is essential for normal embryo development and is important in regulating cell volume. The PDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270733 [Multi-domain]  Cd Length: 278  Bit Score: 61.46  E-value: 7.25e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  581 KDLVQGEHLGRGTRTHIYSGTlmdykdDEGTSEEKKIKVILKVLDPSHRDISLAFFEAASMMRqVSHKHIVYLYGvCVRD 660
Cdd:cd05581      1 NDFKFGKPLGEGSYSTVVLAK------EKETGKEYAIKVLDKRHIIKEKKVKYVTIEKEVLSR-LAHPGIVKLYY-TFQD 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  661 VENI-MVEEFVEGGPLDLFMHRKS--DVLTTpwKFKVAkQLASALSYLEDKDLVHGNVCTKNLLLAREGidsecgpFIKL 737
Cdd:cd05581     73 ESKLyFVLEYAPNGDLLEYIRKYGslDEKCT--RFYTA-EIVLALEYLHSKGIIHRDLKPENILLDEDM-------HIKI 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  738 SD---------PGIPITVLSRQECIERIP------------WIAPECVEDSKnLSVAADKWSFGTTLWEiCYNGEIPLKD 796
Cdd:cd05581    143 TDfgtakvlgpDSSPESTKGDADSQIAYNqaraasfvgtaeYVSPELLNEKP-AGKSSDLWALGCIIYQ-MLTGKPPFRG 220
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1013071061  797 KTliEKERF-------YESRCRPVtpscKELADLMTRCMNYDPNQRP 836
Cdd:cd05581    221 SN--EYLTFqkivkleYEFPENFP----PDAKDLIQKLLVLDPSKRL 261
PHA02988 PHA02988
hypothetical protein; Provisional
902-1150 7.39e-10

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 61.30  E-value: 7.39e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  902 GEQVAVKSLK-PESGGNHIADL-KKEIEILRNLYHENIVKYKGICTE--DGGNGIKLIMEFLPSGSLKEYLPKNKNkINL 977
Cdd:PHA02988    43 NKEVIIRTFKkFHKGHKVLIDItENEIKNLRRIDSNNILKIYGFIIDivDDLPRLSLILEYCTRGYLREVLDKEKD-LSF 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  978 KQQLKYAVQICKGMDYL-GSRQYVHRDLAARNVLVESEHQVKIGDFGLTKaIETDKEYYTVKDdrdspVFWYAPECLMQ- 1055
Cdd:PHA02988   122 KTKLDMAIDCCKGLYNLyKYTNKPYKNLTSVSFLVTENYKLKIICHGLEK-ILSSPPFKNVNF-----MVYFSYKMLNDi 195
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1056 -SKFYIASDVWSFGVTLHELLTYCDsdsspmalflkmigPTHGqMTVTRLVNTL-KEGKRLPCPPNCPDEVYQLMRKCWE 1133
Cdd:PHA02988   196 fSEYTIKDDIYSLGVVLWEIFTGKI--------------PFEN-LTTKEIYDLIiNKNNSLKLPLDCPLEIKCIVEACTS 260
                          250
                   ....*....|....*..
gi 1013071061 1134 FQPSNRTSFQNLIEGFE 1150
Cdd:PHA02988   261 HDSIKRPNIKEILYNLS 277
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
697-836 8.79e-10

Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This subfamily is composed of the catalytically inactive kinases with similarity to yeast Scy1. It includes four mammalian proteins called SCY1-like protein 1 (SCYL1), SCYL2, SCYL3, as well as Testis-EXpressed protein 14 (TEX14). SCYL1 binds to and co-localizes with the membrane trafficking coatomer I (COPI) complex, and regulates COPI-mediated vesicle trafficking. Null mutations in the SCYL1 gene are responsible for the pathology in mdf (muscle-deficient) mice which display progressive motor neuropathy. SCYL2, also called coated vesicle-associated kinase of 104 kDa (CVAK104), is involved in the trafficking of clathrin-coated vesicles. It also binds the HIV-1 accessory protein Vpu and acts as a regulatory factor that promotes the dephosphorylation of Vpu, facilitating the restriction of HIV-1 release. SCYL3, also called ezrin-binding protein PACE-1, may be involved in regulating cell adhesion and migration. TEX14 is required for spermatogenesis and male fertility. It localizes to kinetochores (KT) during mitosis and is a target of the mitotic kinase PLK1. It regulates the maturation of the outer KT and the KT-microtubule attachment. The SCY1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 61.18  E-value: 8.79e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  697 QLASALSYL-EDKDLVHGNVCTKNLLLAREG----------IDSECG----PFIKLSDPGIPitVLSRQEcierIPWIAP 761
Cdd:cd14011    122 QISEALSFLhNDVKLVHGNICPESVVINSNGewklagfdfcISSEQAtdqfPYFREYDPNLP--PLAQPN----LNYLAP 195
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  762 ECVEdSKNLSVAADKWSFGTTLWEICYNGEIPLKD-------KTLIEKERFYESRCRPVTPSckELADLMTRCMNYDPNQ 834
Cdd:cd14011    196 EYIL-SKTCDPASDMFSLGVLIYAIYNKGKPLFDCvnnllsyKKNSNQLRQLSLSLLEKVPE--ELRDHVKTLLNVTPEV 272

                   ..
gi 1013071061  835 RP 836
Cdd:cd14011    273 RP 274
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
635-848 8.83e-10

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 61.06  E-value: 8.83e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  635 FFEAASMMRQVSHKHIVYLYGVCV----RDVENIMveEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDL 710
Cdd:cd05081     52 FQREIQILKALHSDFIVKYRGVSYgpgrRSLRLVM--EYLPSGCLRDFLQRHRARLDASRLLLYSSQICKGMEYLGSRRC 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  711 VHGNVCTKNLLLAREgidsecgPFIKLSDPGIP-ITVLSRQECIERIP------WIAPECVEDSKnLSVAADKWSFGTTL 783
Cdd:cd05081    130 VHRDLAARNILVESE-------AHVKIADFGLAkLLPLDKDYYVVREPgqspifWYAPESLSDNI-FSRQSDVWSFGVVL 201
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  784 WEI-------CYNGEI------PLKDKTLIEK--ERFYESRCRPVTPSC-KELADLMTRCMNYDPNQRPFFRAIMRDINK 847
Cdd:cd05081    202 YELftycdksCSPSAEflrmmgCERDVPALCRllELLEEGQRLPAPPACpAEVHELMKLCWAPSPQDRPSFSALGPQLDM 281

                   .
gi 1013071061  848 L 848
Cdd:cd05081    282 L 282
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
881-1076 9.66e-10

Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like protein kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity DYRKs and YAK1, as well as the S/T kinases (STKs), HIPKs. DYRKs and YAK1 autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. Proteins in this subfamily play important roles in cell proliferation, differentiation, survival, growth, and development. The DYRK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271035 [Multi-domain]  Cd Length: 262  Bit Score: 60.74  E-value: 9.66e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCrYDpegDNTGEQVAVKSLKpesggNHIADLK---KEIEILRNL-YHENIVKYKGICTEDG---GNGIK 953
Cdd:cd14133      7 LGKGTFGQVVKC-YD---LLTGEEVALKIIK-----NNKDYLDqslDEIRLLELLnKKDKADKYHIVRLKDVfyfKNHLC 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  954 LIMEFLpSGSLKEYLPKNKNK-INLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVE--SEHQVKIGDFGltKAIET 1030
Cdd:cd14133     78 IVFELL-SQNLYEFLKQNKFQyLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLAsySRCQIKIIDFG--SSCFL 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1013071061 1031 DKEYYTVKDDRdspvFWYAPECLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd14133    155 TQRLYSYIQSR----YYRAPEVILGLPYDEKIDMWSLGCILAELYT 196
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
587-843 1.01e-09

Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK25 is also called Ste20/oxidant stress response kinase 1 (SOK1) or yeast Sps1/Ste20-related kinase 1 (YSK1). It is localized in the Golgi apparatus through its interaction with the Golgi matrix protein GM130. It may be involved in the regulation of cell migration and polarization. STK25 binds and phosphorylates CCM3 (cerebral cavernous malformation 3), also called PCD10 (programmed cell death 10), and may play a role in apoptosis. Human STK25 is a candidate gene responsible for pseudopseudohypoparathyroidism (PPHP), a disease that shares features with the Albright hereditary osteodystrophy (AHO) phenotype. The STK25 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 60.84  E-value: 1.01e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  587 EHLGRGTRTHIYSGTlmdykdDEGTSEEKKIKVI-LKVLDPSHRDISlaffEAASMMRQVSHKHIVYLYGVCVRDVENIM 665
Cdd:cd06642     10 ERIGKGSFGEVYKGI------DNRTKEVVAIKIIdLEEAEDEIEDIQ----QEITVLSQCDSPYITRYYGSYLKGTKLWI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  666 VEEFVEGGP-LDLFmhrKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGIP- 743
Cdd:cd06642     80 IMEYLGGGSaLDLL---KPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGD-------VKLADFGVAg 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  744 ---ITVLSRQECIERIPWIAPECVEDSKnLSVAADKWSFGTTLWEICyNGEIPLKDKTLIeKERFYESRCRPVT---PSC 817
Cdd:cd06642    150 qltDTQIKRNTFVGTPFWMAPEVIKQSA-YDFKADIWSLGITAIELA-KGEPPNSDLHPM-RVLFLIPKNSPPTlegQHS 226
                          250       260
                   ....*....|....*....|....*.
gi 1013071061  818 KELADLMTRCMNYDPNQRPFFRAIMR 843
Cdd:cd06642    227 KPFKEFVEACLNKDPRFRPTAKELLK 252
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
618-836 1.06e-09

Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Pek1/Skh1 from Schizosaccharomyces pombe and MKK2 from Saccharomyces cerevisiae, and related proteins. Both fission yeast Pek1 and baker's yeast MKK2 are components of the cell integrity MAPK pathway. In fission yeast, Pek1 phosphorylates and activates Pmk1/Spm1 and is regulated by the MAPKK kinase Mkh1. In baker's yeast, the pathway involves the MAPK Slt2, the MAPKKs MKK1 and MKK2, and the MAPKK kinase Bck1. The cell integrity MAPK cascade is activated by multiple stress conditions, and is essential in cell wall construction, morphogenesis, cytokinesis, and ion homeostasis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 60.90  E-value: 1.06e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  618 KVILKVLDPshrDISLAFFEAASMMRQVSHKHIVYLYGVCVRDVE-NI-MVEEFVEGGPLD-LFMHRKSDVLTTPWKF-- 692
Cdd:cd06621     32 KTITTDPNP---DVQKQILRELEINKSCASPYIVKYYGAFLDEQDsSIgIAMEYCEGGSLDsIYKKVKKKGGRIGEKVlg 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  693 KVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGIpitvlsRQECIERIP--------WIAPECV 764
Cdd:cd06621    109 KIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQ-------VKLCDFGV------SGELVNSLAgtftgtsyYMAPERI 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  765 EdSKNLSVAADKWSFGTTLWEICYN-------GEIPLkdkTLIEKERFYESRCRPVTPSC--------KELADLMTRCMN 829
Cdd:cd06621    176 Q-GGPYSITSDVWSLGLTLLEVAQNrfpfppeGEPPL---GPIELLSYIVNMPNPELKDEpengikwsESFKDFIEKCLE 251

                   ....*..
gi 1013071061  830 YDPNQRP 836
Cdd:cd06621    252 KDGTRRP 258
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
877-1127 1.18e-09

Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS2 is an essential mitotic regulator responsible for coordinating accurate cytokinesis completion and governing the stabilization of other mitotic regulators. It is also critical in the maintenance of proper chromosome number, genomic stability, mitotic fidelity, and the integrity of centrosome duplication. Downregulation of LATS2 is associated with poor prognosis in acute lymphoblastic leukemia and breast cancer. The LATS2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 61.57  E-value: 1.18e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  877 RIRDLGEGHFGKVEL-CRYDpegdnTGEQVAVKSLKPES--GGNHIADLKKEIEILRNLYHENIVK-YKGICTEDGgngI 952
Cdd:cd05626      5 KIKTLGIGAFGEVCLaCKVD-----THALYAMKTLRKKDvlNRNQVAHVKAERDILAEADNEWVVKlYYSFQDKDN---L 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  953 KLIMEFLPSGSLKEYLPKNKNkinLKQQLK--YAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIE- 1029
Cdd:cd05626     77 YFVMDYIPGGDMMSLLIRMEV---FPEVLArfYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLCTGFRw 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1030 -TDKEYYT----VKDDRDSPV-FW-------------------------------------YAPECLMQSKFYIASDVWS 1066
Cdd:cd05626    154 tHNSKYYQkgshIRQDSMEPSdLWddvsncrcgdrlktleqratkqhqrclahslvgtpnyIAPEVLLRKGYTQLCDWWS 233
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1013071061 1067 FGVTLHELLTYCDSDSSPMalflkmigPTHGQMTVTRLVNTLKEGKRLPCPPNCPDEVYQL 1127
Cdd:cd05626    234 VGVILFEMLVGQPPFLAPT--------PTETQLKVINWENTLHIPPQVKLSPEAVDLITKL 286
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
875-1075 1.24e-09

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR1 (also called STK38) plays a role in proper centrosome duplication. It is highly expressed in thymus, muscle, lung and spleen. It is not an essential protein because mice deficient of NDR1 remain viable and fertile. However, these mice develop T-cell lymphomas and appear to be hypersenstive to carcinogenic treatment. NDR1 appears to also act as a tumor suppressor. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 61.59  E-value: 1.24e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  875 LKRIRDLGEGHFGKVELCrydpEGDNTGEQVAVKSLKPES--GGNHIADLKKEIEILRNLYHENIVKYKgICTEDGGNgI 952
Cdd:cd05628      3 FESLKVIGRGAFGEVRLV----QKKDTGHVYAMKILRKADmlEKEQVGHIRAERDILVEADSLWVVKMF-YSFQDKLN-L 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  953 KLIMEFLPSGSLKEYLPKnKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIET-- 1030
Cdd:cd05628     77 YLIMEFLPGGDMMTLLMK-KDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLCTGLKKah 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1013071061 1031 DKEYY-----------------------TVKDDRDSPVF-------WYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd05628    156 RTEFYrnlnhslpsdftfqnmnskrkaeTWKRNRRQLAFstvgtpdYIAPEVFMQTGYNKLCDWWSLGVIMYEML 230
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
640-843 1.31e-09

Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LKB1, also called STK11, was first identified as a tumor suppressor responsible for Peutz-Jeghers syndrome, a disorder that leads to an increased risk of spontaneous epithelial cancer. It serves as a master upstream kinase that activates AMP-activated protein kinase (AMPK) and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. To be activated, LKB1 requires the adaptor proteins STe20-Related ADaptor (STRAD) and mouse protein 25 (MO25). The LKB1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271021 [Multi-domain]  Cd Length: 255  Bit Score: 60.35  E-value: 1.31e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  640 SMMRQVSHKHIVYLYGVcVRDVEN---IMVEEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVC 716
Cdd:cd14119     46 QILRRLNHRNVIKLVDV-LYNEEKqklYMVMEYCVGGLQEMLDSAPDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIK 124
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  717 TKNLLLAREGIdsecgpfIKLSDPGIPiTVLSRQECIERI------P-WIAPECVEDSKNLS-VAADKWSFGTTLWEICy 788
Cdd:cd14119    125 PGNLLLTTDGT-------LKISDFGVA-EALDLFAEDDTCttsqgsPaFQPPEIANGQDSFSgFKVDIWSAGVTLYNMT- 195
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1013071061  789 NGEIPLKDKTLIekeRFYE--SRCRPVTPSC--KELADLMTRCMNYDPNQRPFFRAIMR 843
Cdd:cd14119    196 TGKYPFEGDNIY---KLFEniGKGEYTIPDDvdPDLQDLLRGMLEKDPEKRFTIEQIRQ 251
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
902-1076 1.33e-09

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 62.12  E-value: 1.33e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  902 GEQVAVKSLKPESGGNHIAdlkkeieILR---------NLYHENIVK-YK-GictEDGGNGIkLIMEFLPSGSLKEYLpK 970
Cdd:NF033483    32 DRDVAVKVLRPDLARDPEF-------VARfrreaqsaaSLSHPNIVSvYDvG---EDGGIPY-IVMEYVDGRTLKDYI-R 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  971 NKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAI------ETDKEYYTVKddrdsp 1044
Cdd:NF033483   100 EHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIARALssttmtQTNSVLGTVH------ 173
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1013071061 1045 vfwY-APEclmQSKFYIA---SDVWSFGVTLHELLT 1076
Cdd:NF033483   174 ---YlSPE---QARGGTVdarSDIYSLGIVLYEMLT 203
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
881-1075 1.38e-09

Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. cPKCs contain a calcium-binding C2 region in their regulatory domain. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The cPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 60.87  E-value: 1.38e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCrydpEGDNTGEQVAVKSLKPESggnHIAD-------LKKEIEILRNLYHENIVKYKGICTEDGgngIK 953
Cdd:cd05587      4 LGKGSFGKVMLA----ERKGTDELYAIKILKKDV---IIQDddvectmVEKRVLALSGKPPFLTQLHSCFQTMDR---LY 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  954 LIMEFLPSGSLKeYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTK-AIETDK 1032
Cdd:cd05587     74 FVMEYVNGGDLM-YHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCKeGIFGGK 152
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1013071061 1033 EYYTVKDDRDspvfWYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd05587    153 TTRTFCGTPD----YIAPEIIAYQPYGKSVDWWAYGVLLYEML 191
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
640-852 1.44e-09

Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the cAMP-dependent protein kinases, PKA and PRKX, and similar proteins. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. PRKX is also reulated by the R subunit and is is present in many tissues including fetal and adult brain, kidney, and lung. It is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PKA-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270732 [Multi-domain]  Cd Length: 290  Bit Score: 60.67  E-value: 1.44e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  640 SMMRQVSHKHIVYLYGVcVRDVENI-MVEEFVEGGplDLFMH-RKSDVLTTPW-KFKVAkQLASALSYLEDKDLVHGNVC 716
Cdd:cd05580     53 RILSEVRHPFIVNLLGS-FQDDRNLyMVMEYVPGG--ELFSLlRRSGRFPNDVaKFYAA-EVVLALEYLHSLDIVYRDLK 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  717 TKNLLLAREGidsecgpFIKLSDPGIPITVLSRQECIERIP-WIAPECVEdSKNLSVAADKWSFGTTLWEIC-----YNG 790
Cdd:cd05580    129 PENLLLDSDG-------HIKITDFGFAKRVKDRTYTLCGTPeYLAPEIIL-SKGHGKAVDWWALGILIYEMLagyppFFD 200
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1013071061  791 EIPLK--DKTLIEKERFYesrcRPVTPSCKelaDLMTRCMNYDPNQR--------------PFFRAImrDINKLEEQN 852
Cdd:cd05580    201 ENPMKiyEKILEGKIRFP----SFFDPDAK---DLIKRLLVVDLTKRlgnlkngvediknhPWFAGI--DWDALLQRK 269
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
581-844 1.48e-09

Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. PLKs derive their names from homology to polo, a kinase first identified in Drosophila. There are five mammalian PLKs (PLK1-5) from distinct genes. There is good evidence that PLK1 may function as an oncogene while PLK2-5 have tumor suppressive properties. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. PLK2 functions in G1 progression, S-phase arrest, and centriole duplication. PLK3 regulates angiogenesis and responses to DNA damage. PLK4 is required for late mitotic progression, cell survival, and embryonic development. PLK5 was first identified as a pseudogene containing a stop codon within the kinase domain, however, both murine and human genes encode expressed proteins. PLK5 functions in cell cycle arrest.


Pssm-ID: 271001 [Multi-domain]  Cd Length: 258  Bit Score: 59.87  E-value: 1.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  581 KDLVQGEHLGRGTRTHIYSGTLMDykddegTSEEKKIKVILK--VLDPSHRDislAFFEAASMMRQVSHKHIVYLYGvCV 658
Cdd:cd14099      1 KRYRRGKFLGKGGFAKCYEVTDMS------TGKVYAGKVVPKssLTKPKQRE---KLKSEIKIHRSLKHPNIVKFHD-CF 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  659 RDVENI-MVEEFVEGGPLdLFMHRKSDVLTTPwkfKVA---KQLASALSYLEDKDLVHGNVCTKNLLLAREGidsecgpF 734
Cdd:cd14099     71 EDEENVyILLELCSNGSL-MELLKRRKALTEP---EVRyfmRQILSGVKYLHSNRIIHRDLKLGNLFLDENM-------N 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  735 IKLSDPGIPITVLSRQECIERI---P-WIAPECVEDSKNLSVAADKWSFGTtlweICYN---GEIPLKDKTL------IE 801
Cdd:cd14099    140 VKIGDFGLAARLEYDGERKKTLcgtPnYIAPEVLEKKKGHSFEVDIWSLGV----ILYTllvGKPPFETSDVketykrIK 215
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1013071061  802 KERFYESRCRPVTPSCKelaDLMTRCMNYDPNQRPFFRAIMRD 844
Cdd:cd14099    216 KNEYSFPSHLSISDEAK---DLIRSMLQPDPTKRPSLDEILSH 255
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
616-852 1.73e-09

Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KSR1 functions as a transducer of TNFalpha-stimulated C-Raf activation of ERK1/2 and NF-kB. Detected activity of KSR1 is cell type specific and context dependent. It is inactive in normal colon epithelial cells and becomes activated at the onset of inflammatory bowel disease (IBD). Similarly, KSR1 activity is undetectable prior to stimulation by EGF or ceramide in COS-7 or YAMC cells, respectively. KSR proteins are widely regarded as pseudokinases, however, this matter is up for debate as catalytic activity has been detected for KSR1 in some systems. The KSR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 60.37  E-value: 1.73e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  616 KIKVILKVLDPSHRDiSLAFFEAASM-MRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSDVLTTPWKFKV 694
Cdd:cd14152     24 EVAIRLLEIDGNNQD-HLKLFKKEVMnYRQTRHENVVLFMGACMHPPHLAIITSFCKGRTLYSFVRDPKTSLDINKTRQI 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  695 AKQLASALSYLEDKDLVHGNVCTKNLLLAR-EGIDSECGPFiklsdpGIPITVLS-RQECIERIP--WI---APECV--- 764
Cdd:cd14152    103 AQEIIKGMGYLHAKGIVHKDLKSKNVFYDNgKVVITDFGLF------GISGVVQEgRRENELKLPhdWLcylAPEIVrem 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  765 -----EDSKNLSVAADKWSFGTTLWEIcYNGEIPLKDK---TLIEKERFYESRCRPVTPSC--KELADLMTRCMNYDPNQ 834
Cdd:cd14152    177 tpgkdEDCLPFSKAADVYAFGTIWYEL-QARDWPLKNQpaeALIWQIGSGEGMKQVLTTISlgKEVTEILSACWAFDLEE 255
                          250
                   ....*....|....*...
gi 1013071061  835 RPFFRAIMRDINKLEEQN 852
Cdd:cd14152    256 RPSFTLLMDMLEKLPKLN 273
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
876-1075 1.77e-09

Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal STKs including Saccharomyces cerevisiae RCK1 and RCK2, Schizosaccharomyces pombe Sty1-regulated kinase 1 (Srk1), and similar proteins. RCK1, RCK2 (or Rck2p), and Srk1 are MAPK-activated protein kinases. RCK1 and RCK2 are involved in oxidative and metal stress resistance in budding yeast. RCK2 also regulates rapamycin sensitivity in both S. cerevisiae and Candida albicans. Srk1 is activated by Sty1/Spc1 and is involved in negatively regulating cell cycle progression by inhibiting Cdc25. The RCK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270998 [Multi-domain]  Cd Length: 295  Bit Score: 60.53  E-value: 1.77e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  876 KRIRDLGEGHFGKVELCRYDPegdNTGEQVAVKSLKPESGGNH------IADLKKEIEILRNLYHENIVKYkgICTEDGG 949
Cdd:cd14096      4 RLINKIGEGAFSNVYKAVPLR---NTGKPVAIKVVRKADLSSDnlkgssRANILKEVQIMKRLSHPNIVKL--LDFQESD 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  950 NGIKLIMEFLPSGSLkeylpknKNKInlkQQLKY---------AVQICKGMDYLGSRQYVHRDLAARNVL------VESE 1014
Cdd:cd14096     79 EYYYIVLELADGGEI-------FHQI---VRLTYfsedlsrhvITQVASAVKYLHEIGVVHRDIKPENLLfepipfIPSI 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1015 H---------------------------QVKIGDFGLTKAIEtDKEYYTvkddrdsP---VFWYAPECLMQSKFYIASDV 1064
Cdd:cd14096    149 VklrkadddetkvdegefipgvggggigIVKLADFGLSKQVW-DSNTKT-------PcgtVGYTAPEVVKDERYSKKVDM 220
                          250
                   ....*....|.
gi 1013071061 1065 WSFGVTLHELL 1075
Cdd:cd14096    221 WALGCVLYTLL 231
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
666-874 1.86e-09

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. There are three PKB isoforms from different genes, PKB-alpha (or Akt1), PKB-beta (or Akt2), and PKB-gamma (or Akt3). PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. It is activated downstream of phosphoinositide 3-kinase (PI3K) and plays important roles in diverse cellular functions including cell survival, growth, proliferation, angiogenesis, motility, and migration. PKB also has a central role in a variety of human cancers, having been implicated in tumor initiation, progression, and metastasis. The PKB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 60.45  E-value: 1.86e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  666 VEEFVEGGplDLFMH-RKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGidsecgpFIKLSDPGIpi 744
Cdd:cd05571     73 VMEYVNGG--ELFFHlSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDG-------HIKITDFGL-- 141
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  745 tvlsrqeCIERIP-------------WIAPECVEDSkNLSVAADKWSFGTTLWE-ICynGEIP--------LKDKTLIEK 802
Cdd:cd05571    142 -------CKEEISygattktfcgtpeYLAPEVLEDN-DYGRAVDWWGLGVVMYEmMC--GRLPfynrdhevLFELILMEE 211
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  803 ERFyesrcrPVTPScKELADLMTRCMNYDPNQR--------------PFFRAImrDINKLEEQnpDIVSEKKPA--TEVD 866
Cdd:cd05571    212 VRF------PSTLS-PEAKSLLAGLLKKDPKKRlgggprdakeimehPFFASI--NWDDLYQK--KIPPPFKPQvtSETD 280

                   ....*...
gi 1013071061  867 PTHFEKRF 874
Cdd:cd05571    281 TRYFDEEF 288
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
697-838 2.13e-09

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR beta is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR beta forms homodimers or heterodimers with PDGFR alpha, depending on the nature of the PDGF ligand. PDGF-BB and PDGF-DD induce PDGFR beta homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR beta signaling leads to a variety of cellular effects including the stimulation of cell growth and chemotaxis, as well as the inhibition of apoptosis and GAP junctional communication. It is critical in normal angiogenesis as it is involved in the recruitment of pericytes and smooth muscle cells essential for vessel stability. Aberrant PDGFR beta expression is associated with some human cancers. The continuously-active fusion proteins of PDGFR beta with COL1A1 and TEL are associated with dermatofibrosarcoma protuberans (DFSP) and a subset of chronic myelomonocytic leukemia (CMML), respectively. The PDGFR beta subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133238 [Multi-domain]  Cd Length: 401  Bit Score: 61.18  E-value: 2.13e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  697 QLASALSYLEDKDLVHGNVCTKNLLLARegidsecGPFIKLSDPGIPITVLSRQECIER------IPWIAPECVEDSKNL 770
Cdd:cd05107    247 QVANGMEFLASKNCVHRDLAARNVLICE-------GKLVKICDFGLARDIMRDSNYISKgstflpLKWMAPESIFNNLYT 319
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1013071061  771 SVAaDKWSFGTTLWEICYNGEIPLKDktLIEKERFYES-----RCRPVTPSCKELADLMTRCMNYDPNQRPFF 838
Cdd:cd05107    320 TLS-DVWSFGILLWEIFTLGGTPYPE--LPMNEQFYNAikrgyRMAKPAHASDEIYEIMQKCWEEKFEIRPDF 389
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
879-1076 2.17e-09

Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K8 is also called Tumor progression locus 2 (Tpl2) or Cancer Osaka thyroid (Cot), and was first identified as a proto-oncogene in T-cell lymphoma induced by MoMuL virus and in breast carcinoma induced by MMTV. Activated MAP3K8 induces various MAPK pathways including Extracellular Regulated Kinase (ERK) 1/2, c-Jun N-terminal kinase (JNK), and p38. It plays a pivotal role in innate immunity, linking Toll-like receptors to the production of TNF and the activation of ERK in macrophages. It is also required in interleukin-1beta production and is critical in host defense against Gram-positive bacteria. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K8 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 59.64  E-value: 2.17e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  879 RDLGEGH-----FGKVELCRyDPEGDN--TGEQVAVKSLKPEsggnhiadlkkEIEILRNLYHENIVKYKGICTEDggNG 951
Cdd:cd13995      5 RNIGSDFiprgaFGKVYLAQ-DTKTKKrmACKLIPVEQFKPS-----------DVEIQACFRHENIAELYGALLWE--ET 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  952 IKLIMEFLPSGSLKEYL----PKNKNKINLKQQlkyavQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIgDFGLTka 1027
Cdd:cd13995     71 VHLFMEAGEGGSVLEKLescgPMREFEIIWVTK-----HVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAVLV-DFGLS-- 142
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1013071061 1028 IETDKEYYTVKDDRDSPVFwYAPECLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd13995    143 VQMTEDVYVPKDLRGTEIY-MSPEVILCRGHNTKADIYSLGATIIHMQT 190
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
876-1075 2.19e-09

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 60.39  E-value: 2.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  876 KRIRDLGEGHFGKVELCRYDpegdNTGEQVAVK--SLKpesggnhiADLKKEIEILRNLY-HENIVKYKGIcTEDGGNgI 952
Cdd:cd14092      9 LREEALGDGSFSVCRKCVHK----KTGQEFAVKivSRR--------LDTSREVQLLRLCQgHPNIVKLHEV-FQDELH-T 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  953 KLIMEFLPSGSLKEYLPKNKN-----KINLKQQLKYAVQickgmdYLGSRQYVHRDLAARNVLVESEHQ---VKIGDFGL 1024
Cdd:cd14092     75 YLVMELLRGGELLERIRKKKRfteseASRIMRQLVSAVS------FMHSKGVVHRDLKPENLLFTDEDDdaeIKIVDFGF 148
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1013071061 1025 TKAIETDKEYYTvkddrdsPVF---WYAPECLMQSKF---YIAS-DVWSFGVTLHELL 1075
Cdd:cd14092    149 ARLKPENQPLKT-------PCFtlpYAAPEVLKQALStqgYDEScDLWSLGVILYTML 199
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
881-1126 2.44e-09

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 60.01  E-value: 2.44e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRyDPEGDNTGEQVAVKSLKPES------GGNHIADLKKEIEILRNLYHENIVKYkGICTEdggNGIKL 954
Cdd:cd05613      8 LGTGAYGKVFLVR-KVSGHDAGKLYAMKVLKKATivqkakTAEHTRTERQVLEHIRQSPFLVTLHY-AFQTD---TKLHL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPSGSLKEYLPKnKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAI---ETD 1031
Cdd:cd05613     83 ILDYINGGELFTHLSQ-RERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKEFlldENE 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1032 KEYytvkdDRDSPVFWYAPECLM--QSKFYIASDVWSFGVTLHELLT-----YCDSDSSPMA----LFLKMIGPTHGQMT 1100
Cdd:cd05613    162 RAY-----SFCGTIEYMAPEIVRggDSGHDKAVDWWSLGVLMYELLTgaspfTVDGEKNSQAeisrRILKSEPPYPQEMS 236
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1013071061 1101 ------VTRLVntLKE-GKRLPCPPNCPDEVYQ 1126
Cdd:cd05613    237 alakdiIQRLL--MKDpKKRLGCGPNGADEIKK 267
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
872-1075 2.73e-09

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK5 is widely expressed in many tissues. It associates with the membrane though an N-terminal PIP2 binding domain and also binds phospholipids via its C-terminus. GRK5 deficiency is associated with early Alzheimer's disease in humans and mouse models. GRK5 also plays a crucial role in the pathogenesis of sporadic Parkinson's disease. It participates in the regulation and desensitization of PDGFRbeta, a receptor tyrosine kinase involved in a variety of downstream cellular effects including cell growth, chemotaxis, apoptosis, and angiogenesis. GRK5 also regulates Toll-like receptor 4, which is involved in innate and adaptive immunity. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 59.99  E-value: 2.73e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  872 KRFLKRIRDLGEGHFGKVELCRYDPEGDNTG-EQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIV-KYKgicTEDGg 949
Cdd:cd05632      1 KNTFRQYRVLGKGGFGEVCACQVRATGKMYAcKRLEKKRIKKRKGESMALNEKQILEKVNSQFVVNLAyAYE---TKDA- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  950 ngIKLIMEFLPSGSLKEYLPKNKNK-INLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAI 1028
Cdd:cd05632     77 --LCLVLTIMNGGDLKFHIYNMGNPgFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVKI 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1013071061 1029 etdKEYYTVKdDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd05632    155 ---PEGESIR-GRVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMI 197
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
902-1075 2.85e-09

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK2 is expressed in every cell and tissue type. It is specifically translocated to the mitochondria during dopaminergic cell death. Specific substrates include the microtubule-associated proteins DCX and Tau, as well as TIF-IA which is involved in ribosomal RNA synthesis regulation. Mice deficient in Jnk2 show protection against arthritis, type 1 diabetes, atherosclerosis, abdominal aortic aneurysm, cardiac cell death, TNF-induced liver damage, and tumor growth, indicating that JNK2 may play roles in the pathogenesis of these diseases. Initially it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 60.43  E-value: 2.85e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  902 GEQVAVKSL-KPESGGNHIADLKKEIEILRNLYHENIvkykgictedggngIKLIMEFLPSGSLKE----YLPKNKNKIN 976
Cdd:cd07876     46 GINVAVKKLsRPFQNQTHAKRAYRELVLLKCVNHKNI--------------ISLLNVFTPQKSLEEfqdvYLVMELMDAN 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  977 LKQ---------QLKYAV-QICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETD---KEYYTVKddrds 1043
Cdd:cd07876    112 LCQvihmeldheRMSYLLyQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTACTNfmmTPYVVTR----- 186
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1013071061 1044 pvFWYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd07876    187 --YYRAPEVILGMGYKENVDIWSVGCIMGELV 216
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
642-835 2.97e-09

Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MELK is a cell cycle dependent protein which functions in cytokinesis, cell cycle, apoptosis, cell proliferation, and mRNA processing. It is found upregulated in many types of cancer cells, playing an indispensable role in cancer cell survival. It makes an attractive target in the design of inhibitors for use in the treatment of a wide range of human cancer. The MELK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270980 [Multi-domain]  Cd Length: 257  Bit Score: 59.32  E-value: 2.97e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  642 MRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKsDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLL 721
Cdd:cd14078     55 LKNLSHQHICRLYHVIETDNKIFMVLEYCPGGELFDYIVAK-DRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLL 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  722 LAREgidsecgPFIKLSDPGI---PITVLSR--QECIERIPWIAPECVEDSKNLSVAADKWSFGTTLWEIcYNGEIPLKD 796
Cdd:cd14078    134 LDED-------QNLKLIDFGLcakPKGGMDHhlETCCGSPAYAAPELIQGKPYIGSEADVWSMGVLLYAL-LCGFLPFDD 205
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1013071061  797 KT------LIEKERFYESRCrpVTPSCKELADLMtrcMNYDPNQR 835
Cdd:cd14078    206 DNvmalyrKIQSGKYEEPEW--LSPSSKLLLDQM---LQVDPKKR 245
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
876-1075 3.06e-09

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS was originally identified in Drosophila using a screen for genes whose inactivation led to overproliferation of cells. In tetrapods, there are two LATS isoforms, LATS1 and LATS2. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. LATS functions as a tumor suppressor and is implicated in cell cycle regulation. The LATS subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 60.02  E-value: 3.06e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  876 KRIRDLGEGHFGKVELCRydpeGDNTGEQVAVKSLKPES--GGNHIADLKKEIEILRNLYHENIVK-YKGICTEDGgngI 952
Cdd:cd05598      4 EKIKTIGVGAFGEVSLVR----KKDTNALYAMKTLRKKDvlKRNQVAHVKAERDILAEADNEWVVKlYYSFQDKEN---L 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  953 KLIMEFLPSGSLKEYLPKnknKINLKQQLK--YAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIE- 1029
Cdd:cd05598     77 YFVMDYIPGGDLMSLLIK---KGIFEEDLArfYIAELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRw 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1013071061 1030 -TDKEYYTVKDDRDSPVFwYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd05598    154 tHDSKYYLAHSLVGTPNY-IAPEVLLRTGYTQLCDWWSVGVILYEML 199
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
628-850 3.70e-09

Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; Tie1; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie1 is a receptor tyr kinase (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. No specific ligand has been identified for Tie1, although the angiopoietin, Ang-1, binds to Tie1 through integrins at high concentrations. In vivo studies of Tie1 show that it is critical in vascular development.


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 59.24  E-value: 3.70e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  628 HRDISlafFEAASMMRQVSHKHIVYLYGVCV-RDVENIMVEEFVEGGPLDLFmhRKSDVLTTPWKF-------------- 692
Cdd:cd05089     46 HRDFA---GELEVLCKLGHHPNIINLLGACEnRGYLYIAIEYAPYGNLLDFL--RKSRVLETDPAFakehgtastltsqq 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  693 --KVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIDsecgpfiKLSDPGipitvLSRQE------CIERIP--WIAPE 762
Cdd:cd05089    121 llQFASDVAKGMQYLSEKQFIHRDLAARNVLVGENLVS-------KIADFG-----LSRGEevyvkkTMGRLPvrWMAIE 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  763 cvedSKNLSV---AADKWSFGTTLWEICYNGEIPLKDKTLIEKERFYESRCRPVTP-SC-KELADLMTRCMNYDPNQRPF 837
Cdd:cd05089    189 ----SLNYSVyttKSDVWSFGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRMEKPrNCdDEVYELMRQCWRDRPYERPP 264
                          250
                   ....*....|...
gi 1013071061  838 FRAIMRDINKLEE 850
Cdd:cd05089    265 FSQISVQLSRMLE 277
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
885-1139 3.80e-09

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK1 is one of two vertebrate LRRKs which show complementary expression in the brain. It can form heterodimers with LRRK2, and may influence the age of onset of LRRK2-associated Parkinson's disease. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 59.21  E-value: 3.80e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  885 HFGKvelCRYDPEGDNTgeqVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTedggNGIKLIMEFLPSGSL 964
Cdd:cd14067     26 HIKK---CKKRTDGSAD---TMLKHLRAADAMKNFSEFRQEASMLHSLQHPCIVYLIGISI----HPLCFALELAPLGSL 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  965 KEYLPKNKNK---INLKQQL--KYAVQICKGMDYLGSRQYVHRDLAARNVLV----ESEH-QVKIGDFGLTKaietdKEY 1034
Cdd:cd14067     96 NTVLEENHKGssfMPLGHMLtfKIAYQIAAGLAYLHKKNIIFCDLKSDNILVwsldVQEHiNIKLSDYGISR-----QSF 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1035 YTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLtycdSDSSPmalflkMIGptHGQMTVTRlvnTLKEGKRl 1114
Cdd:cd14067    171 HEGALGVEGTPGYQAPEIRPRIVYDEKVDMFSYGMVLYELL----SGQRP------SLG--HHQLQIAK---KLSKGIR- 234
                          250       260       270
                   ....*....|....*....|....*....|
gi 1013071061 1115 PCPPNcPDEV-----YQLMRKCWEFQPSNR 1139
Cdd:cd14067    235 PVLGQ-PEEVqffrlQALMMECWDTKPEKR 263
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
919-1145 4.52e-09

Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle 1 (also called TTK); Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TTK/Mps1 is a spindle checkpoint kinase that was first discovered due to its necessity in centrosome duplication in budding yeast. It was later found to function in the spindle assembly checkpoint, which monitors the proper attachment of chromosomes to the mitotic spindle. In yeast, substrates of Mps1 include the spindle pole body components Spc98p, Spc110p, and Spc42p. The TTK/Mps1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 58.76  E-value: 4.52e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  919 IADLKKEIEILRNLYHE-NIVKYKGICTEDGGNGIKLIMEFlPSGSLKEYL-PKNKNKINLKQQLKYAVQICKGMDYLGS 996
Cdd:cd14131     43 LQSYKNEIELLKKLKGSdRIIQLYDYEVTDEDDYLYMVMEC-GEIDLATILkKKRPKPIDPNFIRYYWKQMLEAVHTIHE 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  997 RQYVHRDLAARN-VLVESehQVKIGDFGLTKAIETDkeyyTVKDDRDSPV--FWY-APECLMQSKFYI----------AS 1062
Cdd:cd14131    122 EGIVHSDLKPANfLLVKG--RLKLIDFGIAKAIQND----TTSIVRDSQVgtLNYmSPEAIKDTSASGegkpkskigrPS 195
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1063 DVWSFGVTLHELL---TYCDSDSSPMALFLKMIGPTHgqmtvtrlvntlkegkRLPCPPNCPDEVYQLMRKCWEFQPSNR 1139
Cdd:cd14131    196 DVWSLGCILYQMVygkTPFQHITNPIAKLQAIIDPNH----------------EIEFPDIPNPDLIDVMKRCLQRDPKKR 259

                   ....*.
gi 1013071061 1140 TSFQNL 1145
Cdd:cd14131    260 PSIPEL 265
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
880-1076 4.57e-09

Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Titin, also called connectin, is a muscle-specific elastic protein and is the largest known protein to date. It contains multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains, and a single kinase domain near the C-terminus. It spans half of the sarcomere, the repeating contractile unit of striated muscle, and performs mechanical and catalytic functions. Titin contributes to the passive force generated when muscle is stretched during relaxation. Its kinase domain phosphorylates and regulates the muscle protein telethonin, which is required for sarcomere formation in differentiating myocytes. In addition, titin binds many sarcomere proteins and acts as a molecular scaffold for filament formation during myofibrillogenesis. The Titin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 58.72  E-value: 4.57e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  880 DLGEGHFGKVELC-RYDPEGDNTGEQVAVKslkpesgGNHIADLKKEIEILRNLYHENIVKYKGicTEDGGNGIKLIMEF 958
Cdd:cd14104      7 ELGRGQFGIVHRCvETSSKKTYMAKFVKVK-------GADQVLVKKEISILNIARHRNILRLHE--SFESHEELVMIFEF 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  959 LPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESE--HQVKIGDFGLTKAIETDKEyyt 1036
Cdd:cd14104     78 ISGVDIFERITTARFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTRrgSYIKIIEFGQSRQLKPGDK--- 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1013071061 1037 VKDDRDSPVFwYAPECLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd14104    155 FRLQYTSAEF-YAPEVHQHESVSTATDMWSLGCLVYVLLS 193
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
950-1076 4.57e-09

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 58.71  E-value: 4.57e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  950 NGIKLIMEFLPSGSLKEYLpKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVL-VESEHQVKIGDFGLTKAI 1028
Cdd:PHA03390    82 KGHVLIMDYIKDGDLFDLL-KKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLyDRAKDRIYLCDYGLCKII 160
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1013071061 1029 ETDKEYytvkddrDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:PHA03390   161 GTPSCY-------DGTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLT 201
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
923-1089 4.63e-09

Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2b (or ActRIIB) belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. ACVR2b is one of two ACVR2 receptors found in vertebrates. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. The ACVR2b subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271042 [Multi-domain]  Cd Length: 291  Bit Score: 58.89  E-value: 4.63e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  923 KKEIEILRNLYHENIVKYkgICTEDGGNGIK----LIMEFLPSGSLKEYLpkNKNKINLKQQLKYAVQICKGMDYL---- 994
Cdd:cd14140     37 EREIFSTPGMKHENLLQF--IAAEKRGSNLEmelwLITAFHDKGSLTDYL--KGNIVSWNELCHIAETMARGLSYLhedv 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  995 ------GSRQYV-HRDLAARNVLVESEHQVKIGDFGLTKAIETDK----EYYTVKDDRdspvfWYAPECL-----MQSKF 1058
Cdd:cd14140    113 prckgeGHKPAIaHRDFKSKNVLLKNDLTAVLADFGLAVRFEPGKppgdTHGQVGTRR-----YMAPEVLegainFQRDS 187
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1013071061 1059 YIASDVWSFGVTLHELLTYCDSDSSPMALFL 1089
Cdd:cd14140    188 FLRIDMYAMGLVLWELVSRCKAADGPVDEYM 218
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
626-842 5.15e-09

Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity kinase Myt1, the protein tyrosine kinase Wee1, and similar proteins. These proteins are cell cycle checkpoint kinases that are involved in the regulation of cyclin-dependent kinase CDK1, the master engine for mitosis. CDK1 is kept inactivated through phosphorylation of N-terminal thr (T14 by Myt1) and tyr (Y15 by Myt1 and Wee1) residues. Mitosis progression is ensured through activation of CDK1 by dephoshorylation and inactivation of Myt1/Wee1. The Wee1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 58.16  E-value: 5.15e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  626 PSHRDISLAFFEAASMMRQvsHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSDVLTTP----WKFkvAKQLASA 701
Cdd:cd13997     40 PKERARALREVEAHAALGQ--HPNIVRYYSSWEEGGHLYIQMELCENGSLQDALEELSPISKLSeaevWDL--LLQVALG 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  702 LSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGIPITVLSRQECIERIP-WIAPECVEDSKNLSVAADKWSFG 780
Cdd:cd13997    116 LAFIHSKGIVHLDIKPDNIFISNKGT-------CKIGDFGLATRLETSGDVEEGDSrYLAPELLNENYTHLPKADIFSLG 188
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  781 TTLWEICYNGEIP--------LKDKTLIEKERFYESrcrpvtpscKELADLMTRCMNYDPNQRPFFRAIM 842
Cdd:cd13997    189 VTVYEAATGEPLPrngqqwqqLRQGKLPLPPGLVLS---------QELTRLLKVMLDPDPTRRPTADQLL 249
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
870-1092 6.16e-09

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 1 subunit (PhKG1) is also referred to as the muscle gamma isoform. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 58.39  E-value: 6.16e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  870 FEKRFLKRIrdLGEGHFGKVELCRYDPegdnTGEQVAVKSLKPESGG----NHIADLK----KEIEILRNLY-HENIVKY 940
Cdd:cd14182      2 YEKYEPKEI--LGRGVSSVVRRCIHKP----TRQEYAVKIIDITGGGsfspEEVQELReatlKEIDILRKVSgHPNIIQL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  941 KGicTEDGGNGIKLIMEFLPSGSLKEYLPKnKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIG 1020
Cdd:cd14182     76 KD--TYETNTFFFLVFDLMKKGELFDYLTE-KVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLT 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1021 DFGLTKAIETDKEyytVKDDRDSPVFwYAPE---CLMQSK---FYIASDVWSFGVTLHELLtycdSDSSPM-----ALFL 1089
Cdd:cd14182    153 DFGFSCQLDPGEK---LREVCGTPGY-LAPEiieCSMDDNhpgYGKEVDMWSTGVIMYTLL----AGSPPFwhrkqMLML 224

                   ...
gi 1013071061 1090 KMI 1092
Cdd:cd14182    225 RMI 227
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
697-851 6.35e-09

Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. Kit signaling is involved in major cellular functions including cell survival, proliferation, differentiation, adhesion, and chemotaxis. Mutations in Kit, which result in constitutive ligand-independent activation, are found in human cancers such as gastrointestinal stromal tumor (GIST) and testicular germ cell tumor (TGCT). The aberrant expression of Kit and/or SCF is associated with other tumor types such as systemic mastocytosis and cancers of the breast, neurons, lung, prostate, colon, and rectum. Although the structure of the human Kit catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. Kit is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of Kit to its ligand, the stem-cell factor (SCF), leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. The Kit subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270682 [Multi-domain]  Cd Length: 375  Bit Score: 59.53  E-value: 6.35e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  697 QLASALSYLEDKDLVHGNVCTKNLLLARegidsecGPFIKLSDPGIPITVLSRQECI----ERIP--WIAPE----CVed 766
Cdd:cd05104    222 QVAKGMEFLASKNCIHRDLAARNILLTH-------GRITKICDFGLARDIRNDSNYVvkgnARLPvkWMAPEsifeCV-- 292
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  767 sknLSVAADKWSFGTTLWEICYNGEIPLKDKTLIEKerFYE---SRCRPVTPSCK--ELADLMTRCMNYDPNQRPFFRAI 841
Cdd:cd05104    293 ---YTFESDVWSYGILLWEIFSLGSSPYPGMPVDSK--FYKmikEGYRMDSPEFApsEMYDIMRSCWDADPLKRPTFKQI 367
                          170
                   ....*....|
gi 1013071061  842 mrdINKLEEQ 851
Cdd:cd05104    368 ---VQLIEQQ 374
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
881-1075 6.53e-09

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK3 (also called cytokine-independent survival kinase or CISK) is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. The SGK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270755 [Multi-domain]  Cd Length: 326  Bit Score: 58.82  E-value: 6.53e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRydpeGDNTGEQVAVKSLKPESGGN-----HIadLKKEIEILRNLYHENIV--KYKGICTEDggngIK 953
Cdd:cd05604      4 IGKGSFGKVLLAK----RKRDGKYYAVKVLQKKVILNrkeqkHI--MAERNVLLKNVKHPFLVglHYSFQTTDK----LY 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  954 LIMEFLPSGSLKEYLPKNKNKINLKQQLkYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKaiETDKE 1033
Cdd:cd05604     74 FVLDFVNGGELFFHLQRERSFPEPRARF-YAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCK--EGISN 150
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1013071061 1034 YYTVKDDRDSPVFwYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd05604    151 SDTTTTFCGTPEY-LAPEVIRKQPYDNTVDWWCLGSVLYEML 191
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
875-1076 6.75e-09

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 7; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK7 is a dual-specificity PK that phosphorylates and activates its downstream target, c-Jun N-terminal kinase (JNK), on specific threonine and tyrosine residues. Although MKK7 is capable of dual phosphorylation, it prefers to phosphorylate the threonine residue of JNK. Thus, optimal activation of JNK requires both MKK4 and MKK7. MKK7 is primarily activated by cytokines. MKK7 is essential for liver formation during embryogenesis. It plays roles in G2/M cell cycle arrest and cell growth. In addition, it is involved in the control of programmed cell death, which is crucial in oncogenesis, cancer chemoresistance, and antagonism to TNFalpha-induced killing, through its inhibition by Gadd45beta and the subsequent suppression of the JNK cascade. The MKK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270791 [Multi-domain]  Cd Length: 295  Bit Score: 58.54  E-value: 6.75e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  875 LKRIRDLGEGHFGKVELCRYDpegdNTGEQVAVKSLkPESGGNHiaDLKKeieILRNL-----YHE--NIVKYKGICTED 947
Cdd:cd06618     17 LENLGEIGSGTCGQVYKMRHK----KTGHVMAVKQM-RRSGNKE--ENKR---ILMDLdvvlkSHDcpYIVKCYGYFITD 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  948 ggNGIKLIMEfLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYV-HRDLAARNVLVESEHQVKIGDFGLTK 1026
Cdd:cd06618     87 --SDVFICME-LMSTCLDKLLKRIQGPIPEDILGKMTVSIVKALHYLKEKHGViHRDVKPSNILLDESGNVKLCDFGISG 163
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1013071061 1027 AIETDKeyytVKDDRDSPVFWYAPECL---MQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd06618    164 RLVDSK----AKTRSAGCAAYMAPERIdppDNPKYDIRADVWSLGISLVELAT 212
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
877-1129 7.79e-09

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS1 functions as a tumor suppressor and is implicated in cell cycle regulation. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. Promoter methylation, loss of heterozygosity, and missense mutations targeting the LATS1 gene have also been found in human sarcomas and ovarian cancers. In addition, decreased expression of LATS1 is associated with an aggressive phenotype and poor prognosis. LATS1 induces G2 arrest and promotes cytokinesis. It may be a component of the mitotic exit network in higher eukaryotes. The LATS1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270775 [Multi-domain]  Cd Length: 382  Bit Score: 59.29  E-value: 7.79e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  877 RIRDLGEGHFGKVELCRydpeGDNTGEQVAVKSLKPESG--GNHIADLKKEIEILRNLYHENIVK-YKGICTEDGgngIK 953
Cdd:cd05625      5 KIKTLGIGAFGEVCLAR----KVDTKALYATKTLRKKDVllRNQVAHVKAERDILAEADNEWVVRlYYSFQDKDN---LY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  954 LIMEFLPSGSLKEYL------PKNKNKINLKQqLKYAVQICKGMDYlgsrqyVHRDLAARNVLVESEHQVKIGDFGLTKA 1027
Cdd:cd05625     78 FVMDYIPGGDMMSLLirmgvfPEDLARFYIAE-LTCAVESVHKMGF------IHRDIKPDNILIDRDGHIKLTDFGLCTG 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1028 IE--TDKEYYTVKD----------------------DRDSPVFW--------------------YAPECLMQSKFYIASD 1063
Cdd:cd05625    151 FRwtHDSKYYQSGDhlrqdsmdfsnewgdpencrcgDRLKPLERraarqhqrclahslvgtpnyIAPEVLLRTGYTQLCD 230
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1013071061 1064 VWSFGVTLHELLTycdsDSSPmalFLKMiGPTHGQMTVTRLVNTLKEGKRLPCPPNCPDEVYQLMR 1129
Cdd:cd05625    231 WWSVGVILFEMLV----GQPP---FLAQ-TPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLCR 288
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
881-1074 7.97e-09

Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of proteins with similarity to Saccharomyces cerevisiae YAK1 (or Yak1p), a dual-specificity kinase that autophosphorylates at tyrosine residues and phosphorylates substrates on S/T residues. YAK1 phosphorylates and activates the transcription factors Hsf1 and Msn2, which play important roles in cellular homeostasis during stress conditions including heat shock, oxidative stress, and nutrient deficiency. It also phosphorylates the protein POP2, a component of a complex that regulates transcription, under glucose-deprived conditions. It functions as a part of a glucose-sensing system that is involved in controlling growth in yeast. The YAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 58.80  E-value: 7.97e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRyDPEgdnTGEQVAVKSLKpesggNHIADLKK---EIEILRNL-------YHENIVK------YKG-- 942
Cdd:cd14212      7 LGQGTFGQVVKCQ-DLK---TNKLVAVKVLK-----NKPAYFRQamlEIAILTLLntkydpeDKHHIVRlldhfmHHGhl 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  943 -ICTEdggngiklimefLPSGSLKEYLPKNKNKiNLKQQL--KYAVQICKGMDYLGSRQYVHRDLAARNVLVESEH--QV 1017
Cdd:cd14212     78 cIVFE------------LLGVNLYELLKQNQFR-GLSLQLirKFLQQLLDALSVLKDARIIHCDLKPENILLVNLDspEI 144
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1013071061 1018 KIGDFGltKAIETDKEYYTVKDDRdspvFWYAPECLMQSKFYIASDVWSFGVTLHEL 1074
Cdd:cd14212    145 KLIDFG--SACFENYTLYTYIQSR----FYRSPEVLLGLPYSTAIDMWSLGCIAAEL 195
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
641-835 8.24e-09

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called Doublecortin-like and CAM kinase-like 3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL3 (or DCAMKL3) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. DCKL3 contains a single DCX domain (instead of a tandem) and a C-terminal kinase domain with similarity to CAMKs. It has been shown to interact with tubulin and JIP1/2. The DCKL3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271087 [Multi-domain]  Cd Length: 258  Bit Score: 58.04  E-value: 8.24e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  641 MMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGplDLFmhrksDVLTTPWKFK------VAKQLASALSYLEDKDLVHGN 714
Cdd:cd14185     51 IIKSLSHPNIVKLFEVYETEKEIYLILEYVRGG--DLF-----DAIIESVKFTehdaalMIIDLCEALVYIHSKHIVHRD 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  715 VCTKNLLLAREGIDSECgpfIKLSDPGIPITVLSRQECIERIP-WIAPECVEDsKNLSVAADKWSFGTTLWeICYNGEIP 793
Cdd:cd14185    124 LKPENLLVQHNPDKSTT---LKLADFGLAKYVTGPIFTVCGTPtYVAPEILSE-KGYGLEVDMWAAGVILY-ILLCGFPP 198
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1013071061  794 LKDKTLIEKERF-------YESRCRPVTPSCKELADLMTRCMNYDPNQR 835
Cdd:cd14185    199 FRSPERDQEELFqiiqlghYEFLPPYWDNISEAAKDLISRLLVVDPEKR 247
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
875-1026 8.29e-09

Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phototropins are blue-light receptors that control responses such as phototropism, stromatal opening, and chloroplast movement in order to optimize the photosynthetic efficiency of plants. They are light-activated STKs that contain an N-terminal photosensory domain and a C-terminal catalytic domain. The N-terminal domain contains two LOV (Light, Oxygen or Voltage) domains that binds FMN. Photoexcitation of the LOV domains results in autophosphorylation at multiple sites and activation of the catalytic domain. In addition to plant phototropins, included in this subfamily are predominantly uncharacterized fungal STKs whose catalytic domains resemble the phototropin kinase domain. One protein from Neurospora crassa is called nrc-2, which plays a role in growth and development by controlling entry into the conidiation program. The phototropin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 58.40  E-value: 8.29e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  875 LKRIRDLGEGHFGKVELCRYDpegdNTGEQVAVKSLKPES--GGNHIADLKKEIEILRNLYHENIVK-YKGICTEDGgng 951
Cdd:cd05574      3 FKKIKLLGKGDVGRVYLVRLK----GTGKLFAMKVLDKEEmiKRNKVKRVLTEREILATLDHPFLPTlYASFQTSTH--- 75
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1013071061  952 IKLIMEFLPSGSLKEYLPKNKNKINLKQQLK-YAVQICKGMDYLGSRQYVHRDLAARNVLV-ESEHqVKIGDFGLTK 1026
Cdd:cd05574     76 LCFVMDYCPGGELFRLLQKQPGKRLPEEVARfYAAEVLLALEYLHLLGFVYRDLKPENILLhESGH-IMLTDFDLSK 151
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
881-1076 8.59e-09

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 58.51  E-value: 8.59e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDpegdNTGEQVAVKSLKPESGGNhiadLKKEIEILRNLY-HENIVKYKGICTEDGGNgiKLIMEFL 959
Cdd:cd14179     15 LGEGSFSICRKCLHK----KTNQEYAVKIVSKRMEAN----TQREIAALKLCEgHPNIVKLHEVYHDQLHT--FLVMELL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  960 PSGSLKEYLPKNK--NKINLKQQLKYAVQICKGMDYLGsrqYVHRDLAARNVLVESEH---QVKIGDFGLTKAIETDKEY 1034
Cdd:cd14179     85 KGGELLERIKKKQhfSETEASHIMRKLVSAVSHMHDVG---VVHRDLKPENLLFTDESdnsEIKIIDFGFARLKPPDNQP 161
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1013071061 1035 YTvkddrdSPVF---WYAPECLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd14179    162 LK------TPCFtlhYAAPELLNYNGYDESCDLWSLGVILYTMLS 200
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
881-1081 8.60e-09

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 58.11  E-value: 8.60e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRydpegdN--TGEQVAVKSLKPESGgnHI-ADLKKEIEILRNLY-HENIVKYKGICTEDggNGIKLIM 956
Cdd:cd14173     10 LGEGAYARVQTCI------NliTNKEYAVKIIEKRPG--HSrSRVFREVEMLYQCQgHRNVLELIEFFEEE--DKFYLVF 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  957 EFLPSGSLKEYLPKNKNkINlKQQLKYAVQ-ICKGMDYLGSRQYVHRDLAARNVLVESEHQ---VKIGDFGLTKAIETDK 1032
Cdd:cd14173     80 EKMRGGSILSHIHRRRH-FN-ELEASVVVQdIASALDFLHNKGIAHRDLKPENILCEHPNQvspVKICDFDLGSGIKLNS 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1013071061 1033 EyytvkddrDSPVfwYAPECLMQ--SKFYIAS-----------------DVWSFGVTLHELLT-------YCDSD 1081
Cdd:cd14173    158 D--------CSPI--STPELLTPcgSAEYMAPevveafneeasiydkrcDLWSLGVILYIMLSgyppfvgRCGSD 222
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
589-836 8.84e-09

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 is required for the transition from metaphase to anaphase. It also plays important roles in mitotic spindle formation and cytokinesis. Activated by Nek9 during mitosis, Nek6 phosphorylates Eg5, a kinesin that is important for spindle bipolarity. Nek6 localizes to spindle microtubules during metaphase and anaphase, and to the midbody during cytokinesis. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 57.73  E-value: 8.84e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  589 LGRGTRTHIYSGT-LMDYKddegTSEEKKIKvILKVLDPSHRDISLaffEAASMMRQVSHKHIVYLYGVCVRDVENIMVE 667
Cdd:cd08228     10 IGRGQFSEVYRATcLLDRK----PVALKKVQ-IFEMMDAKARQDCV---KEIDLLKQLNHPNVIKYLDSFIEDNELNIVL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  668 EFVEGGPLD-LFMHRKSDVLTTP----WKFKVakQLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGI 742
Cdd:cd08228     82 ELADAGDLSqMIKYFKKQKRLIPertvWKYFV--QLCSAVEHMHSRRVMHRDIKPANVFITATGV-------VKLGDLGL 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  743 PITVLSRQECIERIP----WIAPECVEDSkNLSVAADKWSFGTTLWEICYNGEIPLKDK----TLIEKERFYESRCRPVT 814
Cdd:cd08228    153 GRFFSSKTTAAHSLVgtpyYMSPERIHEN-GYNFKSDIWSLGCLLYEMAALQSPFYGDKmnlfSLCQKIEQCDYPPLPTE 231
                          250       260
                   ....*....|....*....|..
gi 1013071061  815 PSCKELADLMTRCMNYDPNQRP 836
Cdd:cd08228    232 HYSEKLRELVSMCIYPDPDQRP 253
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
584-836 9.42e-09

Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Schizosaccharomyces pombe Byr2, Saccharomyces cerevisiae and Cryptococcus neoformans Ste11, and related proteins. They contain an N-terminal SAM (sterile alpha-motif) domain, which mediates protein-protein interaction, and a C-terminal catalytic domain. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Byr2 is regulated by Ras1. It responds to pheromone signaling and controls mating through the MAPK pathway. Budding yeast Ste11 functions in MAPK cascades that regulate mating, high osmolarity glycerol, and filamentous growth responses. The Byr2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270798 [Multi-domain]  Cd Length: 267  Bit Score: 57.93  E-value: 9.42e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  584 VQGEHLGRGTRTHIY------SGTLMDYKD---DEGTSEEKKIKVilKVLDPSHRDISLaffeaasmMRQVSHKHIV-YL 653
Cdd:cd06628      3 IKGALIGSGSFGSVYlgmnasSGELMAVKQvelPSVSAENKDRKK--SMLDALQREIAL--------LRELQHENIVqYL 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  654 YGVCVRDVENIMVEeFVEGGPLdlfmhrkSDVLTTPWKFKVA------KQLASALSYLEDKDLVHGNVCTKNLLLAREGI 727
Cdd:cd06628     73 GSSSDANHLNIFLE-YVPGGSV-------ATLLNNYGAFEESlvrnfvRQILKGLNYLHNRGIIHRDIKGANILVDNKGG 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  728 dsecgpfIKLSDPGIP----ITVLSRQECIER------IPWIAPECVEDSkNLSVAADKWSFGTTLWEIcYNGEIPLKDK 797
Cdd:cd06628    145 -------IKISDFGISkkleANSLSTKNNGARpslqgsVFWMAPEVVKQT-SYTRKADIWSLGCLVVEM-LTGTHPFPDC 215
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1013071061  798 TLIEKERFYESRCRPVTPS-CKELA-DLMTRCMNYDPNQRP 836
Cdd:cd06628    216 TQMQAIFKIGENASPTIPSnISSEArDFLEKTFEIDHNKRP 256
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
881-1075 1.07e-08

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPK-activated protein kinases MK2, MK3, MK5 (also called PRAK for p38-regulated/activated protein kinase), and related proteins. These proteins contain a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. In addition, MK2 and MK3 contain an N-terminal proline-rich region that can bind to SH3 domains. MK2 and MK3 are bonafide substrates for the MAPK p38, while MK5 plays a functional role in the p38 MAPK pathway although their direct interaction has been difficult to detect. MK2 and MK3 are closely related and show, thus far, indistinguishable substrate specificity, while MK5 shows a distinct spectrum of substrates. MK2 and MK3 are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270991 [Multi-domain]  Cd Length: 263  Bit Score: 57.68  E-value: 1.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCrYDPEgdnTGEQVAVKSLK--PESggnhiadlKKEIEI-LRNLYHENIVKykgIC-----TEDGGNGI 952
Cdd:cd14089      9 LGLGINGKVLEC-FHKK---TGEKFALKVLRdnPKA--------RREVELhWRASGCPHIVR---IIdvyenTYQGRKCL 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  953 KLIMEFLPSGSLKEYLPKNKN-KINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEH---QVKIGDFGLTKAI 1028
Cdd:cd14089     74 LVVMECMEGGELFSRIQERADsAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGpnaILKLTDFGFAKET 153
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1029 ETDKEYYTvkddrdsPVF--WY-APECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd14089    154 TTKKSLQT-------PCYtpYYvAPEVLGPEKYDKSCDMWSLGVIMYILL 196
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
913-1076 1.19e-08

Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The pseudokinase domain may function as a regulatory domain or a protein interaction domain. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 57.14  E-value: 1.19e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  913 ESGGNHIADLK-------KEIEILRNLYHENIVKYKGIcTEDGGNGIKLIMEFLPSGSL-KEYLPKNKNKINLKQQLKYA 984
Cdd:cd14109     27 STGRNFLAQLRygdpflmREVDIHNSLDHPNIVQMHDA-YDDEKLAVTVIDNLASTIELvRDNLLPGKDYYTERQVAVFV 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  985 VQICKGMDYLGSRQYVHRDLAARNVLVESEHqVKIGDFGLTKAIETDKEYytvKDDRDSPVFwYAPECLMQSKFYIASDV 1064
Cdd:cd14109    106 RQLLLALKHMHDLGIAHLDLRPEDILLQDDK-LKLADFGQSRRLLRGKLT---TLIYGSPEF-VSPEIVNSYPVTLATDM 180
                          170
                   ....*....|..
gi 1013071061 1065 WSFGVTLHELLT 1076
Cdd:cd14109    181 WSVGVLTYVLLG 192
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
647-848 1.28e-08

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The VEGFR subfamily consists of VEGFR1 (Flt1), VEGFR2 (Flk1), VEGFR3 (Flt4), and similar proteins. VEGFR subfamily members are receptor PTKss (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. There are five VEGF ligands in mammals, which bind, in an overlapping pattern to the three VEGFRs, which can form homo or heterodimers. VEGFRs regulate the cardiovascular system. They are critical for vascular development during embryogenesis and blood vessel formation in adults. They induce cellular functions common to other growth factor receptors such as cell migration, survival, and proliferation. The VEGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 57.89  E-value: 1.28e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  647 HKHIVYLYGVCVRDVENIMV-EEFVEGGPLDLFMHRKSDVLTtPWKFKVAK--------------------------QLA 699
Cdd:cd05054     70 HLNVVNLLGACTKPGGPLMViVEFCKFGNLSNYLRSKREEFV-PYRDKGARdveeeedddelykepltledlicysfQVA 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  700 SALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGIPITVLSRQECIE----RIP--WIAPECVEDsKNLSVA 773
Cdd:cd05054    149 RGMEFLASRKCIHRDLAARNILLSENNV-------VKICDFGLARDIYKDPDYVRkgdaRLPlkWMAPESIFD-KVYTTQ 220
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1013071061  774 ADKWSFGTTLWEICYNGEIPLKDKTLIEK--ERFYE-SRCRPVTPSCKELADLMTRCMNYDPNQRPFFRAIMRDINKL 848
Cdd:cd05054    221 SDVWSFGVLLWEIFSLGASPYPGVQMDEEfcRRLKEgTRMRAPEYTTPEIYQIMLDCWHGEPKERPTFSELVEKLGDL 298
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
881-1139 1.34e-08

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270735 [Multi-domain]  Cd Length: 268  Bit Score: 57.40  E-value: 1.34e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRyDPEGDNTGEQVAVKSLKPESggnhIADLKKEIE----------------ILRNLYHENIVKYKgic 944
Cdd:cd05583      2 LGTGAYGKVFLVR-KVGGHDAGKLYAMKVLKKAT----IVQKAKTAEhtmterqvleavrqspFLVTLHYAFQTDAK--- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  945 tedggngIKLIMEFLPSGSL------KEYLPKNKNKInlkqqlkYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVK 1018
Cdd:cd05583     74 -------LHLILDYVNGGELfthlyqREHFTESEVRI-------YIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVV 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1019 IGDFGLTkaietdKEYYTVKDDRD----SPVFWYAPECLM--QSKFYIASDVWSFGVTLHELLTYCdsdsSPMALflkmI 1092
Cdd:cd05583    140 LTDFGLS------KEFLPGENDRAysfcGTIEYMAPEVVRggSDGHDKAVDWWSLGVLTYELLTGA----SPFTV----D 205
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1013071061 1093 GPTHGQMTVTRLVntLKEGKRLP--CPPNCPDEVYQLMRKcwefQPSNR 1139
Cdd:cd05583    206 GERNSQSEISKRI--LKSHPPIPktFSAEAKDFILKLLEK----DPKKR 248
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
635-838 1.41e-08

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK1 activation is induced by bone morphogenic protein, vascular endothelial growth factor, and thrombin. It plays roles in microtubule disassembly and cell cycle progression, and is critical in the regulation of neurite outgrowth. LIMK1 knockout mice show abnormalities in dendritic spine morphology and synaptic function. LIMK1 is one of the genes deleted in patients with Williams Syndrome, which is characterized by distinct craniofacial features, cardiovascular problems, as well as behavioral and neurological abnormalities. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 57.27  E-value: 1.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  635 FFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMhrKSDVLTTPWKFKV--AKQLASALSYLEDKDLVH 712
Cdd:cd14221     37 FLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGTLRGII--KSMDSHYPWSQRVsfAKDIASGMAYLHSMNIIH 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  713 -------------GNVCTKNLLLAREGIDSECGPFIKLSDpgIPITVLSRQECIERIPWIAPECVeDSKNLSVAADKWSF 779
Cdd:cd14221    115 rdlnshnclvrenKSVVVADFGLARLMVDEKTQPEGLRSL--KKPDRKKRYTVVGNPYWMAPEMI-NGRSYDEKVDVFSF 191
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1013071061  780 GTTLWEIC--YNGEIPLKDKTL---IEKERFYESRCRPVTPSckELADLMTRCMNYDPNQRPFF 838
Cdd:cd14221    192 GIVLCEIIgrVNADPDYLPRTMdfgLNVRGFLDRYCPPNCPP--SFFPIAVLCCDLDPEKRPSF 253
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
881-1112 1.45e-08

Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and -Regulated Kinases 2 and 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of DYRK2 and DYRK3, and similar proteins. Drosophila DYRK2 interacts and phosphorylates the chromatin remodelling factor, SNR1 (Snf5-related 1), and also interacts with the essential chromatin component, trithorax. It may play a role in chromatin remodelling. Vertebrate DYRK2 phosphorylates and regulates the tumor suppressor p53 to induce apoptosis in response to DNA damage. It can also phosphorylate the transcription factor, nuclear factor of activated T cells (NFAT). DYRK2 is overexpressed in lung adenocarcinoma and esophageal carcinomas, and is a predictor for favorable prognosis in lung adenocarcinoma. DYRK3, also called regulatory erythroid kinase (REDK), is highly expressed in erythroid cells and the testis, and is also present in adult kidney and liver. It promotes cell survival by phosphorylating and activating SIRT1, an NAD(+)-dependent protein deacetylase, which promotes p53 deacetylation, resulting in the inhibition of apoptosis. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other S/T kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 58.22  E-value: 1.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVeLCRYDpegDNTGEQVAVKSLKPESGGNHIADlkKEIEIL-----------RNLYH--ENIVKYKGICted 947
Cdd:cd14224     73 IGKGSFGQV-VKAYD---HKTHQHVALKMVRNEKRFHRQAA--EEIRILehlkkqdkdntMNVIHmlESFTFRNHIC--- 143
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  948 ggngikliMEF-LPSGSLKEYLPKNKNK-INLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQ--VKIGDFG 1023
Cdd:cd14224    144 --------MTFeLLSMNLYELIKKNKFQgFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGRsgIKVIDFG 215
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1024 ltKAIETDKEYYTVKDDRdspvFWYAPECLMQSKFYIASDVWSFGVTLHELLT-YC----DSDSSPMALFLKMIGpthgq 1098
Cdd:cd14224    216 --SSCYEHQRIYTYIQSR----FYRAPEVILGARYGMPIDMWSFGCILAELLTgYPlfpgEDEGDQLACMIELLG----- 284
                          250
                   ....*....|....
gi 1013071061 1099 MTVTRLVNTLKEGK 1112
Cdd:cd14224    285 MPPQKLLETSKRAK 298
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
574-847 1.54e-08

Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-A binds and is activated by the atrial and B-type natriuretic peptides, ANP and BNP, which are important in blood pressure regulation and cardiac pathophysiology. GC-B binds the C-type natriuretic peptide, CNP, which is a potent vasorelaxant and functions in vascular remodeling and bone growth regulation. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-A/B subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270944 [Multi-domain]  Cd Length: 279  Bit Score: 57.22  E-value: 1.54e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  574 SFDRILKKDLVQGEHlGRGTRTHIYSGTLmdykddegtseekkikVILKVLDPSHRDISLAFFEAASMMRQVSHKHIVYL 653
Cdd:cd14042      5 SSYGSLMTAASFDQS-QIFTKTGYYKGNL----------------VAIKKVNKKRIDLTREVLKELKHMRDLQHDNLTRF 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  654 YGVCVrDVENI-MVEEFVEGGPL-DLFmhrKSDVLTTPWKFKVA--KQLASALSYLEDKDLV-HGNVCTKNLLlaregID 728
Cdd:cd14042     68 IGACV-DPPNIcILTEYCPKGSLqDIL---ENEDIKLDWMFRYSliHDIVKGMHYLHDSEIKsHGNLKSSNCV-----VD 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  729 SEcgpFI-KLSDPGIP------ITVLSRQECIERIPWIAPECVEDSKNL---SVAADKWSFGTTLWEIC------YNGEI 792
Cdd:cd14042    139 SR---FVlKITDFGLHsfrsgqEPPDDSHAYYAKLLWTAPELLRDPNPPppgTQKGDVYSFGIILQEIAtrqgpfYEEGP 215
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1013071061  793 PLKDKTLIEKERfyESRCRP-----VTPSC--KELADLMTRCMNYDPNQRPFFRAI---MRDINK 847
Cdd:cd14042    216 DLSPKEIIKKKV--RNGEKPpfrpsLDELEcpDEVLSLMQRCWAEDPEERPDFSTLrnkLKKLNK 278
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
640-836 1.55e-08

Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PASK (or PASKIN) is a nutrient and energy sensor and thus, plays an important role in maintaining cellular energy homeostasis. It coordinates the utilization of glucose in response to metabolic demand. It contains an N-terminal PAS domain which directly interacts and inhibits a C-terminal catalytic kinase domain. The PAS domain serves as a sensory module for different environmental signals such as light, redox state, and various metabolites. Binding of ligands to the PAS domain causes structural changes which leads to kinase activation and the phosphorylation of substrates to trigger the appropriate cellular response. The PASK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270906 [Multi-domain]  Cd Length: 256  Bit Score: 57.01  E-value: 1.55e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  640 SMMRQVSHKHIVYLYGVcVRDVENIMVEEFVEGGPLDLF--MHRKSDvLTTPWKFKVAKQLASALSYLEDKDLVHGNVCT 717
Cdd:cd14004     60 DTLNKRSHPNIVKLLDF-FEDDEFYYLVMEKHGSGMDLFdfIERKPN-MDEKEAKYIFRQVADAVKHLHDQGIVHRDIKD 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  718 KNLLLAREGidsecgpFIKLSDPGipitvlsRQECIERIPW---------IAPECVEDSKNLSVAADKWSFGTTLWEICY 788
Cdd:cd14004    138 ENVILDGNG-------TIKLIDFG-------SAAYIKSGPFdtfvgtidyAAPEVLRGNPYGGKEQDIWALGVLLYTLVF 203
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1013071061  789 nGEIPlkdktLIEKERFYESRCRPVTPSCKELADLMTRCMNYDPNQRP 836
Cdd:cd14004    204 -KENP-----FYNIEEILEADLRIPYAVSEDLIDLISRMLNRDVGDRP 245
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
587-836 1.67e-08

Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer T-cell-originated protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TOPK, also called PDZ-binding kinase (PBK), is activated at the early stage of mitosis and plays a critical role in cytokinesis. It partly functions as a mitogen-activated protein kinase (MAPK) kinase and is capable of phosphorylating p38, JNK1, and ERK2. TOPK also plays a role in DNA damage sensing and repair through its phosphorylation of histone H2AX. It contributes to cancer development and progression by downregulating the function of tumor suppressor p53 and reducing cell-cycle regulatory proteins. TOPK is found highly expressed in breast and skin cancer cells. The TOPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 57.41  E-value: 1.67e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  587 EHLGRGTRTHIYsgtLMDYKDDEGTSEEK-KIKVILKVLDPSHR-DISLAFFEAASMMRQVSHKHIV-YLYGVCVRDVEN 663
Cdd:cd14001      5 KKLGYGTGVNVY---LMKRSPRGGSSRSPwAVKKINSKCDKGQRsLYQERLKEEAKILKSLNHPNIVgFRAFTKSEDGSL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  664 IMVEEFVEGGPLDLFMHRKSDVLTT-PWK--FKVAKQLASALSYLE-DKDLVHGNVCTKNLLLAregidsecGPF--IKL 737
Cdd:cd14001     82 CLAMEYGGKSLNDLIEERYEAGLGPfPAAtiLKVALSIARALEYLHnEKKILHGDIKSGNVLIK--------GDFesVKL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  738 SDPGIPI------TVLSRQEC--IERIPWIAPECVEDSKNLSVAADKWSFGTTLWEI---------CYNGEIPLKDKTLI 800
Cdd:cd14001    154 CDFGVSLpltenlEVDSDPKAqyVGTEPWKAKEALEEGGVITDKADIFAYGLVLWEMmtlsvphlnLLDIEDDDEDESFD 233
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1013071061  801 E----KERFYESR-CRP------VTPSCKELADLMTRCMNYDPNQRP 836
Cdd:cd14001    234 EdeedEEAYYGTLgTRPalnlgeLDDSYQKVIELFYACTQEDPKDRP 280
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
580-840 1.70e-08

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK2 is ubiquitously expressed and is essential in autophagy induction. It displays partially redundant functions with ULK1 and is able to compensate for the loss of ULK1 in non-selective autophagy. It also displays neuron-specific functions and is important in axon development. The ULK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 56.94  E-value: 1.70e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  580 KKDLVqgehlGRGTRTHIYSGtlmdyKDDEGTSEEKKIKVILKVlDPSHRDISLAffEAASMMRQVSHKHIVYLYGVCVR 659
Cdd:cd14201     10 RKDLV-----GHGAFAVVFKG-----RHRKKTDWEVAIKSINKK-NLSKSQILLG--KEIKILKELQHENIVALYDVQEM 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  660 DVENIMVEEFVEGGPLDLFMHRKSDVLTTPWKFKVaKQLASALSYLEDKDLVHGNVCTKNLLLAREG--IDSECGPFIKL 737
Cdd:cd14201     77 PNSVFLVMEYCNGGDLADYLQAKGTLSEDTIRVFL-QQIAAAMRILHSKGIIHRDLKPQNILLSYASrkKSSVSGIRIKI 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  738 SDPG----IPITVLSRQECIERIpWIAPECVEdSKNLSVAADKWSFGTTLWEiCYNGEIPLKDKTLIEKERFYESR--CR 811
Cdd:cd14201    156 ADFGfaryLQSNMMAATLCGSPM-YMAPEVIM-SQHYDAKADLWSIGTVIYQ-CLVGKPPFQANSPQDLRMFYEKNknLQ 232
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1013071061  812 PVTPS--CKELADLMTRCMNYDPNQRPFFRA 840
Cdd:cd14201    233 PSIPRetSPYLADLLLGLLQRNQKDRMDFEA 263
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
878-1076 1.93e-08

Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group contains fungal kinases including Schizosaccharomyces pombe Sid2p and Saccharomyces cerevisiae Dbf2p. Group members show similarity to NDR kinases in that they contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Sid2p plays a crucial role in the septum initiation network (SIN) and in the initiation of cytokinesis. Dbf2p is important in regulating the mitotic exit network (MEN) and in cytokinesis. The Sid2p-like group is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270751 [Multi-domain]  Cd Length: 386  Bit Score: 57.73  E-value: 1.93e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVELCRydpeGDNTGEQVAVKSLK--PESGGNHIADLKKEIEILRNLYHENIVK--YKGICTEDggngIK 953
Cdd:cd05600     16 LTQVGQGGYGSVFLAR----KKDTGEICALKIMKkkVLFKLNEVNHVLTERDILTTTNSPWLVKllYAFQDPEN----VY 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  954 LIMEFLPSGSLKEYLpkNKNKINLKQQLK-YAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAI---- 1028
Cdd:cd05600     88 LAMEYVPGGDFRTLL--NNSGILSEEHARfYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDFGLASGTlspk 165
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1013071061 1029 -------------ETDKEYYTVKDDRD------------------SPVFwYAPECLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd05600    166 kiesmkirleevkNTAFLELTAKERRNiyramrkedqnyansvvgSPDY-MAPEVLRGEGYDLTVDYWSLGCILFECLV 243
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
881-1075 2.08e-08

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase signal-integrating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 57.04  E-value: 2.08e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRydpeGDNTGEQVAVKSLKPESGGNHiADLKKEIEILRNLY-HENIVKYKGICTEDggNGIKLIMEFL 959
Cdd:cd14090     10 LGEGAYASVQTCI----NLYTGKEYAVKIIEKHPGHSR-SRVFREVETLHQCQgHPNILQLIEYFEDD--ERFYLVFEKM 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  960 PSGSLKEYLPKNKNkINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQ---VKIGDFGLTKAIETDKEYYT 1036
Cdd:cd14090     83 RGGPLLSHIEKRVH-FTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKvspVKICDFDLGSGIKLSSTSMT 161
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1013071061 1037 --VKDDRDSPVF---WYAPECL----MQSKFYIAS-DVWSFGVTLHELL 1075
Cdd:cd14090    162 pvTTPELLTPVGsaeYMAPEVVdafvGEALSYDKRcDLWSLGVILYIML 210
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
881-1076 2.18e-08

Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L6 is also called CDK8-like and was previously referred to as CDK11. However, this is a confusing nomenclature as CDC2L6 is distinct from CDC2L1, which is represented by the two protein products from its gene, called CDK11(p110) and CDK11(p58), as well as the caspase-processed CDK11(p46). CDK11(p110), CDK11(p58), and CDK11(p46)do not belong to this subfamily. CDC2L6 is an associated protein of Mediator, a multiprotein complex that provides a platform to connect transcriptional and chromatin regulators and cofactors, in order to activate and mediate RNA polymerase II transcription. CDC2L6 is localized mainly in the nucleus amd exerts an opposing effect to CDK8 in VP16-dependent transcriptional activation by being a negative regulator. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270850 [Multi-domain]  Cd Length: 318  Bit Score: 57.39  E-value: 2.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDpEGDNTGEQvavkSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGNGIKLIMEFLP 960
Cdd:cd07867     10 VGRGTYGHVYKAKRK-DGKDEKEY----ALKQIEGTGISMSACREIALLRELKHPNVIALQKVFLSHSDRKVWLLFDYAE 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  961 SG-----SLKEYLPKNKNKINLKQQLKYAV--QICKGMDYLGSRQYVHRDLAARNVLVESE----HQVKIGDFGLTKAIE 1029
Cdd:cd07867     85 HDlwhiiKFHRASKANKKPMQLPRSMVKSLlyQILDGIHYLHANWVLHRDLKPANILVMGEgperGRVKIADMGFARLFN 164
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1013071061 1030 TDKEYYTvkdDRDSPV--FWY-APECLMQSKFYI-ASDVWSFGVTLHELLT 1076
Cdd:cd07867    165 SPLKPLA---DLDPVVvtFWYrAPELLLGARHYTkAIDIWAIGCIFAELLT 212
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
881-1076 2.31e-08

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 57.19  E-value: 2.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDpegdNTGEQVAVKSLKPESGGNhiadLKKEIEILRNLY-HENIVKYKGICTEDGGNgiKLIMEFL 959
Cdd:cd14180     14 LGEGSFSVCRKCRHR----QSGQEYAVKIISRRMEAN----TQREVAALRLCQsHPNIVALHEVLHDQYHT--YLVMELL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  960 PSGSLKEYLPKNK--NKINLKQQLKYAVQickGMDYLGSRQYVHRDLAARNVLVESEHQ---VKIGDFGLTKAIETDKEy 1034
Cdd:cd14180     84 RGGELLDRIKKKArfSESEASQLMRSLVS---AVSFMHEAGVVHRDLKPENILYADESDgavLKVIDFGFARLRPQGSR- 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1013071061 1035 ytvkdDRDSPVF---WYAPECLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd14180    160 -----PLQTPCFtlqYAAPELFSNQGYDESCDLWSLGVILYTMLS 199
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
925-1136 2.67e-08

Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2a (or ActRIIA) belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. ACVR2b is one of two ACVR2 receptors found in vertebrates. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. The ACVR2a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271043 [Multi-domain]  Cd Length: 290  Bit Score: 56.59  E-value: 2.67e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  925 EIEILRNLYHENIVKYKGicTEDGGNGIK----LIMEFLPSGSLKEYLpkNKNKINLKQQLKYAVQICKGMDYL------ 994
Cdd:cd14141     39 EIYSLPGMKHENILQFIG--AEKRGTNLDvdlwLITAFHEKGSLTDYL--KANVVSWNELCHIAQTMARGLAYLhedipg 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  995 ---GSRQYV-HRDLAARNVLVESEHQVKIGDFGLTKAIETDKE----YYTVKDDRdspvfWYAPECL-----MQSKFYIA 1061
Cdd:cd14141    115 lkdGHKPAIaHRDIKSKNVLLKNNLTACIADFGLALKFEAGKSagdtHGQVGTRR-----YMAPEVLegainFQRDAFLR 189
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1013071061 1062 SDVWSFGVTLHELLTYCDSDSSPMALFLKMIGPTHGQM-TVTRLVNTLKEGKRLPcppncpdevyqLMRKCWEFQP 1136
Cdd:cd14141    190 IDMYAMGLVLWELASRCTASDGPVDEYMLPFEEEVGQHpSLEDMQEVVVHKKKRP-----------VLRECWQKHA 254
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
666-874 2.84e-08

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-beta is the predominant PKB isoform expressed in insulin-responsive tissues. It plays a critical role in the regulation of glucose homeostasis. It is also implicated in muscle cell differentiation. Mice deficient in PKB-beta display normal growth weights but exhibit severe insulin resistance and diabetes, accompanied by lipoatrophy and B-cell failure. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain.The PKB-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 56.94  E-value: 2.84e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  666 VEEFVEGGplDLFMH-RKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGidsecgpFIKLSDPGIPI 744
Cdd:cd05595     73 VMEYANGG--ELFFHlSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDG-------HIKITDFGLCK 143
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  745 TVLSRQECIERI----PWIAPECVEDSkNLSVAADKWSFGTTLWE-ICynGEIP--------LKDKTLIEKERFyesrCR 811
Cdd:cd05595    144 EGITDGATMKTFcgtpEYLAPEVLEDN-DYGRAVDWWGLGVVMYEmMC--GRLPfynqdherLFELILMEEIRF----PR 216
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1013071061  812 PVTPSCKEladLMTRCMNYDPNQR-----PFFRAIMRDINKLEEQNPDIVSEK-----KP--ATEVDPTHFEKRF 874
Cdd:cd05595    217 TLSPEAKS---LLAGLLKKDPKQRlgggpSDAKEVMEHRFFLSINWQDVVQKKllppfKPqvTSEVDTRYFDDEF 288
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
587-843 3.34e-08

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST4 is sometimes referred to as MASK (MST3 and SOK1-related kinase). It plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. It influences cell growth and transformation by modulating the extracellular signal-regulated kinase (ERK) pathway. MST4 may also play a role in tumor formation and progression. It localizes in the Golgi apparatus by interacting with the Golgi matrix protein GM130 and may play a role in cell migration. The MST4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 56.21  E-value: 3.34e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  587 EHLGRGTRTHIYSGTlmdykdDEGTSEEKKIKVI-LKVLDPSHRDISlaffEAASMMRQVSHKHIVYLYGVCVRDVENIM 665
Cdd:cd06640     10 ERIGKGSFGEVFKGI------DNRTQQVVAIKIIdLEEAEDEIEDIQ----QEITVLSQCDSPYVTKYYGSYLKGTKLWI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  666 VEEFVEGGP-LDLFMHRKSDvlttpwKFKVA---KQLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPG 741
Cdd:cd06640     80 IMEYLGGGSaLDLLRAGPFD------EFQIAtmlKEILKGLDYLHSEKKIHRDIKAANVLLSEQGD-------VKLADFG 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  742 IP----ITVLSRQECIERIPWIAPECVEDSKNLSvAADKWSFGTTLWEICyNGEIPLKDKTLIeKERFYESRCRPVTPS- 816
Cdd:cd06640    147 VAgqltDTQIKRNTFVGTPFWMAPEVIQQSAYDS-KADIWSLGITAIELA-KGEPPNSDMHPM-RVLFLIPKNNPPTLVg 223
                          250       260
                   ....*....|....*....|....*....
gi 1013071061  817 --CKELADLMTRCMNYDPNQRPFFRAIMR 843
Cdd:cd06640    224 dfSKPFKEFIDACLNKDPSFRPTAKELLK 252
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
588-842 3.86e-08

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MAPKKs are dual-specificity PKs that phosphorylate their downstream targets, MAPKs, at specific threonine and tyrosine residues. The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAPK, which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK or MAP2K), which itself is phosphorylated and activated by a MAPKK kinase (MAPKKK or MKKK or MAP3K). There are three MAPK subfamilies: extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38. In mammalian cells, there are seven MAPKKs (named MKK1-7) and 20 MAPKKKs. Each MAPK subfamily can be activated by at least two cognate MAPKKs and by multiple MAPKKKs. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270782 [Multi-domain]  Cd Length: 265  Bit Score: 55.81  E-value: 3.86e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  588 HLGRGTR------THIYSGTLMDYKDDEGTSEEKKIKVILKVLDPSHRDISlaffeaasmmrqvshKHIVYLYGVCVRDV 661
Cdd:cd06605      8 ELGEGNGgvvskvRHRPSGQIMAVKVIRLEIDEALQKQILRELDVLHKCNS---------------PYIVGFYGAFYSEG 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  662 ENIMVEEFVEGGPLDLFMhRKSDVLTTPWKFKVAKQLASALSYL-EDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDP 740
Cdd:cd06605     73 DISICMEYMDGGSLDKIL-KEVGRIPERILGKIAVAVVKGLIYLhEKHKIIHRDVKPSNILVNSRGQ-------VKLCDF 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  741 GIPiTVLSR---QECIERIPWIAPECVeDSKNLSVAADKWSFGTTLWEiCYNGEIPLK------DKTLIEKERFYESRCR 811
Cdd:cd06605    145 GVS-GQLVDslaKTFVGTRSYMAPERI-SGGKYTVKSDIWSLGLSLVE-LATGRFPYPppnakpSMMIFELLSYIVDEPP 221
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1013071061  812 PVTPS---CKELADLMTRCMNYDPNQRPFFRAIM 842
Cdd:cd06605    222 PLLPSgkfSPDFQDFVSQCLQKDPTERPSYKELM 255
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
924-1076 4.12e-08

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK8 can act as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II (RNAP II)-dependent transcription. CDK8 phosphorylates cyclin H, a subunit of the general transcription factor TFIIH, which results in the inhibition of TFIIH-dependent phosphorylation of the C-terminal domain of RNAP II, facilitating the inhibition of transcription. It has also been shown to promote transcription by a mechanism that is likely to involve RNAP II phosphorylation. CDK8 also functions as a stimulus-specific positive coregulator of p53 transcriptional responses. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270851 [Multi-domain]  Cd Length: 333  Bit Score: 56.60  E-value: 4.12e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  924 KEIEILRNLYHENIVKYKGICTEDGGNGIKLIMEFLPSG-----SLKEYLPKNKNKINLKQQLKYAV--QICKGMDYLGS 996
Cdd:cd07868     63 REIALLRELKHPNVISLQKVFLSHADRKVWLLFDYAEHDlwhiiKFHRASKANKKPVQLPRGMVKSLlyQILDGIHYLHA 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  997 RQYVHRDLAARNVLVESE----HQVKIGDFGLTKAIETDKEYYTvkdDRDSPV--FWY-APECLMQSKFYI-ASDVWSFG 1068
Cdd:cd07868    143 NWVLHRDLKPANILVMGEgperGRVKIADMGFARLFNSPLKPLA---DLDPVVvtFWYrAPELLLGARHYTkAIDIWAIG 219

                   ....*...
gi 1013071061 1069 VTLHELLT 1076
Cdd:cd07868    220 CIFAELLT 227
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
925-1080 4.13e-08

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 56.93  E-value: 4.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  925 EIEILRNLYHENIVKYKGICTEDggngiKLIMEFLP--SGSLKEYLPKNKNkINLKQQLKYAVQICKGMDYLGSRQYVHR 1002
Cdd:PHA03212   133 EAHILRAINHPSIIQLKGTFTYN-----KFTCLILPryKTDLYCYLAAKRN-IAICDILAIERSVLRAIQYLHENRIIHR 206
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1003 DLAARNVLVESEHQVKIGDFGLT--KAIETDKEYY----TVKDDrdspvfwyAPECLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:PHA03212   207 DIKAENIFINHPGDVCLGDFGAAcfPVDINANKYYgwagTIATN--------APELLARDPYGPAVDIWSAGIVLFEMAT 278

                   ....
gi 1013071061 1077 YCDS 1080
Cdd:PHA03212   279 CHDS 282
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
881-1139 4.16e-08

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270765 [Multi-domain]  Cd Length: 332  Bit Score: 56.47  E-value: 4.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRyDPEGDNTGEQVAVKSLKP------ESGGNHIADLKKEIEILRNLYHENIVKYkGICTEdggNGIKL 954
Cdd:cd05614      8 LGTGAYGKVFLVR-KVSGHDANKLYAMKVLRKaalvqkAKTVEHTRTERNVLEHVRQSPFLVTLHY-AFQTD---AKLHL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  955 IMEFLPSGSLKEYLPKNKNKINLKQQLkYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTkaietdKEY 1034
Cdd:cd05614     83 ILDYVSGGELFTHLYQRDHFSEDEVRF-YSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLS------KEF 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061 1035 YTVKDDRD----SPVFWYAPECLM-QSKFYIASDVWSFGVTLHELLTycdsDSSPMALflkmIGPTHGQMTVTRLVntlk 1109
Cdd:cd05614    156 LTEEKERTysfcGTIEYMAPEIIRgKSGHGKAVDWWSLGILMFELLT----GASPFTL----EGEKNTQSEVSRRI---- 223
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1013071061 1110 egkrLPCPPNCPD----EVYQLMRKCWEFQPSNR 1139
Cdd:cd05614    224 ----LKCDPPFPSfigpVARDLLQKLLCKDPKKR 253
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
924-1070 4.27e-08

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 55.69  E-value: 4.27e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  924 KEIEILRNLYHENIVKYKGICTEDggNGIKLIMEfLPSGslKEYLP--KNKNKINLKQQLKYAVQICKGMDYLGSRQYVH 1001
Cdd:cd14110     48 REYQVLRRLSHPRIAQLHSAYLSP--RHLVLIEE-LCSG--PELLYnlAERNSYSEAEVTDYLWQILSAVDYLHSRRILH 122
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1013071061 1002 RDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYTvkDDRDSPVFWYAPECLMQSKFYIASDVWSFGVT 1070
Cdd:cd14110    123 LDLRSENMIITEKNLLKIVDLGNAQPFNQGKVLMT--DKKGDYVETMAPELLEGQGAGPQTDIWAIGVT 189
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
917-1076 4.34e-08

Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This subfamily is composed of the catalytically inactive kinases with similarity to yeast Scy1. It includes four mammalian proteins called SCY1-like protein 1 (SCYL1), SCYL2, SCYL3, as well as Testis-EXpressed protein 14 (TEX14). SCYL1 binds to and co-localizes with the membrane trafficking coatomer I (COPI) complex, and regulates COPI-mediated vesicle trafficking. Null mutations in the SCYL1 gene are responsible for the pathology in mdf (muscle-deficient) mice which display progressive motor neuropathy. SCYL2, also called coated vesicle-associated kinase of 104 kDa (CVAK104), is involved in the trafficking of clathrin-coated vesicles. It also binds the HIV-1 accessory protein Vpu and acts as a regulatory factor that promotes the dephosphorylation of Vpu, facilitating the restriction of HIV-1 release. SCYL3, also called ezrin-binding protein PACE-1, may be involved in regulating cell adhesion and migration. TEX14 is required for spermatogenesis and male fertility. It localizes to kinetochores (KT) during mitosis and is a target of the mitotic kinase PLK1. It regulates the maturation of the outer KT and the KT-microtubule attachment. The SCY1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 56.18  E-value: 4.34e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  917 NHIAD-LKKEIEILRNLYHENIVKYKGiCTEDGGNGIKLIMEFLpSGSLKEYLPKNKNKINLKQQLK----YAV------ 985
Cdd:cd14011     43 EQILElLKRGVKQLTRLRHPRILTVQH-PLEESRESLAFATEPV-FASLANVLGERDNMPSPPPELQdyklYDVeikygl 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  986 -QICKGMDYLGSRQ-YVHRDLAARNVLVESEHQVKIGDFGLTKAIE--TDKEYYTVKDDRDSPVF------WYAPECLMQ 1055
Cdd:cd14011    121 lQISEALSFLHNDVkLVHGNICPESVVINSNGEWKLAGFDFCISSEqaTDQFPYFREYDPNLPPLaqpnlnYLAPEYILS 200
                          170       180
                   ....*....|....*....|.
gi 1013071061 1056 SKFYIASDVWSFGVTLHELLT 1076
Cdd:cd14011    201 KTCDPASDMFSLGVLIYAIYN 221
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
589-841 4.90e-08

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKN has a C-terminal catalytic domain that is highly homologous to PKCs. Its unique N-terminal regulatory region contains antiparallel coiled-coil (ACC) domains. In mammals, there are three PKN isoforms from different genes (designated PKN-alpha, beta, and gamma), which show different enzymatic properties, tissue distribution, and varied functions. PKN can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytokeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. The PKN subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 56.15  E-value: 4.90e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  589 LGRGtrtHIYSGTLMDYKddeGTSEEKKIKViLKVLDPSHRD--ISLA----FFEAASMMRqvsHKHIVYLYGvCVRDVE 662
Cdd:cd05589      7 LGRG---HFGKVLLAEYK---PTGELFAIKA-LKKGDIIARDevESLMcekrIFETVNSAR---HPFLVNLFA-CFQTPE 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  663 NI-MVEEFVEGGplDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGidsecgpFIKLSDPG 741
Cdd:cd05589     76 HVcFVMEYAAGG--DLMMHIHEDVFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEG-------YVKIADFG 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  742 IpitvlsrqeCIERI------------P-WIAPECVEDSkNLSVAADKWSFGTTLWEICYnGEIPLKDKTliEKERF--- 805
Cdd:cd05589    147 L---------CKEGMgfgdrtstfcgtPeFLAPEVLTDT-SYTRAVDWWGLGVLIYEMLV-GESPFPGDD--EEEVFdsi 213
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1013071061  806 --YESRcRPVTPSCKELAdLMTRCMNYDPNQR--------------PFFRAI 841
Cdd:cd05589    214 vnDEVR-YPRFLSTEAIS-IMRRLLRKNPERRlgaserdaedvkkqPFFRNI 263
PK_NRBP1_like cd13984
Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The ...
922-1146 6.07e-08

Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. This subfamily is composed of NRBP1, also called MLF1-adaptor molecule (MADM), and MADML. NRBP1 was originally named based on the presence of nuclear binding and localization motifs prior to functional analyses. It is expressed ubiquitously and is found to localize in the cytoplasm, not the nucleus. NRBP1 is an adaptor protein that interacts with myeloid leukemia factor 1 (MLF1), an oncogene that enhances myeloid development of hematopoietic cells. It also interacts with the small GTPase Rac3. NRBP1 may also be involved in Golgi to ER trafficking. MADML (for MADM-Like) has been shown to be expressed throughout development in Xenopus laevis with highest expression found in the developing lens and retina. The NRBP1-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270886 [Multi-domain]  Cd Length: 256  Bit Score: 55.24  E-value: 6.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  922 LKKEIEILRNLYHENIVKYKGICTEDGGNGIKL--IMEFLPSGSLKEYLPK---NKNKINLKQQLKYAVQICKGMDYLGS 996
Cdd:cd13984     42 IRAVFDNLIQLDHPNIVKFHRYWTDVQEEKARVifITEYMSSGSLKQFLKKtkkNHKTMNEKSWKRWCTQILSALSYLHS 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  997 RQ--YVHRDLAARNVLVESEHQVKIGdfgltkAIETDKEYYTVKDDRD--SPVFWYAPECLMQSKFYIASDVWSFGVTLH 1072
Cdd:cd13984    122 CDppIIHGNLTCDTIFIQHNGLIKIG------SVAPDAIHNHVKTCREehRNLHFFAPEYGYLEDVTTAVDIYSFGMCAL 195
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1013071061 1073 ELltycdsdsspMALFLKMIGP--THGQMTVTRLVNTLKEgkrlpcpPNCPDevyqLMRKCWEFQPSNRTSFQNLI 1146
Cdd:cd13984    196 EM----------AALEIQSNGEkvSANEEAIIRAIFSLED-------PLQKD----FIRKCLSVAPQDRPSARDLL 250
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
641-835 6.88e-08

Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. ULK2 is ubiquitously expressed and is essential in autophagy induction. ULK1 and ULK2 have unique and cell-type specific roles, but also display partially redundant roles in starvation-induced autophagy. They both display neuron-specific functions: ULK1 is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, and axon branching; ULK2 plays a role in axon development. The ULK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271022 [Multi-domain]  Cd Length: 256  Bit Score: 55.07  E-value: 6.88e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  641 MMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSDVLTTPWKFKVaKQLASALSYLEDKDLVHGNVCTKNL 720
Cdd:cd14120     45 ILKELSHENVVALLDCQETSSSVYLVMEYCNGGDLADYLQAKGTLSEDTIRVFL-QQIAAAMKALHSKGIVHRDLKPQNI 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  721 LLARegiDSECGPF-----IKLSDPG----IPITVLSRQECIERIpWIAPEcVEDSKNLSVAADKWSFGTTLWEiCYNGE 791
Cdd:cd14120    124 LLSH---NSGRKPSpndirLKIADFGfarfLQDGMMAATLCGSPM-YMAPE-VIMSLQYDAKADLWSIGTIVYQ-CLTGK 197
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1013071061  792 IPLKDKTLIEKERFYE-SRC-RPVTPS--CKELADLMTRCMNYDPNQR 835
Cdd:cd14120    198 APFQAQTPQELKAFYEkNANlRPNIPSgtSPALKDLLLGLLKRNPKDR 245
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
901-1092 7.43e-08

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 2 subunit (PhKG2) is also referred to as the testis/liver gamma isoform. Mutations in its gene cause autosomal-recessive glycogenosis of the liver. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271083 [Multi-domain]  Cd Length: 279  Bit Score: 55.36  E-value: 7.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  901 TGEQVAVK-------SLKPESGGNHIADLKKEIEILRNLY-HENIVKYkgICTEDGGNGIKLIMEFLPSGSLKEYLPKnk 972
Cdd:cd14181     34 TGQEFAVKiievtaeRLSPEQLEEVRSSTLKEIHILRQVSgHPSIITL--IDSYESSTFIFLVFDLMRRGELFDYLTE-- 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  973 nKINLKQQLKYAVQ--ICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEyytVKDDRDSPVFwYAP 1050
Cdd:cd14181    110 -KVTLSEKETRSIMrsLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGFSCHLEPGEK---LRELCGTPGY-LAP 184
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1013071061 1051 E---CLMQSK---FYIASDVWSFGVTLHELLtycdSDSSPM-----ALFLKMI 1092
Cdd:cd14181    185 EilkCSMDEThpgYGKEVDLWACGVILFTLL----AGSPPFwhrrqMLMLRMI 233
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
608-746 8.77e-08

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called Doublecortin-like and CAM kinase-like); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL (or DCAMKL) proteins belong to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL proteins contain a C-terminal kinase domain with similarity to CAMKs. They are involved in the regulation of cAMP signaling. Vertebrates contain three DCKL proteins (DCKL1-3); DCKL1 and 2 also contain a serine, threonine, and proline rich domain (SP), while DCKL3 contains only a single DCX domain instead of tandem domains. The DCKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 54.64  E-value: 8.77e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  608 DEGTSEEKKIKVI--LKVLDPSHrdisLAFFEAAsMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGplDLFmhrksDV 685
Cdd:cd14095     21 DKATDKEYALKIIdkAKCKGKEH----MIENEVA-ILRRVKHPNIVQLIEEYDTDTELYLVMELVKGG--DLF-----DA 88
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1013071061  686 LTTPWKF------KVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIDSECgpfIKLSDPGIPITV 746
Cdd:cd14095     89 ITSSTKFterdasRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHEDGSKS---LKLADFGLATEV 152
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
881-1075 9.51e-08

Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CRIK (also called citron kinase) is an effector of the small GTPase Rho. It plays an important function during cytokinesis and affects its contractile process. CRIK-deficient mice show severe ataxia and epilepsy as a result of abnormal cytokinesis and massive apoptosis in neuronal precursors. A Down syndrome critical region protein TTC3 interacts with CRIK and inhibits CRIK-dependent neuronal differentiation and neurite extension. CRIK contains a catalytic domain, a central coiled-coil domain, and a C-terminal region containing a Rho-binding domain (RBD), a zinc finger, and a pleckstrin homology (PH) domain, in addition to other motifs. The CRIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 55.39  E-value: 9.51e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRydpeGDNTGEQVAVKSL-KPESGGNH-IADLKKEIEILRNLYHENIVKYKgICTEDGGNgIKLIMEF 958
Cdd:cd05601      9 IGRGHFGEVQVVK----EKATGDIYAMKVLkKSETLAQEeVSFFEEERDIMAKANSPWITKLQ-YAFQDSEN-LYLVMEY 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  959 LPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKeyyTVk 1038
Cdd:cd05601     83 HPGGDLLSLLSRYDDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGSAAKLSSDK---TV- 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1013071061 1039 dDRDSPVF---WYAPECLM------QSKFYIASDVWSFGVTLHELL 1075
Cdd:cd05601    159 -TSKMPVGtpdYIAPEVLTsmnggsKGTYGVECDWWSLGIVAYEML 203
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
923-1076 9.55e-08

Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 54.52  E-value: 9.55e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  923 KKEIEILRNLYHENIVKYKGICTEDggNGIKLIMEFLPSGSLKEYLpkNKNKINLKQQLKYAVQICKGMDYLGSRQYVHR 1002
Cdd:cd14108     46 RRELALLAELDHKSIVRFHDAFEKR--RVVIIVTELCHEELLERIT--KRPTVCESEVRSYMRQLLEGIEYLHQNDVLHL 121
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1013071061 1003 DLAARNVLV--ESEHQVKIGDFGLTKAIETDKEYYTvkdDRDSPVFwYAPECLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd14108    122 DLKPENLLMadQKTDQVRICDFGNAQELTPNEPQYC---KYGTPEF-VAPEIVNQSPVSKVTDIWPVGVIAYLCLT 193
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
642-786 9.55e-08

Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. The PKA subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 55.10  E-value: 9.55e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  642 MRQVSH----KHI---------VYLYgVCVRDVENI-MVEEFVEGGplDLFMH-RKSDVLTTPWKFKVAKQLASALSYLE 706
Cdd:cd14209     42 LKQVEHtlneKRIlqainfpflVKLE-YSFKDNSNLyMVMEYVPGG--EMFSHlRRIGRFSEPHARFYAAQIVLAFEYLH 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  707 DKDLVHGNVCTKNLLLAREGidsecgpFIKLSDPGIPITVLSRQECIERIP-WIAPECVEdSKNLSVAADKWSFGTTLWE 785
Cdd:cd14209    119 SLDLIYRDLKPENLLIDQQG-------YIKVTDFGFAKRVKGRTWTLCGTPeYLAPEIIL-SKGYNKAVDWWALGVLIYE 190

                   .
gi 1013071061  786 I 786
Cdd:cd14209    191 M 191
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
642-836 9.72e-08

Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Yeast contains only one Aurora kinase while most higher eukaryotes have two. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2. Aurora-B is most active at the transition during metaphase to the end of mitosis. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270909 [Multi-domain]  Cd Length: 253  Bit Score: 54.40  E-value: 9.72e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  642 MRQVSHKHIVYLYGvCVRDVENI-MVEEFVEGGplDLFMH-RKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKN 719
Cdd:cd14007     54 QSHLRHPNILRLYG-YFEDKKRIyLILEYAPNG--ELYKElKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPEN 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  720 LLLAREGIdsecgpfIKLSDPGipitvLSRQECIER-------IPWIAPECVEdSKNLSVAADKWSFGTTLWEICYnGEI 792
Cdd:cd14007    131 ILLGSNGE-------LKLADFG-----WSVHAPSNRrktfcgtLDYLPPEMVE-GKEYDYKVDIWSLGVLCYELLV-GKP 196
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1013071061  793 PLKDKTLIEKERFYESrCRPVTPS--CKELADLMTRCMNYDPNQRP 836
Cdd:cd14007    197 PFESKSHQETYKRIQN-VDIKFPSsvSPEAKDLISKLLQKDPSKRL 241
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
954-1086 9.83e-08

Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271009 [Multi-domain]  Cd Length: 257  Bit Score: 54.51  E-value: 9.83e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  954 LIMEFLPSGSLKEYLPKNKNKINLKQQLkYAVQICKGMDYLGSRQYVHRDLAARNVLVES--EHQVKIGDFGLTKAIETD 1031
Cdd:cd14107     75 LILELCSSEELLDRLFLKGVVTEAEVKL-YIQQVLEGIGYLHGMNILHLDIKPDNILMVSptREDIKICDFGFAQEITPS 153
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1013071061 1032 KEYYTvkdDRDSPVFwYAPECLMQSKFYIASDVWSFGVTLHELLTyCdsdSSPMA 1086
Cdd:cd14107    154 EHQFS---KYGSPEF-VAPEIVHQEPVSAATDIWALGVIAYLSLT-C---HSPFA 200
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
881-1075 1.00e-07

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK3 is a Fas-interacting protein that induces FADD (Fas-associated death domain) phosphorylation and mediates FasL-induced JNK activation. Overexpression of HIPK3 does not affect cell death, however its expression in prostate cancer cells contributes to increased resistance to Fas receptor-mediated apoptosis. HIPK3 also plays a role in regulating steroidogenic gene expression. In response to cAMP, HIPK3 activates the phosphorylation of JNK and c-Jun, leading to increased activity of the transcription factor SF-1 (Steroidogenic factor 1), a key regulator for steroid biosynthesis in the gonad and adrenal gland. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 55.42  E-value: 1.00e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRydpeGDNTGEQVAVKSLKpesggNHIADLKK---EIEILRNLYHENIVKYKGI----CTEDGgNGIK 953
Cdd:cd14229      8 LGRGTFGQVVKCW----KRGTNEIVAVKILK-----NHPSYARQgqiEVGILARLSNENADEFNFVrayeCFQHR-NHTC 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  954 LIMEFLPSgSLKEYLPKNK-NKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVL----VESEHQVKIGDFGLTKAI 1028
Cdd:cd14229     78 LVFEMLEQ-NLYDFLKQNKfSPLPLKVIRPILQQVATALKKLKSLGLIHADLKPENIMlvdpVRQPYRVKVIDFGSASHV 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1013071061 1029 ETdkeyyTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd14229    157 SK-----TVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELF 198
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
618-835 1.05e-07

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK6 may play a role in stress responses through its activation by the mitogen-activated protein kinase (MAPK) p38 and MAPK kinase 6 (MKK6) pathway. PAK6 is highly expressed in the brain. It is not required for viability, but together with PAK5, it is required for normal levels of locomotion and activity, and for learning and memory. Increased expression of PAK6 is found in primary and metastatic prostate cancer. PAK6 may play a role in the regulation of motility. PAK6 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 54.99  E-value: 1.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  618 KVILKVLDPSHRDISLAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPL-DLFMHRKsdvLTTPWKFKVAK 696
Cdd:cd06659     48 QVAVKMMDLRKQQRRELLFNEVVIMRDYQHPNVVEMYKSYLVGEELWVLMEYLQGGALtDIVSQTR---LNEEQIATVCE 124
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  697 QLASALSYLEDKDLVHGNVCTKNLLLAREGidsecgpFIKLSDPG----IPITVLSRQECIERIPWIAPECVEDSKnLSV 772
Cdd:cd06659    125 AVLQALAYLHSQGVIHRDIKSDSILLTLDG-------RVKLSDFGfcaqISKDVPKRKSLVGTPYWMAPEVISRCP-YGT 196
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1013071061  773 AADKWSFGTTLWEICyNGEIP-LKDKTLIEKERFYES---RCRPVTPSCKELADLMTRCMNYDPNQR 835
Cdd:cd06659    197 EVDIWSLGIMVIEMV-DGEPPyFSDSPVQAMKRLRDSpppKLKNSHKASPVLRDFLERMLVRDPQER 262
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
640-835 1.06e-07

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. It is Ca2+/calmodulin (CaM)-regulated and actin-associated protein that contains an N-terminal kinase domain followed by an autoinhibitory CaM binding region and a large C-terminal extension with multiple functional domains including ankyrin (ANK) repeats, a cytoskeletal binding domain, a Death domain, and a serine-rich tail. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. The DAPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 54.64  E-value: 1.06e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  640 SMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKsDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKN 719
Cdd:cd14194     60 SILKEIQHPNVITLHEVYENKTDVILILELVAGGELFDFLAEK-ESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPEN 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  720 LLLAREGIDSecgPFIKLSDPGIPITVLSRQEC--IERIP-WIAPECVeDSKNLSVAADKWSFGTTLWeICYNGEIPL-- 794
Cdd:cd14194    139 IMLLDRNVPK---PRIKIIDFGLAHKIDFGNEFknIFGTPeFVAPEIV-NYEPLGLEADMWSIGVITY-ILLSGASPFlg 213
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1013071061  795 --KDKTLIE--------KERFYEsrcrpvtpSCKELA-DLMTRCMNYDPNQR 835
Cdd:cd14194    214 dtKQETLANvsavnyefEDEYFS--------NTSALAkDFIRRLLVKDPKKR 257
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
641-843 1.31e-07

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The specific function of Nek5 is unknown. Nek5 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 54.19  E-value: 1.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  641 MMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSDVLTTP-----WKFkvakQLASALSYLEDKDLVHGNV 715
Cdd:cd08225     52 LLAKMKHPNIVTFFASFQENGRLFIVMEYCDGGDLMKRINRQRGVLFSEdqilsWFV----QISLGLKHIHDRKILHRDI 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  716 CTKNLLLAREGIDSecgpfiKLSDPGIPITVLSRQE----CIERIPWIAPECVEDsKNLSVAADKWSFGTTLWEICyNGE 791
Cdd:cd08225    128 KSQNIFLSKNGMVA------KLGDFGIARQLNDSMElaytCVGTPYYLSPEICQN-RPYNNKTDIWSLGCVLYELC-TLK 199
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1013071061  792 IPLKDKTLIEKE-RFYESRCRPVTPS-CKELADLMTRCMNYDPNQRPFFRAIMR 843
Cdd:cd08225    200 HPFEGNNLHQLVlKICQGYFAPISPNfSRDLRSLISQLFKVSPRDRPSITSILK 253
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
611-835 1.38e-07

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 54.66  E-value: 1.38e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  611 TSEEKKIKVILKVLDPSHRDislaffEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSDVLTTPW 690
Cdd:cd14179     31 TNQEYAVKIVSKRMEANTQR------EIAALKLCEGHPNIVKLHEVYHDQLHTFLVMELLKGGELLERIKKKQHFSETEA 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  691 KFkVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIDSEcgpfIKLSDPGI-----PITVLSRQECIErIPWIAPECVE 765
Cdd:cd14179    105 SH-IMRKLVSAVSHMHDVGVVHRDLKPENLLFTDESDNSE----IKIIDFGFarlkpPDNQPLKTPCFT-LHYAAPELLN 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  766 DSkNLSVAADKWSFGTTLWEIcYNGEIPLK--DKTL-----------IEKERF-YESRC-RPVTpscKELADLMTRCMNY 830
Cdd:cd14179    179 YN-GYDESCDLWSLGVILYTM-LSGQVPFQchDKSLtctsaeeimkkIKQGDFsFEGEAwKNVS---QEAKDLIQGLLTV 253

                   ....*
gi 1013071061  831 DPNQR 835
Cdd:cd14179    254 DPNKR 258
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
587-793 1.55e-07

Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK36, also called Fused (or Fu) kinase, is involved in the Hedgehog signaling pathway. It is activated by the Smoothened (SMO) signal transducer, resulting in the stabilization of GLI transcription factors and the phosphorylation of SUFU to facilitate the nuclear accumulation of GLI. In Drosophila, Fused kinase is maternally required for proper segmentation during embryonic development and for the development of legs and wings during the larval stage. In mice, STK36 is not necessary for embryonic development, although mice deficient in STK36 display growth retardation postnatally. The STK36 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270904 [Multi-domain]  Cd Length: 253  Bit Score: 53.79  E-value: 1.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  587 EHLGRGTRTHIYSGTlmdykdDEGTSEEKKIKVILKVlDPSHRDIsLAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMV 666
Cdd:cd14002      7 ELIGEGSFGKVYKGR------RKYTGQVVALKFIPKR-GKSEKEL-RNLRQEIEILRKLNHPNIIEMLDSFETKKEFVVV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  667 EEFVEGgplDLFmhrksDVL----TTPWKF--KVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDP 740
Cdd:cd14002     79 TEYAQG---ELF-----QILeddgTLPEEEvrSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGV-------VKLCDF 143
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  741 G------IPITVLSRqecIERIP-WIAPECVEDsKNLSVAADKWSFGTTLWEICYnGEIP 793
Cdd:cd14002    144 GfaramsCNTLVLTS---IKGTPlYMAPELVQE-QPYDHTADLWSLGCILYELFV-GQPP 198
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
983-1076 1.66e-07

Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the GRK4-like group include GRK4, GRK5, GRK6, and similar GRKs. They contain an N-terminal RGS homology (RH) domain and a catalytic domain, but lack a G protein betagamma-subunit binding domain. They are localized to the plasma membrane through post-translational lipid modification or direct binding to PIP2. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270756 [Multi-domain]  Cd Length: 285  Bit Score: 54.28  E-value: 1.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  983 YAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLtkAIETdKEYYTVKdDRDSPVFWYAPECLMQSKFYIAS 1062
Cdd:cd05605    107 YAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGL--AVEI-PEGETIR-GRVGTVGYMAPEVVKNERYTFSP 182
                           90
                   ....*....|....
gi 1013071061 1063 DVWSFGVTLHELLT 1076
Cdd:cd05605    183 DWWGLGCLIYEMIE 196
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
640-824 1.69e-07

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called Doublecortin-like and CAM kinase-like 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL2 (or DCAMKL2) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL2 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL2 has been shown to interact with tubulin, JIP1/2, JNK, neurabin 2, and actin. It is associated with the terminal segments of axons and dendrites, and may function as a phosphorylation-dependent switch to control microtubule dynamics in neuronal growth cones. The DCKL2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 53.88  E-value: 1.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  640 SMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGplDLFmhrksDVLTTPWKFK------VAKQLASALSYLEDKDLVHG 713
Cdd:cd14184     51 SILRRVKHPNIIMLIEEMDTPAELYLVMELVKGG--DLF-----DAITSSTKYTerdasaMVYNLASALKYLHGLCIVHR 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  714 NVCTKNLLLAR--EGIDSecgpfIKLSDPGIPITVLSRQECIERIP-WIAPECVEDSkNLSVAADKWSFGTTLWeICYNG 790
Cdd:cd14184    124 DIKPENLLVCEypDGTKS-----LKLGDFGLATVVEGPLYTVCGTPtYVAPEIIAET-GYGLKVDIWAAGVITY-ILLCG 196
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1013071061  791 EIPLK----------DKTLIEKERFYESRCRPVTPSCKELADLM 824
Cdd:cd14184    197 FPPFRsennlqedlfDQILLGKLEFPSPYWDNITDSAKELISHM 240
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
844-1075 1.69e-07

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 54.85  E-value: 1.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  844 DINKLEEQNPDIVSEKKPATEVDPTHFEKRFLKRIRDLGEGHFGKVELC-RYdpeGDNTGEQVAVKSLkpeSGGNhiaDL 922
Cdd:PHA03207    63 DEESLSPQTDVCQEPCETTSSSDPASVVRMQYNILSSLTPGSEGEVFVCtKH---GDEQRKKVIVKAV---TGGK---TP 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  923 KKEIEILRNLYHENIVKYkgICTEDGGNGIKLIMEFLpSGSLKEYLPKnKNKINLKQQLKYAVQICKGMDYLGSRQYVHR 1002
Cdd:PHA03207   134 GREIDILKTISHRAIINL--IHAYRWKSTVCMVMPKY-KCDLFTYVDR-SGPLPLEQAITIQRRLLEALAYLHGRGIIHR 209
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1013071061 1003 DLAARNVLVESEHQVKIGDFGltKAIETDKEYYTVKDdrdspVFWY------APECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:PHA03207   210 DVKTENIFLDEPENAVLGDFG--AACKLDAHPDTPQC-----YGWSgtletnSPELLALDPYCAKTDIWSAGLVLFEMS 281
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
587-836 1.73e-07

Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST3, MST4, STK25, Schizosaccharomyces pombe Nak1 and Sid1, Saccharomyces cerevisiae sporulation-specific protein 1 (SPS1), and related proteins. Nak1 is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Sid1 is a component in the septation initiation network (SIN) signaling pathway, and plays a role in cytokinesis. SPS1 plays a role in regulating proteins required for spore wall formation. MST4 plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. STK25 may play a role in the regulation of cell migration and polarization. The MST3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 54.17  E-value: 1.73e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  587 EHLGRGTRTHIYSGTlmdykdDEGTSEEKKIKVIlkVLDPSHRDISLAFFEAaSMMRQVSHKHIVYLYGVCVRDVENIMV 666
Cdd:cd06609      7 ERIGKGSFGEVYKGI------DKRTNQVVAIKVI--DLEEAEDEIEDIQQEI-QFLSQCDSPYITKYYGSFLKGSKLWII 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  667 EEFVEGGP-LDLFmhrKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGIP-- 743
Cdd:cd06609     78 MEYCGGGSvLDLL---KPGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGD-------VKLADFGVSgq 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  744 --ITVLSRQECIERIPWIAPECVEDSkNLSVAADKWSFGTTLWEICyNGEIPLKDK------TLIEKERFYESRCRPVTP 815
Cdd:cd06609    148 ltSTMSKRNTFVGTPFWMAPEVIKQS-GYDEKADIWSLGITAIELA-KGEPPLSDLhpmrvlFLIPKNNPPSLEGNKFSK 225
                          250       260
                   ....*....|....*....|.
gi 1013071061  816 SCKELADLmtrCMNYDPNQRP 836
Cdd:cd06609    226 PFKDFVEL---CLNKDPKERP 243
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
586-842 1.76e-07

Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2, which also localizes the kinase to spindle microtubules. Aurora-A is overexpressed in many cancer types such as prostate, ovarian, breast, bladder, gastric, and pancreatic. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 53.81  E-value: 1.76e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  586 GEHLGRGTRTHIYsgtlmdykddegTSEEKKIKVIL--KVLDPSHRD---ISLAFFEAASMMRQVSHKHIVYLYGVcVRD 660
Cdd:cd14116     10 GRPLGKGKFGNVY------------LAREKQSKFILalKVLFKAQLEkagVEHQLRREVEIQSHLRHPNILRLYGY-FHD 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  661 VENI-MVEEFVEGGPLdlfmHRKSDVLTTPWKFKVA---KQLASALSYLEDKDLVHGNVCTKNLLLAREGidsecgpFIK 736
Cdd:cd14116     77 ATRVyLILEYAPLGTV----YRELQKLSKFDEQRTAtyiTELANALSYCHSKRVIHRDIKPENLLLGSAG-------ELK 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  737 LSDPGIPITVLS--RQECIERIPWIAPECVEdSKNLSVAADKWSFGTtlweICYN---GEIPLKDKTLIEKERFYeSRCR 811
Cdd:cd14116    146 IADFGWSVHAPSsrRTTLCGTLDYLPPEMIE-GRMHDEKVDLWSLGV----LCYEflvGKPPFEANTYQETYKRI-SRVE 219
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1013071061  812 PVTPS--CKELADLMTRCMNYDPNQRPFFRAIM 842
Cdd:cd14116    220 FTFPDfvTEGARDLISRLLKHNPSQRPMLREVL 252
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
881-1075 1.78e-07

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 3 (MAPKAP3 or MK3) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK3 is a bonafide substrate for the MAPK p38. It is closely related to MK2 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK3 activity is only significant when MK2 is absent. The MK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 53.84  E-value: 1.78e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  881 LGEGHFGKVELCRYDpegdNTGEQVAVKSL--KPE-----------SGGNHIADLkkeIEILRNLYHenivkykgicted 947
Cdd:cd14172     12 LGLGVNGKVLECFHR----RTGQKCALKLLydSPKarrevehhwraSGGPHIVHI---LDVYENMHH------------- 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  948 GGNGIKLIMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQ-ICKGMDYLGSRQYVHRDLAARNVLVESEHQ---VKIGDFG 1023
Cdd:cd14172     72 GKRCLLIIMECMEGGELFSRIQERGDQAFTEREASEIMRdIGTAIQYLHSMNIAHRDVKPENLLYTSKEKdavLKLTDFG 151
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1013071061 1024 LTKaiETdkeyyTVKDDRDSPVF---WYAPECLMQSKFYIASDVWSFGVTLHELL 1075
Cdd:cd14172    152 FAK--ET-----TVQNALQTPCYtpyYVAPEVLGPEKYDKSCDMWSLGVIMYILL 199
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
616-835 1.83e-07

Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SIKs are part of a complex network that regulates Na,K-ATPase to maintain sodium homeostasis and blood pressure. Vertebrates contain three forms of SIKs (SIK1-3) from three distinct genes, which display tissue-specific effects. SIK1, also called SNF1LK, controls steroidogenic enzyme production in adrenocortical cells. In the brain, both SIK1 and SIK2 regulate energy metabolism. SIK2, also called QIK or SNF1LK2, is involved in the regulation of gluconeogenesis in the liver and lipogenesis in adipose tissues, where it phosphorylates the insulin receptor substrate-1. In the liver, SIK3 (also called QSK) regulates cholesterol and bile acid metabolism. In addition, SIK2 plays an important role in the initiation of mitosis and regulates the localization of C-Nap1, a centrosome linker protein. The SIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270973 [Multi-domain]  Cd Length: 253  Bit Score: 53.55  E-value: 1.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  616 KIKVILKVLDPSHRDIS-LA-FFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGplDLFMH-RKSDVLTTPWKF 692
Cdd:cd14071     25 KTEVAIKIIDKSQLDEEnLKkIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVTEYASNG--EIFDYlAQHGRMSEKEAR 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  693 KVAKQLASALSYLEDKDLVHGNVCTKNLLLaregiDSECGpfIKLSDPGIPITVLSRQE----CiERIPWIAPECVEDSK 768
Cdd:cd14071    103 KKFWQILSAVEYCHKRHIVHRDLKAENLLL-----DANMN--IKIADFGFSNFFKPGELlktwC-GSPPYAAPEVFEGKE 174
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  769 NLSVAADKWSFGTTLWE-ICynGEIPLKDKTL-IEKERFYESRCR-PVTPScKELADLMTRCMNYDPNQR 835
Cdd:cd14071    175 YEGPQLDIWSLGVVLYVlVC--GALPFDGSTLqTLRDRVLSGRFRiPFFMS-TDCEHLIRRMLVLDPSKR 241
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
635-836 1.88e-07

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk3, also called lemur tyrosine kinase 3 (Lmtk3) is a receptor kinase containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. The function of Aatyk3 is still unknown. The Aatyk3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271108 [Multi-domain]  Cd Length: 276  Bit Score: 53.80  E-value: 1.88e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  635 FFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFM--HRKSDVLTTPWKF-------KVAKQLASALSYL 705
Cdd:cd14206     44 FISEAQPYRSLQHPNILQCLGLCTETIPFLLIMEFCQLGDLKRYLraQRKADGMTPDLPTrdlrtlqRMAYEITLGLLHL 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  706 EDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGIPITVLSRQECI--ER--IP--WIAPECVEDSKNLSVAADK--- 776
Cdd:cd14206    124 HKNNYIHSDLALRNCLLTSDLT-------VRIGDYGLSHNNYKEDYYLtpDRlwIPlrWVAPELLDELHGNLIVVDQske 196
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  777 ---WSFGTTLWEICYNGEIP---LKDK---TLIEKERFYE-SRCRPVTPSCKELADLMTRCMnYDPNQRP 836
Cdd:cd14206    197 snvWSLGVTIWELFEFGAQPyrhLSDEevlTFVVREQQMKlAKPRLKLPYADYWYEIMQSCW-LPPSQRP 265
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
581-836 2.04e-07

Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Byr1 from Schizosaccharomyces pombe, FUZ7 from Ustilago maydis, and related proteins. Byr1 phosphorylates its downstream target, the MAPK Spk1, and is regulated by the MAPKK kinase Byr2. The Spk1 cascade is pheromone-responsive and is essential for sporulation and sexual differentiation in fission yeast. FUZ7 phosphorylates and activates its target, the MAPK Crk1, which is required in mating and virulence in U. maydis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The Byr-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 53.98  E-value: 2.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  581 KDLVQGEHLGRGTR------THIYSGTLMDYKDDEGTSEEKKIKVILKVLDpshrdislaffeaasMMRQVSHKHIVYLY 654
Cdd:cd06620      5 QDLETLKDLGAGNGgsvskvLHIPTGTIMAKKVIHIDAKSSVRKQILRELQ---------------ILHECHSPYIVSFY 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  655 GVCVRDVENI-MVEEFVEGGPLDLfMHRKSDVLTTPWKFKVAKQLASALSYLEDK-DLVHGNVCTKNLLLAREGidsecg 732
Cdd:cd06620     70 GAFLNENNNIiICMEYMDCGSLDK-ILKKKGPFPEEVLGKIAVAVLEGLTYLYNVhRIIHRDIKPSNILVNSKG------ 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  733 pFIKLSDPGIpitvlSRqECIERIP--------WIAPECVEdSKNLSVAADKWSFGTTLWEICyNGEIPLKDKT------ 798
Cdd:cd06620    143 -QIKLCDFGV-----SG-ELINSIAdtfvgtstYMSPERIQ-GGKYSVKSDVWSLGLSIIELA-LGEFPFAGSNddddgy 213
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1013071061  799 --------LIEK------ERFYESRCRPvtpscKELADLMTRCMNYDPNQRP 836
Cdd:cd06620    214 ngpmgildLLQRivneppPRLPKDRIFP-----KDLRDFVDRCLLKDPRERP 260
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
617-844 2.64e-07

Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include Saccharomyces cerevisiae Rim15, Schizosaccharomyces pombe cek1, and similar fungal proteins. They contain a central catalytic domain, which contains an insert relative to MAST kinases. In addition, Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. Rim15 (or Rim15p) functions as a regulator of meiosis. It acts as a downstream effector of PKA and regulates entry into stationary phase (G0). Thus, it plays a crucial role in regulating yeast proliferation, differentiation, and aging. Cek1 may facilitate progression of mitotic anaphase. The Rim15-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270762 [Multi-domain]  Cd Length: 263  Bit Score: 53.25  E-value: 2.64e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  617 IKVILKVLDPSHRDISLAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMhRKSDVLTTPWKFKVAK 696
Cdd:cd05611     26 IKVLKKSDMIAKNQVTNVKAERAIMMIQGESPYVAKLYYSFQSKDYLYLVMEYLNGGDCASLI-KTLGGLPEDWAKQYIA 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  697 QLASALSYLEDKDLVHGNVCTKNLLLAREGidsecgpFIKLSDPGipitvLSRQECIERIP--------WIAPECVEdSK 768
Cdd:cd05611    105 EVVLGVEDLHQRGIIHRDIKPENLLIDQTG-------HLKLTDFG-----LSRNGLEKRHNkkfvgtpdYLAPETIL-GV 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  769 NLSVAADKWSFGTTLWEICY-----NGEIPLKDKTLIEKERFYESRcRPVTPSCKELADLMTRCMNYDPNQR-------- 835
Cdd:cd05611    172 GDDKMSDWWSLGCVIFEFLFgyppfHAETPDAVFDNILSRRINWPE-EVKEFCSPEAVDLINRLLCMDPAKRlgangyqe 250
                          250
                   ....*....|...
gi 1013071061  836 ----PFFRAIMRD 844
Cdd:cd05611    251 ikshPFFKSINWD 263
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
878-1076 2.90e-07

Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PRP4 phosphorylates a number of factors involved in the formation of active spliceosomes, which catalyze pre-mRNA splicing. It phosphorylates PRP6 and PRP31, components of the U4/U6-U5 tri-small nuclear ribonucleoprotein (snRNP), during spliceosomal complex formation. In fission yeast, PRP4 phosphorylates the splicing factor PRP1 (U5-102 kD in mammals). Thus, PRP4 plays a key role in regulating spliceosome assembly and pre-mRNA splicing. It also plays an important role in mitosis by acting as a spindle assembly checkpoint kinase that is required for chromosome alignment and the recruitment of the checkpoint proteins MPS1, MAD1, and MAD2 at kinetochores. The PRP4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 53.77  E-value: 2.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  878 IRDLGEGHFGKVELCRydpEGDNTGEQVAVKSLKpesgGN---HIADLKkEIEILRNL--------YH----ENIVKYKG 942
Cdd:cd14135      5 YGYLGKGVFSNVVRAR---DLARGNQEVAIKIIR----NNelmHKAGLK-ELEILKKLndadpddkKHcirlLRHFEHKN 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  943 -ICtedggngikLIMEFLpSGSLKEYLPK-NKNK-INLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLV-ESEHQVK 1018
Cdd:cd14135     77 hLC---------LVFESL-SMNLREVLKKyGKNVgLNIKAVRSYAQQLFLALKHLKKCNILHADIKPDNILVnEKKNTLK 146
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1013071061 1019 IGDFGLTKAI-ETDKEYYTVKddRdspvFWYAPECLMQSKFYIASDVWSFGVTLHELLT 1076
Cdd:cd14135    147 LCDFGSASDIgENEITPYLVS--R----FYRAPEIILGLPYDYPIDMWSVGCTLYELYT 199
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
643-836 3.90e-07

Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of HAL4, Saccharomyces cerevisiae Ptk2/Stk2, and similar fungal proteins. Proteins in this subfamily are involved in regulating ion transporters. In budding and fission yeast, HAL4 promotes potassium ion uptake, which increases cellular resistance to other cations such as sodium, lithium, and calcium ions. HAL4 stabilizes the major high-affinity K+ transporter Trk1 at the plasma membrane under low K+ conditions, which prevents endocytosis and vacuolar degradation. Budding yeast Ptk2 phosphorylates and regulates the plasma membrane H+ ATPase, Pma1. The HAL4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270896 [Multi-domain]  Cd Length: 265  Bit Score: 52.69  E-value: 3.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  643 RQVSHKHIVYLYGVCVRDVENI-MVEEFVEGGPLDLFMhRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLL 721
Cdd:cd13994     52 SKLHHPNIVKVLDLCQDLHGKWcLVMEYCPGGDLFTLI-EKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENIL 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  722 LAREGIdsecgpfIKLSDPGIPITVLSRQE---CIER-----IPWIAPECVEDSKNLSVAADKWSFGTTLWEIcYNGEIP 793
Cdd:cd13994    131 LDEDGV-------LKLTDFGTAEVFGMPAEkesPMSAglcgsEPYMAPEVFTSGSYDGRAVDVWSCGIVLFAL-FTGRFP 202
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1013071061  794 LKDKTLIEK--ERFYESRCRPVTPSCKELADLMTRC-------MNYDPNQRP 836
Cdd:cd13994    203 WRSAKKSDSayKAYEKSGDFTNGPYEPIENLLPSECrrliyrmLHPDPEKRI 254
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
586-786 4.19e-07

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 53.89  E-value: 4.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  586 GEHLGRGTRTHIYSGTLMDykddegTSEEKKIKVILKvlDPSHRDISLAffeaasMMRQVSHKHIVYL----YGVCVRDV 661
Cdd:PTZ00036    71 GNIIGNGSFGVVYEAICID------TSEKVAIKKVLQ--DPQYKNRELL------IMKNLNHINIIFLkdyyYTECFKKN 136
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  662 E-NI---MVEEFVEGGPLDLFMHRKSDVLTTPWkFKV---AKQLASALSYLEDKDLVHGNVCTKNLLlaregIDSECGPf 734
Cdd:PTZ00036   137 EkNIflnVVMEFIPQTVHKYMKHYARNNHALPL-FLVklySYQLCRALAYIHSKFICHRDLKPQNLL-----IDPNTHT- 209
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1013071061  735 IKLSDPGIPITVLSRQECIERIP---WIAPECVEDSKNLSVAADKWSFGTTLWEI 786
Cdd:PTZ00036   210 LKLCDFGSAKNLLAGQRSVSYICsrfYRAPELMLGATNYTTHIDLWSLGCIIAEM 264
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
641-842 4.43e-07

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek8 contains an N-terminal kinase catalytic domain and a C-terminal RCC1 (regulator of chromosome condensation) domain. A double point mutation in Nek8 causes cystic kidney disease in mice that genetically resembles human autosomal recessive polycystic kidney disease (ARPKD). Nek8 is also associated with a rare form of juvenile renal cystic disease, nephronophthisis type 9. It has been suggested that a defect in the ciliary localization of Nek8 contributes to the development of cysts manifested by these diseases. Nek8 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270859 [Multi-domain]  Cd Length: 256  Bit Score: 52.43  E-value: 4.43e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  641 MMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSDVLTTPWK-FKVAKQLASALSYLEDKDLVHGNVCTKN 719
Cdd:cd08220     52 VLSMLHHPNIIEYYESFLEDKALMIVMEYAPGGTLFEYIQQRKGSLLSEEEiLHFFVQILLALHHVHSKQILHRDLKTQN 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  720 LLLAREGIdsecgpFIKLSDPGIPITVLSRQECIERI--P-WIAPECVEdSKNLSVAADKWSFGTTLWEIC-----YNGE 791
Cdd:cd08220    132 ILLNKKRT------VVKIGDFGISKILSSKSKAYTVVgtPcYISPELCE-GKPYNQKSDIWALGCVLYELAslkraFEAA 204
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1013071061  792 ----IPLKdktlIEKERFyesrcRPVTPS-CKELADLMTRCMNYDPNQRPFFRAIM 842
Cdd:cd08220    205 nlpaLVLK----IMRGTF-----APISDRySEELRHLILSMLHLDPNKRPTLSEIM 251
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
589-836 5.57e-07

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek7 is required for mitotic spindle formation and cytokinesis. It is enriched in the centrosome and is critical for microtubule nucleation. Nek7 is activated by Nek9 during mitosis, and may regulate the p70 ribosomal S6 kinase. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 52.73  E-value: 5.57e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  589 LGRGTRTHIYSGTlmdYKDDEGTSEEKKIKvILKVLDPSHRDISLaffEAASMMRQVSHKHIVYLYGVCVRDVENIMVEE 668
Cdd:cd08229     32 IGRGQFSEVYRAT---CLLDGVPVALKKVQ-IFDLMDAKARADCI---KEIDLLKQLNHPNVIKYYASFIEDNELNIVLE 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  669 FVEGGPLD-LFMHRKSDVLTTP----WKFKVakQLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGIP 743
Cdd:cd08229    105 LADAGDLSrMIKHFKKQKRLIPektvWKYFV--QLCSALEHMHSRRVMHRDIKPANVFITATGV-------VKLGDLGLG 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  744 ITVLSRQECIERIP----WIAPECVEDSkNLSVAADKWSFGTTLWEICyngeiPLKDKTLIEKERFYeSRCR-------P 812
Cdd:cd08229    176 RFFSSKTTAAHSLVgtpyYMSPERIHEN-GYNFKSDIWSLGCLLYEMA-----ALQSPFYGDKMNLY-SLCKkieqcdyP 248
                          250       260
                   ....*....|....*....|....*..
gi 1013071061  813 VTPS---CKELADLMTRCMNYDPNQRP 836
Cdd:cd08229    249 PLPSdhySEELRQLVNMCINPDPEKRP 275
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
610-835 6.12e-07

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK5 is mainly expressed in the brain. It is not required for viability, but together with PAK6, it is required for normal levels of locomotion and activity, and for learning and memory. PAK5 cooperates with Inca (induced in neural crest by AP2) in the regulation of cell adhesion and cytoskeletal organization in the embryo and in neural crest cells during craniofacial development. PAK5 may also play a role in controlling the signaling of Raf-1, an effector of Ras, at the mitochondria. PAK5 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132989 [Multi-domain]  Cd Length: 292  Bit Score: 52.73  E-value: 6.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  610 GTSEEKKIKVILKVLDPSHRDISLAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPL-DLFMHRKsdvLTT 688
Cdd:cd06658     41 ATEKHTGKQVAVKKMDLRKQQRRELLFNEVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLEGGALtDIVTHTR---MNE 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  689 PWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGidsecgpFIKLSDPG----IPITVLSRQECIERIPWIAPECV 764
Cdd:cd06658    118 EQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDG-------RIKLSDFGfcaqVSKEVPKRKSLVGTPYWMAPEVI 190
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1013071061  765 EDSKnLSVAADKWSFGTTLWEICyNGEIPLKDKTLIEKERFYESRCRP-------VTPSCKELADLMtrcMNYDPNQR 835
Cdd:cd06658    191 SRLP-YGTEVDIWSLGIMVIEMI-DGEPPYFNEPPLQAMRRIRDNLPPrvkdshkVSSVLRGFLDLM---LVREPSQR 263
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
640-801 6.28e-07

Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include human PRKX (X chromosome-encoded protein kinase), Drosophila DC2, and similar proteins. PRKX is present in many tissues including fetal and adult brain, kidney, and lung. The PRKX gene is located in the Xp22.3 subregion and has a homolog called PRKY on the Y chromosome. An abnormal interchange between PRKX aand PRKY leads to the sex reversal disorder of XX males and XY females. PRKX is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PRKX-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270763 [Multi-domain]  Cd Length: 292  Bit Score: 52.44  E-value: 6.28e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  640 SMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMhRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKN 719
Cdd:cd05612     53 RVLKEVSHPFIIRLFWTEHDQRFLYMLMEYVPGGELFSYL-RNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPEN 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  720 LLLAREGidsecgpFIKLSDPGIPITVLSRQECIERIP-WIAPECVEdSKNLSVAADKWSFGTTLWEIcYNGEIPLKDKT 798
Cdd:cd05612    132 ILLDKEG-------HIKLTDFGFAKKLRDRTWTLCGTPeYLAPEVIQ-SKGHNKAVDWWALGILIYEM-LVGYPPFFDDN 202

                   ...
gi 1013071061  799 LIE 801
Cdd:cd05612    203 PFG 205
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
579-835 7.01e-07

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I gamma; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 52.30  E-value: 7.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  579 LKKDLVQGEHLGRGTRTHIYsgtLMDYKDdegTSEEKKIKVILKVldPSHRDISLAffEAASMMRQVSHKHIVYLYGVCV 658
Cdd:cd14166      1 IRETFIFMEVLGSGAFSEVY---LVKQRS---TGKLYALKCIKKS--PLSRDSSLE--NEIAVLKRIKHENIVTLEDIYE 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  659 RDVENIMVEEFVEGGPL-DLFMHRksDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIDSEcgpfIKL 737
Cdd:cd14166     71 STTHYYLVMQLVSGGELfDRILER--GVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYLTPDENSK----IMI 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  738 SDPGipitvLSRQE--------CieRIP-WIAPEcVEDSKNLSVAADKWSFGTTLWeICYNGEIPLKDKT---LIEK--E 803
Cdd:cd14166    145 TDFG-----LSKMEqngimstaC--GTPgYVAPE-VLAQKPYSKAVDCWSIGVITY-ILLCGYPPFYEETesrLFEKikE 215
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1013071061  804 RFYESRcRPVTPSCKELADLMTRCM-NYDPNQR 835
Cdd:cd14166    216 GYYEFE-SPFWDDISESAKDFIRHLlEKNPSKR 247
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
639-782 8.74e-07

Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This family is composed of MLCKs and related MLCK-like kinase domains from giant STKs such as titin, obscurin, SPEG, Unc-89, Trio, kalirin, and Twitchin. Also included in this family are Death-Associated Protein Kinases (DAPKs) and Death-associated protein kinase-Related Apoptosis-inducing protein Kinase (DRAKs). MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. Titin, obscurin, Twitchin, and SPEG are muscle proteins involved in the contractile apparatus. The giant STKs are multidomain proteins containing immunoglobulin (Ig), fibronectin type III (FN3), SH3, RhoGEF, PH and kinase domains. Titin, obscurin, Twitchin, and SPEG contain many Ig domain repeats at the N-terminus, while Trio and Kalirin contain spectrin-like repeats. The MLCK-like family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270908 [Multi-domain]  Cd Length: 247  Bit Score: 51.50  E-value: 8.74e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  639 ASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPL-DLFMHRksDVLTTPwkfKVA---KQLASALSYLEDKDLVHGN 714
Cdd:cd14006     40 ISILNQLQHPRIIQLHEAYESPTELVLILELCSGGELlDRLAER--GSLSEE---EVRtymRQLLEGLQYLHNHHILHLD 114
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1013071061  715 VCTKNLLLAREGIDSecgpfIKLSDPGI--PITVLSRQECIERIP-WIAPECVEDSKnLSVAADKWSFGTT 782
Cdd:cd14006    115 LKPENILLADRPSPQ-----IKIIDFGLarKLNPGEELKEIFGTPeFVAPEIVNGEP-VSLATDMWSIGVL 179
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
582-875 9.97e-07

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. Although T-cells also express other PKC isoforms, PKC-theta is unique in that upon antigen stimulation, it is translocated to the plasma membrane at the immunological synapse, where it mediates signals essential for T-cell activation. It is essential for TCR-induced proliferation, cytokine production, T-cell survival, and the differentiation and effector function of T-helper (Th) cells, particularly Th2 and Th17. PKC-theta is being developed as a therapeutic target for Th2-mediated allergic inflammation and Th17-mediated autoimmune diseases. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 52.23  E-value: 9.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  582 DLVQGEHLGRGTRTHIYSGTLmdykddEGTSEEKKIKVILKVLDPSHRDISLAFFEAASMMRQVSHKHIVYLYgVCVRDV 661
Cdd:cd05619      6 DFVLHKMLGKGSFGKVFLAEL------KGTNQFFAIKALKKDVVLMDDDVECTMVEKRVLSLAWEHPFLTHLF-CTFQTK 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  662 ENIM-VEEFVEGGplDLFMHRKS-DVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGidsecgpFIKLSD 739
Cdd:cd05619     79 ENLFfVMEYLNGG--DLMFHIQScHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDG-------HIKIAD 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  740 PGIpitvlsrqeCIERI-------------PWIAPECVEDSK-NLSVaaDKWSFGTTLWEICYnGEIPLKDKTliEKERF 805
Cdd:cd05619    150 FGM---------CKENMlgdaktstfcgtpDYIAPEILLGQKyNTSV--DWWSFGVLLYEMLI-GQSPFHGQD--EEELF 215
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  806 YESRC-RPVTPS--CKELADLMTRCMNYDPNQR----------PFFRAImrDINKLEEQNPDIVSEKKPATEVDPTHFEK 872
Cdd:cd05619    216 QSIRMdNPFYPRwlEKEAKDILVKLFVREPERRlgvrgdirqhPFFREI--NWEALEEREIEPPFKPKVKSPFDCSNFDK 293

                   ...
gi 1013071061  873 RFL 875
Cdd:cd05619    294 EFL 296
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
643-783 1.03e-06

Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chk1 is implicated in many major checkpoints of the cell cycle, providing a link between upstream sensors and the cell cycle engine. It plays an important role in DNA damage response and maintaining genomic stability. Chk1 acts as an effector of the sensor kinase, ATR (ATM and Rad3-related), a member of the PI3K family, which is activated upon DNA replication stress. Chk1 delays mitotic entry in response to replication blocks by inhibiting cyclin dependent kinase (Cdk) activity. In addition, Chk1 contributes to the function of centrosome and spindle-based checkpoints, inhibits firing of origins of DNA replication (Ori), and represses transcription of cell cycle proteins including cyclin B and Cdk1. The Chk1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270971 [Multi-domain]  Cd Length: 261  Bit Score: 51.56  E-value: 1.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  643 RQVSHKHIVYLYGvCVRDVE-NIMVEEFVEGGplDLFMHRKSDVLTTPwkfKVA----KQLASALSYLEDKDLVHGNVCT 717
Cdd:cd14069     55 KMLSHKNVVRFYG-HRREGEfQYLFLEYASGG--ELFDKIEPDVGMPE---DVAqfyfQQLMAGLKYLHSCGITHRDIKP 128
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1013071061  718 KNLLLAREGIdsecgpfIKLSDPGIPiTVLSRQ-------ECIERIPWIAPECVEDSKNLSVAADKWSFGTTL 783
Cdd:cd14069    129 ENLLLDENDN-------LKISDFGLA-TVFRYKgkerllnKMCGTLPYVAPELLAKKKYRAEPVDVWSCGIVL 193
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
664-793 1.10e-06

Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of fungal Wee1 proteins, also called Swe1 in budding yeast and Mik1 in fission yeast. Yeast Wee1 is required to control cell size. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The fungal Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 51.65  E-value: 1.10e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  664 IMVEeFVEGGPLDLFMHRKSD--VLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPG 741
Cdd:cd14052     80 IQTE-LCENGSLDVFLSELGLlgRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGT-------LKIGDFG 151
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1013071061  742 IPiTVLSRQECIER---IPWIAPEcVEDSKNLSVAADKWSFGTTLWEICYNGEIP 793
Cdd:cd14052    152 MA-TVWPLIRGIERegdREYIAPE-ILSEHMYDKPADIFSLGLILLEAAANVVLP 204
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
608-877 1.15e-06

N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), p90-RSKs, or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 52.02  E-value: 1.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  608 DEGTSEEKKI--KVILKVLD----PSHRDIsLAffeaasmmrQVSHKHIVYLYGVCVRDVENIMVEEFVEGGplDLFMHR 681
Cdd:cd05582     21 DAGTLYAMKVlkKATLKVRDrvrtKMERDI-LA---------DVNHPFIVKLHYAFQTEGKLYLILDFLRGG--DLFTRL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  682 KSDVLTTP--WKFKVAkQLASALSYLEDKDLVHGNVCTKNLLLAREGidsecgpFIKLSDPGipitvLSRqECIER---- 755
Cdd:cd05582     89 SKEVMFTEedVKFYLA-ELALALDHLHSLGIIYRDLKPENILLDEDG-------HIKLTDFG-----LSK-ESIDHekka 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  756 ------IPWIAPECVeDSKNLSVAADKWSFGTTLWEIcYNGEIPLKDK------TLIEKERFyeSRCRPVTPSCKE-LAD 822
Cdd:cd05582    155 ysfcgtVEYMAPEVV-NRRGHTQSADWWSFGVLMFEM-LTGSLPFQGKdrketmTMILKAKL--GMPQFLSPEAQSlLRA 230
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1013071061  823 LMTRC----MNYDPN------QRPFFRAImrDINKLEeqNPDIVSEKKPA-TEVDPTH-FEKRFLKR 877
Cdd:cd05582    231 LFKRNpanrLGAGPDgveeikRHPFFATI--DWNKLY--RKEIKPPFKPAvSRPDDTFyFDPEFTSR 293
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
618-836 1.28e-06

Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC family consists of Cyclin-Dependent protein Kinases (CDKs), Mitogen-activated protein kinases (MAPKs) such as Extracellular signal-regulated kinase (ERKs), c-Jun N-terminal kinases (JNKs), and p38, and other kinases. CDKs belong to a large subfamily of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Other members of the CMGC family include casein kinase 2 (CK2), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK), Glycogen Synthase Kinase 3 (GSK3), among many others. The CMGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 51.08  E-value: 1.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  618 KVILKVLDPSHRDISLAFFEAASMMR---QVSHKHIVYLYGVcVRDVENI---MVEEFVEggpLDL--FMHRKSDVLTTP 689
Cdd:cd05118     26 KVAIKKIKNDFRHPKAALREIKLLKHlndVEGHPNIVKLLDV-FEHRGGNhlcLVFELMG---MNLyeLIKDYPRGLPLD 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  690 WKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIDsecgpfIKLSDPGIPiTVLSRQECIERI---PWIAPECVED 766
Cdd:cd05118    102 LIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLELGQ------LKLADFGLA-RSFTSPPYTPYVatrWYRAPEVLLG 174
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1013071061  767 SKNLSVAADKWSFGTTLWEIcYNGEI------PLKDKTLIEKerfyesrcrpvTPSCKELADLMTRCMNYDPNQRP 836
Cdd:cd05118    175 AKPYGSSIDIWSLGCILAEL-LTGRPlfpgdsEVDQLAKIVR-----------LLGTPEALDLLSKMLKYDPAKRI 238
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
605-842 1.34e-06

Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDKL1-5 and similar proteins. Some CDKLs, like CDKL1 and CDKL3, may be implicated in transformation and others, like CDKL3 and CDKL5, are associated with mental retardation when impaired. CDKL2 plays a role in learning and memory. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270827 [Multi-domain]  Cd Length: 288  Bit Score: 51.55  E-value: 1.34e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  605 YKDDEGTSEEKKIKVilkvldpshRDISlaffeaasMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSD 684
Cdd:cd07833     34 FKESEDDEDVKKTAL---------REVK--------VLRQLRHENIVNLKEAFRRKGRLYLVFEYVERTLLELLEASPGG 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  685 -----VLTTPWkfkvakQLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGI--PITVLSRQECIERIP 757
Cdd:cd07833     97 lppdaVRSYIW------QLLQAIAYCHSHNIIHRDIKPENILVSESGV-------LKLCDFGFarALTARPASPLTDYVA 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  758 --WI-APECVEDSKNLSVAADKWSFGTTLWEIC-----YNGEIPLKDKTLIEK----------ERFYE----SRCRPVTP 815
Cdd:cd07833    164 trWYrAPELLVGDTNYGKPVDVWAIGCIMAELLdgeplFPGDSDIDQLYLIQKclgplppshqELFSSnprfAGVAFPEP 243
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1013071061  816 SCKE-------------LADLMTRCMNYDPNQRPFFRAIM 842
Cdd:cd07833    244 SQPEslerrypgkvsspALDFLKACLRMDPKERLTCDELL 283
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
619-835 1.42e-06

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK4 regulates cell morphology and cytoskeletal organization. It is essential for embryonic viability and proper neural development. Mice lacking PAK4 die due to defects in the fetal heart. In addition, their spinal cord motor neurons showed failure to differentiate and migrate. PAK4 also plays a role in cell survival and tumorigenesis. It is overexpressed in many primary tumors including colon, esophageal, and mammary tumors. PAK4 has also been implicated in viral and bacterial infection pathways. PAK4 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 51.56  E-value: 1.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  619 VILKVLDPSHRDISLAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPL-DLFMHRKsdvLTTPWKFKVAKQ 697
Cdd:cd06657     48 VAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALtDIVTHTR---MNEEQIAAVCLA 124
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  698 LASALSYLEDKDLVHGNVCTKNLLLAREGidsecgpFIKLSDPGIPITV---LSRQECIERIP-WIAPECVEDSKnLSVA 773
Cdd:cd06657    125 VLKALSVLHAQGVIHRDIKSDSILLTHDG-------RVKLSDFGFCAQVskeVPRRKSLVGTPyWMAPELISRLP-YGPE 196
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1013071061  774 ADKWSFGTTLWEIC-----YNGEIPLKDKTLIEKERFYESR-CRPVTPSCKELADlmtRCMNYDPNQR 835
Cdd:cd06657    197 VDIWSLGIMVIEMVdgeppYFNEPPLKAMKMIRDNLPPKLKnLHKVSPSLKGFLD---RLLVRDPAQR 261
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
622-848 1.45e-06

Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK16 is associated with many names including Myristylated and Palmitylated Serine/threonine Kinase 1 (MPSK1), Kinase related to cerevisiae and thaliana (Krct), and Protein Kinase expressed in day 12 fetal liver (PKL12). It is widely expressed in mammals with highest levels found in liver, testis, and kidney. It is localized in the Golgi but is translocated to the nucleus upon disorganization of the Golgi. STK16 is constitutively active and is capable of phosphorylating itself and other substrates. It may be involved in regulating stromal-epithelial interactions during mammary gland ductal morphogenesis. It may also function as a transcriptional co-activator of type-C natriuretic peptide and VEGF. The STK16 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270888 [Multi-domain]  Cd Length: 282  Bit Score: 51.14  E-value: 1.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  622 KVLDPSHRDISLAFFEAaSMMRQVSHKHIVYLYGVCVRDVEN-----IMVEEFVEGGPL-DLF--MHRKSDVLTTPWKFK 693
Cdd:cd13986     32 KILCHSKEDVKEAMREI-ENYRLFNHPNILRLLDSQIVKEAGgkkevYLLLPYYKRGSLqDEIerRLVKGTFFPEDRILH 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  694 VAKQLASALSYL---EDKDLVHGNVCTKNLLLAREGIdsecgPFikLSDPG----IPITVLSRQECIER---------IP 757
Cdd:cd13986    111 IFLGICRGLKAMhepELVPYAHRDIKPGNVLLSEDDE-----PI--LMDLGsmnpARIEIEGRREALALqdwaaehctMP 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  758 WIAPE-------CVEDSKnlsvaADKWSFGTTLWEICYnGEIPLkDKTLIEKERFYESRCRPVT--PSC----KELADLM 824
Cdd:cd13986    184 YRAPElfdvkshCTIDEK-----TDIWSLGCTLYALMY-GESPF-ERIFQKGDSLALAVLSGNYsfPDNsrysEELHQLV 256
                          250       260
                   ....*....|....*....|....
gi 1013071061  825 TRCMNYDPNQRPFFRAIMRDINKL 848
Cdd:cd13986    257 KSMLVVNPAERPSIDDLLSRVHDL 280
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
697-843 3.20e-06

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek1 is associated with centrosomes throughout the cell cycle. It is involved in the formation of primary cilium and in the maintenance of centrosomes. It cycles through the nucleus and may be capable of relaying signals between the cilium and the nucleus. Nek1 is implicated in the development of polycystic kidney disease, which is characterized by benign polycystic tumors formed by abnormal overgrowth of renal epithelial cells. It appears also to be involved in DNA damage response, and may be important for both correct DNA damage checkpoint activation and DNA repair. Nek1 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 49.81  E-value: 3.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  697 QLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGIPITVLSRQE----CIERIPWIAPECVEDsKNLSV 772
Cdd:cd08218    109 QLCLALKHVHDRKILHRDIKSQNIFLTKDGI-------IKLGDFGIARVLNSTVElartCIGTPYYLSPEICEN-KPYNN 180
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1013071061  773 AADKWSFGTTLWEICyngeiPLKD-------KTLIEKerFYESRCRPVTPS-CKELADLMTRCMNYDPNQRPFFRAIMR 843
Cdd:cd08218    181 KSDIWALGCVLYEMC-----TLKHafeagnmKNLVLK--IIRGSYPPVPSRySYDLRSLVSQLFKRNPRDRPSINSILE 252
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
619-847 3.23e-06

Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-2D is allso called Retinal Guanylyl Cyclase 1 (RETGC-1) or Rod Outer Segment membrane Guanylate Cyclase (ROS-GC). It is found in the photoreceptors of the retina where it anchors the reciprocal feedback loop between calcium and cGMP, which regulates the dark, light, and recovery phases in phototransduction. It is also found in other sensory neurons and may be a universal transduction component that plays a role in the perception of all senses. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-2D subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270945 [Multi-domain]  Cd Length: 267  Bit Score: 50.10  E-value: 3.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  619 VILKVLDP-SHRDISLAFFEAASMMRQVSHKHI-VYLYGVCVRDVENIMVEEFVEGGPLDLFmhRKSDVlTTPWKFKVA- 695
Cdd:cd14043     26 VWLKKFPGgSHTELRPSTKNVFSKLRELRHENVnLFLGLFVDCGILAIVSEHCSRGSLEDLL--RNDDM-KLDWMFKSSl 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  696 -KQLASALSYLEDKDLVHGNVCTKNLLlaregIDsecGPFI-KLSDPGIPitVLSRQECIERIP-------WIAPECVED 766
Cdd:cd14043    103 lLDLIKGMRYLHHRGIVHGRLKSRNCV-----VD---GRFVlKITDYGYN--EILEAQNLPLPEpapeellWTAPELLRD 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  767 ---SKNLSVAADKWSFGTTLWEICYNGE----IPLKDKTLIEKERFYESRCRP-VTPSCK--ELADLMTRCMNYDPNQRP 836
Cdd:cd14043    173 prlERRGTFPGDVFSFAIIMQEVIVRGApycmLGLSPEEIIEKVRSPPPLCRPsVSMDQAplECIQLMKQCWSEAPERRP 252
                          250
                   ....*....|....
gi 1013071061  837 FFRAI---MRDINK 847
Cdd:cd14043    253 TFDQIfdqFKSINK 266
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
584-836 3.71e-06

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK1 is a MAPK kinase kinase (MAPKKK or MKKK) that phosphorylates and activates activates the ERK1/2 and c-Jun N-terminal kinase (JNK) pathways by activating their respective MAPKKs, MEK1/2 and MKK4/MKK7, respectively. MEKK1 is important in regulating cell survival and apoptosis. MEKK1 also plays a role in cell migration, tissue maintenance and homeostasis, and wound healing. The MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270800 [Multi-domain]  Cd Length: 268  Bit Score: 49.74  E-value: 3.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  584 VQGEHLGRGTRTHIY------SGTLMDYKD----DEGTSEEKKikvilkVLDPSHRDISlaffeaasMMRQVSHKHIVYL 653
Cdd:cd06630      3 LKGPLLGTGAFSSCYqardvkTGTLMAVKQvsfcRNSSSEQEE------VVEAIREEIR--------MMARLNHPNIVRM 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  654 YGVCVRDVENIMVEEFVEGGPLDLFMHRK---SDVLTTpwkfKVAKQLASALSYLEDKDLVHGNVCTKNLLlaregIDSe 730
Cdd:cd06630     69 LGATQHKSHFNIFVEWMAGGSVASLLSKYgafSENVII----NYTLQILRGLAYLHDNQIIHRDLKGANLL-----VDS- 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  731 CGPFIKLSDPGIPITVLSRQ--------ECIERIPWIAPEcVEDSKNLSVAADKWSFGTTLWEIC-----YNGEIPLKDK 797
Cdd:cd06630    139 TGQRLRIADFGAAARLASKGtgagefqgQLLGTIAFMAPE-VLRGEQYGRSCDVWSVGCVIIEMAtakppWNAEKISNHL 217
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1013071061  798 TLIekerfYESRCRPVTPSCKE-----LADLMTRCMNYDPNQRP 836
Cdd:cd06630    218 ALI-----FKIASATTPPPIPEhlspgLRDVTLRCLELQPEDRP 256
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
637-780 3.74e-06

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs, also called STK17, were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. They may play a role in apoptotic signaling. The DRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271008 [Multi-domain]  Cd Length: 268  Bit Score: 50.04  E-value: 3.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  637 EAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGplDLFMHRKSD-VLTTPWKFKVAKQLASALSYLEDKDLVHGNV 715
Cdd:cd14106     57 EIAVLELCKDCPRVVNLHEVYETRSELILILELAAGG--ELQTLLDEEeCLTEADVRRLMRQILEGVQYLHERNIVHLDL 134
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1013071061  716 CTKNLLLAREGIDSEcgpfIKLSDPGIPiTVLSRQECIERI----PWIAPEcVEDSKNLSVAADKWSFG 780
Cdd:cd14106    135 KPQNILLTSEFPLGD----IKLCDFGIS-RVIGEGEEIREIlgtpDYVAPE-ILSYEPISLATDMWSIG 197
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
607-835 4.01e-06

Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal STKs including Saccharomyces cerevisiae RCK1 and RCK2, Schizosaccharomyces pombe Sty1-regulated kinase 1 (Srk1), and similar proteins. RCK1, RCK2 (or Rck2p), and Srk1 are MAPK-activated protein kinases. RCK1 and RCK2 are involved in oxidative and metal stress resistance in budding yeast. RCK2 also regulates rapamycin sensitivity in both S. cerevisiae and Candida albicans. Srk1 is activated by Sty1/Spc1 and is involved in negatively regulating cell cycle progression by inhibiting Cdc25. The RCK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270998 [Multi-domain]  Cd Length: 295  Bit Score: 50.13  E-value: 4.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  607 DDEGTSEEKKIKVILKVlDPSHRDI----SLAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPL------- 675
Cdd:cd14096     22 PLRNTGKPVAIKVVRKA-DLSSDNLkgssRANILKEVQIMKRLSHPNIVKLLDFQESDEYYYIVLELADGGEIfhqivrl 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  676 -----DLFMHrksdvlttpwkfkVAKQLASALSYLEDKDLVHGNVCTKNLL------------LAREGIDSEC---GPF- 734
Cdd:cd14096    101 tyfseDLSRH-------------VITQVASAVKYLHEIGVVHRDIKPENLLfepipfipsivkLRKADDDETKvdeGEFi 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  735 ----------IKLSDPGIPITVLSRQeciERIP-----WIAPECVEDsKNLSVAADKWSFGTTLWEI-CynGEIPLKDK- 797
Cdd:cd14096    168 pgvggggigiVKLADFGLSKQVWDSN---TKTPcgtvgYTAPEVVKD-ERYSKKVDMWALGCVLYTLlC--GFPPFYDEs 241
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1013071061  798 --TLIEK-ERFYESRCRP----VTPSCKelaDLMTRCMNYDPNQR 835
Cdd:cd14096    242 ieTLTEKiSRGDYTFLSPwwdeISKSAK---DLISHLLTVDPAKR 283
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
615-836 4.73e-06

Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related kinase 6 and 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 and Nek7 are the shortest Neks, consisting only of the catalytic domain and a very short N-terminal extension. They show distinct expression patterns and both appear to be downstream substrates of Nek9. They are required for mitotic spindle formation and cytokinesis. They may also be regulators of the p70 ribosomal S6 kinase. Nek6/7 is part of a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 49.58  E-value: 4.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  615 KKIKvILKVLDPSHRDISLaffEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLD-LFMHRKSDVLTTP---- 689
Cdd:cd08224     31 KKVQ-IFEMMDAKARQDCL---KEIDLLQQLNHPNIIKYLASFIENNELNIVLELADAGDLSrLIKHFKKQKRLIPerti 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  690 WKFKVakQLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGipitvLSRQECIERI--------P-WIA 760
Cdd:cd08224    107 WKYFV--QLCSALEHMHSKRIMHRDIKPANVFITANGV-------VKLGDLG-----LGRFFSSKTTaahslvgtPyYMS 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  761 PECV-EDSKNLSvaADKWSFGTTLWEIC------YNGEIPLKDK-TLIEKERFyesrcRPVTPSC--KELADLMTRCMNY 830
Cdd:cd08224    173 PERIrEQGYDFK--SDIWSLGCLLYEMAalqspfYGEKMNLYSLcKKIEKCEY-----PPLPADLysQELRDLVAACIQP 245

                   ....*.
gi 1013071061  831 DPNQRP 836
Cdd:cd08224    246 DPEKRP 251
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
643-835 4.78e-06

Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Pat1 (also called Ran1), Saccharomyces cerevisiae VHS1 and KSP1, and similar fungal STKs. Pat1 blocks Mei2, an RNA-binding protein which is indispensable in the initiation of meiosis. Pat1 is inactivated and Mei2 activated, which initiates meiosis, under nutrient-deprived conditions through a signaling cascade involving Ste11. Meiosis induced by Pat1 inactivation may show different characteristics than normal meiosis including aberrant positioning of centromeres. VHS1 was identified in a screen for suppressors of cell cycle arrest at the G1/S transition, while KSP1 may be involved in regulating PRP20, which is required for mRNA export and maintenance of nuclear structure. The Pat1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 49.66  E-value: 4.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  643 RQVS-HKHIVYLYGVCVRDVENIMVEEFVEGGPL-DLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNL 720
Cdd:cd13993     59 RRVSrHPNIITLHDVFETEVAIYIVLEYCPNGDLfEAITENRIYVGKTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENI 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  721 LLAREGIDsecgpfIKLSDPGIPIT-VLSRQECIERIPWIAPECVEDSKNL-----SVAADKWSFGTTLWEICYnGEIPL 794
Cdd:cd13993    139 LLSQDEGT------VKLCDFGLATTeKISMDFGVGSEFYMAPECFDEVGRSlkgypCAAGDIWSLGIILLNLTF-GRNPW 211
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1013071061  795 KDKTLIEKERFYESRCRPVT-----PSCKELADLMTRCMNYDPNQR 835
Cdd:cd13993    212 KIASESDPIFYDYYLNSPNLfdvilPMSDDFYNLLRQIFTVNPNNR 257
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
666-875 5.05e-06

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. It slows down cell proliferation, inducing cell cycle arrest and enhancing cell differentiation. PKC-delta is also involved in the regulation of transcription as well as immune and inflammatory responses. It plays a central role in the genotoxic stress response that leads to DNA damaged-induced apoptosis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 49.94  E-value: 5.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  666 VEEFVEGGPLDLFMHRKSDVLTTPWKFkVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGidsecgpFIKLSDPGI--- 742
Cdd:cd05620     74 VMEFLNGGDLMFHIQDKGRFDLYRATF-YAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDG-------HIKIADFGMcke 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  743 PITVLSRQECIERIP-WIAPECVEDSKnLSVAADKWSFGTTLWEICYnGEIPLKDKtliEKERFYESrCRPVTPS----- 816
Cdd:cd05620    146 NVFGDNRASTFCGTPdYIAPEILQGLK-YTFSVDWWSFGVLLYEMLI-GQSPFHGD---DEDELFES-IRVDTPHyprwi 219
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1013071061  817 CKELADLMTRCMNYDPNQR----------PFFRAImrDINKLEEQNPDIVSEKKPATEVDPTHFEKRFL 875
Cdd:cd05620    220 TKESKDILEKLFERDPTRRlgvvgnirghPFFKTI--NWTALEKRELDPPFKPKVKSPSDYSNFDREFL 286
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
589-836 6.41e-06

Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily are mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs) and include ASK1, ASK2, and MAPKKK15. ASK1 (also called MAPKKK5) functions in the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. It plays important roles in cytokine and stress responses, as well as in reactive oxygen species-mediated cellular responses. ASK1 is implicated in various diseases mediated by oxidative stress including inschemic heart disease, hypertension, vessel injury, brain ischemia, Fanconi anemia, asthma, and pulmonary edema, among others. ASK2 (also called MAPKKK6) functions only in a heteromeric complex with ASK1, and can activate ASK1 by direct phosphorylation. The function of MAPKKK15 is still unknown. The ASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270794 [Multi-domain]  Cd Length: 268  Bit Score: 49.33  E-value: 6.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  589 LGRGTRTHIYSGTlmdykdDEGTSEEKKIKVI----LKVLDPSHRDISLaffeaasmMRQVSHKHIV-YLYGVCVRDVEN 663
Cdd:cd06624     16 LGKGTFGVVYAAR------DLSTQVRIAIKEIperdSREVQPLHEEIAL--------HSRLSHKNIVqYLGSVSEDGFFK 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  664 IMVEEfVEGGPLdlfmhrkSDVLTTPW----------KFkVAKQLASALSYLEDKDLVHGNVCTKNLLlaregIDSECGp 733
Cdd:cd06624     82 IFMEQ-VPGGSL-------SALLRSKWgplkdnentiGY-YTKQILEGLKYLHDNKIVHRDIKGDNVL-----VNTYSG- 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  734 FIKLSDPGIPITVLSRQECIER----IPWIAPECVEDS-KNLSVAADKWSFGTTLWEICyNGEIPLKD----KTLIEKER 804
Cdd:cd06624    147 VVKISDFGTSKRLAGINPCTETftgtLQYMAPEVIDKGqRGYGPPADIWSLGCTIIEMA-TGKPPFIElgepQAAMFKVG 225
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1013071061  805 FYesRCRPVTPS--CKELADLMTRCMNYDPNQRP 836
Cdd:cd06624    226 MF--KIHPEIPEslSEEAKSFILRCFEPDPDKRA 257
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
612-835 7.26e-06

Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK2 is localized in the sperm neck, equatorial segment, and mid-piece of the sperm tail. Both TSSK1 and TSSK2 phosphorylate their common substrate TSKS (testis-specific-kinase-substrate). TSSK1/TSSK2 double knock-out mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 49.01  E-value: 7.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  612 SEEKKIKVILKVLDpsHRDISLAFFE-----AASMMRQVSHKHIVYLYGVC-VRDVENIMVEEFVEGGPLDLFMHRKSDV 685
Cdd:cd14165     22 SERLKCNVAIKIID--KKKAPDDFVEkflprELEILARLNHKSIIKTYEIFeTSDGKVYIVMELGVQGDLLEFIKLRGAL 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  686 LTTPWKfKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREgidsecgpF-IKLSDPGI--PI-------TVLSRQECiER 755
Cdd:cd14165    100 PEDVAR-KMFHQLSSAIKYCHELDIVHRDLKCENLLLDKD--------FnIKLTDFGFskRClrdengrIVLSKTFC-GS 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  756 IPWIAPECVEDSKNLSVAADKWSFGTTLWeICYNGEIPLKDKTL-----IEKE-RFYESRCRPVTPSCKelaDLMTRCMN 829
Cdd:cd14165    170 AAYAAPEVLQGIPYDPRIYDIWSLGVILY-IMVCGSMPYDDSNVkkmlkIQKEhRVRFPRSKNLTSECK---DLIYRLLQ 245

                   ....*.
gi 1013071061  830 YDPNQR 835
Cdd:cd14165    246 PDVSQR 251
PTKc_Aatyk2 cd05086
Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs ...
635-796 8.16e-06

Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk2 is a member of the Aatyk subfamily of proteins, which are receptor kinases containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk2 is also called lemur tyrosine kinase 2 (Lmtk2) or brain-enriched kinase (Brek). It is expressed at high levels in early postnatal brain, and has been shown to play a role in nerve growth factor (NGF) signaling. Studies with knockout mice reveal that Aatyk2 is essential for late stage spermatogenesis. Although it is classified as a PTK based on sequence similarity and the phylogenetic tree, Aatyk2 has been functionally characterized as a serine/threonine kinase. The Aatyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270669 [Multi-domain]  Cd Length: 271  Bit Score: 48.71  E-value: 8.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  635 FFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFM-----HRKSDVLTTPWKfKVAKQLASALSYLEDKD 709
Cdd:cd05086     44 FLQQGEPYYILQHPNILQCVGQCVEAIPYLLVFEFCDLGDLKTYLanqqeKLRGDSQIMLLQ-RMACEIAAGLAHMHKHN 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  710 LVHGNVCTKNLLLAREGIdsecgpfIKLSDPGIPIT------VLSRQECIERIPWIAPECVEDSKNLSVAADK------W 777
Cdd:cd05086    123 FLHSDLALRNCYLTSDLT-------VKVGDYGIGFSrykedyIETDDKKYAPLRWTAPELVTSFQDGLLAAEQtkysniW 195
                          170
                   ....*....|....*....
gi 1013071061  778 SFGTTLWEICYNGEIPLKD 796
Cdd:cd05086    196 SLGVTLWELFENAAQPYSD 214
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
634-821 8.51e-06

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK1 plays a role in the activation of IRF3/7, STAT, and NFkB. It mediates IL-6 and IFN-gamma responses following IL-1 and IL-18 stimulation, respectively. It also plays an essential role in IFN-alpha induction downstream of TLR7 and TLR9. The IRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 49.05  E-value: 8.51e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  634 AFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSDVLTTPW--KFKVAKQLASALSYLED--KD 709
Cdd:cd14159     38 SFLTEVEKLSRFRHPNIVDLAGYSAQQGNYCLIYVYLPNGSLEDRLHCQVSCPCLSWsqRLHVLLGTARAIQYLHSdsPS 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  710 LVHGNVCTKNLLLArEGIDSECGPF------IKLSDPGIPITVLSRQECIERIPWIAPECVEDSKnLSVAADKWSFGTTL 783
Cdd:cd14159    118 LIHGDVKSSNILLD-AALNPKLGDFglarfsRRPKQPGMSSTLARTQTVRGTLAYLPEEYVKTGT-LSVEIDVYSFGVVL 195
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1013071061  784 WEIcYNGEIPLK----DKTLIEKERFYESRCRPVTPSCKELA 821
Cdd:cd14159    196 LEL-LTGRRAMEvdscSPTKYLKDLVKEEEEAQHTPTTMTHS 236
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
611-794 8.62e-06

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKbeta is involved in the classical pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. It involves NEMO (NF-kB Essential MOdulator)- and IKKbeta-dependent phosphorylation and degradation of the Inhibitor of NF-kB (IkB), which liberates NF-kB dimers (typified by the p50-p65 heterodimer) from an inactive IkB/dimeric NF-kB complex, enabling them to migrate to the nucleus where they regulate gene transcription. The IKKbeta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 48.81  E-value: 8.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  611 TSEEKKIKVILKVLDPSHRDislAFFEAASMMRQVSHKHIVylygvCVRDVEN-----------IMVEEFVEGGPLDLFM 679
Cdd:cd14038     18 TGEQVAIKQCRQELSPKNRE---RWCLEIQIMKRLNHPNVV-----AARDVPEglqklapndlpLLAMEYCQGGDLRKYL 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  680 H--------RKSDVLTtpwkfkVAKQLASALSYLEDKDLVHGNVCTKNLLLARegidSECGPFIKLSDPGIPITVLSRQE 751
Cdd:cd14038     90 NqfenccglREGAILT------LLSDISSALRYLHENRIIHRDLKPENIVLQQ----GEQRLIHKIIDLGYAKELDQGSL 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1013071061  752 CIE---RIPWIAPECVEDSKnLSVAADKWSFGTTLWEiCYNGEIPL 794
Cdd:cd14038    160 CTSfvgTLQYLAPELLEQQK-YTVTVDYWSFGTLAFE-CITGFRPF 203
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
616-844 9.56e-06

Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIM1 is a widely-expressed kinase belonging to the AMP-activated protein kinase (AMPK) subfamily. Although present in most tissues, NIM1 kinase activity is only observed in the brain and testis. NIM1 is capable of autophosphorylating and activating itself, but may be present in other tissues in the inactive form. The physiological function of NIM1 has yet to be elucidated. The NIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270977 [Multi-domain]  Cd Length: 255  Bit Score: 48.49  E-value: 9.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  616 KIKVILKVLDPSHRD---ISLAFFEAASMMRqVSHKHIVYLYGVcvrdVENI----MVEEFVEGGplDLFMHrksdvLTT 688
Cdd:cd14075     27 KEKVAIKILDKTKLDqktQRLLSREISSMEK-LHHPNIIRLYEV----VETLsklhLVMEYASGG--ELYTK-----IST 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  689 PWKFK--VAK----QLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGIPiTVLSRQECIERI----PW 758
Cdd:cd14075     95 EGKLSesEAKplfaQIVSAVKHMHENNIIHRDLKAENVFYASNNC-------VKVGDFGFS-THAKRGETLNTFcgspPY 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  759 IAPECVEDSKNLSVAADKWSFGTTLWeICYNGEIPL------KDKTLIEKERFYESRCrpVTPSCKEladLMTRCMNYDP 832
Cdd:cd14075    167 AAPELFKDEHYIGIYVDIWALGVLLY-FMVTGVMPFraetvaKLKKCILEGTYTIPSY--VSEPCQE---LIRGILQPVP 240
                          250
                   ....*....|..
gi 1013071061  833 NQRPFFRAIMRD 844
Cdd:cd14075    241 SDRYSIDEIKNS 252
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
633-836 1.41e-05

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk1 (or simply Aatyk) is also called lemur tyrosine kinase 1 (Lmtk1). It is a cytoplasmic (or nonreceptor) kinase containing a long C-terminal region. The expression of Aatyk1 is upregulated during growth arrest and apoptosis in myeloid cells. Aatyk1 has been implicated in neural differentiation, and is a regulator of the Na-K-2Cl cotransporter, a membrane protein involved in cell proliferation and survival, epithelial transport, and blood pressure control. The Aatyk1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270670 [Multi-domain]  Cd Length: 271  Bit Score: 48.06  E-value: 1.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  633 LAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMH--RKSDVLT-TPWKF-KVAKQLASALSYLEDK 708
Cdd:cd05087     42 MQFLEEAQPYRALQHTNLLQCLAQCAEVTPYLLVMEFCPLGDLKGYLRscRAAESMApDPLTLqRMACEVACGLLHLHRN 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  709 DLVHGNVCTKNLLLAREGIdsecgpfIKLSDPGIP-------ITVLSRQECIErIPWIAPECVED-SKNLSVA-----AD 775
Cdd:cd05087    122 NFVHSDLALRNCLLTADLT-------VKIGDYGLShckykedYFVTADQLWVP-LRWIAPELVDEvHGNLLVVdqtkqSN 193
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1013071061  776 KWSFGTTLWEICYNGEIPLK---DKTLIEKErFYESRCRPVTPSCK-ELADLMTRCMNY---DPNQRP 836
Cdd:cd05087    194 VWSLGVTIWELFELGNQPYRhysDRQVLTYT-VREQQLKLPKPQLKlSLAERWYEVMQFcwlQPEQRP 260
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
635-793 1.42e-05

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Aatyk subfamily is also referred to as the lemur tyrosine kinase (Lmtk) subfamily. It consists of Aatyk1 (Lmtk1), Aatyk2 (Lmtk2, Brek), Aatyk3 (Lmtk3), and similar proteins. Aatyk proteins are mostly receptor PTKs (RTKs) containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk1 does not contain a transmembrane segment and is a cytoplasmic (or nonreceptor) kinase. Aatyk proteins are classified as PTKs based on overall sequence similarity and the phylogenetic tree. However, analysis of catalytic residues suggests that Aatyk proteins may be multispecific kinases, functioning also as serine/threonine kinases. They are involved in neural differentiation, nerve growth factor (NGF) signaling, apoptosis, and spermatogenesis. The Aatyk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270638 [Multi-domain]  Cd Length: 269  Bit Score: 47.97  E-value: 1.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  635 FFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSDVLTTPWKF----KVAKQLASALSYLEDKDL 710
Cdd:cd05042     42 FLKEGQPYRILQHPNILQCLGQCVEAIPYLLVMEFCDLGDLKAYLRSEREHERGDSDTrtlqRMACEVAAGLAHLHKLNF 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  711 VHGNVCTKNLLLAREGIdsecgpfIKLSDPGIPIT------VLSRQECIERIPWIAPECVEDSKNLSVAADK------WS 778
Cdd:cd05042    122 VHSDLALRNCLLTSDLT-------VKIGDYGLAHSrykedyIETDDKLWFPLRWTAPELVTEFHDRLLVVDQtkysniWS 194
                          170
                   ....*....|....*
gi 1013071061  779 FGTTLWEICYNGEIP 793
Cdd:cd05042    195 LGVTLWELFENGAQP 209
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
636-835 1.47e-05

Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of yeast Kin1, Kin2, and similar proteins. Fission yeast Kin1 is a membrane-associated kinase that is involved in regulating cell surface cohesiveness during interphase. It also plays a role during mitosis, linking actomyosin ring assembly with septum synthesis and membrane closure to ensure separation of daughter cells. Budding yeast Kin1 and Kin2 act downstream of the Rab-GTPase Sec4 and are associated with the exocytic apparatus; they play roles in the secretory pathway. The Kin1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270979 [Multi-domain]  Cd Length: 267  Bit Score: 48.21  E-value: 1.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  636 FEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGP-LDLFMHRKSdvLTTPWKFKVAKQLASALSYLEDKDLVHGN 714
Cdd:cd14077     61 IREAALSSLLNHPHICRLRDFLRTPNHYYMLFEYVDGGQlLDYIISHGK--LKEKQARKFARQIASALDYLHRNSIVHRD 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  715 VCTKNLLLAREGIdsecgpfIKLSDPGI-----PITVLSR---------QECIERIPWIAPEcvedsknlsvaADKWSFG 780
Cdd:cd14077    139 LKIENILISKSGN-------IKIIDFGLsnlydPRRLLRTfcgslyfaaPELLQAQPYTGPE-----------VDVWSFG 200
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1013071061  781 TTLWEI-CynGEIPLKDKTL------IEKERFyeSRCRPVTPSCKEladLMTRCMNYDPNQR 835
Cdd:cd14077    201 VVLYVLvC--GKVPFDDENMpalhakIKKGKV--EYPSYLSSECKS---LISRMLVVDPKKR 255
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
636-786 1.55e-05

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 48.44  E-value: 1.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  636 FEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSDVLTTPWKFkVAKQLASALSYLEDKDLVHGNV 715
Cdd:PTZ00426    79 FSERKILNYINHPFCVNLYGSFKDESYLYLVLEFVIGGEFFTFLRRNKRFPNDVGCF-YAAQIVLIFEYLQSLNIVYRDL 157
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1013071061  716 CTKNLLLAREGidsecgpFIKLSDPGIPITVLSRQECIERIP-WIAPECVEDSKNlSVAADKWSFGTTLWEI 786
Cdd:PTZ00426   158 KPENLLLDKDG-------FIKMTDFGFAKVVDTRTYTLCGTPeYIAPEILLNVGH-GKAADWWTLGIFIYEI 221
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
641-836 1.92e-05

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK2 is one of two vertebrate LRRKs which show complementary expression in the brain. Mutations in LRRK2, found in the kinase, ROC-COR, and WD40 domains, are linked to both familial and sporadic forms of Parkinson's disease. The most prevalent mutation, G2019S located in the activation loop of the kinase domain, increases kinase activity. The R1441C/G mutations in the GTPase domain have also been reported to influence kinase activity. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 47.64  E-value: 1.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  641 MMRQVSHKHIVYLYGVCVRdvENIMVEEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNL 720
Cdd:cd14068     40 VLSHLHHPSLVALLAAGTA--PRMLVMELAPKGSLDALLQQDNASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNV 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  721 LLARegIDSECGPFIKLSDPGIP--ITVLSRQECIERIPWIAPECVEDSKNLSVAADKWSFGTTLWEICYNGE------- 791
Cdd:cd14068    118 LLFT--LYPNCAIIAKIADYGIAqyCCRMGIKTSEGTPGFRAPEVARGNVIYNQQADVYSFGLLLYDILTCGEriveglk 195
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1013071061  792 IPLK-DKTLIEK---ERFYESRCRPvtpsCKELADLMTRCMNYDPNQRP 836
Cdd:cd14068    196 FPNEfDELAIQGklpDPVKEYGCAP----WPGVEALIKDCLKENPQCRP 240
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
637-835 2.21e-05

Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CASK belongs to the MAGUK (membrane-associated guanylate kinase) protein family, which functions as multiple domain adaptor proteins and is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The enzymatically inactive GuK domain in MAGUK proteins mediates protein-protein interactions and associates intramolecularly with the SH3 domain. In addition, CASK contains a catalytic kinase and two L27 domains. It is highly expressed in the nervous system and plays roles in synaptic protein targeting, neural development, and regulation of gene expression. Binding partners include parkin (a Parkinson's disease molecule), neurexin (adhesion molecule), syndecans, calcium channel proteins, CINAP (nucleosome assembly protein), transcription factor Tbr-1, and the cytoplasmic adaptor proteins Mint1, Veli/mLIN-7/MALS, SAP97, caskin, and CIP98. Deletion or mutations in the CASK gene have been implicated in X-linked mental retardation. The CASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 47.92  E-value: 2.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  637 EAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSD---VLTTPWKFKVAKQLASALSYLEDKDLVHG 713
Cdd:cd14094     54 REASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLCFEIVKRADagfVYSEAVASHYMRQILEALRYCHDNNIIHR 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  714 NVCTKNLLLAREGIDSE---CGPFIKLSDPGIPITVLSRQECIEripWIAPECVEdSKNLSVAADKWSFGTTLWeICYNG 790
Cdd:cd14094    134 DVKPHCVLLASKENSAPvklGGFGVAIQLGESGLVAGGRVGTPH---FMAPEVVK-REPYGKPVDVWGCGVILF-ILLSG 208
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1013071061  791 EIPLkdktLIEKERFYESRCR-------PVTPSCKELA-DLMTRCMNYDPNQR 835
Cdd:cd14094    209 CLPF----YGTKERLFEGIIKgkykmnpRQWSHISESAkDLVRRMLMLDPAER 257
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
587-836 2.39e-05

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIB myosin is expressed highly in retina. It is also present in the brain and testis. The human class IIIB myosin gene maps to a region that overlaps the locus for Bardet-Biedl syndrome, which is characterized by dysmorphic extremities, retinal dystrophy, obesity, male hypogenitalism, and renal abnormalities. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. They may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. They may also function as cargo carriers during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 47.68  E-value: 2.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  587 EHLGRGTRTHIYSGTlmDYKDDEGTSeekkikviLKVLDPSHrDISLAFFEAASMMRQVS-HKHIVYLYGVCVRDVENI- 664
Cdd:cd06639     28 ETIGKGTYGKVYKVT--NKKDGSLAA--------VKILDPIS-DVDEEIEAEYNILRSLPnHPNVVKFYGMFYKADQYVg 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  665 ----MVEEFVEGGPL-DLF--MHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGidsecgpFIKL 737
Cdd:cd06639     97 gqlwLVLELCNGGSVtELVkgLLKCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEG-------GVKL 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  738 SDPGIPI----TVLSRQECIERIPWIAPECV--EDSKNLSVAA--DKWSFGTTLWEICyNGEIPLKD----KTLIEKERF 805
Cdd:cd06639    170 VDFGVSAqltsARLRRNTSVGTPFWMAPEVIacEQQYDYSYDArcDVWSLGITAIELA-DGDPPLFDmhpvKALFKIPRN 248
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1013071061  806 YESRCRPVTPSCKELADLMTRCMNYDPNQRP 836
Cdd:cd06639    249 PPPTLLNPEKWCRGFSHFISQCLIKDFEKRP 279
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
587-836 2.50e-05

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. No function has yet been ascribed to Nek10. The gene encoding Nek10 is a putative causative gene for breast cancer; it is located within a breast cancer susceptibility loci on chromosome 3p24. Nek10 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270867 [Multi-domain]  Cd Length: 270  Bit Score: 47.50  E-value: 2.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  587 EHLGRGT-------RTHIYSGTLMDYKD-------DEGTSEEKkikvilkvlDPSHRDIslaFFEAASMMRQVSHKHIVY 652
Cdd:cd08528      6 ELLGSGAfgcvykvRKKSNGQTLLALKEinmtnpaFGRTEQER---------DKSVGDI---ISEVNIIKEQLRHPNIVR 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  653 LYGVCVRDVENIMVEEFVEGGPL-DLF--MHRKSDVLTTPWKFKVAKQLASALSYL-EDKDLVHGNVCTKNLLLareGID 728
Cdd:cd08528     74 YYKTFLENDRLYIVMELIEGAPLgEHFssLKEKNEHFTEDRIWNIFVQMVLALRYLhKEKQIVHRDLKPNNIML---GED 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  729 SEcgpfIKLSDPGipitvLSRQECIER---------IPWIAPECVEdSKNLSVAADKWSFGTTLWEICYNGEIPLKDKTL 799
Cdd:cd08528    151 DK----VTITDFG-----LAKQKGPESskmtsvvgtILYSCPEIVQ-NEPYGEKADIWALGCILYQMCTLQPPFYSTNML 220
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1013071061  800 IEKERFYESRCRPVTPS--CKELADLMTRCMNYDPNQRP 836
Cdd:cd08528    221 TLATKIVEAEYEPLPEGmySDDITFVIRSCLTPDPEARP 259
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
586-841 3.07e-05

Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Dusty protein kinase is also called Receptor-interacting protein kinase 5 (RIPK5 or RIP5) or RIP-homologous kinase. It is widely distributed in the central nervous system, and may be involved in inducing both caspase-dependent and caspase-independent cell death. The Dusty subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 47.10  E-value: 3.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  586 GEHLGRGTRTHIYSGtlmdykDDEGTSEEKKIKVILKVLDPSHRDISLAFFEAASMMRqvsHKHIVYLYGvCVRD----- 660
Cdd:cd13975      5 GRELGRGQYGVVYAC------DSWGGHFPCALKSVVPPDDKHWNDLALEFHYTRSLPK---HERIVSLHG-SVIDysygg 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  661 VENIMVEEFVEGGPLDLFMHRKSDvLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIDsecgpfiKLSDP 740
Cdd:cd13975     75 GSSIAVLLIMERLHRDLYTGIKAG-LSLEERLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRA-------KITDL 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  741 GIPITVLSRQECIERIP-WIAPECVEDSKNLSVaaDKWSFGTTLWEICyNGEIPLKD--KTLIEKERFYESRCRPVTPSC 817
Cdd:cd13975    147 GFCKPEAMMSGSIVGTPiHMAPELFSGKYDNSV--DVYAFGILFWYLC-AGHVKLPEafEQCASKDHLWNNVRKGVRPER 223
                          250       260
                   ....*....|....*....|....*....
gi 1013071061  818 KELAD-----LMTRCMNYDPNQRPFFRAI 841
Cdd:cd13975    224 LPVFDeecwnLMEACWSGDPSQRPLLGIV 252
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
641-838 3.52e-05

The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GSK3 is a mutifunctional kinase involved in many cellular processes including cell division, proliferation, differentiation, adhesion, and apoptosis. In plants, GSK3 plays a role in the response to osmotic stress. In Caenorhabditis elegans, it plays a role in regulating normal oocyte-to-embryo transition and response to oxidative stress. In Chlamydomonas reinhardtii, GSK3 regulates flagellar length and assembly. In mammals, there are two isoforms, GSK3alpha and GSK3beta, which show both distinct and redundant functions. The two isoforms differ mainly in their N-termini. They are both involved in axon formation and in Wnt signaling.They play distinct roles in cardiogenesis, with GSKalpha being essential in cardiomyocyte survival, and GSKbeta regulating heart positioning and left-right symmetry. GSK3beta was first identified as a regulator of glycogen synthesis, but has since been determined to play other roles. It regulates the degradation of beta-catenin and IkB. Beta-catenin is the main effector of Wnt, which is involved in normal haematopoiesis and stem cell function. IkB is a central inhibitor of NF-kB, which is critical in maintaining leukemic cell growth. GSK3beta is enriched in the brain and is involved in regulating neuronal signaling pathways. It is implicated in the pathogenesis of many diseases including Type II diabetes, obesity, mood disorders, Alzheimer's disease, osteoporosis, and some types of cancer, among others. The GSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271039 [Multi-domain]  Cd Length: 293  Bit Score: 47.11  E-value: 3.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  641 MMRQVSHKHIVYLYGVCVRDVEN------IMVEEFVeggPLDL--FMHRKSDVLTT-PWKF-KV-AKQLASALSYLEDKD 709
Cdd:cd14137     50 IMRRLKHPNIVKLKYFFYSSGEKkdevylNLVMEYM---PETLyrVIRHYSKNKQTiPIIYvKLySYQLFRGLAYLHSLG 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  710 LVHGNVCTKNLLlaregIDSECGpFIKLSDPGiPITVLSRQEciERIPWI------APECVEDSKNLSVAADKWSFGTTL 783
Cdd:cd14137    127 ICHRDIKPQNLL-----VDPETG-VLKLCDFG-SAKRLVPGE--PNVSYIcsryyrAPELIFGATDYTTAIDIWSAGCVL 197
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  784 WEIC-----YNGEIPLKDKTLI-------------EKERFYESRCRPVTPSC-----------KELADLMTRCMNYDPNQ 834
Cdd:cd14137    198 AELLlgqplFPGESSVDQLVEIikvlgtptreqikAMNPNYTEFKFPQIKPHpwekvfpkrtpPDAIDLLSKILVYNPSK 277
                          250
                   ....*....|...
gi 1013071061  835 R---------PFF 838
Cdd:cd14137    278 RltalealahPFF 290
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
660-836 3.58e-05

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek9, also called Nercc1, is primarily a cytoplasmic protein but can also localize in the nucleus. It is involved in modulating chromosome alignment and splitting during mitosis. It interacts with the gamma-tubulin ring complex and the Ran GTPase, and is implicated in microtubule organization. Nek9 associates with FACT (FAcilitates Chromatin Transcription) and modulates interphase progression. It also interacts with Nek6, and Nek7, during mitosis, resulting in their activation. Nek9 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 46.65  E-value: 3.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  660 DVENIMVE-EFVEGGPL-DLFMHRKSDVL---TTPWKFKvakQLASALSYLEDKDLVHGNVCTKNLLLAREGIdsecgpf 734
Cdd:cd08221     70 DGESLFIEmEYCNGGNLhDKIAQQKNQLFpeeVVLWYLY---QIVSAVSHIHKAGILHRDIKTLNIFLTKADL------- 139
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  735 IKLSDPGIPITVLSRQECIERIP----WIAPECVEDSKnLSVAADKWSFGTTLWEI-----CYNGEIPLKDKTLIEKERF 805
Cdd:cd08221    140 VKLGDFGISKVLDSESSMAESIVgtpyYMSPELVQGVK-YNFKSDIWAVGCVLYELltlkrTFDATNPLRLAVKIVQGEY 218
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1013071061  806 YESrcrpVTPSCKELADLMTRCMNYDPNQRP 836
Cdd:cd08221    219 EDI----DEQYSEEIIQLVHDCLHQDPEDRP 245
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
612-836 4.73e-05

Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle 1 (also called TTK); Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TTK/Mps1 is a spindle checkpoint kinase that was first discovered due to its necessity in centrosome duplication in budding yeast. It was later found to function in the spindle assembly checkpoint, which monitors the proper attachment of chromosomes to the mitotic spindle. In yeast, substrates of Mps1 include the spindle pole body components Spc98p, Spc110p, and Spc42p. The TTK/Mps1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 46.44  E-value: 4.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  612 SEEKKI----KVILKVLDPSHRDislAFFEAASMMRQVSH-KHIVYLYGVCVRDVEN--IMVEEFvegGPLDL--FMHRK 682
Cdd:cd14131     22 NPKKKIyalkRVDLEGADEQTLQ---SYKNEIELLKKLKGsDRIIQLYDYEVTDEDDylYMVMEC---GEIDLatILKKK 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  683 SDVLTTPWKFK-VAKQLASALSYLEDKDLVHGNVCTKNLLLArEGIdsecgpfIKLSDPGIP------ITVLSRQECIER 755
Cdd:cd14131     96 RPKPIDPNFIRyYWKQMLEAVHTIHEEGIVHSDLKPANFLLV-KGR-------LKLIDFGIAkaiqndTTSIVRDSQVGT 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  756 IPWIAPECVEDSKN---------LSVAADKWSFGTTLWEICYnGEIPLKD-KTLIEK-----ERFYESRCRPVTPscKEL 820
Cdd:cd14131    168 LNYMSPEAIKDTSAsgegkpkskIGRPSDVWSLGCILYQMVY-GKTPFQHiTNPIAKlqaiiDPNHEIEFPDIPN--PDL 244
                          250
                   ....*....|....*.
gi 1013071061  821 ADLMTRCMNYDPNQRP 836
Cdd:cd14131    245 IDVMKRCLQRDPKKRP 260
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
621-836 5.95e-05

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 46.74  E-value: 5.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  621 LKVLDPSHRD-ISLAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDlfmhrKSDVLTTPWKFKVAKQLA 699
Cdd:PLN00034   104 LKVIYGNHEDtVRRQICREIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGSLE-----GTHIADEQFLADVARQIL 178
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  700 SALSYLEDKDLVHGNVCTKNLLlaregIDSecGPFIKLSDPGIP-ITVLSRQEC---IERIPWIAPECV----EDSKNLS 771
Cdd:PLN00034   179 SGIAYLHRRHIVHRDIKPSNLL-----INS--AKNVKIADFGVSrILAQTMDPCnssVGTIAYMSPERIntdlNHGAYDG 251
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1013071061  772 VAADKWSFGTTLWEIcYNGEIPLK-----D-KTLIEKERFYESRCRPVTPScKELADLMTRCMNYDPNQRP 836
Cdd:PLN00034   252 YAGDIWSLGVSILEF-YLGRFPFGvgrqgDwASLMCAICMSQPPEAPATAS-REFRHFISCCLQREPAKRW 320
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
622-835 8.78e-05

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK1, also called CaMKK alpha, is involved in the regulation of glucose uptake in skeletal muscles, independently of AMPK and PKB activation. It also play roles in learning and memory. Studies on CaMKK1 knockout mice reveal deficits in fear conditioning. The CaMKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 45.71  E-value: 8.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  622 KVLDPSHRdislaFFEAASMMRQVSHKHIVYLYGVCVRDVEN--IMVEEFVEGGPLdlfMHRKSDvltTPWKFKVAK--- 696
Cdd:cd14200     62 KPLAPLER-----VYQEIAILKKLDHVNIVKLIEVLDDPAEDnlYMVFDLLRKGPV---MEVPSD---KPFSEDQARlyf 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  697 -QLASALSYLEDKDLVHGNVCTKNLLLAREGidsecgpFIKLSDPGIPITVLSRQECIERI----PWIAPECVEDS-KNL 770
Cdd:cd14200    131 rDIVLGIEYLHYQKIVHRDIKPSNLLLGDDG-------HVKIADFGVSNQFEGNDALLSSTagtpAFMAPETLSDSgQSF 203
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1013071061  771 S-VAADKWSFGTTLWEICYnGEIPLKDKTLIEKERFYESRCR--PVTPS-CKELADLMTRCMNYDPNQR 835
Cdd:cd14200    204 SgKALDVWAMGVTLYCFVY-GKCPFIDEFILALHNKIKNKPVefPEEPEiSEELKDLILKMLDKNPETR 271
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
642-848 8.90e-05

Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270947 [Multi-domain]  Cd Length: 269  Bit Score: 45.62  E-value: 8.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  642 MRQVSHKHIVYLYGVCVrDVENI-MVEEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNL 720
Cdd:cd14045     56 VRELDHPNLCKFIGGCI-EVPNVaIITEYCPKGSLNDVLLNEDIPLNWGFRFSFATDIARGMAYLHQHKIYHGRLKSSNC 134
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  721 LLAREGIdsecgpfIKLSDPGIpiTVLSRQECIERIP---------WIAPECVEDSKNL-SVAADKWSFGTTLWEICYNG 790
Cdd:cd14045    135 VIDDRWV-------CKIADYGL--TTYRKEDGSENASgyqqrlmqvYLPPENHSNTDTEpTQATDVYSYAIILLEIATRN 205
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1013071061  791 E-IPLKDKTLIEKERF---------YESRCrpvtPSCKELADLMTRCMNYDPNQRPFFRAIMRDINKL 848
Cdd:cd14045    206 DpVPEDDYSLDEAWCPplpelisgkTENSC----PCPADYVELIRRCRKNNPAQRPTFEQIKKTLHKI 269
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
644-802 9.67e-05

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 and MEK2 are MAPK kinases (MAPKKs or MKKs), and are dual-specificity PKs that phosphorylate and activate the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1/2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. This cascade has also been implicated in synaptic plasticity, migration, morphological determination, and stress response immunological reactions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1/2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 45.89  E-value: 9.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  644 QVSHK----HIVYLYGVCVRDVENIMVEEFVEGGPLDLFMhRKSDVLTTPWKFKVAKQLASALSYLEDK-DLVHGNVCTK 718
Cdd:cd06615     51 KVLHEcnspYIVGFYGAFYSDGEISICMEHMDGGSLDQVL-KKAGRIPENILGKISIAVLRGLTYLREKhKIMHRDVKPS 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  719 NLLLAREGIdsecgpfIKLSDPGIP---ITVLSRQECIERiPWIAPECVEDSKnLSVAADKWSFGTTLWEIC---YngEI 792
Cdd:cd06615    130 NILVNSRGE-------IKLCDFGVSgqlIDSMANSFVGTR-SYMSPERLQGTH-YTVQSDIWSLGLSLVEMAigrY--PI 198
                          170
                   ....*....|
gi 1013071061  793 PLKDKTLIEK 802
Cdd:cd06615    199 PPPDAKELEA 208
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
666-874 1.03e-04

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-gamma is predominantly expressed in neuronal tissues. Mice deficient in PKB-gamma show a reduction in brain weight due to the decreases in cell size and cell number. PKB-gamma has also been shown to be upregulated in estrogen-deficient breast cancer cells, androgen-independent prostate cancer cells, and primary ovarian tumors. It acts as a key mediator in the genesis of ovarian cancer. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 45.84  E-value: 1.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  666 VEEFVEGGPLDLFMHRKSDVLTTPWKFKVAkQLASALSYLEDKDLVHGNVCTKNLLLAREGidsecgpFIKLSDPGI--- 742
Cdd:cd05593     93 VMEYVNGGELFFHLSRERVFSEDRTRFYGA-EIVSALDYLHSGKIVYRDLKLENLMLDKDG-------HIKITDFGLcke 164
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  743 PITVLSRQECIERIP-WIAPECVEDSkNLSVAADKWSFGTTLWE-ICynGEIPLKDKtliEKERFYESRCR-----PVTP 815
Cdd:cd05593    165 GITDAATMKTFCGTPeYLAPEVLEDN-DYGRAVDWWGLGVVMYEmMC--GRLPFYNQ---DHEKLFELILMedikfPRTL 238
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1013071061  816 ScKELADLMTRCMNYDPNQR-----PFFRAIMRD-----INKLEEQNPDIVSEKKP--ATEVDPTHFEKRF 874
Cdd:cd05593    239 S-ADAKSLLSGLLIKDPNKRlgggpDDAKEIMRHsfftgVNWQDVYDKKLVPPFKPqvTSETDTRYFDEEF 308
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
611-784 1.06e-04

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 45.75  E-value: 1.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  611 TSEEKKIKVILKVLDPShRDISLaffeaasmMRQV-SHKHIVYLYGVCVRDVENIMVEEFVEGGPLdLFMHRKSDVLTTP 689
Cdd:cd14092     30 TGQEFAVKIVSRRLDTS-REVQL--------LRLCqGHPNIVKLHEVFQDELHTYLVMELLRGGEL-LERIRKKKRFTES 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  690 WKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIDSEcgpfIKLSDPGI----PITVLSRQECIErIPWIAPECVE 765
Cdd:cd14092    100 EASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDEDDDAE----IKIVDFGFarlkPENQPLKTPCFT-LPYAAPEVLK 174
                          170       180
                   ....*....|....*....|..
gi 1013071061  766 DSKNLS---VAADKWSFGTTLW 784
Cdd:cd14092    175 QALSTQgydESCDLWSLGVILY 196
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
666-875 1.09e-04

Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. There are four nPKC isoforms, delta, epsilon, eta, and theta. The nPKC-theta-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270744 [Multi-domain]  Cd Length: 320  Bit Score: 45.84  E-value: 1.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  666 VEEFVEGGplDLFMHRKSDvlttpWKFKVAK------QLASALSYLEDKDLVHGNVCTKNLLLAREGidsecgpFIKLSD 739
Cdd:cd05592     74 VMEYLNGG--DLMFHIQQS-----GRFDEDRarfygaEIICGLQFLHSRGIIYRDLKLDNVLLDREG-------HIKIAD 139
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  740 PGIpitvlsrqeCIERI-------------PWIAPECVEDSK-NLSVaaDKWSFGTTLWEIC-----YNGEiplkdktli 800
Cdd:cd05592    140 FGM---------CKENIygenkastfcgtpDYIAPEILKGQKyNQSV--DWWSFGVLLYEMLigqspFHGE--------- 199
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  801 EKERFYESRC--RPVTPS--CKELADLMTRCMNYDPNQR--------------PFFRAImrDINKLE--EQNPDIVSEKK 860
Cdd:cd05592    200 DEDELFWSICndTPHYPRwlTKEAASCLSLLLERNPEKRlgvpecpagdirdhPFFKTI--DWDKLErrEIDPPFKPKVK 277
                          250
                   ....*....|....*
gi 1013071061  861 PATevDPTHFEKRFL 875
Cdd:cd05592    278 SAN--DVSNFDPDFT 290
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
611-836 1.26e-04

Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK6, also called SSTK, is expressed at the head of elongated sperm. It can phosphorylate histones and associate with heat shock protens HSP90 and HSC70. Male mice deficient in TSSK6 are infertile, showing spermatogenic impairment including reduced sperm counts, impaired DNA condensation, abnormal morphology and decreased motility rates. The TSSK6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 45.24  E-value: 1.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  611 TSEEKKIKVILKVLDpsHRDISLAFFEA-----ASMMRQVSHKHIVYLYGVCvrDVENIMVEEFVEGGPLDLFMH-RKSD 684
Cdd:cd14164     20 TSQKYCCKVAIKIVD--RRRASPDFVQKflpreLSILRRVNHPNIVQMFECI--EVANGRLYIVMEAAATDLLQKiQEVH 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  685 VLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLaregidSECGPFIKLSDPGIPITV-----LSRQECIERiPWI 759
Cdd:cd14164     96 HIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILL------SADDRKIKIADFGFARFVedypeLSTTFCGSR-AYT 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  760 APECV----EDSKNLsvaaDKWSFGTTLWeICYNGEIPLkDKTLIEKERFYEsrcRPVT-PSCKELAD----LMTRCMNY 830
Cdd:cd14164    169 PPEVIlgtpYDPKKY----DVWSLGVVLY-VMVTGTMPF-DETNVRRLRLQQ---RGVLyPSGVALEEpcraLIRTLLQF 239

                   ....*.
gi 1013071061  831 DPNQRP 836
Cdd:cd14164    240 NPSTRP 245
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
614-836 1.30e-04

Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Rad53 and Cds1 are the checkpoint kinase 2 (Chk2) homologs found in budding and fission yeast, respectively. They play a central role in the cell's response to DNA lesions to prevent genome rearrangements and maintain genome integrity. They are phosphorylated in response to DNA damage and incomplete replication, and are essential for checkpoint control. They help promote DNA repair by stalling the cell cycle prior to mitosis in the presence of DNA damage. The Rad53/Cds1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 45.16  E-value: 1.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  614 EKKIKVILKVLDPSHRDISLaffeaasmMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSDVLTTPWKfK 693
Cdd:cd14098     35 KRKVAGNDKNLQLFQREINI--------LKSLEHPGIVRLIDWYEDDQHIYLVMEYVEGGDLMDFIMAWGAIPEQHAR-E 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  694 VAKQLASALSYLEDKDLVHGNVCTKNLLLAREgidsecGPFI-KLSDPGIPiTVLSRQECIER----IPWIAPECVEdSK 768
Cdd:cd14098    106 LTKQILEAMAYTHSMGITHRDLKPENILITQD------DPVIvKISDFGLA-KVIHTGTFLVTfcgtMAYLAPEILM-SK 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  769 NLSV------AADKWSFGTTLWEICyNGEIPLKDKT------LIEKERFYESRCRPVTPScKELADLMTRCMNYDPNQRP 836
Cdd:cd14098    178 EQNLqggysnLVDMWSVGCLVYVML-TGALPFDGSSqlpvekRIRKGRYTQPPLVDFNIS-EEAIDFILRLLDVDPEKRM 255
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
585-786 1.33e-04

Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized proteins with similarity to MEKK3, MEKK2, and related proteins; they contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKKs), proteins that phosphorylate and activate MAPK kinases (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MEKK2 and MEKK3 activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270819 [Multi-domain]  Cd Length: 264  Bit Score: 45.02  E-value: 1.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  585 QGEHLGRGTRTHIYsgtlMDYKDDEGtseeKKIKVILKVLDPSHRDIS--LAFFEAA-SMMRQVSHKHIVYLYGvCVRDV 661
Cdd:cd06653      6 LGKLLGRGAFGEVY----LCYDADTG----RELAVKQVPFDPDSQETSkeVNALECEiQLLKNLRHDRIVQYYG-CLRDP 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  662 ENIMVEEFVE---GGPLDLFMhRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGidsecgpFIKLS 738
Cdd:cd06653     77 EEKKLSIFVEympGGSVKDQL-KAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAG-------NVKLG 148
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1013071061  739 DPGIP--ITVLSRQ----ECIERIP-WIAPECVeDSKNLSVAADKWSFGTTLWEI 786
Cdd:cd06653    149 DFGASkrIQTICMSgtgiKSVTGTPyWMSPEVI-SGEGYGRKADVWSVACTVVEM 202
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
665-874 1.59e-04

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270765 [Multi-domain]  Cd Length: 332  Bit Score: 45.30  E-value: 1.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  665 MVEEFVEGGPLDLFMHRKSDVLTTPWKFKVAkQLASALSYLEDKDLVHGNVCTKNLLLAREGidsecgpFIKLSDPGIPI 744
Cdd:cd05614     82 LILDYVSGGELFTHLYQRDHFSEDEVRFYSG-EIILALEHLHKLGIVYRDIKLENILLDSEG-------HVVLTDFGLSK 153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  745 TVLSRQEciER-------IPWIAPECVEDSKNLSVAADKWSFGTTLWEIcYNGEIPLKdktlIEKERFYES-------RC 810
Cdd:cd05614    154 EFLTEEK--ERtysfcgtIEYMAPEIIRGKSGHGKAVDWWSLGILMFEL-LTGASPFT----LEGEKNTQSevsrrilKC 226
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  811 RPVTPSC--KELADLMTRCMNYDPNQR--------------PFFRAImrDINKLEEQNpdIVSEKKPA--TEVDPTHFEK 872
Cdd:cd05614    227 DPPFPSFigPVARDLLQKLLCKDPKKRlgagpqgaqeikehPFFKGL--DWEALALRK--VNPPFRPSirSELDVGNFAE 302

                   ..
gi 1013071061  873 RF 874
Cdd:cd05614    303 EF 304
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
587-877 1.70e-04

Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Polymyxin B resistance protein 2 (PBS2) from Saccharomyces cerevisiae, Wis1 from Schizosaccharomyces pombe, and related proteins. PBS2 and Wis1 are components of stress-activated MAPK cascades in budding and fission yeast, respectively. PBS2 is the specific activator of the MAPK Hog1, which plays a central role in the response of budding yeast to stress including exposure to arsenite and hyperosmotic environments. Wis1 phosphorylates and activates the MAPK Sty1 (also called Spc1 or Phh1), which stimulates a transcriptional response to a wide range of cellular insults through the bZip transcription factors Atf1, Pcr1, and Pap1. The PBS2 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 44.84  E-value: 1.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  587 EHLGRGTRTHIY------SGTLMDYKDDEGTSEEKKIKVILKVLDPSHRDISlaffeaasmmrqvshKHIVYLYGVCVRD 660
Cdd:cd06622      7 DELGKGNYGSVYkvlhrpTGVTMAMKEIRLELDESKFNQIIMELDILHKAVS---------------PYIVDFYGAFFIE 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  661 VENIMVEEFVEGGPLDLFMHRKSDVLTTPWKF--KVAKQLASALSYL-EDKDLVHGNVCTKNLLLAREGIdsecgpfIKL 737
Cdd:cd06622     72 GAVYMCMEYMDAGSLDKLYAGGVATEGIPEDVlrRITYAVVKGLKFLkEEHNIIHRDVKPTNVLVNGNGQ-------VKL 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  738 SDPGIP---ITVLSRQEcIERIPWIAPECVE-----DSKNLSVAADKWSFGTTLWEiCYNGEIPLKDKTLIEKERFYESR 809
Cdd:cd06622    145 CDFGVSgnlVASLAKTN-IGCQSYMAPERIKsggpnQNPTYTVQSDVWSLGLSILE-MALGRYPYPPETYANIFAQLSAI 222
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1013071061  810 CR---PVTPS--CKELADLMTRCMNYDPNQRPFFRAIMrdinkleeQNPDIVSEKKPatEVDPTHFEKRFLKR 877
Cdd:cd06622    223 VDgdpPTLPSgySDDAQDFVAKCLNKIPNRRPTYAQLL--------EHPWLVKYKNA--DVDMAEWVTGALKR 285
PK_NRBP1_like cd13984
Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The ...
644-836 1.79e-04

Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. This subfamily is composed of NRBP1, also called MLF1-adaptor molecule (MADM), and MADML. NRBP1 was originally named based on the presence of nuclear binding and localization motifs prior to functional analyses. It is expressed ubiquitously and is found to localize in the cytoplasm, not the nucleus. NRBP1 is an adaptor protein that interacts with myeloid leukemia factor 1 (MLF1), an oncogene that enhances myeloid development of hematopoietic cells. It also interacts with the small GTPase Rac3. NRBP1 may also be involved in Golgi to ER trafficking. MADML (for MADM-Like) has been shown to be expressed throughout development in Xenopus laevis with highest expression found in the developing lens and retina. The NRBP1-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270886 [Multi-domain]  Cd Length: 256  Bit Score: 44.45  E-value: 1.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  644 QVSHKHIV----YLYGVCVRDVENIMVEEFVEGGPLDLFMHR-KSDVLTTP---WKfKVAKQLASALSYLE--DKDLVHG 713
Cdd:cd13984     51 QLDHPNIVkfhrYWTDVQEEKARVIFITEYMSSGSLKQFLKKtKKNHKTMNeksWK-RWCTQILSALSYLHscDPPIIHG 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  714 NVCTKNLLLAREGIdsecgpfIKLSD---PGIPITVLSRQECIERIPWIAPECvEDSKNLSVAADKWSFGT-----TLWE 785
Cdd:cd13984    130 NLTCDTIFIQHNGL-------IKIGSvapDAIHNHVKTCREEHRNLHFFAPEY-GYLEDVTTAVDIYSFGMcalemAALE 201
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1013071061  786 ICYNGE-IPLKDKTLIEKERFYESrcrpvtPSCKelaDLMTRCMNYDPNQRP 836
Cdd:cd13984    202 IQSNGEkVSANEEAIIRAIFSLED------PLQK---DFIRKCLSVAPQDRP 244
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
639-844 1.97e-04

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 11; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek11 is involved, through direct phosphorylation, in regulating the degradation of Cdc25A (Cell Division Cycle 25 homolog A), which plays a role in cell cycle progression and in activating cyclin dependent kinases. Nek11 is activated by CHK1 (CHeckpoint Kinase 1) and may be involved in the G2/M checkpoint. Nek11 may also play a role in the S-phase checkpoint as well as in DNA replication and genotoxic stress responses. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270861 [Multi-domain]  Cd Length: 260  Bit Score: 44.34  E-value: 1.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  639 ASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLD--LFMHRKSDvlTTPWKFKVAK---QLASALSYLEDKDLVHG 713
Cdd:cd08222     53 AKLLSKLDHPAIVKFHDSFVEKESFCIVTEYCEGGDLDdkISEYKKSG--TTIDENQILDwfiQLLLAVQYMHERRILHR 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  714 NVCTKNLLLAREgidsecgpFIKLSDPGIPITVLSRQECIERIP----WIAPECVE----DSKnlsvaADKWSFGTTLWE 785
Cdd:cd08222    131 DLKAKNIFLKNN--------VIKVGDFGISRILMGTSDLATTFTgtpyYMSPEVLKhegyNSK-----SDIWSLGCILYE 197
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  786 IC-----YNGE----IPLKdktLIEKErfyesrcRPVTPSC--KELADLMTRCMNYDPNQRPFFRAIMRD 844
Cdd:cd08222    198 MCclkhaFDGQnllsVMYK---IVEGE-------TPSLPDKysKELNAIYSRMLNKDPALRPSAAEILKI 257
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
646-786 2.41e-04

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-eta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 44.51  E-value: 2.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  646 SHKHIVYLYgVCVRDVENIM-VEEFVEGGplDLFMH-RKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLA 723
Cdd:cd05590     54 NHPFLTQLY-CCFQTPDRLFfVMEFVNGG--DLMFHiQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLD 130
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1013071061  724 REGidsECgpfiKLSDPGIpitvlsrqeCIERI-------------PWIAPECVEDSKnLSVAADKWSFGTTLWEI 786
Cdd:cd05590    131 HEG---HC----KLADFGM---------CKEGIfngkttstfcgtpDYIAPEILQEML-YGPSVDWWAMGVLLYEM 189
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
611-794 3.20e-04

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 44.25  E-value: 3.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  611 TSEEKKIKVILKVLDPSHrdiSLAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLdLFMHRKSDVLTTPW 690
Cdd:cd14174     26 NGKEYAVKIIEKNAGHSR---SRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLRGGSI-LAHIQKRKHFNERE 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  691 KFKVAKQLASALSYLEDKDLVHGNVCTKNLLL-AREGI------DSECGPFIKLSDPGIPITVLSRQECIERIPWIAPEC 763
Cdd:cd14174    102 ASRVVRDIASALDFLHTKGIAHRDLKPENILCeSPDKVspvkicDFDLGSGVKLNSACTPITTPELTTPCGSAEYMAPEV 181
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1013071061  764 VEDSKNLSVAADK----WSFGTTLWeICYNGEIPL 794
Cdd:cd14174    182 VEVFTDEATFYDKrcdlWSLGVILY-IMLSGYPPF 215
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
640-786 3.68e-04

Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. They activate the MAPKs, p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating the respective MAP/ERK kinases (MEKs, also known as MKKs or MAPKKs), MEK3/MEK6 and MKK4/MKK7. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. Vertebrates contain three TAO subfamily members, named TAO1, TAO2, and TAO3. The TAO subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270784 [Multi-domain]  Cd Length: 258  Bit Score: 43.59  E-value: 3.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  640 SMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLF-MHRKSdvLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTK 718
Cdd:cd06607     53 KFLRQLRHPNTIEYKGCYLREHTAWLVMEYCLGSASDIVeVHKKP--LQEVEIAAICHGALQGLAYLHSHNRIHRDVKAG 130
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  719 NLLLAREGIdsecgpfIKLSDPGIPITVLSRQECIERIPWIAPECV--EDSKNLSVAADKWSFGTTLWEI 786
Cdd:cd06607    131 NILLTEPGT-------VKLADFGSASLVCPANSFVGTPYWMAPEVIlaMDEGQYDGKVDVWSLGITCIEL 193
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
617-848 3.92e-04

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK4 plays a critical role in NFkB activation by its interaction with MyD88, which acts as a scaffold that enables IRAK4 to phosphorylate and activate IRAK1 and/or IRAK2. It also plays an important role in type I IFN production induced by TLR7/8/9. The IRAK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 43.64  E-value: 3.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  617 IKVILKVLDPSHRDISLAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSDVLTTPW--KFKV 694
Cdd:cd14158     43 VKKLAAMVDISTEDLTKQFEQEIQVMAKCQHENLVELLGYSCDGPQLCLVYTYMPNGSLLDRLACLNDTPPLSWhmRCKI 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  695 AKQLASALSYLEDKDLVHGNVCTKNLLLArEGIDSECGPF-IKLSDPGIPITVLSrqeciERI----PWIAPECVEDSkn 769
Cdd:cd14158    123 AQGTANGINYLHENNHIHRDIKSANILLD-ETFVPKISDFgLARASEKFSQTIMT-----ERIvgttAYMAPEALRGE-- 194
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  770 LSVAADKWSFGTTLWEIC-----------------YNGEIPLKDKTLiekERFYESRCRPV-TPSCKELADLMTRCMNYD 831
Cdd:cd14158    195 ITPKSDIFSFGVVLLEIItglppvdenrdpqllldIKEEIEDEEKTI---EDYVDKKMGDWdSTSIEAMYSVASQCLNDK 271
                          250
                   ....*....|....*..
gi 1013071061  832 PNQRPFFRAIMRDINKL 848
Cdd:cd14158    272 KNRRPDIAKVQQLLQEL 288
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
640-835 3.96e-04

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called Doublecortin-like and CAM kinase-like 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL1 (or DCAMKL1) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL1 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL1 interacts with tubulin, glucocorticoid receptor, dynein, JIP1/2, caspases (3 and 8), and calpain, among others. It plays roles in neurogenesis, neuronal migration, retrograde transport, and neuronal apoptosis. The DCKL1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271085 [Multi-domain]  Cd Length: 268  Bit Score: 43.83  E-value: 3.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  640 SMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGplDLFmhrksDVLTTPWKFK------VAKQLASALSYLEDKDLVHG 713
Cdd:cd14183     56 SILRRVKHPNIVLLIEEMDMPTELYLVMELVKGG--DLF-----DAITSTNKYTerdasgMLYNLASAIKYLHSLNIVHR 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  714 NVCTKNLLLAREGIDSECgpfIKLSDPGIPITVLSRQECIERIP-WIAPECVEDSkNLSVAADKWSFGTTLWeICYNGEI 792
Cdd:cd14183    129 DIKPENLLVYEHQDGSKS---LKLGDFGLATVVDGPLYTVCGTPtYVAPEIIAET-GYGLKVDIWAAGVITY-ILLCGFP 203
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1013071061  793 PLK----------DKTLIEKERFYESRCRPVTPSCKELADLMtrcMNYDPNQR 835
Cdd:cd14183    204 PFRgsgddqevlfDQILMGQVDFPSPYWDNVSDSAKELITMM---LQVDVDQR 253
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
644-836 4.18e-04

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 1; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. MEK1 also plays a role in cell cycle control. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 43.89  E-value: 4.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  644 QVSHK----HIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSDVlttPWKF--KVAKQLASALSYLEDK-DLVHGNVC 716
Cdd:cd06650     55 QVLHEcnspYIVGFYGAFYSDGEISICMEHMDGGSLDQVLKKAGRI---PEQIlgKVSIAVIKGLTYLREKhKIMHRDVK 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  717 TKNLLLAREGidsecgpFIKLSDPGIPITVLSR--QECIERIPWIAPECVEDSkNLSVAADKWSFGTTLWEICYnGEIPL 794
Cdd:cd06650    132 PSNILVNSRG-------EIKLCDFGVSGQLIDSmaNSFVGTRSYMSPERLQGT-HYSVQSDIWSMGLSLVEMAV-GRYPI 202
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1013071061  795 KDKTLIEKERFY---------ESRCRPVTPSckeladlmTRCMNYDPNQRP 836
Cdd:cd06650    203 PPPDAKELELMFgcqvegdaaETPPRPRTPG--------RPLSSYGMDSRP 245
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
584-787 5.04e-04

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK7 plays essential roles in the cell cycle and in transcription. It associates with cyclin H and MAT1 and acts as a CDK-Activating Kinase (CAK) by phosphorylating and activating cell cycle CDKs (CDK1/2/4/6). In the brain, it activates CDK5. CDK7 is also a component of the general transcription factor TFIIH, which phosphorylates the C-terminal domain (CTD) of RNA polymerase II when it is bound with unphosphorylated DNA, as present in the pre-initiation complex. Following phosphorylation, the CTD dissociates from the DNA which allows transcription initiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270833 [Multi-domain]  Cd Length: 298  Bit Score: 43.33  E-value: 5.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  584 VQGEHLGRGTRTHIYSGTlmdykdDEGTSEE---KKIKVILKV-----LDPSH-RDISLaffeaasmMRQVSHKHIVYLY 654
Cdd:cd07841      3 EKGKKLGEGTYAVVYKAR------DKETGRIvaiKKIKLGERKeakdgINFTAlREIKL--------LQELKHPNIIGLL 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  655 GVCVRDvENI-MVEEFVEGgplDLFM--HRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIdsec 731
Cdd:cd07841     69 DVFGHK-SNInLVFEFMET---DLEKviKDKSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGV---- 140
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1013071061  732 gpfIKLSDPGI------PITVLSRQeCIERipWI-APECVEDSKNLSVAADKWSFGTTLWEIC 787
Cdd:cd07841    141 ---LKLADFGLarsfgsPNRKMTHQ-VVTR--WYrAPELLFGARHYGVGVDMWSVGCIFAELL 197
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
582-793 5.20e-04

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 4; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK4 is a dual-specificity PK that phosphorylates and activates the downstream targets, c-Jun N-terminal kinase (JNK) and p38 MAPK, on specific threonine and tyrosine residues. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. Their activation is associated with the induction of cell death. Mice deficient in MKK4 die during embryogenesis and display anemia, severe liver hemorrhage, and abnormal hepatogenesis. MKK4 may also play roles in the immune system and in cardiac hypertrophy. It plays a major role in cancer as a tumor and metastasis suppressor. Under certain conditions, MKK4 is pro-oncogenic. The MKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 43.51  E-value: 5.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  582 DLVQGEHLGRGT------RTHIYSGTLMDYKDDEGTSEEKKIKVILKVLDpshrdislaffeaaSMMRQVSHKHIVYLYG 655
Cdd:cd06616      7 DLKDLGEIGRGAfgtvnkMLHKPSGTIMAVKRIRSTVDEKEQKRLLMDLD--------------VVMRSSDCPYIVKFYG 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  656 VCVRDVENIMVEEFVEGGpLDLFMHRKSDVLTT--PWKF--KVAKQLASALSYL-EDKDLVHGNVCTKNLLLAREGIdse 730
Cdd:cd06616     73 ALFREGDCWICMELMDIS-LDKFYKYVYEVLDSviPEEIlgKIAVATVKALNYLkEELKIIHRDVKPSNILLDRNGN--- 148
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1013071061  731 cgpfIKLSDPGIPITVlsrQECIERI------PWIAPECVEDSKNLS---VAADKWSFGTTLWEICyNGEIP 793
Cdd:cd06616    149 ----IKLCDFGISGQL---VDSIAKTrdagcrPYMAPERIDPSASRDgydVRSDVWSLGITLYEVA-TGKFP 212
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
609-786 5.56e-04

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The IKK complex functions as a master regulator of Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. It is composed of two kinases, IKKalpha and IKKbeta, and the regulatory subunit IKKgamma or NEMO (NF-kB Essential MOdulator). IKKs facilitate the release of NF-kB dimers from an inactive state, allowing them to migrate to the nucleus where they regulate gene transcription. There are two IKK pathways that regulate NF-kB signaling, called the classical (involving IKKbeta and NEMO) and non-canonical (involving IKKalpha) pathways. The classical pathway regulates the majority of genes activated by NF-kB. The IKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270891 [Multi-domain]  Cd Length: 289  Bit Score: 43.21  E-value: 5.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  609 EGTSEEKKIKVILKVLDPSHRDISLAFFEAASMMRQVsHKHIV-------YLYGVCVRDVEnIMVEEFVEGGPLDLFMHR 681
Cdd:cd13989     15 QDTGEYVAIKKCRQELSPSDKNRERWCLEVQIMKKLN-HPNVVsardvppELEKLSPNDLP-LLAMEYCSGGDLRKVLNQ 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  682 --------KSDVLTtpwkfkVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGidsecGPFI-KLSDPGIPITVLSRQEC 752
Cdd:cd13989     93 penccglkESEVRT------LLSDISSAISYLHENRIIHRDLKPENIVLQQGG-----GRVIyKLIDLGYAKELDQGSLC 161
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1013071061  753 IE---RIPWIAPECVEdSKNLSVAADKWSFGTTLWEI 786
Cdd:cd13989    162 TSfvgTLQYLAPELFE-SKKYTCTVDYWSFGTLAFEC 197
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
665-850 6.64e-04

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1b, also called Activin receptor-Like Kinase 6 (ALK6), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Mutations in BMPR1b that led to inhibition of chondrogenesis can cause Brachydactyly (BD) type A2, a dominant hand malformation characterized by shortening and lateral deviation of the index fingers. A point mutation in the BMPR1b kinase domain is also associated with the Booroola phenotype, characterized by precocious differentiation of ovarian follicles. BMPR1b belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1b, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1b subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271121 [Multi-domain]  Cd Length: 305  Bit Score: 43.11  E-value: 6.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  665 MVEEFVEGGplDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDK--------DLVHGNVCTKNLLLAREGidSECgpfik 736
Cdd:cd14219     80 LITDYHENG--SLYDYLKSTTLDTKAMLKLAYSSVSGLCHLHTEifstqgkpAIAHRDLKSKNILVKKNG--TCC----- 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  737 LSDPGIPITVLSRQECIERIP--------WIAPECVEDSKNLS-----VAADKWSFGTTLWEI---CYNG------EIPL 794
Cdd:cd14219    151 IADLGLAVKFISDTNEVDIPPntrvgtkrYMPPEVLDESLNRNhfqsyIMADMYSFGLILWEVarrCVSGgiveeyQLPY 230
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1013071061  795 KDktLIEKERFYE--------SRCRPVTPS-------CKELADLMTRCMNYDPNQRPFFRAIMRDINKLEE 850
Cdd:cd14219    231 HD--LVPSDPSYEdmreivciKRLRPSFPNrwssdecLRQMGKLMTECWAHNPASRLTALRVKKTLAKMSE 299
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
587-784 1.10e-03

Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They contain N-terminal cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. The PKD subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 42.01  E-value: 1.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  587 EHLGRGTRTHIYSGTLmdykddEGTSEEKKIKVILKVLDPSHRDISLAffEAASMMRQVSHKHIVYLYGVCVRDVENIMV 666
Cdd:cd14082      9 EVLGSGQFGIVYGGKH------RKTGRDVAIKVIDKLRFPTKQESQLR--NEVAILQQLSHPGVVNLECMFETPERVFVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  667 EEFVEGGPLDLFM-HRKSDVLTTPWKFKVAkQLASALSYLEDKDLVHGNVCTKNLLLAregiDSECGPFIKLSDPGIP-- 743
Cdd:cd14082     81 MEKLHGDMLEMILsSEKGRLPERITKFLVT-QILVALRYLHSKNIVHCDLKPENVLLA----SAEPFPQVKLCDFGFAri 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1013071061  744 ITVLSRQECIERIP-WIAPEcVEDSKNLSVAADKWSFGTTLW 784
Cdd:cd14082    156 IGEKSFRRSVVGTPaYLAPE-VLRNKGYNRSLDMWSVGVIIY 196
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
640-796 1.13e-03

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L1, also called PITSLRE, exists in different isoforms which are named using the alias CDK11(p). The CDC2L1 gene produces two protein products, CDK11(p110) and CDK11(p58). CDC2L1 is also represented by the caspase-processed CDK11(p46). CDK11(p110), the major isoform, associates with cyclin L and is expressed throughout the cell cycle. It is involved in RNA processing and the regulation of transcription. CDK11(p58) associates with cyclin D3 and is expressed during the G2/M phase of the cell cycle. It plays roles in spindle morphogenesis, centrosome maturation, sister chromatid cohesion, and the completion of mitosis. CDK11(p46) is formed from the larger isoforms by caspases during TNFalpha- and Fas-induced apoptosis. It functions as a downstream effector kinase in apoptotic signaling pathways and interacts with eukaryotic initiation factor 3f (eIF3f), p21-activated kinase (PAK1), and Ran-binding protein (RanBPM). CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 42.21  E-value: 1.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  640 SMMRQVSHKHIVYLYGVCV-RDVENI-MVEEFVEGGPLDLFMHRKSDVLTTPWKFKVaKQLASALSYLEDKDLVHGNVCT 717
Cdd:cd07843     56 NILLKLQHPNIVTVKEVVVgSNLDKIyMVMEYVEHDLKSLMETMKQPFLQSEVKCLM-LQLLSGVAHLHDNWILHRDLKT 134
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  718 KNLLLAREGIdsecgpfIKLSDPGI------PITVLSRqecIERIPWI-APECVEDSKNLSVAADKWSFGttlweiCYNG 790
Cdd:cd07843    135 SNLLLNNRGI-------LKICDFGLareygsPLKPYTQ---LVVTLWYrAPELLLGAKEYSTAIDMWSVG------CIFA 198

                   ....*.
gi 1013071061  791 EIPLKD 796
Cdd:cd07843    199 ELLTKK 204
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
586-780 1.24e-03

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type IV; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKIV is found predominantly in neurons and immune cells. It is activated by the binding of calcium/CaM and phosphorylation by CaMKK (alpha or beta). The CaMKK-CaMKIV cascade participates in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors. It also is implicated in T-cell development and signaling, cytokine secretion, and signaling through Toll-like receptors, and is thus, pivotal in immune response and inflammation. The CaMKIV subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270987 [Multi-domain]  Cd Length: 294  Bit Score: 42.12  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  586 GEHLGRGTRTHIYSGTlmdykdDEGTSEEKKIKVILKVLDPShrdislAFFEAASMMRQVSHKHIVYLYGVCVRDVENIM 665
Cdd:cd14085      8 ESELGRGATSVVYRCR------QKGTQKPYAVKKLKKTVDKK------IVRTEIGVLLRLSHPNIIKLKEIFETPTEISL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  666 VEEFVEGGPL-DLFMHR----KSDVLttpwkfKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIDSEcgpfIKLSDP 740
Cdd:cd14085     76 VLELVTGGELfDRIVEKgyysERDAA------DAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPDAP----LKIADF 145
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1013071061  741 G----IPITVLSRQECieRIP-WIAPEcVEDSKNLSVAADKWSFG 780
Cdd:cd14085    146 GlskiVDQQVTMKTVC--GTPgYCAPE-ILRGCAYGPEVDMWSVG 187
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
649-857 1.43e-03

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 5; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK5 (also called MEK5) is a dual-specificity PK that phosphorylates its downstream target, extracellular signal-regulated kinase 5 (ERK5), on specific threonine and tyrosine residues. MKK5 is activated by MEKK2 and MEKK3 in response to mitogenic and stress stimuli. The ERK5 cascade promotes cell proliferation, differentiation, neuronal survival, and neuroprotection. This cascade plays an essential role in heart development. Mice deficient in either ERK5 or MKK5 die around embryonic day 10 due to cardiovascular defects including underdevelopment of the myocardium. In addition, MKK5 is associated with metastasis and unfavorable prognosis in prostate cancer. The MKK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 41.79  E-value: 1.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  649 HIVYLYGVCVrdVEN--IMVEEFVEGGPLDLFMHRKSDVLTtpwkfKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREG 726
Cdd:cd06619     60 YIIGFYGAFF--VENriSICTEFMDGGSLDVYRKIPEHVLG-----RIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRG 132
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  727 idsecgpFIKLSDPGIPITVLSR--QECIERIPWIAPECVEdSKNLSVAADKWSFGTTLWEIC------------YNGEI 792
Cdd:cd06619    133 -------QVKLCDFGVSTQLVNSiaKTYVGTNAYMAPERIS-GEQYGIHSDVWSLGISFMELAlgrfpypqiqknQGSLM 204
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1013071061  793 PLKDKTLIEKErfyESRCRPVTPSCKELADLMTRCMNYDPNQRPFFRAIMRD--INKLEEQNPDIVS 857
Cdd:cd06619    205 PLQLLQCIVDE---DPPVLPVGQFSEKFVHFITQCMRKQPKERPAPENLMDHpfIVQYNDGNAEVVS 268
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
629-835 1.62e-03

Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The pseudokinase domain may function as a regulatory domain or a protein interaction domain. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 41.73  E-value: 1.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  629 RDISLAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLF--MHRKSDVLTTPWKFKVAKQLASALSYLE 706
Cdd:cd14109     37 RYGDPFLMREVDIHNSLDHPNIVQMHDAYDDEKLAVTVIDNLASTIELVRdnLLPGKDYYTERQVAVFVRQLLLALKHMH 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  707 DKDLVHGNVCTKNLLLAREgidsecgpFIKLSDPGipitvLSRQecIER---------IP-WIAPECVeDSKNLSVAADK 776
Cdd:cd14109    117 DLGIAHLDLRPEDILLQDD--------KLKLADFG-----QSRR--LLRgklttliygSPeFVSPEIV-NSYPVTLATDM 180
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1013071061  777 WSFGTTLWeICYNGEIPL---KDKTLIEKERfyESRCR----PVTPSCKELADLMTRCMNYDPNQR 835
Cdd:cd14109    181 WSVGVLTY-VLLGGISPFlgdNDRETLTNVR--SGKWSfdssPLGNISDDARDFIKKLLVYIPESR 243
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
690-842 1.83e-03

Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Myt1 is a cytoplasmic cell cycle checkpoint kinase that can keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of N-terminal thr (T14) and tyr (Y15) residues, leading to the delay of meiosis I entry. Meiotic progression is ensured by a two-step inhibition and downregulation of Myt1 by CDK1/XRINGO and p90Rsk during oocyte maturation. In addition, Myt1 targets cyclin B1/B2 and is essential for Golgi and ER assembly during telophase. In Drosophila, Myt1 may be a downstream target of Notch during eye development. The Myt1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270952 [Multi-domain]  Cd Length: 249  Bit Score: 41.53  E-value: 1.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  690 WKFKVakQLASALSYLEDKDLVHGNVCTKNLLLAREGIdseCgpfiKLSDPGIPITV-----LSRQECIERipWIAPECV 764
Cdd:cd14050    103 WNILL--DLLKGLKHLHDHGLIHLDIKPANIFLSKDGV---C----KLGDFGLVVELdkediHDAQEGDPR--YMAPELL 171
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  765 EDSknLSVAADKWSFGTTLWEI-CY--------------NGEIPlkdktliekERFYEsrcrPVTPSCKELADLMtrcMN 829
Cdd:cd14050    172 QGS--FTKAADIFSLGITILELaCNlelpsggdgwhqlrQGYLP---------EEFTA----GLSPELRSIIKLM---MD 233
                          170
                   ....*....|...
gi 1013071061  830 YDPNQRPFFRAIM 842
Cdd:cd14050    234 PDPERRPTAEDLL 246
PK_GC-C cd14044
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain ...
602-848 1.97e-03

Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-C binds and is activated by the intestinal hormones, guanylin (GN) and uroguanylin (UGN), which are secreted after salty meals to inhibit sodium absorption and induce the secretion of chloride, bicarbonate, and water. GN and UGN are also present in the kidney, where they induce increased salt and water secretion. This prevents the development of hypernatremia and hypervolemia after ingestion of high amounts of salt. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-C subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270946 [Multi-domain]  Cd Length: 271  Bit Score: 41.41  E-value: 1.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  602 LMDYKDDEGTSEEKKIKVILKVLdpshrdislaffeaasmmrQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHR 681
Cdd:cd14044     36 LKDLKNNEGNFTEKQKIELNKLL-------------------QIDYYNLTKFYGTVKLDTMIFGVIEYCERGSLRDVLND 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  682 K---SDVLTTPWKFK--VAKQLASALSYLE-DKDLVHGNVCTKNLLlaregIDSECgpFIKLSDPGIPiTVLSRqeciER 755
Cdd:cd14044     97 KisyPDGTFMDWEFKisVMYDIAKGMSYLHsSKTEVHGRLKSTNCV-----VDSRM--VVKITDFGCN-SILPP----SK 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  756 IPWIAPECVEDSkNLSVAADKWSFGTTLWEIcyngeiplkdktLIEKERFYESRCR----------------PVTPSC-- 817
Cdd:cd14044    165 DLWTAPEHLRQA-GTSQKGDVYSYGIIAQEI------------ILRKETFYTAACSdrkekiyrvqnpkgmkPFRPDLnl 231
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1013071061  818 -------KELADLMTRCMNYDPNQRPFFRAIMRDINKL 848
Cdd:cd14044    232 esagereREVYGLVKNCWEEDPEKRPDFKKIENTLAKI 269
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
640-847 2.16e-03

Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes cyclin G-Associated Kinase (GAK), Drosophila melanogaster Numb-Associated Kinase (NAK)-like proteins, and similar protein kinases. GAK plays regulatory roles in clathrin-mediated membrane trafficking, the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses. NAK plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. The GAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270887 [Multi-domain]  Cd Length: 272  Bit Score: 41.17  E-value: 2.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  640 SMMRQVS-HKHIVYLYGVCVRDVEN----IMVEEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKD--LVH 712
Cdd:cd13985     49 EIMKRLCgHPNIVQYYDSAILSSEGrkevLLLMEYCPGSLVDILEKSPPSPLSEEEVLRIFYQICQAVGHLHSQSppIIH 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  713 GNVCTKNLLLAREGIdsecgpfIKLSDPGIPITVLSRQECIERIPWI-------------APECVE--DSKNLSVAADKW 777
Cdd:cd13985    129 RDIKIENILFSNTGR-------FKLCDFGSATTEHYPLERAEEVNIIeeeiqknttpmyrAPEMIDlySKKPIGEKADIW 201
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1013071061  778 SFGTTLWEICY-----NGEIPLKDKTLiekerfyesRCR-PVTPSC-KELADLMTRCMNYDPNQRPFFRAIMRDINK 847
Cdd:cd13985    202 ALGCLLYKLCFfklpfDESSKLAIVAG---------KYSiPEQPRYsPELHDLIRHMLTPDPAERPDIFQVINIITK 269
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
629-835 2.24e-03

Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK, CDK2, and CDK3. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression while the CDK1/cyclin B complex is critical for G2 to M phase transition. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. Studies in knockout mice revealed that CDK1 can compensate for the loss of the cdk2 gene as it can also bind cyclin E and drive G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270829 [Multi-domain]  Cd Length: 283  Bit Score: 41.51  E-value: 2.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  629 RDISLaffeaasmMRQVSHKHIVYLYGVCVRDVENIMVEEFVEggpLDL--FM-HRKSDVLTTPWKFKVAKQLASALSYL 705
Cdd:cd07835     47 REISL--------LKELNHPNIVRLLDVVHSENKLYLVFEFLD---LDLkkYMdSSPLTGLDPPLIKSYLYQLLQGIAFC 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  706 EDKDLVHGNVCTKNLLLAREGIdsecgpfIKLSDPG------IPItvlsRQECIERIP-WI-APECVEDSKNLSVAADKW 777
Cdd:cd07835    116 HSHRVLHRDLKPQNLLIDTEGA-------LKLADFGlarafgVPV----RTYTHEVVTlWYrAPEILLGSKHYSTPVDIW 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  778 SFGTTLWEIC-----YNG--EI------------PLKD-----KTLIE-KERFYESRCRP---VTPSCKELA-DLMTRCM 828
Cdd:cd07835    185 SVGCIFAEMVtrrplFPGdsEIdqlfrifrtlgtPDEDvwpgvTSLPDyKPTFPKWARQDlskVVPSLDEDGlDLLSQML 264

                   ....*..
gi 1013071061  829 NYDPNQR 835
Cdd:cd07835    265 VYDPAKR 271
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
637-797 2.27e-03

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 41.40  E-value: 2.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  637 EAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGplDLFMHRKSDVLTTPWKF-KVAKQLASALSYLEDKDLVHGNV 715
Cdd:cd14180     50 EVAALRLCQSHPNIVALHEVLHDQYHTYLVMELLRGG--ELLDRIKKKARFSESEAsQLMRSLVSAVSFMHEAGVVHRDL 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  716 CTKNLLLAREGIdsecGPFIKLSDPGI----PITVLSRQECIERIPWIAPECVEDSkNLSVAADKWSFGTTLWEIcYNGE 791
Cdd:cd14180    128 KPENILYADESD----GAVLKVIDFGFarlrPQGSRPLQTPCFTLQYAAPELFSNQ-GYDESCDLWSLGVILYTM-LSGQ 201

                   ....*.
gi 1013071061  792 IPLKDK 797
Cdd:cd14180    202 VPFQSK 207
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
586-786 2.66e-03

Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mos (or c-Mos) is a germ-cell specific kinase that plays roles in both the release of primary arrest and the induction of secondary arrest in oocytes. It is expressed towards the end of meiosis I and is quickly degraded upon fertilization. It is a component of the cytostatic factor (CSF), which is responsible for metaphase II arrest. In addition, Mos activates a phoshorylation cascade that leads to the activation of the p34 subunit of MPF (mitosis-promoting factor or maturation promoting factor), a cyclin-dependent kinase that is responsible for the release of primary arrest in meiosis I. The Mos subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270881 [Multi-domain]  Cd Length: 265  Bit Score: 41.22  E-value: 2.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  586 GEHLGRGTRTHIYSGTlmdYKDdegtsEEKKIKVILKVLDPSHRDISlafFEAASMMRQVSHKHIVYLYGVCVRDVEN-- 663
Cdd:cd13979      8 QEPLGSGGFGSVYKAT---YKG-----ETVAVKIVRRRRKNRASRQS---FWAELNAARLRHENIVRVLAAETGTDFAsl 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  664 ---IMveEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIdseCgpfiKLSDP 740
Cdd:cd13979     77 gliIM--EYCGNGTLQQLIYEGSEPLPLAHRILISLDIARALRFCHSHGIVHLDVKPANILISEQGV---C----KLCDF 147
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1013071061  741 GIPITVLSRQECIERIPWI-------APECVEdSKNLSVAADKWSFGTTLWEI 786
Cdd:cd13979    148 GCSVKLGEGNEVGTPRSHIggtytyrAPELLK-GERVTPKADIYSFGITLWQM 199
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
640-780 3.53e-03

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270985 [Multi-domain]  Cd Length: 259  Bit Score: 40.43  E-value: 3.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  640 SMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPL-DLFMHRKSdvLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTK 718
Cdd:cd14083     53 AVLRKIKHPNIVQLLDIYESKSHLYLVMELVTGGELfDRIVEKGS--YTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPE 130
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1013071061  719 NLLLAREGIDSEcgpfIKLSDPGipitvLSRQECIERIP-------WIAPEcVEDSKNLSVAADKWSFG 780
Cdd:cd14083    131 NLLYYSPDEDSK----IMISDFG-----LSKMEDSGVMStacgtpgYVAPE-VLAQKPYGKAVDCWSIG 189
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
640-836 4.34e-03

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270892 [Multi-domain]  Cd Length: 279  Bit Score: 40.38  E-value: 4.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  640 SMMRQVSHKHIVYLYGVCVRDVEN-IMVEEFVEGGPLDLFMHRKSDVLTtpwkfKVAK----QLASALSYLEDKD--LVH 712
Cdd:cd13990     56 EIHKSLDHPRIVKLYDVFEIDTDSfCTVLEYCDGNDLDFYLKQHKSIPE-----REARsiimQVVSALKYLNEIKppIIH 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  713 GNVCTKNLLLAREGIDSECgpfiKLSDPGIPITVLSRQECIERIP---------W-IAPECVEDSKN---LSVAADKWSF 779
Cdd:cd13990    131 YDLKPGNILLHSGNVSGEI----KITDFGLSKIMDDESYNSDGMEltsqgagtyWyLPPECFVVGKTppkISSKVDVWSV 206
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1013071061  780 GTTLWEICY---------NGEIPLKDKTLIEKERFyESRCRPVTPSckELADLMTRCMNYDPNQRP 836
Cdd:cd13990    207 GVIFYQMLYgrkpfghnqSQEAILEENTILKATEV-EFPSKPVVSS--EAKDFIRRCLTYRKEDRP 269
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
665-835 4.43e-03

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1 functions as a receptor for morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Vertebrates contain two type I BMP receptors, BMPR1a and BMPR1b. BMPR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that also includes TGFbeta, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 40.54  E-value: 4.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  665 MVEEFVEGGPLDLFMhrKSDVLTTPWKFKVAKQLASALSYLEDK--------DLVHGNVCTKNLLLAREGidSECgpfik 736
Cdd:cd14144     70 LITDYHENGSLYDFL--RGNTLDTQSMLKLAYSAACGLAHLHTEifgtqgkpAIAHRDIKSKNILVKKNG--TCC----- 140
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  737 LSDPGIPITVLSRQECIERIP--------WIAPECVEDSKNLS-----VAADKWSFGTTLWEI---CYNG------EIPL 794
Cdd:cd14144    141 IADLGLAVKFISETNEVDLPPntrvgtkrYMAPEVLDESLNRNhfdayKMADMYSFGLVLWEIarrCISGgiveeyQLPY 220
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1013071061  795 KDktLIEKERFYES--------RCRPVTPS-------CKELADLMTRCMNYDPNQR 835
Cdd:cd14144    221 YD--AVPSDPSYEDmrrvvcveRRRPSIPNrwssdevLRTMSKLMSECWAHNPAAR 274
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
641-786 4.97e-03

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK10, also called PISSLRE, is essential for cell growth and proliferation, and acts through the G2/M phase of the cell cycle. CDK10 has also been identified as an important factor in endocrine therapy resistance in breast cancer. CDK10 silencing increases the transcription of c-RAF and the activation of the p42/p44 MAPK pathway, which leads to antiestrogen resistance. Patients who express low levels of CDK10 relapse early on tamoxifen. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK10 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173742 [Multi-domain]  Cd Length: 309  Bit Score: 40.43  E-value: 4.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  641 MMRQVSHKHIVYLYGVCV-RDVENI-MVEEFVEGgplDLfmHRKSDVLTTPWKFKVAK----QLASALSYLEDKDLVHGN 714
Cdd:cd07845     59 LLLNLRHPNIVELKEVVVgKHLDSIfLVMEYCEQ---DL--ASLLDNMPTPFSESQVKclmlQLLRGLQYLHENFIIHRD 133
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1013071061  715 VCTKNLLLAREGIdsecgpfIKLSDPGIPIT----VLSRQECIERIPWIAPECVEDSKNLSVAADKWSFGTTLWEI 786
Cdd:cd07845    134 LKVSNLLLTDKGC-------LKIADFGLARTyglpAKPMTPKVVTLWYRAPELLLGCTTYTTAIDMWAVGCILAEL 202
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
611-844 5.80e-03

Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase (also called MAK-V); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HUNK/MAK-V was identified from a mammary tumor in an MMTV-neu transgenic mouse. It is required for the metastasis of c-myc-induced mammary tumors, but is not necessary for c-myc-induced primary tumor formation or normal development. It is required for HER2/neu-induced tumor formation and maintenance of the cells' tumorigenic phenotype. It is over-expressed in aggressive subsets of ovary, colon, and breast carcinomas. HUNK interacts with synaptopodin, and may also play a role in synaptic plasticity. The HUNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270972 [Multi-domain]  Cd Length: 262  Bit Score: 39.80  E-value: 5.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  611 TSEEKKIKVILKVLDPSHRDISLAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLdlfMHR--KSDVLTT 688
Cdd:cd14070     26 TGEKVAIKVIDKKKAKKDSYVTKNLRREGRIQQMIRHPNITQLLDILETENSYYLVMELCPGGNL---MHRiyDKKRLEE 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  689 PWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREG----ID---SECGPFIKLSDPgipitvLSRQeCiERIPWIAP 761
Cdd:cd14070    103 REARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDniklIDfglSNCAGILGYSDP------FSTQ-C-GSPAYAAP 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  762 ECVEdSKNLSVAADKWSFGTTLWEIcYNGEI-----PLKDKTLIEKERFYESRCRP--VTPSCKEladLMTRCMNYDPNQ 834
Cdd:cd14070    175 ELLA-RKKYGPKVDVWSIGVNMYAM-LTGTLpftvePFSLRALHQKMVDKEMNPLPtdLSPGAIS---FLRSLLEPDPLK 249
                          250
                   ....*....|
gi 1013071061  835 RPFFRAIMRD 844
Cdd:cd14070    250 RPNIKQALAN 259
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
643-801 9.45e-03

Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK9 and CDK12 from higher eukaryotes, yeast BUR1, C-type plant CDKs (CdkC), and similar proteins. CDK9, BUR1, and CdkC are functionally equivalent. They act as a kinase for the C-terminal domain of RNA polymerase II and participate in regulating mutliple steps of gene expression including transcription elongation and RNA processing. CDK9 and CdkC associate with T-type cyclins while BUR1 associates with the cyclin BUR2. CDK12 is a unique CDK that contains an arginine/serine-rich (RS) domain, which is predominantly found in splicing factors. CDK12 interacts with cyclins L1 and L2, and participates in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270832 [Multi-domain]  Cd Length: 291  Bit Score: 39.47  E-value: 9.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  643 RQVSHKHIVYLYGVCV-RDVENI-----MVEEFVEGgplDL--FMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGN 714
Cdd:cd07840     53 QKLDHPNVVRLKEIVTsKGSAKYkgsiyMVFEYMDH---DLtgLLDNPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRD 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013071061  715 VCTKNLLLAREGIdsecgpfIKLSDPGI--PITVLSRQECIERIP--WI-APECVEDSKNLSVAADKWSFGTTLWEiCYN 789
Cdd:cd07840    130 IKGSNILINNDGV-------LKLADFGLarPYTKENNADYTNRVItlWYrPPELLLGATRYGPEVDMWSVGCILAE-LFT 201
                          170
                   ....*....|..
gi 1013071061  790 GEIPLKDKTLIE 801
Cdd:cd07840    202 GKPIFQGKTELE 213
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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