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Conserved domains on  [gi|2038291632|ref|XP_041490629|]
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ephrin type-A receptor 1 [Microtus oregoni]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
619-884 1.78e-156

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member cd05033:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 266  Bit Score: 461.46  E-value: 1.78e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 619 LDPTWLIVDTVIGEGEFGEVYRGALRFPSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPI 698
Cdd:cd05033     1 IDASYVTIEKVIGGGEFGEVCSGSLKLPGKKEIDVAIKTLKSGYSDKQRLDFLTEASIMGQFDHPNVIRLEGVVTKSRPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 699 MIVTEFMENGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFD 778
Cdd:cd05033    81 MIVTEYMENGSLDKFLRENDGKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDFGLSRRLEDSE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 779 GTYETQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLYEL 858
Cdd:cd05033   161 ATYTTKGGKIPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSYGERPYWDMSNQDVIKAVEDGYRLPPPMDCPSALYQL 240
                         250       260
                  ....*....|....*....|....*.
gi 2038291632 859 MKNCWAYDRARRPHFLQLQAHLEQLL 884
Cdd:cd05033   241 MLDCWQKDRNERPTFSQIVSTLDKMI 266
EphR_LBD_A1 cd10479
Ligand Binding Domain of Ephrin type-A Receptor 1; Ephrin receptors (EphRs) comprise the ...
27-203 1.32e-131

Ligand Binding Domain of Ephrin type-A Receptor 1; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (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. EphA1 is downregulated in some advanced colorectal and myeloid cancers and upregulated in neuroblasoma and glioblastoma. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine 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.


:

Pssm-ID: 198447  Cd Length: 177  Bit Score: 393.63  E-value: 1.32e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632  27 EVTLMDTSKAQGELGWLLDPPEDGWSEVQQMLNGTPLYMYQDCPVEESGDTNHWLRSNWIYRGEEASRVHVELQFTVRDC 106
Cdd:cd10479     1 EVTLMDTSTAQGELGWLLDPPEVGWSEVQQMLNGTPLYMYQDCPVQSEGDTDHWLRSNWIYRGEEASRIYVELQFTVRDC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 107 KSFPGGAGPMGCKETFNLLYMESDQDVGIQLRRPLFQKVTTVAADQSFTIRDLASGAVKLNVERCSLGRLTHRGLYLAFH 186
Cdd:cd10479    81 KSFPGGAGPLGCKETFNLYYMESDQDVGIQLRRPLFQKVTTVAADQSFTIRDLASGSVKLNVERCSLGKLTRRGLYLAFH 160
                         170
                  ....*....|....*..
gi 2038291632 187 NPGSCVALVSVRVFYQR 203
Cdd:cd10479   161 NPGACVALVSVRVFYQR 177
SAM_EPH-A1 cd09542
SAM domain of EPH-A1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
912-974 8.51e-41

SAM domain of EPH-A1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A1 subfamily of the receptor tyrosine kinases is a C-terminal protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A1 receptors and appears to mediate cell-cell initiated signal transduction. Activation of these receptors leads to inhibition of cell spreading and migration in a RhoA-ROCK-dependent manner. EPH-A1 receptors are known to bind ILK (integrin-linked kinase) which is the mediator of interactions between integrin and the actin cytoskeleton. However SAM is not sufficient for this interaction; it rather plays an ancillary role. SAM domains of Eph-A1 receptors do not form homo/hetero dimers/oligomers. EphA1 gene was found expressed widely in differentiated epithelial cells. In a number of different malignant tumors EphA1 genes are downregulated. In breast carcinoma the downregulation is associated with invasive behavior of the cell.


:

Pssm-ID: 188941  Cd Length: 63  Bit Score: 143.99  E-value: 8.51e-41
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038291632 912 GIPYRSVSEWLESIRMKRYILHFRSAGLDTMECVLELTAEDLTQMGITLPGHQKRILCSIQGF 974
Cdd:cd09542     1 GIPYRSVSEWLESIRMKRYILHFRSAGLDTMECVLELTAEDLTQMGITLPGHQKRILCSIQGF 63
TM_EphA1 cd12841
Transmembrane domain of Ephrin Receptor A1 Protein Tyrosine Kinase; Ephrin receptors (EphRs) ...
536-568 3.92e-15

Transmembrane domain of Ephrin Receptor A1 Protein Tyrosine Kinase; Ephrin receptors (EphRs) comprise the largest subfamily of receptor PTKs, and are classified into two classes (EphA and EphB), corresponding 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. EphA1 has been associated with late-onset Alzheimer's disease and certain cancers such as colorectal and gastric carcinomas. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a single-span transmembrane (TM) domain, 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 TM domain mediates dimerization.


:

Pssm-ID: 214014  Cd Length: 38  Bit Score: 69.70  E-value: 3.92e-15
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2038291632 536 SPPVSRSLTGGEIVAIIFGVLLGIALLIGIYVF 568
Cdd:cd12841     1 SPPVSRGLTGGEIVAIIFGLLLGVALLLGILVF 33
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
453-535 1.42e-09

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 55.97  E-value: 1.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 453 LRLVKKEPRQLELAWagSRPRTPGGN-LSYELHVLNQDE-EWHQM----VLEPRVLLTKLQPDTTYIVRVRTMTPLGPGP 526
Cdd:cd00063     7 LRVTDVTSTSVTLSW--TPPEDDGGPiTGYVVEYREKGSgDWKEVevtpGSETSYTLTGLKPGTEYEFRVRAVNGGGESP 84

                  ....*....
gi 2038291632 527 FSPDHEFRT 535
Cdd:cd00063    85 PSESVTVTT 93
fn3 pfam00041
Fibronectin type III domain;
334-425 4.42e-09

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 54.34  E-value: 4.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 334 SAPQNLSFSA-SGTQLSLCWEPPRDTGGrHDIRYSVDCLQCRgiaqDGGPCQPcgkgvRFTPGasglTESTVQVEGLEPY 412
Cdd:pfam00041   1 SAPSNLTVTDvTSTSLTVSWTPPPDGNG-PITGYEVEYRPKN----SGEPWNE-----ITVPG----TTTSVTLTGLKPG 66
                          90
                  ....*....|...
gi 2038291632 413 ANYTFTIKSQNRV 425
Cdd:pfam00041  67 TEYEVRVQAVNGG 79
 
Name Accession Description Interval E-value
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
619-884 1.78e-156

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: 461.46  E-value: 1.78e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 619 LDPTWLIVDTVIGEGEFGEVYRGALRFPSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPI 698
Cdd:cd05033     1 IDASYVTIEKVIGGGEFGEVCSGSLKLPGKKEIDVAIKTLKSGYSDKQRLDFLTEASIMGQFDHPNVIRLEGVVTKSRPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 699 MIVTEFMENGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFD 778
Cdd:cd05033    81 MIVTEYMENGSLDKFLRENDGKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDFGLSRRLEDSE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 779 GTYETQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLYEL 858
Cdd:cd05033   161 ATYTTKGGKIPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSYGERPYWDMSNQDVIKAVEDGYRLPPPMDCPSALYQL 240
                         250       260
                  ....*....|....*....|....*.
gi 2038291632 859 MKNCWAYDRARRPHFLQLQAHLEQLL 884
Cdd:cd05033   241 MLDCWQKDRNERPTFSQIVSTLDKMI 266
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
624-880 3.13e-134

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: 403.42  E-value: 3.13e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 624 LIVDTVIGEGEFGEVYRGALRF-PSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVT 702
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKGeGENTKIKVAVKTLKEGADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 703 EFMENGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYE 782
Cdd:pfam07714  81 EYMPGGDLLDFLRKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDIYDDDYYRK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 783 TQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLYELMKNC 862
Cdd:pfam07714 161 RGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEFLEDGYRLPQPENCPDELYDLMKQC 240
                         250
                  ....*....|....*...
gi 2038291632 863 WAYDRARRPHFLQLQAHL 880
Cdd:pfam07714 241 WAYDPEDRPTFSELVEDL 258
EphR_LBD_A1 cd10479
Ligand Binding Domain of Ephrin type-A Receptor 1; Ephrin receptors (EphRs) comprise the ...
27-203 1.32e-131

Ligand Binding Domain of Ephrin type-A Receptor 1; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (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. EphA1 is downregulated in some advanced colorectal and myeloid cancers and upregulated in neuroblasoma and glioblastoma. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine 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.


Pssm-ID: 198447  Cd Length: 177  Bit Score: 393.63  E-value: 1.32e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632  27 EVTLMDTSKAQGELGWLLDPPEDGWSEVQQMLNGTPLYMYQDCPVEESGDTNHWLRSNWIYRGEEASRVHVELQFTVRDC 106
Cdd:cd10479     1 EVTLMDTSTAQGELGWLLDPPEVGWSEVQQMLNGTPLYMYQDCPVQSEGDTDHWLRSNWIYRGEEASRIYVELQFTVRDC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 107 KSFPGGAGPMGCKETFNLLYMESDQDVGIQLRRPLFQKVTTVAADQSFTIRDLASGAVKLNVERCSLGRLTHRGLYLAFH 186
Cdd:cd10479    81 KSFPGGAGPLGCKETFNLYYMESDQDVGIQLRRPLFQKVTTVAADQSFTIRDLASGSVKLNVERCSLGKLTRRGLYLAFH 160
                         170
                  ....*....|....*..
gi 2038291632 187 NPGSCVALVSVRVFYQR 203
Cdd:cd10479   161 NPGACVALVSVRVFYQR 177
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
624-880 1.79e-128

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 388.43  E-value: 1.79e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632  624 LIVDTVIGEGEFGEVYRGALRFPSQDCK-TVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVT 702
Cdd:smart00219   1 LTLGKKLGEGAFGEVYKGKLKGKGGKKKvEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYIVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632  703 EFMENGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDfDGTYE 782
Cdd:smart00219  81 EYMEGGDLLSYLRKNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYD-DDYYR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632  783 TQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLYELMKNC 862
Cdd:smart00219 160 KRGGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEYLKNGYRLPQPPNCPPELYDLMLQC 239
                          250
                   ....*....|....*...
gi 2038291632  863 WAYDRARRPHFLQLQAHL 880
Cdd:smart00219 240 WAEDPEDRPTFSELVEIL 257
EPH_lbd smart00615
Ephrin receptor ligand binding domain;
27-203 7.59e-82

Ephrin receptor ligand binding domain;


Pssm-ID: 128877  Cd Length: 177  Bit Score: 262.22  E-value: 7.59e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632   27 EVTLMDTSKAQGELGWLLDPPEdGWSEVQQM-LNGTPLYMYQDCPVEEsGDTNHWLRSNWIYRGEeASRVHVELQFTVRD 105
Cdd:smart00615   1 EVVLLDTKTETGELGWTTYPPE-GWEEVSGMdENGTPIRTYQVCNVQE-GNQNNWLRTNFIRRRG-AQRIYVELKFTVRD 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632  106 CKSFPGGAGPmgCKETFNLLYMESDQDVGIQ----LRRPLFQKVTTVAADQSFTIRDLASGAVKLNVERCSLGRLTHRGL 181
Cdd:smart00615  78 CSSLPGVGGS--CKETFNLYYYESDTDTATNtlpnWMENPYTKVDTIAADESFTGGDVGKRNVKLNTEVRSLGPLSKKGF 155
                          170       180
                   ....*....|....*....|..
gi 2038291632  182 YLAFHNPGSCVALVSVRVFYQR 203
Cdd:smart00615 156 YLAFQDQGACVALVSVRVFYKK 177
Ephrin_lbd pfam01404
Ephrin receptor ligand binding domain; The Eph receptors, which bind to ephrins pfam00812 are ...
28-204 1.24e-74

Ephrin receptor ligand binding domain; The Eph receptors, which bind to ephrins pfam00812 are a large family of receptor tyrosine kinases. This family represents the amino terminal domain which binds the ephrin ligand.


Pssm-ID: 460198  Cd Length: 177  Bit Score: 242.96  E-value: 1.24e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632  28 VTLMDTSKAQGELGWLLDPPEDGWSEVQQM-LNGTPLYMYQDCPVEEsGDTNHWLRSNWIYRGEeASRVHVELQFTVRDC 106
Cdd:pfam01404   1 EVLLDTTSATSDLGWTTYPYDGGWEEVSGLdENGRTIRTYQVCNVEE-PNQNNWLRTPFIPRGG-ASRVYVELKFTVRDC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 107 KSFPGGAGPmgCKETFNLLYMESDQDVGI----QLRRPLFQKVTTVAADQSFTIRDlASGAVKLNVERCSLGRLTHRGLY 182
Cdd:pfam01404  79 SSIPGVSGT--CKETFNLYYYESDADAATatppAWRENPYKKIDTIAADESFTDTG-KGRVMKLNTETRSIGPLSKRGFY 155
                         170       180
                  ....*....|....*....|..
gi 2038291632 183 LAFHNPGSCVALVSVRVFYQRC 204
Cdd:pfam01404 156 LAFQDQGACIALLSVRVFYKKC 177
SAM_EPH-A1 cd09542
SAM domain of EPH-A1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
912-974 8.51e-41

SAM domain of EPH-A1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A1 subfamily of the receptor tyrosine kinases is a C-terminal protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A1 receptors and appears to mediate cell-cell initiated signal transduction. Activation of these receptors leads to inhibition of cell spreading and migration in a RhoA-ROCK-dependent manner. EPH-A1 receptors are known to bind ILK (integrin-linked kinase) which is the mediator of interactions between integrin and the actin cytoskeleton. However SAM is not sufficient for this interaction; it rather plays an ancillary role. SAM domains of Eph-A1 receptors do not form homo/hetero dimers/oligomers. EphA1 gene was found expressed widely in differentiated epithelial cells. In a number of different malignant tumors EphA1 genes are downregulated. In breast carcinoma the downregulation is associated with invasive behavior of the cell.


Pssm-ID: 188941  Cd Length: 63  Bit Score: 143.99  E-value: 8.51e-41
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038291632 912 GIPYRSVSEWLESIRMKRYILHFRSAGLDTMECVLELTAEDLTQMGITLPGHQKRILCSIQGF 974
Cdd:cd09542     1 GIPYRSVSEWLESIRMKRYILHFRSAGLDTMECVLELTAEDLTQMGITLPGHQKRILCSIQGF 63
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
626-905 6.71e-39

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 151.70  E-value: 6.71e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 626 VDTVIGEGEFGEVYRGalRFPSQDcKTVAIKTLKDTSPDGQWW--NFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTE 703
Cdd:COG0515    11 ILRLLGRGGMGVVYLA--RDLRLG-RPVALKVLRPELAADPEAreRFRREARALARLNHPNIVRVYDVGEEDGRPYLVME 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 704 FMENGALDAFLKEREdQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDfdgTYET 783
Cdd:COG0515    88 YVEGESLADLLRRRG-PLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGG---ATLT 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 784 QGGKIP--IRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSIEEGYRLPPPV---DCPAPLYEL 858
Cdd:COG0515   164 QTGTVVgtPGYMAPEQARGEPVDPRSDVYSLGVTLYELLT-GRPPFDGDSPAELLRAHLREPPPPPSElrpDLPPALDAI 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2038291632 859 MKNCWAYDRARRPH-FLQLQAHLEQLLTDPHSLRTIANFDPRVTLRLP 905
Cdd:COG0515   243 VLRALAKDPEERYQsAAELAAALRAVLRSLAAAAAAAAAAAAAAAAAA 290
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
911-975 2.51e-23

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 93.87  E-value: 2.51e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2038291632 911 DGIPYRSVSEWLESIRMKRYILHFRsAGLDTMECVLELTAEDLTQMGITLPGHQKRILCSIQGFK 975
Cdd:pfam00536   1 DGWSVEDVGEWLESIGLGQYIDSFR-AGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRLK 64
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
911-976 5.46e-20

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 84.65  E-value: 5.46e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2038291632  911 DGIPYRSVSEWLESIRMKRYILHFRSAGLDTMECVLELTAEDLTQMGITLPGHQKRILCSIQGFKD 976
Cdd:smart00454   2 SQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLKE 67
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
626-821 1.41e-18

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 88.28  E-value: 1.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 626 VDTVIGEGEFGEVYRGalrFPSQDCKTVAIKTLK------DTSPDGQW-----WNF--LREATIMGQFNHPHILRLEGVV 692
Cdd:PTZ00024   13 KGAHLGEGTYGKVEKA---YDTLTGKIVAIKKVKiieisnDVTKDRQLvgmcgIHFttLRELKIMNEIKHENIMGLVDVY 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 693 TKRKPIMIVTEFMEnGALDAFLkEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTR 772
Cdd:PTZ00024   90 VEGDFINLVMDIMA-SDLKKVV-DRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGLAR 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038291632 773 --LLDDFDGTYETQGGKIPIR----------WTAPEAI--AHRiFTTASDVWSFGIVMWEVLS 821
Cdd:PTZ00024  168 ryGYPPYSDTLSKDETMQRREemtskvvtlwYRAPELLmgAEK-YHFAVDMWSVGCIFAELLT 229
TM_EphA1 cd12841
Transmembrane domain of Ephrin Receptor A1 Protein Tyrosine Kinase; Ephrin receptors (EphRs) ...
536-568 3.92e-15

Transmembrane domain of Ephrin Receptor A1 Protein Tyrosine Kinase; Ephrin receptors (EphRs) comprise the largest subfamily of receptor PTKs, and are classified into two classes (EphA and EphB), corresponding 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. EphA1 has been associated with late-onset Alzheimer's disease and certain cancers such as colorectal and gastric carcinomas. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a single-span transmembrane (TM) domain, 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 TM domain mediates dimerization.


Pssm-ID: 214014  Cd Length: 38  Bit Score: 69.70  E-value: 3.92e-15
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2038291632 536 SPPVSRSLTGGEIVAIIFGVLLGIALLIGIYVF 568
Cdd:cd12841     1 SPPVSRGLTGGEIVAIIFGLLLGVALLLGILVF 33
EphA2_TM pfam14575
Ephrin type-A receptor 2 transmembrane domain; Epha2_TM represents the left-handed dimer ...
548-621 1.09e-11

Ephrin type-A receptor 2 transmembrane domain; Epha2_TM represents the left-handed dimer transmembrane domain of of EphA2 receptor. This domain oligomerises and is important for the active signalling process.


Pssm-ID: 464211  Cd Length: 72  Bit Score: 61.08  E-value: 1.09e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038291632 548 IVAIIFGVLLGIALLIGIYVFRSRRGQRQRQQRqreraTNVDREDKL---WLKPYVDLQAYEDPAQGALDFAQELDP 621
Cdd:pfam14575   1 VVASVAGGLVLLLVVGVVLIRRRRCCGRKKSQD-----DDEEEFHQYkppGRKTYIDPHTYEDPNQAVLEFAKEIDA 72
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
626-829 3.08e-11

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 67.13  E-value: 3.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 626 VDTVIGEGEFGEVYRGalrfpsQDCK---TVAIKTLK-DTSPDGqwwNFL----REATIMGQFNHPHILRL------EGV 691
Cdd:NF033483   11 IGERIGRGGMAEVYLA------KDTRldrDVAVKVLRpDLARDP---EFVarfrREAQSAASLSHPNIVSVydvgedGGI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 692 VtkrkpiMIVTEFMENGALDAFLKEREdQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLT 771
Cdd:NF033483   82 P------YIVMEYVDGRTLKDYIREHG-PLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIA 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2038291632 772 RLLddfDGTYETQGGKI--PIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPY-GE 829
Cdd:NF033483  155 RAL---SSTTMTQTNSVlgTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLT-GRPPFdGD 211
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
453-535 1.42e-09

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 55.97  E-value: 1.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 453 LRLVKKEPRQLELAWagSRPRTPGGN-LSYELHVLNQDE-EWHQM----VLEPRVLLTKLQPDTTYIVRVRTMTPLGPGP 526
Cdd:cd00063     7 LRVTDVTSTSVTLSW--TPPEDDGGPiTGYVVEYREKGSgDWKEVevtpGSETSYTLTGLKPGTEYEFRVRAVNGGGESP 84

                  ....*....
gi 2038291632 527 FSPDHEFRT 535
Cdd:cd00063    85 PSESVTVTT 93
fn3 pfam00041
Fibronectin type III domain;
334-425 4.42e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 54.34  E-value: 4.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 334 SAPQNLSFSA-SGTQLSLCWEPPRDTGGrHDIRYSVDCLQCRgiaqDGGPCQPcgkgvRFTPGasglTESTVQVEGLEPY 412
Cdd:pfam00041   1 SAPSNLTVTDvTSTSLTVSWTPPPDGNG-PITGYEVEYRPKN----SGEPWNE-----ITVPG----TTTSVTLTGLKPG 66
                          90
                  ....*....|...
gi 2038291632 413 ANYTFTIKSQNRV 425
Cdd:pfam00041  67 TEYEVRVQAVNGG 79
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
333-424 4.41e-08

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 51.73  E-value: 4.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 333 PSAPQNLSFSA-SGTQLSLCWEPPRDTGGRHDiRYSVDCLQCrgiaqDGGPCQPCGKGVrftpgasgLTESTVQVEGLEP 411
Cdd:cd00063     1 PSPPTNLRVTDvTSTSVTLSWTPPEDDGGPIT-GYVVEYREK-----GSGDWKEVEVTP--------GSETSYTLTGLKP 66
                          90
                  ....*....|...
gi 2038291632 412 YANYTFTIKSQNR 424
Cdd:cd00063    67 GTEYEFRVRAVNG 79
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
333-425 4.95e-08

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 51.08  E-value: 4.95e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632  333 PSAPQNLSFSA-SGTQLSLCWEPPRDTGGRHDI-RYSVdclqcrgiaqdggpcQPCGKGVRFTPGASGLTESTVQVEGLE 410
Cdd:smart00060   1 PSPPSNLRVTDvTSTSVTLSWEPPPDDGITGYIvGYRV---------------EYREEGSEWKEVNVTPSSTSYTLTGLK 65
                           90
                   ....*....|....*
gi 2038291632  411 PYANYTFTIKSQNRV 425
Cdd:smart00060  66 PGTEYEFRVRAVNGA 80
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
453-525 7.43e-07

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 47.99  E-value: 7.43e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2038291632  453 LRLVKKEPRQLELAWagSRPRTPGGN---LSYELHVLNQDEEWHQM---VLEPRVLLTKLQPDTTYIVRVRTMTPLGPG 525
Cdd:smart00060   7 LRVTDVTSTSVTLSW--EPPPDDGITgyiVGYRVEYREEGSEWKEVnvtPSSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
fn3 pfam00041
Fibronectin type III domain;
460-528 8.64e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 47.79  E-value: 8.64e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2038291632 460 PRQLELAWagSRPRTPGGNL-SYELHVLNQDEE--WHQMVL---EPRVLLTKLQPDTTYIVRVRTMTPLGPGPFS 528
Cdd:pfam00041  13 STSLTVSW--TPPPDGNGPItGYEVEYRPKNSGepWNEITVpgtTTSVTLTGLKPGTEYEVRVQAVNGGGEGPPS 85
 
Name Accession Description Interval E-value
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
619-884 1.78e-156

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: 461.46  E-value: 1.78e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 619 LDPTWLIVDTVIGEGEFGEVYRGALRFPSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPI 698
Cdd:cd05033     1 IDASYVTIEKVIGGGEFGEVCSGSLKLPGKKEIDVAIKTLKSGYSDKQRLDFLTEASIMGQFDHPNVIRLEGVVTKSRPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 699 MIVTEFMENGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFD 778
Cdd:cd05033    81 MIVTEYMENGSLDKFLRENDGKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDFGLSRRLEDSE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 779 GTYETQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLYEL 858
Cdd:cd05033   161 ATYTTKGGKIPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSYGERPYWDMSNQDVIKAVEDGYRLPPPMDCPSALYQL 240
                         250       260
                  ....*....|....*....|....*.
gi 2038291632 859 MKNCWAYDRARRPHFLQLQAHLEQLL 884
Cdd:cd05033   241 MLDCWQKDRNERPTFSQIVSTLDKMI 266
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
624-880 3.13e-134

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: 403.42  E-value: 3.13e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 624 LIVDTVIGEGEFGEVYRGALRF-PSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVT 702
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKGeGENTKIKVAVKTLKEGADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 703 EFMENGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYE 782
Cdd:pfam07714  81 EYMPGGDLLDFLRKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDIYDDDYYRK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 783 TQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLYELMKNC 862
Cdd:pfam07714 161 RGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEFLEDGYRLPQPENCPDELYDLMKQC 240
                         250
                  ....*....|....*...
gi 2038291632 863 WAYDRARRPHFLQLQAHL 880
Cdd:pfam07714 241 WAYDPEDRPTFSELVEDL 258
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
618-884 7.89e-133

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: 400.50  E-value: 7.89e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 618 ELDPTWLIVDTVIGEGEFGEVYRGALRFPSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKP 697
Cdd:cd05063     1 EIHPSHITKQKVIGAGEFGEVFRGILKMPGRKEVAVAIKTLKPGYTEKQRQDFLSEASIMGQFSHHNIIRLEGVVTKFKP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 698 IMIVTEFMENGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDF 777
Cdd:cd05063    81 AMIITEYMENGALDKYLRDHDGEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSRVLEDD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 778 -DGTYETQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLY 856
Cdd:cd05063   161 pEGTYTTSGGKIPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSFGERPYWDMSNHEVMKAINDGFRLPAPMDCPSAVY 240
                         250       260
                  ....*....|....*....|....*...
gi 2038291632 857 ELMKNCWAYDRARRPHFLQLQAHLEQLL 884
Cdd:cd05063   241 QLMLQCWQQDRARRPRFVDIVNLLDKLL 268
EphR_LBD_A1 cd10479
Ligand Binding Domain of Ephrin type-A Receptor 1; Ephrin receptors (EphRs) comprise the ...
27-203 1.32e-131

Ligand Binding Domain of Ephrin type-A Receptor 1; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (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. EphA1 is downregulated in some advanced colorectal and myeloid cancers and upregulated in neuroblasoma and glioblastoma. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine 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.


Pssm-ID: 198447  Cd Length: 177  Bit Score: 393.63  E-value: 1.32e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632  27 EVTLMDTSKAQGELGWLLDPPEDGWSEVQQMLNGTPLYMYQDCPVEESGDTNHWLRSNWIYRGEEASRVHVELQFTVRDC 106
Cdd:cd10479     1 EVTLMDTSTAQGELGWLLDPPEVGWSEVQQMLNGTPLYMYQDCPVQSEGDTDHWLRSNWIYRGEEASRIYVELQFTVRDC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 107 KSFPGGAGPMGCKETFNLLYMESDQDVGIQLRRPLFQKVTTVAADQSFTIRDLASGAVKLNVERCSLGRLTHRGLYLAFH 186
Cdd:cd10479    81 KSFPGGAGPLGCKETFNLYYMESDQDVGIQLRRPLFQKVTTVAADQSFTIRDLASGSVKLNVERCSLGKLTRRGLYLAFH 160
                         170
                  ....*....|....*..
gi 2038291632 187 NPGSCVALVSVRVFYQR 203
Cdd:cd10479   161 NPGACVALVSVRVFYQR 177
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
619-884 2.71e-131

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: 396.54  E-value: 2.71e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 619 LDPTWLIVDTVIGEGEFGEVYRGALRFPSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPI 698
Cdd:cd05066     1 IDASCIKIEKVIGAGEFGEVCSGRLKLPGKREIPVAIKTLKAGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTRSKPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 699 MIVTEFMENGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLL-DDF 777
Cdd:cd05066    81 MIVTEYMENGSLDAFLRKHDGQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSRVLeDDP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 778 DGTYETQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLYE 857
Cdd:cd05066   161 EAAYTTRGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWEMSNQDVIKAIEEGYRLPAPMDCPAALHQ 240
                         250       260
                  ....*....|....*....|....*..
gi 2038291632 858 LMKNCWAYDRARRPHFLQLQAHLEQLL 884
Cdd:cd05066   241 LMLDCWQKDRNERPKFEQIVSILDKLI 267
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
619-884 2.02e-129

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: 391.54  E-value: 2.02e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 619 LDPTWLIVDTVIGEGEFGEVYRGALRFPSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPI 698
Cdd:cd05065     1 IDVSCVKIEEVIGAGEFGEVCRGRLKLPGKREIFVAIKTLKSGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTKSRPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 699 MIVTEFMENGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDD-- 776
Cdd:cd05065    81 MIITEFMENGALDSFLRQNDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRFLEDdt 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 777 FDGTYETQ-GGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPL 855
Cdd:cd05065   161 SDPTYTSSlGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVINAIEQDYRLPPPMDCPTAL 240
                         250       260
                  ....*....|....*....|....*....
gi 2038291632 856 YELMKNCWAYDRARRPHFLQLQAHLEQLL 884
Cdd:cd05065   241 HQLMLDCWQKDRNLRPKFGQIVNTLDKMI 269
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
624-880 1.79e-128

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 388.43  E-value: 1.79e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632  624 LIVDTVIGEGEFGEVYRGALRFPSQDCK-TVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVT 702
Cdd:smart00219   1 LTLGKKLGEGAFGEVYKGKLKGKGGKKKvEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYIVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632  703 EFMENGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDfDGTYE 782
Cdd:smart00219  81 EYMEGGDLLSYLRKNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYD-DDYYR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632  783 TQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLYELMKNC 862
Cdd:smart00219 160 KRGGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEYLKNGYRLPQPPNCPPELYDLMLQC 239
                          250
                   ....*....|....*...
gi 2038291632  863 WAYDRARRPHFLQLQAHL 880
Cdd:smart00219 240 WAEDPEDRPTFSELVEIL 257
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
624-880 8.75e-127

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: 384.21  E-value: 8.75e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632  624 LIVDTVIGEGEFGEVYRGALRFPSQDCK-TVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVT 702
Cdd:smart00221   1 LTLGKKLGEGAFGEVYKGTLKGKGDGKEvEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632  703 EFMENGALDAFLKEREDQ-LAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDfDGTY 781
Cdd:smart00221  81 EYMPGGDLLDYLRKNRPKeLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYD-DDYY 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632  782 ETQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLYELMKN 861
Cdd:smart00221 160 KVKGGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEEPYPGMSNAEVLEYLKKGYRLPKPPNCPPELYKLMLQ 239
                          250
                   ....*....|....*....
gi 2038291632  862 CWAYDRARRPHFLQLQAHL 880
Cdd:smart00221 240 CWAEDPEDRPTFSELVEIL 258
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
629-881 7.20e-123

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: 374.18  E-value: 7.20e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRFPSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENG 708
Cdd:cd00192     2 KLGEGAFGEVYKGKLKGGDGKTVDVAVKTLKEDASESERKDFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYMEGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 ALDAFLKER--------EDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGT 780
Cdd:cd00192    82 DLLDFLRKSrpvfpspePSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLSRDIYDDDYY 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 781 YETQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLYELMK 860
Cdd:cd00192   162 RKKTGGKLPIRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTLGATPYPGLSNEEVLEYLRKGYRLPKPENCPDELYELML 241
                         250       260
                  ....*....|....*....|.
gi 2038291632 861 NCWAYDRARRPHFLQLQAHLE 881
Cdd:cd00192   242 SCWQLDPEDRPTFSELVERLE 262
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
618-884 9.13e-105

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: 326.88  E-value: 9.13e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 618 ELDPTWLIVDTVIGEGEFGEVYRGALRFPSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKP 697
Cdd:cd05064     1 ELDNKSIKIERILGTGRFGELCRGCLKLPSKRELPVAIHTLRAGCSDKQRRGFLAEALTLGQFDHSNIVRLEGVITRGNT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 698 IMIVTEFMENGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGltRLLDD- 776
Cdd:cd05064    81 MMIVTEYMSNGALDSFLRKHEGQLVAGQLMGMLPGLASGMKYLSEMGYVHKGLAAHKVLVNSDLVCKISGFR--RLQEDk 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 777 FDGTYETQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLY 856
Cdd:cd05064   159 SEAIYTTMSGKSPVLWAAPEAIQYHHFSSASDVWSFGIVMWEVMSYGERPYWDMSGQDVIKAVEDGFRLPAPRNCPNLLH 238
                         250       260
                  ....*....|....*....|....*...
gi 2038291632 857 ELMKNCWAYDRARRPHFLQLQAHLEQLL 884
Cdd:cd05064   239 QLMLDCWQKERGERPRFSQIHSILSKMV 266
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
630-881 5.06e-98

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: 308.44  E-value: 5.06e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFPSQdcktVAIKTLK--DTSPDgqwwNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMEN 707
Cdd:cd05034     3 LGAGQFGEVWMGVWNGTTK----VAVKTLKpgTMSPE----AFLQEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTELMSK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GALDAFLKEREDQ-LAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDfdGTYET-QG 785
Cdd:cd05034    75 GSLLDYLRTGEGRaLRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNVCKVADFGLARLIED--DEYTArEG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 786 GKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLYELMKNCWAY 865
Cdd:cd05034   153 AKFPIKWTAPEAALYGRFTIKSDVWSFGILLYEIVTYGRVPYPGMTNREVLEQVERGYRMPKPPGCPDELYDIMLQCWKK 232
                         250
                  ....*....|....*.
gi 2038291632 866 DRARRPHFLQLQAHLE 881
Cdd:cd05034   233 EPEERPTFEYLQSFLE 248
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
630-880 1.11e-93

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: 297.05  E-value: 1.11e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRfpSQDCKtVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGA 709
Cdd:cd05041     3 IGRGNFGDVYRGVLK--PDNTE-VAVKTCRETLPPDLKRKFLQEARILKQYDHPNIVKLIGVCVQKQPIMIVMELVPGGS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 710 LDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRllDDFDGTYETQGG--K 787
Cdd:cd05041    80 LLTFLRKKGARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSR--EEEDGEYTVSDGlkQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 788 IPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLYELMKNCWAYDR 867
Cdd:cd05041   158 IPIKWTAPEALNYGRYTSESDVWSFGILLWEIFSLGATPYPGMSNQQTREQIESGYRMPAPELCPEAVYRLMLQCWAYDP 237
                         250
                  ....*....|...
gi 2038291632 868 ARRPHFLQLQAHL 880
Cdd:cd05041   238 ENRPSFSEIYNEL 250
EphR_LBD_A cd10473
Ligand Binding Domain of Ephrin type-A Receptors; Ephrin receptors (EphRs) comprise the ...
27-203 1.42e-93

Ligand Binding Domain of Ephrin type-A Receptors; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (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 a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine 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.


Pssm-ID: 198441  Cd Length: 173  Bit Score: 293.58  E-value: 1.42e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632  27 EVTLMDTSKAQGELGWLLDPPEdGWSEVQQMLNG-TPLYMYQDCPVEEsGDTNHWLRSNWIYRGEeASRVHVELQFTVRD 105
Cdd:cd10473     1 EVVLLDSKTAQGELGWITYPPN-GWEEISEMDEDyTPIRTYQVCNVME-PNQNNWLRTNWIYRGE-AQRIYIELKFTLRD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 106 CKSFPGGAGpmGCKETFNLLYMESDQDVGIQLRRPLFQKVTTVAADQSFTIRDLASGAVKLNVERCSLGRLTHRGLYLAF 185
Cdd:cd10473    78 CNSFPGVLG--TCKETFNLYYMESDLDLGRNIRENQFTKIDTIAADESFTQGDLGDRIMKLNTEVREVGPLTKKGFYLAF 155
                         170
                  ....*....|....*...
gi 2038291632 186 HNPGSCVALVSVRVFYQR 203
Cdd:cd10473   156 QDVGACVALVSVRVYYKK 173
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
630-883 1.38e-91

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: 291.56  E-value: 1.38e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRfpsqdCKTVAIKTLKDTSPDGQwwNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGA 709
Cdd:cd05039    14 IGKGEFGDVMLGDYR-----GQKVAVKCLKDDSTAAQ--AFLAEASVMTTLRHPNLVQLLGVVLEGNGLYIVTEYMAKGS 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 710 LDAFLKEREDQLAPG-QLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRllddfDGTYETQGGKI 788
Cdd:cd05039    87 LVDYLRSRGRAVITRkDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAK-----EASSNQDGGKL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 789 PIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLYELMKNCWAYDRA 868
Cdd:cd05039   162 PIKWTAPEALREKKFSTKSDVWSFGILLWEIYSFGRVPYPRIPLKDVVPHVEKGYRMEAPEGCPPEVYKVMKNCWELDPA 241
                         250
                  ....*....|....*
gi 2038291632 869 RRPHFLQLQAHLEQL 883
Cdd:cd05039   242 KRPTFKQLREKLEHI 256
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
630-885 3.42e-90

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: 288.15  E-value: 3.42e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALrfpsQDCKTVAIKTLKDTSPDGQwwNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGA 709
Cdd:cd05068    16 LGSGQFGEVWEGLW----NNTTPVAVKTLKPGTMDPE--DFLREAQIMKKLRHPKLIQLYAVCTLEEPIYIITELMKHGS 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 710 LDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDgTYETQ-GGKI 788
Cdd:cd05068    90 LLEYLQGKGRSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVGENNICKVADFGLARVIKVED-EYEAReGAKF 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 789 PIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLYELMKNCWAYDRA 868
Cdd:cd05068   169 PIKWTAPEAANYNRFSIKSDVWSFGILLTEIVTYGRIPYPGMTNAEVLQQVERGYRMPCPPNCPPQLYDIMLECWKADPM 248
                         250
                  ....*....|....*..
gi 2038291632 869 RRPHFLQLQAHLEQLLT 885
Cdd:cd05068   249 ERPTFETLQWKLEDFFV 265
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
630-876 8.09e-88

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: 281.55  E-value: 8.09e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFPSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVvTKRKPIMIVTEFMENGA 709
Cdd:cd05060     3 LGHGNFGSVRKGVYLMKSGKEVEVAVKTLKQEHEKAGKKEFLREASVMAQLDHPCIVRLIGV-CKGEPLMLVMELAPLGP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 710 LDAFLKEREDqLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNIL-VNQNLCcKVSDFGLTRLLDdFDGTY--ETQGG 786
Cdd:cd05060    82 LLKYLKKRRE-IPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLlVNRHQA-KISDFGMSRALG-AGSDYyrATTAG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 787 KIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLYELMKNCWAYD 866
Cdd:cd05060   159 RWPLKWYAPECINYGKFSSKSDVWSYGVTLWEAFSYGAKPYGEMKGPEVIAMLESGERLPRPEECPQEIYSIMLSCWKYR 238
                         250
                  ....*....|
gi 2038291632 867 RARRPHFLQL 876
Cdd:cd05060   239 PEDRPTFSEL 248
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
618-881 1.36e-85

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: 276.53  E-value: 1.36e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 618 ELDPTWLIVDTVIGEGEFGEVYRG-ALRFPSQDCKT-VAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKR 695
Cdd:cd05032     2 ELPREKITLIRELGQGSFGMVYEGlAKGVVKGEPETrVAIKTVNENASMRERIEFLNEASVMKEFNCHHVVRLLGVVSTG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 696 KPIMIVTEFMENGALDAFLKER--EDQLAPG-------QLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVS 766
Cdd:cd05032    82 QPTLVVMELMAKGDLKSYLRSRrpEAENNPGlgpptlqKFIQMAAEIADGMAYLAAKKFVHRDLAARNCMVAEDLTVKIG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 767 DFGLTRLLDDFDgtYETQGGK--IPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYR 844
Cdd:cd05032   162 DFGMTRDIYETD--YYRKGGKglLPVRWMAPESLKDGVFTTKSDVWSFGVVLWEMATLAEQPYQGLSNEEVLKFVIDGGH 239
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2038291632 845 LPPPVDCPAPLYELMKNCWAYDRARRPHFLQLQAHLE 881
Cdd:cd05032   240 LDLPENCPDKLLELMRMCWQYNPKMRPTFLEIVSSLK 276
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
618-884 3.12e-85

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: 275.07  E-value: 3.12e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 618 ELDPTWLIVDTVIGEGEFGEVYRGALRFPSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKrKP 697
Cdd:cd05056     2 EIQREDITLGRCIGEGQFGDVYQGVYMSPENEKIAVAVKTCKNCTSPSVREKFLQEAYIMRQFDHPHIVKLIGVITE-NP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 698 IMIVTEFMENGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDf 777
Cdd:cd05056    81 VWIVMELAPLGELRSYLQVNKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLSRYMED- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 778 DGTYETQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLYE 857
Cdd:cd05056   160 ESYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMLGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYS 239
                         250       260
                  ....*....|....*....|....*..
gi 2038291632 858 LMKNCWAYDRARRPHFLQLQAHLEQLL 884
Cdd:cd05056   240 LMTKCWAYDPSKRPRFTELKAQLSDIL 266
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
611-880 4.94e-83

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: 269.63  E-value: 4.94e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 611 GALDFAQELdptwlivdtviGEGEFGEVYRGALRFPSQD--CKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRL 688
Cdd:cd05048     5 SAVRFLEEL-----------GEGAFGKVYKGELLGPSSEesAISVAIKTLKENASPKTQQDFRREAELMSDLQHPNIVCL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 689 EGVVTKRKPIMIVTEFMENGALDAFLKER---------------EDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAAR 753
Cdd:cd05048    74 LGVCTKEQPQCMLFEYMAHGDLHEFLVRHsphsdvgvssdddgtASSLDQSDFLHIAIQIAAGMEYLSSHHYVHRDLAAR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 754 NILVNQNLCCKVSDFGLTRllDDFDGTYETQGGK--IPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMN 831
Cdd:cd05048   154 NCLVGDGLTVKISDFGLSR--DIYSSDYYRVQSKslLPVRWMPPEAILYGKFTTESDVWSFGVVLWEIFSYGLQPYYGYS 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2038291632 832 NQEVMKSIEEGYRLPPPVDCPAPLYELMKNCWAYDRARRPHFLQLQAHL 880
Cdd:cd05048   232 NQEVIEMIRSRQLLPCPEDCPARVYSLMVECWHEIPSRRPRFKEIHTRL 280
EPH_lbd smart00615
Ephrin receptor ligand binding domain;
27-203 7.59e-82

Ephrin receptor ligand binding domain;


Pssm-ID: 128877  Cd Length: 177  Bit Score: 262.22  E-value: 7.59e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632   27 EVTLMDTSKAQGELGWLLDPPEdGWSEVQQM-LNGTPLYMYQDCPVEEsGDTNHWLRSNWIYRGEeASRVHVELQFTVRD 105
Cdd:smart00615   1 EVVLLDTKTETGELGWTTYPPE-GWEEVSGMdENGTPIRTYQVCNVQE-GNQNNWLRTNFIRRRG-AQRIYVELKFTVRD 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632  106 CKSFPGGAGPmgCKETFNLLYMESDQDVGIQ----LRRPLFQKVTTVAADQSFTIRDLASGAVKLNVERCSLGRLTHRGL 181
Cdd:smart00615  78 CSSLPGVGGS--CKETFNLYYYESDTDTATNtlpnWMENPYTKVDTIAADESFTGGDVGKRNVKLNTEVRSLGPLSKKGF 155
                          170       180
                   ....*....|....*....|..
gi 2038291632  182 YLAFHNPGSCVALVSVRVFYQR 203
Cdd:smart00615 156 YLAFQDQGACVALVSVRVFYKK 177
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
619-884 3.27e-79

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: 258.53  E-value: 3.27e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 619 LDPTWLIVDTVIGEGEFGEVYRGALRFPSQdcktVAIKTLKDTSPDGQwwNFLREATIMGQFNHPHILRLEGVVTKRKPI 698
Cdd:cd05059     1 IDPSELTFLKELGSGQFGVVHLGKWRGKID----VAIKMIKEGSMSED--DFIEEAKVMMKLSHPKLVQLYGVCTKQRPI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 699 MIVTEFMENGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDfD 778
Cdd:cd05059    75 FIVTEYMANGCLLNYLRERRGKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLARYVLD-D 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 779 GTYETQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLYEL 858
Cdd:cd05059   154 EYTSSVGTKFPVKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSEGKMPYERFSNSEVVEHISQGYRLYRPHLAPTEVYTI 233
                         250       260
                  ....*....|....*....|....*.
gi 2038291632 859 MKNCWAYDRARRPHFLQLqahLEQLL 884
Cdd:cd05059   234 MYSCWHEKPEERPTFKIL---LSQLT 256
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
630-885 5.17e-79

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: 258.28  E-value: 5.17e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFPSQdcktVAIKTLKD--TSPDGqwwnFLREATIMGQFNHPHILRLEGVVTKrKPIMIVTEFMEN 707
Cdd:cd05067    15 LGAGQFGEVWMGYYNGHTK----VAIKSLKQgsMSPDA----FLAEANLMKQLQHQRLVRLYAVVTQ-EPIYIITEYMEN 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GALDAFLKERED-QLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYEtQGG 786
Cdd:cd05067    86 GSLVDFLKTPSGiKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARLIEDNEYTAR-EGA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 787 KIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLYELMKNCWAYD 866
Cdd:cd05067   165 KFPIKWTAPEAINYGTFTIKSDVWSFGILLTEIVTHGRIPYPGMTNPEVIQNLERGYRMPRPDNCPEELYQLMRLCWKER 244
                         250
                  ....*....|....*....
gi 2038291632 867 RARRPHFLQLQAHLEQLLT 885
Cdd:cd05067   245 PEDRPTFEYLRSVLEDFFT 263
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
629-887 2.08e-78

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: 256.96  E-value: 2.08e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRFPSQDCKT-VAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGV-VTKRkpIMIVTEFME 706
Cdd:cd05057    14 VLGSGAFGTVYKGVWIPEGEKVKIpVAIKVLREETGPKANEEILDEAYVMASVDHPHLVRLLGIcLSSQ--VQLITQLMP 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 707 NGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYETQGG 786
Cdd:cd05057    92 LGCLLDYVRNHRDNIGSQLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFGLAKLLDVDEKEYHAEGG 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 787 KIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLYELMKNCWAYD 866
Cdd:cd05057   172 KVPIKWMALESIQYRIYTHKSDVWSYGVTVWELMTFGAKPYEGIPAVEIPDLLEKGERLPQPPICTIDVYMVLVKCWMID 251
                         250       260
                  ....*....|....*....|.
gi 2038291632 867 RARRPHFLQLQAHLEQLLTDP 887
Cdd:cd05057   252 AESRPTFKELANEFSKMARDP 272
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
630-880 5.68e-78

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: 255.05  E-value: 5.68e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFPSQdcktVAIKTLKDTSPDGQWwNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGA 709
Cdd:cd05148    14 LGSGYFGEVWEGLWKNRVR----VAIKILKSDDLLKQQ-DFQKEVQALKRLRHKHLISLFAVCSVGEPVYIITELMEKGS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 710 LDAFLKEREDQ-LAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLL-DDFdgtYETQGGK 787
Cdd:cd05148    89 LLAFLRSPEGQvLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLARLIkEDV---YLSSDKK 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 788 IPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLYELMKNCWAYDR 867
Cdd:cd05148   166 IPYKWTAPEAASHGTFSTKSDVWSFGILLYEMFTYGQVPYPGMNNHEVYDQITAGYRMPCPAKCPQEIYKIMLECWAAEP 245
                         250
                  ....*....|...
gi 2038291632 868 ARRPHFLQLQAHL 880
Cdd:cd05148   246 EDRPSFKALREEL 258
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
630-880 7.40e-78

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: 254.38  E-value: 7.40e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRfpSQDcktVAIKTLKDTSPDGQWWN-FLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENG 708
Cdd:cd13999     1 IGSGSFGEVYKGKWR--GTD---VAIKKLKVEDDNDELLKeFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 ALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFD-------GTY 781
Cdd:cd13999    76 SLYDLLHKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTTekmtgvvGTP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 782 etqggkipiRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNN-QEVMKSIEEGYRLPPPVDCPAPLYELMK 860
Cdd:cd13999   156 ---------RWMAPEVLRGEPYTEKADVYSFGIVLWELLT-GEVPFKELSPiQIAAAVVQKGLRPPIPPDCPPELSKLIK 225
                         250       260
                  ....*....|....*....|
gi 2038291632 861 NCWAYDRARRPHFLQLQAHL 880
Cdd:cd13999   226 RCWNEDPEKRPSFSEIVKRL 245
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
630-880 8.42e-78

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: 254.47  E-value: 8.42e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRfpsQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGA 709
Cdd:cd05084     4 IGRGNFGEVFSGRLR---ADNTPVAVKSCRETLPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 710 LDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRllDDFDGTYETQGG--K 787
Cdd:cd05084    81 FLTFLRTEGPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSR--EEEDGVYAATGGmkQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 788 IPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLYELMKNCWAYDR 867
Cdd:cd05084   159 IPVKWTAPEALNYGRYSSESDVWSFGILLWETFSLGAVPYANLSNQQTREAVEQGVRLPCPENCPDEVYRLMEQCWEYDP 238
                         250
                  ....*....|...
gi 2038291632 868 ARRPHFLQLQAHL 880
Cdd:cd05084   239 RKRPSFSTVHQDL 251
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
629-880 1.33e-77

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: 253.77  E-value: 1.33e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRfpsqDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENG 708
Cdd:cd05085     3 LLGKGNFGEVYKGTLK----DKTPVAVKTCKEDLPQELKIKFLSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVPGG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 ALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDdfDGTYETQGGK- 787
Cdd:cd05085    79 DFLSFLRKKKDELKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSRQED--DGVYSSSGLKq 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 788 IPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLYELMKNCWAYDR 867
Cdd:cd05085   157 IPIKWTAPEALNYGRYSSESDVWSFGILLWETFSLGVCPYPGMTNQQAREQVEKGYRMSAPQRCPEDIYKIMQRCWDYNP 236
                         250
                  ....*....|...
gi 2038291632 868 ARRPHFLQLQAHL 880
Cdd:cd05085   237 ENRPKFSELQKEL 249
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
630-881 4.55e-77

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: 253.11  E-value: 4.55e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALR---FPSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFME 706
Cdd:cd05044     3 LGSGAFGEVFEGTAKdilGDGSGETKVAVKTLRKGATDQEKAEFLKEAHLMSNFKHPNILKLLGVCLDNDPQYIILELME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 707 NGALDAFLKEREDQLAPG------QLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCC----KVSDFGLTRLLDD 776
Cdd:cd05044    83 GGDLLSYLRAARPTAFTPplltlkDLLSICVDVAKGCVYLEDMHFVHRDLAARNCLVSSKDYRervvKIGDFGLARDIYK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 777 FDgTYETQG-GKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPL 855
Cdd:cd05044   163 ND-YYRKEGeGLLPVRWMAPESLVDGVFTTQSDVWAFGVLMWEILTLGQQPYPARNNLEVLHFVRAGGRLDQPDNCPDDL 241
                         250       260
                  ....*....|....*....|....*.
gi 2038291632 856 YELMKNCWAYDRARRPHFLQLQAHLE 881
Cdd:cd05044   242 YELMLRCWSTDPEERPSFARILEQLQ 267
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
630-881 3.88e-76

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: 249.83  E-value: 3.88e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFPSQdcktVAIKTLK--DTSPDGqwwnFLREATIMGQFNHPHILRLEGVVTKrKPIMIVTEFMEN 707
Cdd:cd14203     3 LGQGCFGEVWMGTWNGTTK----VAIKTLKpgTMSPEA----FLEEAQIMKKLRHDKLVQLYAVVSE-EPIYIVTEFMSK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GALDAFLKEREDQ-LAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTyETQGG 786
Cdd:cd14203    74 GSLLDFLKDGEGKyLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYT-ARQGA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 787 KIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLYELMKNCWAYD 866
Cdd:cd14203   153 KFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPPGCPESLHELMCQCWRKD 232
                         250
                  ....*....|....*
gi 2038291632 867 RARRPHFLQLQAHLE 881
Cdd:cd14203   233 PEERPTFEYLQSFLE 247
Ephrin_lbd pfam01404
Ephrin receptor ligand binding domain; The Eph receptors, which bind to ephrins pfam00812 are ...
28-204 1.24e-74

Ephrin receptor ligand binding domain; The Eph receptors, which bind to ephrins pfam00812 are a large family of receptor tyrosine kinases. This family represents the amino terminal domain which binds the ephrin ligand.


Pssm-ID: 460198  Cd Length: 177  Bit Score: 242.96  E-value: 1.24e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632  28 VTLMDTSKAQGELGWLLDPPEDGWSEVQQM-LNGTPLYMYQDCPVEEsGDTNHWLRSNWIYRGEeASRVHVELQFTVRDC 106
Cdd:pfam01404   1 EVLLDTTSATSDLGWTTYPYDGGWEEVSGLdENGRTIRTYQVCNVEE-PNQNNWLRTPFIPRGG-ASRVYVELKFTVRDC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 107 KSFPGGAGPmgCKETFNLLYMESDQDVGI----QLRRPLFQKVTTVAADQSFTIRDlASGAVKLNVERCSLGRLTHRGLY 182
Cdd:pfam01404  79 SSIPGVSGT--CKETFNLYYYESDADAATatppAWRENPYKKIDTIAADESFTDTG-KGRVMKLNTETRSIGPLSKRGFY 155
                         170       180
                  ....*....|....*....|..
gi 2038291632 183 LAFHNPGSCVALVSVRVFYQRC 204
Cdd:pfam01404 156 LAFQDQGACIALLSVRVFYKKC 177
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
630-885 4.68e-74

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: 244.95  E-value: 4.68e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGalrFPSQDCKtVAIKTLKDTSPDGQwwNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGA 709
Cdd:cd05072    15 LGAGQFGEVWMG---YYNNSTK-VAVKTLKPGTMSVQ--AFLEEANLMKTLQHDKLVRLYAVVTKEEPIYIITEYMAKGS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 710 LDAFLKERE-DQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYEtQGGKI 788
Cdd:cd05072    89 LLDFLKSDEgGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIEDNEYTAR-EGAKF 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 789 PIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLYELMKNCWAYDRA 868
Cdd:cd05072   168 PIKWTAPEAINFGSFTIKSDVWSFGILLYEIVTYGKIPYPGMSNSDVMSALQRGYRMPRMENCPDELYDIMKTCWKEKAE 247
                         250
                  ....*....|....*..
gi 2038291632 869 RRPHFLQLQAHLEQLLT 885
Cdd:cd05072   248 ERPTFDYLQSVLDDFYT 264
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
629-870 4.05e-73

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: 242.76  E-value: 4.05e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALR--FPSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFME 706
Cdd:cd05049    12 ELGEGAFGKVFLGECYnlEPEQDKMLVAVKTLKDASSPDARKDFEREAELLTNLQHENIVKFYGVCTEGDPLLMVFEYME 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 707 NGALDAFLK-------------EREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRl 773
Cdd:cd05049    92 HGDLNKFLRshgpdaaflasedSAPGELTLSQLLHIAVQIASGMVYLASQHFVHRDLATRNCLVGTNLVVKIGDFGMSR- 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 774 lDDFDGTYETQGGK--IPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDC 851
Cdd:cd05049   171 -DIYSTDYYRVGGHtmLPIRWMPPESILYRKFTTESDVWSFGVVLWEIFTYGKQPWFQLSNTEVIECITQGRLLQRPRTC 249
                         250
                  ....*....|....*....
gi 2038291632 852 PAPLYELMKNCWAYDRARR 870
Cdd:cd05049   250 PSEVYAVMLGCWKREPQQR 268
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
629-882 8.99e-73

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: 242.24  E-value: 8.99e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEV----------YRGALRFPSQD---CKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKR 695
Cdd:cd05051    12 KLGEGQFGEVhlceanglsdLTSDDFIGNDNkdePVLVAVKMLRPDASKNAREDFLKEVKIMSQLKDPNIVRLLGVCTRD 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 696 KPIMIVTEFMENGALDAFLKERED-----------QLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCK 764
Cdd:cd05051    92 EPLCMIVEYMENGDLNQFLQKHEAetqgasatnskTLSYGTLLYMATQIASGMKYLESLNFVHRDLATRNCLVGPNYTIK 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 765 VSDFGLTRLLDDFDgTYETQGGKI-PIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFG-DKPYGEMNNQEVMKSIEEG 842
Cdd:cd05051   172 IADFGMSRNLYSGD-YYRIEGRAVlPIRWMAWESILLGKFTTKSDVWAFGVTLWEILTLCkEQPYEHLTDEQVIENAGEF 250
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2038291632 843 YR-------LPPPVDCPAPLYELMKNCWAYDRARRPHFLQLQAHLEQ 882
Cdd:cd05051   251 FRddgmevyLSRPPNCPKEIYELMLECWRRDEEDRPTFREIHLFLQR 297
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
618-883 1.02e-72

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: 241.17  E-value: 1.02e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 618 ELDPTWLIVDTVIGEGEFGEVYRGALRfpsQDCKTVAIKTLK-DTSPDGQwwnFLREATIMGQFNHPHILRLEGVVTKRK 696
Cdd:cd05052     2 EIERTDITMKHKLGGGQYGEVYEGVWK---KYNLTVAVKTLKeDTMEVEE---FLKEAAVMKEIKHPNLVQLLGVCTREP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 697 PIMIVTEFMENGALDAFLKER-EDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLD 775
Cdd:cd05052    76 PFYIITEFMPYGNLLDYLRECnREELNAVVLLYMATQIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 776 DfdGTYETQ-GGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAP 854
Cdd:cd05052   156 G--DTYTAHaGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEKGYRMERPEGCPPK 233
                         250       260
                  ....*....|....*....|....*....
gi 2038291632 855 LYELMKNCWAYDRARRPHFLQLQAHLEQL 883
Cdd:cd05052   234 VYELMRACWQWNPSDRPSFAEIHQALETM 262
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
630-880 2.43e-71

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: 236.86  E-value: 2.43e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFPSQDCKTVAIKTLKDTSP--DGQWWNFLREATIMGQFNHPHILRLEGVVTKrKPIMIVTEFMEN 707
Cdd:cd05040     3 LGDGSFGVVRRGEWTTPSGKVIQVAVKCLKSDVLsqPNAMDDFLKEVNAMHSLDHPNLIRLYGVVLS-SPLMMVTELAPL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYETQGG- 786
Cdd:cd05040    82 GSLLDRLRKDQGHFLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGDFGLMRALPQNEDHYVMQEHr 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 787 KIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIE-EGYRLPPPVDCPAPLYELMKNCWAY 865
Cdd:cd05040   162 KVPFAWCAPESLKTRKFSHASDVWMFGVTLWEMFTYGEEPWLGLNGSQILEKIDkEGERLERPDDCPQDIYNVMLQCWAH 241
                         250
                  ....*....|....*
gi 2038291632 866 DRARRPHFLQLQAHL 880
Cdd:cd05040   242 KPADRPTFVALRDFL 256
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
624-877 4.26e-69

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: 231.37  E-value: 4.26e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 624 LIVDTVIGEGEFGEVYRGALRFPSQDCKtVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVtKRKPIMIVTE 703
Cdd:cd05115     6 LIDEVELGSGNFGCVKKGVYKMRKKQID-VAIKVLKQGNEKAVRDEMMREAQIMHQLDNPYIVRMIGVC-EAEALMLVME 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 704 FMENGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNIL-VNQNLCcKVSDFGLTRLLDDFDGTYE 782
Cdd:cd05115    84 MASGGPLNKFLSGKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLlVNQHYA-KISDFGLSKALGADDSYYK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 783 TQ-GGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLYELMKN 861
Cdd:cd05115   163 ARsAGKWPLKWYAPECINFRKFSSRSDVWSYGVTMWEAFSYGQKPYKKMKGPEVMSFIEQGKRMDCPAECPPEMYALMSD 242
                         250
                  ....*....|....*.
gi 2038291632 862 CWAYDRARRPHFLQLQ 877
Cdd:cd05115   243 CWIYKWEDRPNFLTVE 258
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
630-884 6.08e-69

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: 231.50  E-value: 6.08e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFPS-QDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTK--RKPIMIVTEFME 706
Cdd:cd05038    12 LGEGHFGSVELCRYDPLGdNTGEQVAVKSLQPSGEEQHMSDFKREIEILRTLDHEYIVKYKGVCESpgRRSLRLIMEYLP 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 707 NGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLL-DDFDGTYETQG 785
Cdd:cd05038    92 SGSLRDYLQRHRDQIDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGLAKVLpEDKEYYYVKEP 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 786 GKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSI--------------EEGYRLPPPVDC 851
Cdd:cd05038   172 GESPIFWYAPECLRESRFSSASDVWSFGVTLYELFTYGDPSQSPPALFLRMIGIaqgqmivtrllellKSGERLPRPPSC 251
                         250       260       270
                  ....*....|....*....|....*....|...
gi 2038291632 852 PAPLYELMKNCWAYDRARRPHFLQLQAHLEQLL 884
Cdd:cd05038   252 PDEVYDLMKECWEYEPQDRPSFSDLILIIDRLR 284
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
630-881 6.99e-69

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: 231.12  E-value: 6.99e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFPSQDCKT--VAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMEN 707
Cdd:cd05036    14 LGQGAFGEVYEGTVSGMPGDPSPlqVAVKTLPELCSEQDEMDFLMEALIMSKFNHPNIVRCIGVCFQRLPRFILLELMAG 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GALDAFLKE------REDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILvnqnLCC-------KVSDFGLTRll 774
Cdd:cd05036    94 GDLKSFLREnrprpeQPSSLTMLDLLQLAQDVAKGCRYLEENHFIHRDIAARNCL----LTCkgpgrvaKIGDFGMAR-- 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 775 DDFDGTYETQGGK--IPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCP 852
Cdd:cd05036   168 DIYRADYYRKGGKamLPVKWMPPEAFLDGIFTSKTDVWSFGVLLWEIFSLGYMPYPGKSNQEVMEFVTSGGRMDPPKNCP 247
                         250       260
                  ....*....|....*....|....*....
gi 2038291632 853 APLYELMKNCWAYDRARRPHFLQLQAHLE 881
Cdd:cd05036   248 GPVYRIMTQCWQHIPEDRPNFSTILERLN 276
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
619-883 1.02e-68

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: 229.84  E-value: 1.02e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 619 LDPTWLIVDTVIGEGEFGEVYRGALrfpsQDCKTVAIKTLKDTSPDGQwwNFLREATIMGQFNHPHILRLEGVVTKRKPI 698
Cdd:cd05112     1 IDPSELTFVQEIGSGQFGLVHLGYW----LNKDKVAIKTIREGAMSEE--DFIEEAEVMMKLSHPKLVQLYGVCLEQAPI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 699 MIVTEFMENGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDfD 778
Cdd:cd05112    75 CLVFEFMEHGCLSDYLRTQRGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMTRFVLD-D 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 779 GTYETQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLYEL 858
Cdd:cd05112   154 QYTSSTGTKFPVKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSEGKIPYENRSNSEVVEDINAGFRLYKPRLASTHVYEI 233
                         250       260
                  ....*....|....*....|....*
gi 2038291632 859 MKNCWAYDRARRPHFLQLqahLEQL 883
Cdd:cd05112   234 MNHCWKERPEDRPSFSLL---LRQL 255
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
619-885 1.03e-68

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: 231.15  E-value: 1.03e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 619 LDPTW------LIVDTVIGEGEFGEVYRGALR----FPSQDCkTVAIKTLKDTSPDGQWWNFLREATIM---GQfnHPHI 685
Cdd:cd05053     3 LDPEWelprdrLTLGKPLGEGAFGQVVKAEAVgldnKPNEVV-TVAVKMLKDDATEKDLSDLVSEMEMMkmiGK--HKNI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 686 LRLEGVVTKRKPIMIVTEFMENGALDAFLKER---------------EDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDL 750
Cdd:cd05053    80 INLLGACTQDGPLYVVVEYASKGNLREFLRARrppgeeaspddprvpEEQLTQKDLVSFAYQVARGMEYLASKKCIHRDL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 751 AARNILVNQNLCCKVSDFGLTRLLDDFDGTYETQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEM 830
Cdd:cd05053   160 AARNVLVTEDNVMKIADFGLARDIHHIDYYRKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGI 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2038291632 831 NNQEVMKSIEEGYRLPPPVDCPAPLYELMKNCWAYDRARRPHFLQLQAHLEQLLT 885
Cdd:cd05053   240 PVEELFKLLKEGHRMEKPQNCTQELYMLMRDCWHEVPSQRPTFKQLVEDLDRILT 294
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
629-883 1.77e-68

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: 229.10  E-value: 1.77e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRfpsqdCKTVAIKTLKDtspDGQWWNFLREATIMGQFNHPHILRLEGVVTKRK-PIMIVTEFMEN 707
Cdd:cd05082    13 TIGKGEFGDVMLGDYR-----GNKVAVKCIKN---DATAQAFLAEASVMTQLRHSNLVQLLGVIVEEKgGLYIVTEYMAK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GALDAFLKEREDQLAPGQ-LVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRlldDFDGTYETqgG 786
Cdd:cd05082    85 GSLVDYLRSRGRSVLGGDcLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTK---EASSTQDT--G 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 787 KIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLYELMKNCWAYD 866
Cdd:cd05082   160 KLPVKWTAPEALREKKFSTKSDVWSFGILLWEIYSFGRVPYPRIPLKDVVPRVEKGYKMDAPDGCPPAVYDVMKNCWHLD 239
                         250
                  ....*....|....*..
gi 2038291632 867 RARRPHFLQLQAHLEQL 883
Cdd:cd05082   240 AAMRPSFLQLREQLEHI 256
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
624-885 3.04e-68

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: 229.18  E-value: 3.04e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 624 LIVDTVIGEGEFGEVYRGALRFPSQdcktVAIKTLK--DTSPDgqwwNFLREATIMGQFNHPHILRLEGVVTKRkPIMIV 701
Cdd:cd05070    11 LQLIKRLGNGQFGEVWMGTWNGNTK----VAIKTLKpgTMSPE----SFLEEAQIMKKLKHDKLVQLYAVVSEE-PIYIV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 702 TEFMENGALDAFLKEREDQ-LAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGT 780
Cdd:cd05070    82 TEYMSKGSLLDFLKDGEGRaLKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIEDNEYT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 781 YEtQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLYELMK 860
Cdd:cd05070   162 AR-QGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPQDCPISLHELMI 240
                         250       260
                  ....*....|....*....|....*
gi 2038291632 861 NCWAYDRARRPHFLQLQAHLEQLLT 885
Cdd:cd05070   241 HCWKKDPEERPTFEYLQGFLEDYFT 265
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
630-880 6.45e-68

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: 228.74  E-value: 6.45e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFPSQD-CKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENG 708
Cdd:cd05090    13 LGECAFGKIYKGHLYLPGMDhAQLVAIKTLKDYNNPQQWNEFQQEASLMTELHHPNIVCLLGVVTQEQPVCMLFEFMNQG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 ALDAFLKER-----------ED-----QLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTR 772
Cdd:cd05090    93 DLHEFLIMRsphsdvgcssdEDgtvksSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILVGEQLHVKISDLGLSR 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 773 LLDDFDGTYETQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCP 852
Cdd:cd05090   173 EIYSSDYYRVQNKSLLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQLLPCSEDCP 252
                         250       260
                  ....*....|....*....|....*...
gi 2038291632 853 APLYELMKNCWAYDRARRPHFLQLQAHL 880
Cdd:cd05090   253 PRMYSLMTECWQEIPSRRPRFKDIHARL 280
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
616-885 2.03e-67

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: 226.88  E-value: 2.03e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 616 AQELDPTWLIVDTVIGEGEFGEVYRGALRFPSQdcktVAIKTLK--DTSPDGqwwnFLREATIMGQFNHPHILRLEGVVT 693
Cdd:cd05071     3 AWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTR----VAIKTLKpgTMSPEA----FLQEAQVMKKLRHEKLVQLYAVVS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 694 KrKPIMIVTEFMENGALDAFLK-EREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTR 772
Cdd:cd05071    75 E-EPIYIVTEYMSKGSLLDFLKgEMGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLAR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 773 LLDDFDGTYEtQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCP 852
Cdd:cd05071   154 LIEDNEYTAR-QGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVERGYRMPCPPECP 232
                         250       260       270
                  ....*....|....*....|....*....|...
gi 2038291632 853 APLYELMKNCWAYDRARRPHFLQLQAHLEQLLT 885
Cdd:cd05071   233 ESLHDLMCQCWRKEPEERPTFEYLQAFLEDYFT 265
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
619-882 3.97e-67

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: 225.14  E-value: 3.97e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 619 LDPTWLIVDTVIGEGEFGEVYRGalRFPSQdckTVAIKTLKdtsPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKpI 698
Cdd:cd05083     3 LNLQKLTLGEIIGEGEFGAVLQG--EYMGQ---KVAVKNIK---CDVTAQAFLEETAVMTKLQHKNLVRLLGVILHNG-L 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 699 MIVTEFMENGALDAFLKEREDQLAP-GQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLlddf 777
Cdd:cd05083    74 YIVMELMSKGNLVNFLRSRGRALVPvIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFGLAKV---- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 778 dGTYETQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLYE 857
Cdd:cd05083   150 -GSMGVDNSRLPVKWTAPEALKNKKFSSKSDVWSYGVLLWEVFSYGRAPYPKMSVKEVKEAVEKGYRMEPPEGCPPDVYS 228
                         250       260
                  ....*....|....*....|....*
gi 2038291632 858 LMKNCWAYDRARRPHFLQLQAHLEQ 882
Cdd:cd05083   229 IMTSCWEAEPGKRPSFKKLREKLEK 253
EphR_LBD_A2 cd10480
Ligand Binding Domain of Ephrin type-A Receptor 2; EphRs comprise the largest subfamily of ...
27-204 6.01e-67

Ligand Binding Domain of Ephrin type-A Receptor 2; EphRs comprise the largest subfamily of receptor tyr kinases (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. EphA2 negatively regulates cell differentiation and has been shown to be 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 contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine 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.


Pssm-ID: 198448  Cd Length: 174  Bit Score: 221.64  E-value: 6.01e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632  27 EVTLMDTSKAQGELGWLLDPPEDGWSEVQQMLNGTPLYMYQDCPVeESGDTNHWLRSNWIYRGeEASRVHVELQFTVRDC 106
Cdd:cd10480     1 EVVLLDFAAAGGELGWLTHPYGKGWDLMQNVMNDSPIYMYSVCNV-MSGEQDNWLRTNWIYRS-EAERIFIELKFTVRDC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 107 KSFPGGAGpmGCKETFNLLYMESDQDVGIQLRRPLFQKVTTVAADQSFTIRDLASGAVKLNVERCSLGRLTHRGLYLAFH 186
Cdd:cd10480    79 NSFPGGAG--SCKETFNLYYAESDVDYGTNFQKRQFRKIDTIAPDEITVSSDFETRNVKLNVEERSVGPLTRKGFYLAFQ 156
                         170
                  ....*....|....*...
gi 2038291632 187 NPGSCVALVSVRVFYQRC 204
Cdd:cd10480   157 DIGACVALLSVRVYYKKC 174
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
616-881 8.11e-67

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: 224.91  E-value: 8.11e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 616 AQELDPTWLIVDTVIGEGEFGEVYRGALRFPSQdcktVAIKTLKDTSPDGQwwNFLREATIMGQFNHPHILRLEGVVTkR 695
Cdd:cd05073     5 AWEIPRESLKLEKKLGAGQFGEVWMATYNKHTK----VAVKTMKPGSMSVE--AFLAEANVMKTLQHDKLVKLHAVVT-K 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 696 KPIMIVTEFMENGALDAFLKEREDQLAP-GQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLL 774
Cdd:cd05073    78 EPIYIITEFMAKGSLLDFLKSDEGSKQPlPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARVI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 775 DDFDGTYEtQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAP 854
Cdd:cd05073   158 EDNEYTAR-EGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLMEIVTYGRIPYPGMSNPEVIRALERGYRMPRPENCPEE 236
                         250       260
                  ....*....|....*....|....*..
gi 2038291632 855 LYELMKNCWAYDRARRPHFLQLQAHLE 881
Cdd:cd05073   237 LYNIMMRCWKNRPEERPTFEYIQSVLD 263
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
619-884 4.80e-66

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: 223.66  E-value: 4.80e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 619 LDPTWLIVDTVIGEGEFGEVYRGALRFPSQDCKTVAIKTLK-DTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKR-- 695
Cdd:cd14204     4 IDRNLLSLGKVLGEGEFGSVMEGELQQPDGTNHKVAVKTMKlDNFSQREIEEFLSEAACMKDFNHPNVIRLLGVCLEVgs 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 696 ----KPiMIVTEFMENGALDAFL----KEREDQLAPGQ-LVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVS 766
Cdd:cd14204    84 qripKP-MVILPFMKYGDLHSFLlrsrLGSGPQHVPLQtLLKFMIDIALGMEYLSSRNFLHRDLAARNCMLRDDMTVCVA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 767 DFGLTRLLddFDGTYETQG--GKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYR 844
Cdd:cd14204   163 DFGLSKKI--YSGDYYRQGriAKMPVKWIAVESLADRVYTVKSDVWAFGVTMWEIATRGMTPYPGVQNHEIYDYLLHGHR 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2038291632 845 LPPPVDCPAPLYELMKNCWAYDRARRPHFLQLQAHLEQLL 884
Cdd:cd14204   241 LKQPEDCLDELYDIMYSCWRSDPTDRPTFTQLRENLEKLL 280
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
616-885 7.77e-66

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: 222.64  E-value: 7.77e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 616 AQELDPTWLIVDTVIGEGEFGEVYRGALRFPSQdcktVAIKTLK--DTSPDGqwwnFLREATIMGQFNHPHILRLEGVVT 693
Cdd:cd05069     6 AWEIPRESLRLDVKLGQGCFGEVWMGTWNGTTK----VAIKTLKpgTMMPEA----FLQEAQIMKKLRHDKLVPLYAVVS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 694 KrKPIMIVTEFMENGALDAFLKEREDQ-LAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTR 772
Cdd:cd05069    78 E-EPIYIVTEFMGKGSLLDFLKEGDGKyLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLAR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 773 LLDDFDGTYEtQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCP 852
Cdd:cd05069   157 LIEDNEYTAR-QGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMVNREVLEQVERGYRMPCPQGCP 235
                         250       260       270
                  ....*....|....*....|....*....|...
gi 2038291632 853 APLYELMKNCWAYDRARRPHFLQLQAHLEQLLT 885
Cdd:cd05069   236 ESLHELMKLCWKKDPDERPTFEYIQSFLEDYFT 268
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
629-884 7.69e-65

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: 220.17  E-value: 7.69e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRFPSQDCKTVAIKTLK---DTSPDGQwwNFLREATIMGQFNHPHILRLEGVVTKRK-----PI-M 699
Cdd:cd05074    16 MLGKGEFGSVREAQLKSEDGSFQKVAVKMLKadiFSSSDIE--EFLREAACMKEFDHPNVIKLIGVSLRSRakgrlPIpM 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 700 IVTEFMENGALDAFL-----KEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLL 774
Cdd:cd05074    94 VILPFMKHGDLHTFLlmsriGEEPFTLPLQTLVRFMIDIASGMEYLSSKNFIHRDLAARNCMLNENMTVCVADFGLSKKI 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 775 ddFDGTYETQG--GKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCP 852
Cdd:cd05074   174 --YSGDYYRQGcaSKLPVKWLALESLADNVYTTHSDVWAFGVTMWEIMTRGQTPYAGVENSEIYNYLIKGNRLKQPPDCL 251
                         250       260       270
                  ....*....|....*....|....*....|..
gi 2038291632 853 APLYELMKNCWAYDRARRPHFLQLQAHLEQLL 884
Cdd:cd05074   252 EDVYELMCQCWSPEPKCRPSFQHLRDQLELIW 283
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
627-925 1.79e-64

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: 220.28  E-value: 1.79e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 627 DTVIGEGEFGEVYRGALRFPSQDCKT-VAIKTLKD-TSPDGQWwNFLREATIMGQFNHPHILRLEGVVTKrKPIMIVTEF 704
Cdd:cd05108    12 IKVLGSGAFGTVYKGLWIPEGEKVKIpVAIKELREaTSPKANK-EILDEAYVMASVDNPHVCRLLGICLT-STVQLITQL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 705 MENGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYETQ 784
Cdd:cd05108    90 MPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAE 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 785 GGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLYELMKNCWA 864
Cdd:cd05108   170 GGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWM 249
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2038291632 865 YDRARRPHFLQLQAHLEQLLTDPHSLRTIANFDPrvtLRLPSLSGSDGIPYRSVSEWLESI 925
Cdd:cd05108   250 IDADSRPKFRELIIEFSKMARDPQRYLVIQGDER---MHLPSPTDSNFYRALMDEEDMDDV 307
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
624-884 2.08e-64

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: 218.56  E-value: 2.08e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 624 LIVDTVIGEGEFGEVYRGALRFPSQDCKTVAIKTLK-DTSPDGQWWNFLREATIMGQFNHPHILRLEGVV-----TKRKP 697
Cdd:cd05035     1 LKLGKILGEGEFGSVMEAQLKQDDGSQLKVAVKTMKvDIHTYSEIEEFLSEAACMKDFDHPNVMRLIGVCftasdLNKPP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 698 I-MIVTEFMENGALDAFL-----KEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLT 771
Cdd:cd05035    81 SpMVILPFMKHGDLHSYLlysrlGGLPEKLPLQTLLKFMVDIAKGMEYLSNRNFIHRDLAARNCMLDENMTVCVADFGLS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 772 RLLddFDGTYETQG--GKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPV 849
Cdd:cd05035   161 RKI--YSGDYYRQGriSKMPVKWIALESLADNVYTSKSDVWSFGVTMWEIATRGQTPYPGVENHEIYDYLRNGNRLKQPE 238
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2038291632 850 DCPAPLYELMKNCWAYDRARRPHFLQLQAHLEQLL 884
Cdd:cd05035   239 DCLDEVYFLMYFCWTVDPKDRPTFTKLREVLENIL 273
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
630-882 2.88e-64

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: 218.55  E-value: 2.88e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVY--RGALRFPSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMEN 707
Cdd:cd05050    13 IGQGAFGRVFqaRAPGLLPYEPFTMVAVKMLKEEASADMQADFQREAALMAEFDHPNIVKLLGVCAVGKPMCLLFEYMAY 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GALDAFLKERED---------------------QLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVS 766
Cdd:cd05050    93 GDLNEFLRHRSPraqcslshstssarkcglnplPLSCTEQLCIAKQVAAGMAYLSERKFVHRDLATRNCLVGENMVVKIA 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 767 DFGLTRLLDDFDGTYETQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLP 846
Cdd:cd05050   173 DFGLSRNIYSADYYKASENDAIPIRWMPPESIFYNRYTTESDVWAYGVVLWEIFSYGMQPYYGMAHEEVIYYVRDGNVLS 252
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2038291632 847 PPVDCPAPLYELMKNCWAYDRARRPHFLQLQAHLEQ 882
Cdd:cd05050   253 CPDNCPLELYNLMRLCWSKLPSDRPSFASINRILQR 288
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
619-881 3.80e-64

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: 217.06  E-value: 3.80e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 619 LDPTWLIVDTVIGEGEFGEVYRGALRFPSQdcktVAIKTLKDTSPDGQwwNFLREATIMGQFNHPHILRLEGVVTKRKPI 698
Cdd:cd05113     1 IDPKDLTFLKELGTGQFGVVKYGKWRGQYD----VAIKMIKEGSMSED--EFIEEAKVMMNLSHEKLVQLYGVCTKQRPI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 699 MIVTEFMENGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDfD 778
Cdd:cd05113    75 FIITEYMANGCLLNYLREMRKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYVLD-D 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 779 GTYETQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLYEL 858
Cdd:cd05113   154 EYTSSVGSKFPVRWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSLGKMPYERFTNSETVEHVSQGLRLYRPHLASEKVYTI 233
                         250       260
                  ....*....|....*....|...
gi 2038291632 859 MKNCWAYDRARRPHFLQLQAHLE 881
Cdd:cd05113   234 MYSCWHEKADERPTFKILLSNIL 256
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
630-880 3.98e-63

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: 214.44  E-value: 3.98e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFpSQDCKTVAIKTLKDTSPDGQWWN-FLREATIMGQFNHPHILRLEGVVtKRKPIMIVTEFMENG 708
Cdd:cd05116     3 LGSGNFGTVKKGYYQM-KKVVKTVAVKILKNEANDPALKDeLLREANVMQQLDNPYIVRMIGIC-EAESWMLVMEMAELG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 ALDAFLKEREdQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYETQG-GK 787
Cdd:cd05116    81 PLNKFLQKNR-HVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKALRADENYYKAQThGK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 788 IPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLYELMKNCWAYDR 867
Cdd:cd05116   160 WPVKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSYGQKPYKGMKGNEVTQMIEKGERMECPAGCPPEMYDLMKLCWTYDV 239
                         250
                  ....*....|...
gi 2038291632 868 ARRPHFLQLQAHL 880
Cdd:cd05116   240 DERPGFAAVELRL 252
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
630-881 5.05e-63

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: 214.83  E-value: 5.05e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALR--FPSQDCKTVAIKTLKDTSPDGQWwNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMEN 707
Cdd:cd05092    13 LGEGAFGKVFLAECHnlLPEQDKMLVAVKALKEATESARQ-DFQREAELLTVLQHQHIVRFYGVCTEGEPLIMVFEYMRH 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GALDAFLK----------ERED----QLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRl 773
Cdd:cd05092    92 GDLNRFLRshgpdakildGGEGqapgQLTLGQMLQIASQIASGMVYLASLHFVHRDLATRNCLVGQGLVVKIGDFGMSR- 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 774 lDDFDGTYETQGGK--IPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDC 851
Cdd:cd05092   171 -DIYSTDYYRVGGRtmLPIRWMPPESILYRKFTTESDIWSFGVVLWEIFTYGKQPWYQLSNTEAIECITQGRELERPRTC 249
                         250       260       270
                  ....*....|....*....|....*....|
gi 2038291632 852 PAPLYELMKNCWAYDRARRPHFLQLQAHLE 881
Cdd:cd05092   250 PPEVYAIMQGCWQREPQQRHSIKDIHSRLQ 279
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
630-886 5.10e-63

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: 214.87  E-value: 5.10e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALrfpSQD--CKTVAIKTLK-DTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKR-------KPIM 699
Cdd:cd05075     8 LGEGEFGSVMEGQL---NQDdsVLKVAVKTMKiAICTRSEMEDFLSEAVCMKEFDHPNVMRLIGVCLQNtesegypSPVV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 700 IVTeFMENGALDAFL--KEREDQ--LAPGQ-LVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLL 774
Cdd:cd05075    85 ILP-FMKHGDLHSFLlySRLGDCpvYLPTQmLVKFMTDIASGMEYLSSKNFIHRDLAARNCMLNENMNVCVADFGLSKKI 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 775 ddFDGTYETQG--GKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCP 852
Cdd:cd05075   164 --YNGDYYRQGriSKMPVKWIAIESLADRVYTTKSDVWSFGVTMWEIATRGQTPYPGVENSEIYDYLRQGNRLKQPPDCL 241
                         250       260       270
                  ....*....|....*....|....*....|....
gi 2038291632 853 APLYELMKNCWAYDRARRPHFLQLQAHLEQLLTD 886
Cdd:cd05075   242 DGLYELMSSCWLLNPKDRPSFETLRCELEKILKD 275
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
619-884 4.40e-62

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: 213.67  E-value: 4.40e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 619 LDPTW------LIVDTVIGEGEFGEVYR----GALRFPSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFN-HPHILR 687
Cdd:cd05099     3 LDPKWefprdrLVLGKPLGEGCFGQVVRaeayGIDKSRPDQTVTVAVKMLKDNATDKDLADLISEMELMKLIGkHKNIIN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 688 LEGVVTKRKPIMIVTEFMENGALDAFLKER---------------EDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAA 752
Cdd:cd05099    83 LLGVCTQEGPLYVIVEYAAKGNLREFLRARrppgpdytfditkvpEEQLSFKDLVSCAYQVARGMEYLESRRCIHRDLAA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 753 RNILVNQNLCCKVSDFGLTRLLDDFDGTYETQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNN 832
Cdd:cd05099   163 RNVLVTEDNVMKIADFGLARGVHDIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILMWEIFTLGGSPYPGIPV 242
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2038291632 833 QEVMKSIEEGYRLPPPVDCPAPLYELMKNCWAYDRARRPHFLQLQAHLEQLL 884
Cdd:cd05099   243 EELFKLLREGHRMDKPSNCTHELYMLMRECWHAVPTQRPTFKQLVEALDKVL 294
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
630-888 4.99e-62

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: 212.52  E-value: 4.99e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALR--FPSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMEN 707
Cdd:cd05061    14 LGQGSFGMVYEGNARdiIKGEAETRVAVKTVNESASLRERIEFLNEASVMKGFTCHHVVRLLGVVSKGQPTLVVMELMAH 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GALDAFLKE-RED-QLAPG-------QLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRllDDFD 778
Cdd:cd05061    94 GDLKSYLRSlRPEaENNPGrppptlqEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVKIGDFGMTR--DIYE 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 779 GTYETQGGK--IPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLY 856
Cdd:cd05061   172 TDYYRKGGKglLPVRWMAPESLKDGVFTTSSDMWSFGVVLWEITSLAEQPYQGLSNEQVLKFVMDGGYLDQPDNCPERVT 251
                         250       260       270
                  ....*....|....*....|....*....|..
gi 2038291632 857 ELMKNCWAYDRARRPHFLQLqahLEQLLTDPH 888
Cdd:cd05061   252 DLMRMCWQFNPKMRPTFLEI---VNLLKDDLH 280
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
619-876 5.93e-62

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: 211.26  E-value: 5.93e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 619 LDPTWLIVDTVIGEGEFGEVYRGALRFPSQdcktVAIKTLKDTSPDGQwwNFLREATIMGQFNHPHILRLEGVVTKRKPI 698
Cdd:cd05114     1 INPSELTFMKELGSGLFGVVRLGKWRAQYK----VAIKAIREGAMSEE--DFIEEAKVMMKLTHPKLVQLYGVCTQQKPI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 699 MIVTEFMENGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDfD 778
Cdd:cd05114    75 YIVTEFMENGCLLNYLRQRRGKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTRYVLD-D 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 779 GTYETQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLYEL 858
Cdd:cd05114   154 QYTSSSGAKFPVKWSPPEVFNYSKFSSKSDVWSFGVLMWEVFTEGKMPFESKSNYEVVEMVSRGHRLYRPKLASKSVYEV 233
                         250
                  ....*....|....*...
gi 2038291632 859 MKNCWAYDRARRPHFLQL 876
Cdd:cd05114   234 MYSCWHEKPEGRPTFADL 251
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
624-884 9.38e-62

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: 211.75  E-value: 9.38e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 624 LIVDTVIGEGEFGEVYRG-ALRFPSQ-DCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIV 701
Cdd:cd05045     2 LVLGKTLGEGEFGKVVKAtAFRLKGRaGYTTVAVKMLKENASSSELRDLLSEFNLLKQVNHPHVIKLYGACSQDGPLLLI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 702 TEFMENGALDAFLKER-----------------------EDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVN 758
Cdd:cd05045    82 VEYAKYGSLRSFLRESrkvgpsylgsdgnrnssyldnpdERALTMGDLISFAWQISRGMQYLAEMKLVHRDLAARNVLVA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 759 QNLCCKVSDFGLTRLLDDFDGTYETQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKS 838
Cdd:cd05045   162 EGRKMKISDFGLSRDVYEEDSYVKRSKGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIAPERLFNL 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2038291632 839 IEEGYRLPPPVDCPAPLYELMKNCWAYDRARRPHFLQLQAHLEQLL 884
Cdd:cd05045   242 LKTGYRMERPENCSEEMYNLMLTCWKQEPDKRPTFADISKELEKMM 287
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
629-884 2.43e-61

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: 209.64  E-value: 2.43e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRFPSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPI-MIVTEFMEN 707
Cdd:cd05058     2 VIGKGHFGCVYHGTLIDSDGQKIHCAVKSLNRITDIEEVEQFLKEGIIMKDFSHPNVLSLLGICLPSEGSpLVVLPYMKH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRllDDFDGTY----ET 783
Cdd:cd05058    82 GDLRNFIRSETHNPTVKDLIGFGLQVAKGMEYLASKKFVHRDLAARNCMLDESFTVKVADFGLAR--DIYDKEYysvhNH 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 784 QGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLYELMKNCW 863
Cdd:cd05058   160 TGAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELMTRGAPPYPDVDSFDITVYLLQGRRLLQPEYCPDPLYEVMLSCW 239
                         250       260
                  ....*....|....*....|.
gi 2038291632 864 AYDRARRPHFLQLQAHLEQLL 884
Cdd:cd05058   240 HPKPEMRPTFSELVSRISQIF 260
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
630-880 3.21e-61

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: 210.26  E-value: 3.21e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGAL--RFPSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMEN 707
Cdd:cd05091    14 LGEDRFGKVYKGHLfgTAPGEQTQAVAIKTLKDKAEGPLREEFRHEAMLRSRLQHPNIVCLLGVVTKEQPMSMIFSYCSH 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GALDAFLKER---------------EDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTR 772
Cdd:cd05091    94 GDLHEFLVMRsphsdvgstdddktvKSTLEPADFLHIVTQIAAGMEYLSSHHVVHKDLATRNVLVFDKLNVKISDLGLFR 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 773 LLDDFDgTYETQGGK-IPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDC 851
Cdd:cd05091   174 EVYAAD-YYKLMGNSlLPIRWMSPEAIMYGKFSIDSDIWSYGVVLWEVFSYGLQPYCGYSNQDVIEMIRNRQVLPCPDDC 252
                         250       260
                  ....*....|....*....|....*....
gi 2038291632 852 PAPLYELMKNCWAYDRARRPHFLQLQAHL 880
Cdd:cd05091   253 PAWVYTLMLECWNEFPSRRPRFKDIHSRL 281
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
629-893 1.41e-60

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: 207.95  E-value: 1.41e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRFPSQDCKT-VAIKTLKD-TSPDGQWwNFLREATIMGQFNHPHILRLEGVVTKrKPIMIVTEFME 706
Cdd:cd05109    14 VLGSGAFGTVYKGIWIPDGENVKIpVAIKVLREnTSPKANK-EILDEAYVMAGVGSPYVCRLLGICLT-STVQLVTQLMP 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 707 NGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYETQGG 786
Cdd:cd05109    92 YGCLLDYVRENKDRIGSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGG 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 787 KIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLYELMKNCWAYD 866
Cdd:cd05109   172 KVPIKWMALESILHRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKCWMID 251
                         250       260
                  ....*....|....*....|....*..
gi 2038291632 867 RARRPHFLQLQAHLEQLLTDPHSLRTI 893
Cdd:cd05109   252 SECRPRFRELVDEFSRMARDPSRFVVI 278
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
628-882 4.52e-60

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: 206.55  E-value: 4.52e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 628 TVIGEGEFGEVYRGALRFP--SQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFM 705
Cdd:cd05046    11 TTLGRGEFGEVFLAKAKGIeeEGGETLVLVKALQKTKDENLQSEFRRELDMFRKLSHKNVVRLLGLCREAEPHYMILEYT 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 706 ENGALDAFL---KEREDQLAPG-----QLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRllDDF 777
Cdd:cd05046    91 DLGDLKQFLratKSKDEKLKPPplstkQKVALCTQIALGMDHLSNARFVHRDLAARNCLVSSQREVKVSLLSLSK--DVY 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 778 DGTY-ETQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEG-YRLPPPVDCPAPL 855
Cdd:cd05046   169 NSEYyKLRNALIPLRWLAPEAVQEDDFSTKSDVWSFGVLMWEVFTQGELPFYGLSDEEVLNRLQAGkLELPVPEGCPSRL 248
                         250       260
                  ....*....|....*....|....*..
gi 2038291632 856 YELMKNCWAYDRARRPHFLQLQAHLEQ 882
Cdd:cd05046   249 YKLMTRCWAVNPKDRPSFSELVSALGE 275
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
629-910 5.45e-60

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: 207.23  E-value: 5.45e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRFPSQDCKT-VAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKrKPIMIVTEFMEN 707
Cdd:cd05110    14 VLGSGAFGTVYKGIWVPEGETVKIpVAIKILNETTGPKANVEFMDEALIMASMDHPHLVRLLGVCLS-PTIQLVTQLMPH 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYETQGGK 787
Cdd:cd05110    93 GCLLDYVHEHKDNIGSQLLLNWCVQIAKGMMYLEERRLVHRDLAARNVLVKSPNHVKITDFGLARLLEGDEKEYNADGGK 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 788 IPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLYELMKNCWAYDR 867
Cdd:cd05110   173 MPIKWMALECIHYRKFTHQSDVWSYGVTIWELMTFGGKPYDGIPTREIPDLLEKGERLPQPPICTIDVYMVMVKCWMIDA 252
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 2038291632 868 ARRPHFLQLQAHLEQLLTDPHSLRTIANFDprvTLRLPSLSGS 910
Cdd:cd05110   253 DSRPKFKELAAEFSRMARDPQRYLVIQGDD---RMKLPSPNDS 292
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
624-880 1.16e-59

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: 206.32  E-value: 1.16e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 624 LIVDTVIGEGEFGEVYR---------GALRFPSQDCK----TVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEG 690
Cdd:cd05096     7 LLFKEKLGEGQFGEVHLcevvnpqdlPTLQFPFNVRKgrplLVAVKILRPDANKNARNDFLKEVKILSRLKDPNIIRLLG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 691 VVTKRKPIMIVTEFMENGALDAFLKER--EDQLAPGQ----------------LVAMLLGIASGMNYLSGHNYVHRDLAA 752
Cdd:cd05096    87 VCVDEDPLCMITEYMENGDLNQFLSSHhlDDKEENGNdavppahclpaisyssLLHVALQIASGMKYLSSLNFVHRDLAT 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 753 RNILVNQNLCCKVSDFGLTRLLDDFDgTYETQGGKI-PIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSF-GDKPYGEM 830
Cdd:cd05096   167 RNCLVGENLTIKIADFGMSRNLYAGD-YYRIQGRAVlPIRWMAWECILMGKFTTASDVWAFGVTLWEILMLcKEQPYGEL 245
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2038291632 831 NNQEVMKSIEEGYR-------LPPPVDCPAPLYELMKNCWAYDRARRPHFLQLQAHL 880
Cdd:cd05096   246 TDEQVIENAGEFFRdqgrqvyLFRPPPCPQGLYELMLQCWSRDCRERPSFSDIHAFL 302
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
630-876 5.97e-59

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: 203.34  E-value: 5.97e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFPSQDC--KTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMEN 707
Cdd:cd05062    14 LGQGSFGMVYEGIAKGVVKDEpeTRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQGQPTLVIMELMTR 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GALDAFLK--EREDQLAPGQ-------LVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRllDDFD 778
Cdd:cd05062    94 GDLKSYLRslRPEMENNPVQappslkkMIQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFTVKIGDFGMTR--DIYE 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 779 GTYETQGGK--IPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLY 856
Cdd:cd05062   172 TDYYRKGGKglLPVRWMSPESLKDGVFTTYSDVWSFGVVLWEIATLAEQPYQGMSNEQVLRFVMEGGLLDKPDNCPDMLF 251
                         250       260
                  ....*....|....*....|
gi 2038291632 857 ELMKNCWAYDRARRPHFLQL 876
Cdd:cd05062   252 ELMRMCWQYNPKMRPSFLEI 271
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
629-886 3.41e-58

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: 201.53  E-value: 3.41e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRFPSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTK-RKPIMIVTEFMEN 707
Cdd:cd05043    13 LLQEGTFGRIFHGILRDEKGKEEEVLVKTVKDHASEIQVTMLLQESSLLYGLSHQNLLPILHVCIEdGEKPMVLYPYMNW 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GALDAFLKEREDQLAPG-------QLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRllDDFDGT 780
Cdd:cd05043    93 GNLKLFLQQCRLSEANNpqalstqQLVHMALQIACGMSYLHRRGVIHKDIAARNCVIDDELQVKITDNALSR--DLFPMD 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 781 YETQGGK--IPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLYEL 858
Cdd:cd05043   171 YHCLGDNenRPIKWMSLESLVNKEYSSASDVWSFGVLLWELMTLGQTPYVEIDPFEMAAYLKDGYRLAQPINCPDELFAV 250
                         250       260
                  ....*....|....*....|....*...
gi 2038291632 859 MKNCWAYDRARRPHFLQLQAHLEQLLTD 886
Cdd:cd05043   251 MACCWALDPEERPSFQQLVQCLTDFHAQ 278
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
630-880 3.83e-58

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: 201.74  E-value: 3.83e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVY----RGALRF-----PSQDCK--TVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPI 698
Cdd:cd05097    13 LGEGQFGEVHlceaEGLAEFlgegaPEFDGQpvLVAVKMLRADVTKTARNDFLKEIKIMSRLKNPNIIRLLGVCVSDDPL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 699 MIVTEFMENGALDAFLKERE-----------DQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSD 767
Cdd:cd05097    93 CMITEYMENGDLNQFLSQREiestfthanniPSVSIANLLYMAVQIASGMKYLASLNFVHRDLATRNCLVGNHYTIKIAD 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 768 FGLTRLLDDFDgTYETQGGKI-PIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSF-GDKPYGEMNNQEVMKSIEEGYR- 844
Cdd:cd05097   173 FGMSRNLYSGD-YYRIQGRAVlPIRWMAWESILLGKFTTASDVWAFGVTLWEMFTLcKEQPYSLLSDEQVIENTGEFFRn 251
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2038291632 845 ------LPPPVDCPAPLYELMKNCWAYDRARRPHFLQLQAHL 880
Cdd:cd05097   252 qgrqiyLSQTPLCPSPVFKLMMRCWSRDIKDRPTFNKIHHFL 293
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
620-885 7.96e-58

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: 201.78  E-value: 7.96e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 620 DPTW------LIVDTVIGEGEFGEVYR----GALRFPSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQF-NHPHILRL 688
Cdd:cd05101    16 DPKWefprdkLTLGKPLGEGCFGQVVMaeavGIDKDKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIgKHKNIINL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 689 EGVVTKRKPIMIVTEFMENGALDAFLKER---------------EDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAAR 753
Cdd:cd05101    96 LGACTQDGPLYVIVEYASKGNLREYLRARrppgmeysydinrvpEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAAR 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 754 NILVNQNLCCKVSDFGLTRLLDDFDGTYETQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQ 833
Cdd:cd05101   176 NVLVTENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVE 255
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2038291632 834 EVMKSIEEGYRLPPPVDCPAPLYELMKNCWAYDRARRPHFLQLQAHLEQLLT 885
Cdd:cd05101   256 ELFKLLKEGHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRILT 307
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
630-882 1.05e-57

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: 200.60  E-value: 1.05e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVY----RGALRFPSQDCK---------TVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRK 696
Cdd:cd05095    13 LGEGQFGEVHlceaEGMEKFMDKDFAlevsenqpvLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIRLLAVCITDD 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 697 PIMIVTEFMENGALDAFLKEREDQLAPGQLVAMLLG-----------IASGMNYLSGHNYVHRDLAARNILVNQNLCCKV 765
Cdd:cd05095    93 PLCMITEYMENGDLNQFLSRQQPEGQLALPSNALTVsysdlrfmaaqIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKI 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 766 SDFGLTRLLDDFDgTYETQGGKI-PIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSF-GDKPYGEMNNQEVMKSIEEGY 843
Cdd:cd05095   173 ADFGMSRNLYSGD-YYRIQGRAVlPIRWMSWESILLGKFTTASDVWAFGVTLWETLTFcREQPYSQLSDEQVIENTGEFF 251
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2038291632 844 R-------LPPPVDCPAPLYELMKNCWAYDRARRPHFLQLQAHLEQ 882
Cdd:cd05095   252 RdqgrqtyLPQPALCPDSVYKLMLSCWRRDTKDRPSFQEIHTLLQE 297
EphR_LBD cd10319
Ligand Binding Domain of Ephrin Receptors; Ephrin receptors (EphRs) comprise the largest ...
28-201 2.14e-56

Ligand Binding Domain of Ephrin Receptors; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). They are subdivided into 2 groups, A and B type receptors, depending on their ligand ephrin-A or ephrin-B, respectively. 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. Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EhpB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine 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.


Pssm-ID: 198439  Cd Length: 177  Bit Score: 192.62  E-value: 2.14e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632  28 VTLMDTSKAQGELGWLLDPP-EDGWSEVQ-QMLNGTPLYMYQDCPVEESGdTNHWLRSNWIYRGEeASRVHVELQFTVRD 105
Cdd:cd10319     1 VVLLDTTLATSDLGWLTYPYgHGGWDEESgLDPDGANIRTYVVCNVAMPN-QDNWLRTPFIERRG-AQRIYVELKFTVRD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 106 CKSFPGGAGpmGCKETFNLLYMESDQDVGIQLRRPL----FQKVTTVAADQSFTIRDlASGAVKLNVERCSLGRLTHRGL 181
Cdd:cd10319    79 CESFPGNAR--SCKETFNLYYYESDHDTATKEFPPWnedpYTKIDTIAADESFKSSN-EDTTEKLNTETRSIGPLTKRGF 155
                         170       180
                  ....*....|....*....|
gi 2038291632 182 YLAFHNPGSCVALVSVRVFY 201
Cdd:cd10319   156 YLAFQDQGACMSLLSVKVYY 175
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
605-884 1.26e-54

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: 192.32  E-value: 1.26e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 605 YEDPAQGALDFAQELDPTWLIVDTVIGEGEFGEVYRGALR--FPSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQF-N 681
Cdd:cd05055    18 YIDPTQLPYDLKWEFPRNNLSFGKTLGAGAFGKVVEATAYglSKSDAVMKVAVKMLKPTAHSSEREALMSELKIMSHLgN 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 682 HPHILRLEGVVTKRKPIMIVTEFMENGALDAFL-KEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQN 760
Cdd:cd05055    98 HENIVNLLGACTIGGPILVITEYCCYGDLLNFLrRKRESFLTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLLTHG 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 761 LCCKVSDFGLTRLLDDfDGTYETQG-GKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPY-GEMNNQEVMKS 838
Cdd:cd05055   178 KIVKICDFGLARDIMN-DSNYVVKGnARLPVKWMAPESIFNCVYTFESDVWSYGILLWEIFSLGSNPYpGMPVDSKFYKL 256
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2038291632 839 IEEGYRLPPPVDCPAPLYELMKNCWAYDRARRPHFLQLQAHLEQLL 884
Cdd:cd05055   257 IKEGYRMAQPEHAPAEIYDIMKTCWDADPLKRPTFKQIVQLIGKQL 302
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
630-872 1.37e-54

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: 191.41  E-value: 1.37e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALR--FPSQDCKTVAIKTLKDTSPDGQWwNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMEN 707
Cdd:cd05093    13 LGEGAFGKVFLAECYnlCPEQDKILVAVKTLKDASDNARK-DFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKH 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GALDAFLK------------EREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRllD 775
Cdd:cd05093    92 GDLNKFLRahgpdavlmaegNRPAELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSR--D 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 776 DFDGTYETQGGK--IPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPA 853
Cdd:cd05093   170 VYSTDYYRVGGHtmLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPRTCPK 249
                         250
                  ....*....|....*....
gi 2038291632 854 PLYELMKNCWaydrARRPH 872
Cdd:cd05093   250 EVYDLMLGCW----QREPH 264
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
620-885 4.13e-54

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: 190.61  E-value: 4.13e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 620 DPTW------LIVDTVIGEGEFGEVYR----GALRFPSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQF-NHPHILRL 688
Cdd:cd05098     5 DPRWelprdrLVLGKPLGEGCFGQVVLaeaiGLDKDKPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIgKHKNIINL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 689 EGVVTKRKPIMIVTEFMENGALDAFLKER---------------EDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAAR 753
Cdd:cd05098    85 LGACTQDGPLYVIVEYASKGNLREYLQARrppgmeycynpshnpEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAAR 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 754 NILVNQNLCCKVSDFGLTRLLDDFDGTYETQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQ 833
Cdd:cd05098   165 NVLVTEDNVMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSPYPGVPVE 244
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2038291632 834 EVMKSIEEGYRLPPPVDCPAPLYELMKNCWAYDRARRPHFLQLQAHLEQLLT 885
Cdd:cd05098   245 ELFKLLKEGHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIVA 296
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
620-885 6.27e-54

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: 191.39  E-value: 6.27e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 620 DPTW------LIVDTVIGEGEFGEVYR----GALRFPSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQF-NHPHILRL 688
Cdd:cd05100     4 DPKWelsrtrLTLGKPLGEGCFGQVVMaeaiGIDKDKPNKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 689 EGVVTKRKPIMIVTEFMENGALDAFLKER---------------EDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAAR 753
Cdd:cd05100    84 LGACTQDGPLYVLVEYASKGNLREYLRARrppgmdysfdtcklpEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAAR 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 754 NILVNQNLCCKVSDFGLTRLLDDFDGTYETQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQ 833
Cdd:cd05100   164 NVLVTEDNVMKIADFGLARDVHNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVE 243
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2038291632 834 EVMKSIEEGYRLPPPVDCPAPLYELMKNCWAYDRARRPHFLQLQAHLEQLLT 885
Cdd:cd05100   244 ELFKLLKEGHRMDKPANCTHELYMIMRECWHAVPSQRPTFKQLVEDLDRVLT 295
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
616-888 1.76e-53

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: 188.24  E-value: 1.76e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 616 AQELDPTWLIVDTVIGEGEFGEVYRGaLRFPSQDCKT--VAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVT 693
Cdd:cd05111     1 ARIFKETELRKLKVLGSGVFGTVHKG-IWIPEGDSIKipVAIKVIQDRSGRQSFQAVTDHMLAIGSLDHAYIVRLLGICP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 694 KRKpIMIVTEFMENGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRL 773
Cdd:cd05111    80 GAS-LQLVTQLLPLGSLLDHVRQHRGSLGPQLLLNWCVQIAKGMYYLEEHRMVHRNLAARNVLLKSPSQVQVADFGVADL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 774 LDDFDGTYETQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPA 853
Cdd:cd05111   159 LYPDDKKYFYSEAKTPIKWMALESIHFGKYTHQSDVWSYGVTVWEMMTFGAEPYAGMRLAEVPDLLEKGERLAQPQICTI 238
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2038291632 854 PLYELMKNCWAYDRARRPHFLQLQAHLEQLLTDPH 888
Cdd:cd05111   239 DVYMVMVKCWMIDENIRPTFKELANEFTRMARDPP 273
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
629-879 7.13e-53

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 185.43  E-value: 7.13e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632  629 VIGEGEFGEVYRGalrfpsQDCKT---VAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFM 705
Cdd:smart00220   6 KLGEGSFGKVYLA------RDKKTgklVAIKVIKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYC 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632  706 ENGALDAFLKEReDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDD------FDG 779
Cdd:smart00220  80 EGGDLFDLLKKR-GRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPgeklttFVG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632  780 TYEtqggkipirWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPY-GEMNNQEVMKSIEEGYR--LPPPVDCPAPLY 856
Cdd:smart00220 159 TPE---------YMAPEVLLGKGYGKAVDIWSLGVILYELLT-GKPPFpGDDQLLELFKKIGKPKPpfPPPEWDISPEAK 228
                          250       260
                   ....*....|....*....|...
gi 2038291632  857 ELMKNCWAYDRARRPHFLQLQAH 879
Cdd:smart00220 229 DLIRKLLVKDPEKRLTAEEALQH 251
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
630-880 1.18e-52

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: 183.24  E-value: 1.18e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGalrFPSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGA 709
Cdd:cd00180     1 LGKGSFGKVYKA---RDKETGKKVAVKVIPKEKLKKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 710 LDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYETQGGKIP 789
Cdd:cd00180    78 LKDLLKENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLLKTTGGTTP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 790 IRWTAPEAIAHRIFTTASDVWSFGIVMWEVlsfgdkpygemnnqevmksieegyrlpppvdcpAPLYELMKNCWAYDRAR 869
Cdd:cd00180   158 PYYAPPELLGGRYYGPKVDIWSLGVILYEL---------------------------------EELKDLIRRMLQYDPKK 204
                         250
                  ....*....|.
gi 2038291632 870 RPHFLQLQAHL 880
Cdd:cd00180   205 RPSAKELLEHL 215
EphR_LBD_A8 cd10486
Ligand Binding Domain of Ephrin type-A Receptor 8; Ephrin receptors (EphRs) comprise the ...
27-203 1.23e-52

Ligand Binding Domain of Ephrin type-A Receptor 8; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (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. EphA8 has been implicated in various cancers. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine 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).


Pssm-ID: 198454  Cd Length: 173  Bit Score: 181.77  E-value: 1.23e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632  27 EVTLMDTSKAQGELGWLLDPPEdGWSEVQQMLNG-TPLYMYQDCPVEeSGDTNHWLRSNWIYRgEEASRVHVELQFTVRD 105
Cdd:cd10486     1 EVNLLDTSTISGDWGWLTYPSH-GWDSINEMDEYfSPIHTYQVCNVM-SPNQNNWLRTNWVQR-DGARRVYAEIKFTLRD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 106 CKSFPGGAGPmgCKETFNLLYMESDQDVGIQLRRPLFQKVTTVAADQSFTIRDLASGAVKLNVERCSLGRLTHRGLYLAF 185
Cdd:cd10486    78 CNSMPGVLGT--CKETFNLYYYESDRDLGTSTWESQFLKIDTIAADESFTNVDLGVRRLKLNTEVRGVGPLSKRGFYLAF 155
                         170
                  ....*....|....*...
gi 2038291632 186 HNPGSCVALVSVRVFYQR 203
Cdd:cd10486   156 QDIGACIAIVSVRVYYKK 173
EphR_LBD_A7 cd10485
Ligand Binding Domain of Ephrin type-A Receptor 7; Ephrin receptors (EphRs) comprise the ...
25-204 1.85e-52

Ligand Binding Domain of Ephrin type-A Receptor 7; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (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. EphA7 has been implicated in various cancers, including prostate, gastic and colorectal cancers. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine 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).


Pssm-ID: 198453  Cd Length: 177  Bit Score: 181.38  E-value: 1.85e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632  25 AEEVTLMDTSKAQGELGWLLDPPeDGWSEVQQM-LNGTPLYMYQDCPVEESgDTNHWLRSNWIYRGeEASRVHVELQFTV 103
Cdd:cd10485     1 AKEVILLDSKAQQTELEWISSPP-SGWEEISGLdENYTPIRTYQVCQVMEP-NQNNWLRTNWISKG-NAQRIFVELKFTL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 104 RDCKSFPGGAGPmgCKETFNLLYMESDQDVGIQLRRPLFQKVTTVAADQSFTIRDLASGAVKLNVERCSLGRLTHRGLYL 183
Cdd:cd10485    78 RDCNSLPGVLGT--CKETFNLYYYETDYDTGRNIRENQYVKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSKKGFYL 155
                         170       180
                  ....*....|....*....|.
gi 2038291632 184 AFHNPGSCVALVSVRVFYQRC 204
Cdd:cd10485   156 AFQDVGACIALVSVKVYYKKC 176
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
629-884 4.33e-52

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: 183.70  E-value: 4.33e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRfPSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQF-NHPHILRLEGVVTKRKPIMIVTEFMEN 707
Cdd:cd05047     2 VIGEGNFGQVLKARIK-KDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GALDAFLKERE---------------DQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTR 772
Cdd:cd05047    81 GNLLDFLRKSRvletdpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 773 LLDDFdgtYETQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCP 852
Cdd:cd05047   161 GQEVY---VKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPLNCD 237
                         250       260       270
                  ....*....|....*....|....*....|..
gi 2038291632 853 APLYELMKNCWAYDRARRPHFLQLQAHLEQLL 884
Cdd:cd05047   238 DEVYDLMRQCWREKPYERPSFAQILVSLNRML 269
EphR_LBD_A10 cd10487
Ligand Binding Domain of Ephrin type-A Receptor 10; Ephrin receptors (EphRs) comprise the ...
27-203 6.07e-52

Ligand Binding Domain of Ephrin type-A Receptor 10; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (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. 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. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine 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 results in cell-cell repulsion or adhesion.


Pssm-ID: 198455  Cd Length: 173  Bit Score: 179.84  E-value: 6.07e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632  27 EVTLMDTSKAQGELGWLlDPPEDGWSEVQQM-LNGTPLYMYQDCPVEESgDTNHWLRSNWIYRGEeASRVHVELQFTVRD 105
Cdd:cd10487     1 EVVLLDSKESQAELGWT-SLPSNGWEEISGVdEHYKPIRTYQVCNVMEP-NQNNWLQTGWISRGR-GQRIFIELQFTLRD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 106 CKSFPGGAGPmgCKETFNLLYMESDQDVGIQLRRPLFQKVTTVAADQSFTIRDLASGAVKLNVERCSLGRLTHRGLYLAF 185
Cdd:cd10487    78 CNSIPGVAGT--CKETFNLYYAESDADLGRRLRESRPRKIDTIAADESFTQGDLGERKMKLNTEVREIGHLSRRGFHLAF 155
                         170
                  ....*....|....*...
gi 2038291632 186 HNPGSCVALVSVRVFYQR 203
Cdd:cd10487   156 QDVGACVALVSVRVYYKQ 173
EphR_LBD_A4 cd10482
Ligand Binding Domain of Ephrin type-A Receptor 4; Ephrin receptors (EphRs) comprise the ...
27-203 8.97e-52

Ligand Binding Domain of Ephrin type-A Receptor 4; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (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. A loss of EphA4, as well as EphB2, precedes memory decline in a murine model of Alzheimers disease. EphA4 has been shown to have a negative effect on axon regeneration and functional restoration in corticospinal lesions and is downregulated in some cervical cancers. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine 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).


Pssm-ID: 198450  Cd Length: 174  Bit Score: 179.47  E-value: 8.97e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632  27 EVTLMDTSKAQGELGWLLDPPEDGWSEVQQM-LNGTPLYMYQDCPVEESGDtNHWLRSNWIYRGEeASRVHVELQFTVRD 105
Cdd:cd10482     1 EVTLLDSRSVQGELGWIASPLEGGWEEVSIMdEKNTPIRTYQVCNVMEPSQ-NNWLRTDWIPREG-AQRVYIEIKFTLRD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 106 CKSFPGGAGPmgCKETFNLLYMESDQDVGIQLRRPLFQKVTTVAADQSFTIRDLASGAVKLNVERCSLGRLTHRGLYLAF 185
Cdd:cd10482    79 CNSLPGVMGT--CKETFNLYYYESNNDKERFIRENQFVKIDTIAADESFTQVDIGDRIMKLNTEVRDVGPLSKKGFYLAF 156
                         170
                  ....*....|....*...
gi 2038291632 186 HNPGSCVALVSVRVFYQR 203
Cdd:cd10482   157 QDVGACIALVSVRVFYKK 174
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
624-883 1.10e-51

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: 183.29  E-value: 1.10e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 624 LIVDTVIGEGEFGEVYRGALR--FPSQDCKTVAIKTLKDTSPDGQWwNFLREATIMGQFNHPHILRLEGVVTKRKPIMIV 701
Cdd:cd05094     7 IVLKRELGEGAFGKVFLAECYnlSPTKDKMLVAVKTLKDPTLAARK-DFQREAELLTNLQHDHIVKFYGVCGDGDPLIMV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 702 TEFMENGALDAFLK---------------EREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVS 766
Cdd:cd05094    86 FEYMKHGDLNKFLRahgpdamilvdgqprQAKGELGLSQMLHIATQIASGMVYLASQHFVHRDLATRNCLVGANLLVKIG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 767 DFGLTRllDDFDGTYETQGGK--IPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYR 844
Cdd:cd05094   166 DFGMSR--DVYSTDYYRVGGHtmLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTYGKQPWFQLSNTEVIECITQGRV 243
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2038291632 845 LPPPVDCPAPLYELMKNCWAYDRARRPHFLQLQAHLEQL 883
Cdd:cd05094   244 LERPRVCPKEVYDIMLGCWQREPQQRLNIKEIYKILHAL 282
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
629-883 3.08e-51

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: 182.30  E-value: 3.08e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRgALRF---PSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQF-NHPHILRLEGVVTK-RKPIMIVTE 703
Cdd:cd05054    14 PLGRGAFGKVIQ-ASAFgidKSATCRTVAVKMLKEGATASEHKALMTELKILIHIgHHLNVVNLLGACTKpGGPLMVIVE 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 704 FMENGALDAFLKEREDQLAPGQ-------------------------LVAMLLGIASGMNYLSGHNYVHRDLAARNILVN 758
Cdd:cd05054    93 FCKFGNLSNYLRSKREEFVPYRdkgardveeeedddelykepltledLICYSFQVARGMEFLASRKCIHRDLAARNILLS 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 759 QNLCCKVSDFGLTR-LLDDFDgtYETQG-GKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPY-GEMNNQEV 835
Cdd:cd05054   173 ENNVVKICDFGLARdIYKDPD--YVRKGdARLPLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFSLGASPYpGVQMDEEF 250
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2038291632 836 MKSIEEGYRLPPPVDCPAPLYELMKNCWAYDRARRPHFLQLQAHLEQL 883
Cdd:cd05054   251 CRRLKEGTRMRAPEYTTPEIYQIMLDCWHGEPKERPTFSELVEKLGDL 298
EphR_LBD_A3 cd10481
Ligand Binding Domain of Ephrin type-A Receptor 3; Ephrin receptors (EphRs) comprise the ...
27-203 3.96e-51

Ligand Binding Domain of Ephrin type-A Receptor 3; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (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. EphA3 has been implicated in leukemia, lung and other cancers. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine 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.


Pssm-ID: 198449  Cd Length: 173  Bit Score: 177.55  E-value: 3.96e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632  27 EVTLMDTSKAQGELGWLlDPPEDGWSEVQQM-LNGTPLYMYQDCPVEESgDTNHWLRSNWIYRgEEASRVHVELQFTVRD 105
Cdd:cd10481     1 EVNLLDSKAIQGELGWI-SYPSHGWEEISGVdEHYTPIRTYQVCNVMDH-SQNNWLRTNWIPR-NSAQKIYVELKFTLRD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 106 CKSFPGGAGPmgCKETFNLLYMESDQDVGIQLRRPLFQKVTTVAADQSFTIRDLASGAVKLNVERCSLGRLTHRGLYLAF 185
Cdd:cd10481    78 CNSIPLVLGT--CKETFNLYYMESDEDQGVKFREHQFTKIDTIAADESFTQMDLGDRILKLNTEVREVGPVSKKGFYLAF 155
                         170
                  ....*....|....*...
gi 2038291632 186 HNPGSCVALVSVRVFYQR 203
Cdd:cd10481   156 QDVGACVALVSVRVYFKK 173
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
627-884 4.95e-51

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: 181.74  E-value: 4.95e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 627 DTVIGEGEFGEVYRGALRFPSQDcKTVAIKTLKDTSPDGQWWNFLREATIMGQF-NHPHILRLEGVVTKRKPIMIVTEFM 705
Cdd:cd05089     7 EDVIGEGNFGQVIKAMIKKDGLK-MNAAIKMLKEFASENDHRDFAGELEVLCKLgHHPNIINLLGACENRGYLYIAIEYA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 706 ENGALDAFLKERE---------------DQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGL 770
Cdd:cd05089    86 PYGNLLDFLRKSRvletdpafakehgtaSTLTSQQLLQFASDVAKGMQYLSEKQFIHRDLAARNVLVGENLVSKIADFGL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 771 TRLLDDFdgtYETQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVD 850
Cdd:cd05089   166 SRGEEVY---VKKTMGRLPVRWMAIESLNYSVYTTKSDVWSFGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRMEKPRN 242
                         250       260       270
                  ....*....|....*....|....*....|....
gi 2038291632 851 CPAPLYELMKNCWAYDRARRPHFLQLQAHLEQLL 884
Cdd:cd05089   243 CDDEVYELMRQCWRDRPYERPPFSQISVQLSRML 276
EphR_LBD_A5 cd10483
Ligand Binding Domain of Ephrin type-A Receptor 5; Ephrin receptors (EphRs) comprise the ...
27-203 3.74e-50

Ligand Binding Domain of Ephrin type-A Receptor 5; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (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. EphA5 is almost exclusively expressed in the nervous system. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine 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).


Pssm-ID: 198451  Cd Length: 173  Bit Score: 174.83  E-value: 3.74e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632  27 EVTLMDTSKAQGELGWLLdPPEDGWSEVQQM-LNGTPLYMYQDCPVEESgDTNHWLRSNWIyRGEEASRVHVELQFTVRD 105
Cdd:cd10483     1 EVNLLDSRSVMGDLGWIA-YPKNGWEEIGEVdENYAPIHTYQVCKVMEQ-NQNNWLLTSWI-SNEGASRIFIELKFTLRD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 106 CKSFPGGAGPmgCKETFNLLYMESDQDVGIQLRRPLFQKVTTVAADQSFTIRDLASGAVKLNVERCSLGRLTHRGLYLAF 185
Cdd:cd10483    78 CNSLPGGLGT--CKETFNVYYFESNDEDGRNIRENQYIKIDTIAADESFTELDLGDRVMKLNTEVRDVGPLTKKGFYLAF 155
                         170
                  ....*....|....*...
gi 2038291632 186 HNPGSCVALVSVRVFYQR 203
Cdd:cd10483   156 QDLGACIALVSVRVYYKK 173
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
628-883 1.24e-49

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: 177.39  E-value: 1.24e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 628 TVIGEGEFGEVYrgALRF-PSQDC--KTVAIKTLKDTSPDgQWWNFLREATIMGQFNHPHILRLEGVVTK--RKPIMIVT 702
Cdd:cd05081    10 SQLGKGNFGSVE--LCRYdPLGDNtgALVAVKQLQHSGPD-QQRDFQREIQILKALHSDFIVKYRGVSYGpgRRSLRLVM 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 703 EFMENGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLL-DDFDGTY 781
Cdd:cd05081    87 EYLPSGCLRDFLQRHRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKLLpLDKDYYV 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 782 ETQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKP----------YGEMNNQEVMKS----IEEGYRLPP 847
Cdd:cd05081   167 VREPGQSPIFWYAPESLSDNIFSRQSDVWSFGVVLYELFTYCDKScspsaeflrmMGCERDVPALCRllelLEEGQRLPA 246
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2038291632 848 PVDCPAPLYELMKNCWAYDRARRPHFLQLQAHLEQL 883
Cdd:cd05081   247 PPACPAEVHELMKLCWAPSPQDRPSFSALGPQLDML 282
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
630-884 1.89e-49

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: 176.66  E-value: 1.89e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYrgALRFPSQDCKT---VAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKR--KPIMIVTEF 704
Cdd:cd05079    12 LGEGHFGKVE--LCRYDPEGDNTgeqVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDggNGIKLIMEF 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 705 MENGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYETQ 784
Cdd:cd05079    90 LPSGSLKEYLPRNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYTVK 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 785 GGK-IPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPY--------------GEMNNQEVMKSIEEGYRLPPPV 849
Cdd:cd05079   170 DDLdSPVFWYAPECLIQSKFYIASDVWSFGVTLYELLTYCDSESspmtlflkmigpthGQMTVTRLVRVLEEGKRLPRPP 249
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2038291632 850 DCPAPLYELMKNCWAYDRARRPHFLQLQAHLEQLL 884
Cdd:cd05079   250 NCPEEVYQLMRKCWEFQPSKRTTFQNLIEGFEAIL 284
EphR_LBD_A6 cd10484
Ligand Binding Domain of Ephrin type-A Receptor 6; Ephrin receptors (EphRs) comprise the ...
27-203 1.70e-48

Ligand Binding Domain of Ephrin type-A Receptor 6; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (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. EphA6, like other Eph receptors and their ephrin ligands, seems to play a role in neural development, underlying learning and memory. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine 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).


Pssm-ID: 198452  Cd Length: 173  Bit Score: 169.81  E-value: 1.70e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632  27 EVTLMDTSKAQGELGWLLDPPeDGWSEVQQM--LNgTPLYMYQDCPVEESgDTNHWLRSNWIYRgEEASRVHVELQFTVR 104
Cdd:cd10484     1 QVVLLDTTMVLGELNWKTYPC-NGWDAITEMdeYN-RPIHTYQVCNVMEP-NQNNWLRTNWISR-DAAQKIYVEMKFTLR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 105 DCKSFPGGAGPmgCKETFNLLYMESDQDVGIQLRRPLFQKVTTVAADQSFTIRDLASGAVKLNVERCSLGRLTHRGLYLA 184
Cdd:cd10484    77 DCNSIPWVVGT--CKETFNLHYMESDEAHAVKFKPNQYSKIDTIAADESFTQMDLGDRILKLNTEVREVGPITRKGFYLA 154
                         170
                  ....*....|....*....
gi 2038291632 185 FHNPGSCVALVSVRVFYQR 203
Cdd:cd10484   155 FQDIGACIALVSVRVYYKK 173
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
630-883 3.88e-47

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: 170.20  E-value: 3.88e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRgaLRF-PSQD--CKTVAIKTLKDTSPDgQWWNFLREATIMGQFNHPHILRLEGVV--TKRKPIMIVTEF 704
Cdd:cd14205    12 LGKGNFGSVEM--CRYdPLQDntGEVVAVKKLQHSTEE-HLRDFEREIEILKSLQHDNIVKYKGVCysAGRRNLRLIMEY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 705 MENGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDfDGTYET- 783
Cdd:cd14205    89 LPYGSLRDYLQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLPQ-DKEYYKv 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 784 -QGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSF---------------GDKPYGEMNNQEVMKSIEEGYRLPP 847
Cdd:cd14205   168 kEPGESPIFWYAPESLTESKFSVASDVWSFGVVLYELFTYieksksppaefmrmiGNDKQGQMIVFHLIELLKNNGRLPR 247
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2038291632 848 PVDCPAPLYELMKNCWAYDRARRPHFLQLQAHLEQL 883
Cdd:cd14205   248 PDGCPDEIYMIMTECWNNNVNQRPSFRDLALRVDQI 283
EphR_LBD_B cd10472
Ligand Binding Domain of Ephrin type-B receptors; Ephrin receptors (EphRs) comprise the ...
29-203 1.46e-46

Ligand Binding Domain of Ephrin type-B receptors; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphB receptors bind to transmembrane ephrin-B ligands. They play important roles in synapse formation and plasticity, spine morphogenesis, axon guidance, and angiogenesis. In the intestinal epithelium, EphB receptors are Wnt signaling target genes that control cell compartmentalization. They function as suppressors of colon cancer progression. There are six vertebrate EhpB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine 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.


Pssm-ID: 198440  Cd Length: 176  Bit Score: 164.67  E-value: 1.46e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632  29 TLMDTSKAQGELGWLLDPpEDGWSEVQ---QMLNgtPLYMYQDCPVEESgDTNHWLRSNWIYRgEEASRVHVELQFTVRD 105
Cdd:cd10472     2 TLMDTRTATAELGWTAHP-PSGWEEVSgydENMN--TIRTYQVCNVFES-NQNNWLRTKFIRR-RGAHRVYVEMKFTVRD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 106 CKSFPGGAGpmGCKETFNLLYMESDQDVGIQLRRPLFQ----KVTTVAADQSFTIRDLASGAVKLNVERCSLGRLTHRGL 181
Cdd:cd10472    77 CSSIPNVPG--SCKETFNLYYYESDSDIATKTSPFWMEnpyvKVDTIAADESFSQVDLGGRVMKVNTEVRSFGPLSRNGF 154
                         170       180
                  ....*....|....*....|..
gi 2038291632 182 YLAFHNPGSCVALVSVRVFYQR 203
Cdd:cd10472   155 YLAFQDYGACMSLISVRVFYKK 176
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
626-871 3.24e-46

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: 166.61  E-value: 3.24e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 626 VDTVIGEGEFGEVYRGalRFPSQDcKTVAIKTLK-DTSPDGQWWN-FLREATIMGQFNHPHILRLEGVVTKRKPIMIVTE 703
Cdd:cd14014     4 LVRLLGRGGMGEVYRA--RDTLLG-RPVAIKVLRpELAEDEEFRErFLREARALARLSHPNIVRVYDVGEDDGRPYIVME 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 704 FMENGALDAFLKEREdQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDfdgTYET 783
Cdd:cd14014    81 YVEGGSLADLLRERG-PLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGD---SGLT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 784 QGGKIP--IRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSIEEGYRLPPPV---DCPAPLYEL 858
Cdd:cd14014   157 QTGSVLgtPAYMAPEQARGGPVDPRSDIYSLGVVLYELLT-GRPPFDGDSPAAVLAKHLQEAPPPPSPlnpDVPPALDAI 235
                         250
                  ....*....|...
gi 2038291632 859 MKNCWAYDRARRP 871
Cdd:cd14014   236 ILRALAKDPEERP 248
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
629-886 3.54e-46

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: 168.25  E-value: 3.54e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRFPSQDCKTvAIKTLKDTSPDGQWWNFLREATIMGQFN-HPHILRLEGVVTKRKPIMIVTEFMEN 707
Cdd:cd05088    14 VIGEGNFGQVLKARIKKDGLRMDA-AIKRMKEYASKDDHRDFAGELEVLCKLGhHPNIINLLGACEHRGYLYLAIEYAPH 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GALDAFLKERE---------------DQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTR 772
Cdd:cd05088    93 GNLLDFLRKSRvletdpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSR 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 773 LLDDFdgtYETQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCP 852
Cdd:cd05088   173 GQEVY---VKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPLNCD 249
                         250       260       270
                  ....*....|....*....|....*....|....
gi 2038291632 853 APLYELMKNCWAYDRARRPHFLQLQAHLEQLLTD 886
Cdd:cd05088   250 DEVYDLMRQCWREKPYERPSFAQILVSLNRMLEE 283
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
630-884 9.46e-46

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: 168.24  E-value: 9.46e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRgALRF---PSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQF-NHPHILRLEGVVTKRK-PIMIVTEF 704
Cdd:cd05103    15 LGRGAFGQVIE-ADAFgidKTATCRTVAVKMLKEGATHSEHRALMSELKILIHIgHHLNVVNLLGACTKPGgPLMVIVEF 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 705 MENGALDAFL-------------------------------KEREDQLAPGQ---------------------------- 725
Cdd:cd05103    94 CKFGNLSAYLrskrsefvpyktkgarfrqgkdyvgdisvdlKRRLDSITSSQssassgfveekslsdveeeeagqedlyk 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 726 -------LVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRllDDF-DGTYETQG-GKIPIRWTAPE 796
Cdd:cd05103   174 dfltledLICYSFQVAKGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLAR--DIYkDPDYVRKGdARLPLKWMAPE 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 797 AIAHRIFTTASDVWSFGIVMWEVLSFGDKPY-GEMNNQEVMKSIEEGYRLPPPVDCPAPLYELMKNCWAYDRARRPHFLQ 875
Cdd:cd05103   252 TIFDRVYTIQSDVWSFGVLLWEIFSLGASPYpGVKIDEEFCRRLKEGTRMRAPDYTTPEMYQTMLDCWHGEPSQRPTFSE 331

                  ....*....
gi 2038291632 876 LQAHLEQLL 884
Cdd:cd05103   332 LVEHLGNLL 340
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
630-874 7.28e-44

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: 159.93  E-value: 7.28e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGAlrfpSQDCKT-VAIKTLK-DTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMEN 707
Cdd:cd13978     1 LGSGGFGTVSKAR----HVSWFGmVAIKCLHsSPNCIEERKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMEN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GALDAFLKEREDQLAPGQLVAMLLGIASGMNYLsgHNY----VHRDLAARNILVNQNLCCKVSDFGLTRL-----LDDFD 778
Cdd:cd13978    77 GSLKSLLEREIQDVPWSLRFRIIHEIALGMNFL--HNMdpplLHHDLKPENILLDNHFHVKISDFGLSKLgmksiSANRR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 779 GTYETQGGKipIRWTAPEAI--AHRIFTTASDVWSFGIVMWEVLSfGDKPY-GEMNNQEVMKSIEEGYR-------LPPP 848
Cdd:cd13978   155 RGTENLGGT--PIYMAPEAFddFNKKPTSKSDVYSFAIVIWAVLT-RKEPFeNAINPLLIMQIVSKGDRpslddigRLKQ 231
                         250       260
                  ....*....|....*....|....*.
gi 2038291632 849 VDCPAPLYELMKNCWAYDRARRPHFL 874
Cdd:cd13978   232 IENVQELISLMIRCWDGNPDARPTFL 257
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
630-881 1.12e-43

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: 158.43  E-value: 1.12e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRfpsqdCKTVAIKTLKDtspdgqwwnfLREATI--MGQFNHPHILRLEGVVTKRKPIMIVTEFMEN 707
Cdd:cd14059     1 LGSGAQGAVFLGKFR-----GEEVAVKKVRD----------EKETDIkhLRKLNHPNIIKFKGVCTQAPCYCILMEYCPY 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GALDAFLKEREdQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDD------FDGTy 781
Cdd:cd14059    66 GQLYEVLRAGR-EITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKELSEkstkmsFAGT- 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 782 etqggkipIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSI-EEGYRLPPPVDCPAPLYELMK 860
Cdd:cd14059   144 --------VAWMAPEVIRNEPCSEKVDIWSFGVVLWELLT-GEIPYKDVDSSAIIWGVgSNSLQLPVPSTCPDGFKLLMK 214
                         250       260
                  ....*....|....*....|.
gi 2038291632 861 NCWAYDRARRPHFLQLQAHLE 881
Cdd:cd14059   215 QCWNSKPRNRPSFRQILMHLD 235
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
629-883 2.29e-43

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: 158.33  E-value: 2.29e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRfpsqdCKTVAIKTLK-DTSPDGQWW--NFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFM 705
Cdd:cd14061     1 VIGVGGFGKVYRGIWR-----GEEVAVKAARqDPDEDISVTleNVRQEARLFWMLRHPNIIALRGVCLQPPNLCLVMEYA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 706 ENGALDAFLKERedQLAPGQLVAMLLGIASGMNYLsgHN-----YVHRDLAARNILV-----NQNLC---CKVSDFGLTR 772
Cdd:cd14061    76 RGGALNRVLAGR--KIPPHVLVDWAIQIARGMNYL--HNeapvpIIHRDLKSSNILIleaieNEDLEnktLKITDFGLAR 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 773 LLD-----DFDGTYEtqggkipirWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEV-----MKSIEeg 842
Cdd:cd14061   152 EWHkttrmSAAGTYA---------WMAPEVIKSSTFSKASDVWSYGVLLWELLT-GEVPYKGIDGLAVaygvaVNKLT-- 219
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2038291632 843 yrLPPPVDCPAPLYELMKNCWAYDRARRPHFLQLqahLEQL 883
Cdd:cd14061   220 --LPIPSTCPEPFAQLMKDCWQPDPHDRPSFADI---LKQL 255
EphR_LBD_B2 cd10477
Ligand Binding Domain of Ephrin type-B Receptor 2; Ephrin receptors (EphRs) comprise the ...
27-203 2.90e-43

Ligand Binding Domain of Ephrin type-B Receptor 2; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EhpB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. EphB2 plays a role in cell positioning in the gastrointestinal tract by being expressed in proliferating progenitor cells. It also has been implicated in colorectal cancer. A loss of EphB2, as well as EphA4, also precedes memory decline in a murine model of Alzheimers disease. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine 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).


Pssm-ID: 198445  Cd Length: 178  Bit Score: 155.22  E-value: 2.90e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632  27 EVTLMDTSKAQGELGWLLDPPEdGWSEVQQM-LNGTPLYMYQDCPVEESgDTNHWLRSNWIYRgEEASRVHVELQFTVRD 105
Cdd:cd10477     2 EETLMDSTTATAELGWMVHPPS-GWEEVSGYdENMNTIRTYQVCNVFES-SQNNWLRTKYIRR-RGAHRIHVEMKFSVRD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 106 CKSFPggAGPMGCKETFNLLYMESDQDVGIQLRRPLFQ----KVTTVAADQSFTIRDLASGAVKLNVERCSLGRLTHRGL 181
Cdd:cd10477    79 CSSIP--SVPGSCKETFNLYYYESDFDSATKTFPNWMEnpwvKVDTIAADESFSQVDLGGRVMKINTEVRSFGPVSRNGF 156
                         170       180
                  ....*....|....*....|..
gi 2038291632 182 YLAFHNPGSCVALVSVRVFYQR 203
Cdd:cd10477   157 YLAFQDYGGCMSLIAVRVFYRK 178
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
605-885 8.64e-43

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: 161.33  E-value: 8.64e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 605 YEDPAQGALDFAQELDPTWLIVDTVIGEGEFGEVYRGALR--FPSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFN- 681
Cdd:cd05107    20 YVDPMQLPYDSAWEMPRDNLVLGRTLGSGAFGRVVEATAHglSHSQSTMKVAVKMLKSTARSSEKQALMSELKIMSHLGp 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 682 HPHILRLEGVVTKRKPIMIVTEFMENGALDAFL-------------KER------------EDQL--------------- 721
Cdd:cd05107   100 HLNIVNLLGACTKGGPIYIITEYCRYGDLVDYLhrnkhtflqyyldKNRddgslisggstpLSQRkshvslgsesdggym 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 722 ----------------------------------------APGQ-----------------LVAMLLGIASGMNYLSGHN 744
Cdd:cd05107   180 dmskdesadyvpmqdmkgtvkyadiessnyespydqylpsAPERtrrdtlinespalsymdLVGFSYQVANGMEFLASKN 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 745 YVHRDLAARNILVNQNLCCKVSDFGLTRLLDDfDGTYETQGGK-IPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFG 823
Cdd:cd05107   260 CVHRDLAARNVLICEGKLVKICDFGLARDIMR-DSNYISKGSTfLPLKWMAPESIFNNLYTTLSDVWSFGILLWEIFTLG 338
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038291632 824 DKPYGEMN-NQEVMKSIEEGYRLPPPVDCPAPLYELMKNCWAYDRARRPHFLQLQAHLEQLLT 885
Cdd:cd05107   339 GTPYPELPmNEQFYNAIKRGYRMAKPAHASDEIYEIMQKCWEEKFEIRPDFSQLVHLVGDLLT 401
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
605-884 1.69e-42

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: 160.58  E-value: 1.69e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 605 YEDPAQGALDFAQELDPTWLIVDTVIGEGEFGEVYRGALR--FPSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFN- 681
Cdd:cd05105    20 YVDPMQLPYDSRWEFPRDGLVLGRILGSGAFGKVVEGTAYglSRSQPVMKVAVKMLKPTARSSEKQALMSELKIMTHLGp 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 682 HPHILRLEGVVTKRKPIMIVTEFMENGALDAFL-KEREDQLAPG------------------------------------ 724
Cdd:cd05105   100 HLNIVNLLGACTKSGPIYIITEYCFYGDLVNYLhKNRDNFLSRHpekpkkdldifginpadestrsyvilsfenkgdymd 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 725 -------QLVAML---------------------------------------------------LGIASGMNYLSGHNYV 746
Cdd:cd05105   180 mkqadttQYVPMLeikeaskysdiqrsnydrpasykgsndsevknllsddgseglttldllsftYQVARGMEFLASKNCV 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 747 HRDLAARNILVNQNLCCKVSDFGLTRLLDDfDGTYETQGGK-IPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDK 825
Cdd:cd05105   260 HRDLAARNVLLAQGKIVKICDFGLARDIMH-DSNYVSKGSTfLPVKWMAPESIFDNLYTTLSDVWSYGILLWEIFSLGGT 338
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 826 PY-GEMNNQEVMKSIEEGYRLPPPVDCPAPLYELMKNCWAYDRARRPHFLQLQAHLEQLL 884
Cdd:cd05105   339 PYpGMIVDSTFYNKIKSGYRMAKPDHATQEVYDIMVKCWNSEPEKRPSFLHLSDIVESLL 398
EphR_LBD_B3 cd10478
Ligand Binding Domain of Ephrin type-B Receptor 3; Ephrin receptors (EphRs) comprise the ...
27-203 1.88e-42

Ligand Binding Domain of Ephrin type-B Receptor 3; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EhpB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. EphB3 plays a role in cell positioning in the gastrointestinal tract by being preferentially expressed in Paneth cells. It also has been implicated in early colorectal cancer and early stage squamous cell lung cancer. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine 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).


Pssm-ID: 198446  Cd Length: 173  Bit Score: 152.86  E-value: 1.88e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632  27 EVTLMDTSKAQGELGWLLDPpEDGWSEVQ---QMLNgtPLYMYQDCPVEESgDTNHWLRSNWIYRgEEASRVHVELQFTV 103
Cdd:cd10478     1 EETLMDTKWVTSELAWTTHP-ESGWEEVSgydEAMN--PIRTYQVCNVRES-NQNNWLRTGFIPR-RDVQRVYVELKFTV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 104 RDCKSFPGGAGpmGCKETFNLLYMESDQDVGIQLRRPLFQ----KVTTVAADQSFTIRDlaSGAVKLNVErcSLGRLTHR 179
Cdd:cd10478    76 RDCNSIPNIPG--SCKETFNLFYYESDSDSASASSPFWMEnpyvKVDTIAPDESFSRLD--SGRVNTKVR--SFGPLSKA 149
                         170       180
                  ....*....|....*....|....
gi 2038291632 180 GLYLAFHNPGSCVALVSVRVFYQR 203
Cdd:cd10478   150 GFYLAFQDLGACMSLISVRAFFKK 173
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
630-883 2.56e-42

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: 155.89  E-value: 2.56e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRfpsqDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGA 709
Cdd:cd14066     1 IGSGGFGTVYKGVLE----NGTVVAVKRLNEMNCAASKKEFLTELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPNGS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 710 LDAFLKEREDQ--LAPGQLVAMLLGIASGMNYL---SGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYETQ 784
Cdd:cd14066    77 LEDRLHCHKGSppLPWPQRLKIAKGIARGLEYLheeCPPPIIHGDIKSSNILLDEDFEPKLTDFGLARLIPPSESVSKTS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 785 GGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNN--------QEVMKSIEEGYR---LPPPVDCPA 853
Cdd:cd14066   157 AVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLT-GKPAVDENREnasrkdlvEWVESKGKEELEdilDKRLVDDDG 235
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2038291632 854 PLYELMKN-------CWAYDRARRPHFLQLQAHLEQL 883
Cdd:cd14066   236 VEEEEVEAllrlallCTRSDPSLRPSMKEVVQMLEKL 272
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
629-884 2.92e-42

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: 157.83  E-value: 2.92e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGAL--RFPSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQF-NHPHILRLEGVVTKRK-PIMIVTEF 704
Cdd:cd05102    14 VLGHGAFGKVVEASAfgIDKSSSCETVAVKMLKEGATASEHKALMSELKILIHIgNHLNVVNLLGACTKPNgPLMVIVEF 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 705 MENGALDAFLKEREDQLAP---------GQLVAML--------------------------------------------- 730
Cdd:cd05102    94 CKYGNLSNFLRAKREGFSPyrersprtrSQVRSMVeavradrrsrqgsdrvasftestsstnqprqevddlwqspltmed 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 731 -----LGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRllDDF-DGTYETQG-GKIPIRWTAPEAIAHRIF 803
Cdd:cd05102   174 licysFQVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLAR--DIYkDPDYVRKGsARLPLKWMAPESIFDKVY 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 804 TTASDVWSFGIVMWEVLSFGDKPY-GEMNNQEVMKSIEEGYRLPPPVDCPAPLYELMKNCWAYDRARRPHFLQLQAHLEQ 882
Cdd:cd05102   252 TTQSDVWSFGVLLWEIFSLGASPYpGVQINEEFCQRLKDGTRMRAPEYATPEIYRIMLSCWHGDPKERPTFSDLVEILGD 331

                  ..
gi 2038291632 883 LL 884
Cdd:cd05102   332 LL 333
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
605-884 2.25e-41

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: 156.22  E-value: 2.25e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 605 YEDPAQGALDFAQELDPTWLIVDTVIGEGEFGEVYRGALR--FPSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQF-N 681
Cdd:cd05104    18 YIDPTQLPYDHKWEFPRDRLRFGKTLGAGAFGKVVEATAYglAKADSAMTVAVKMLKPSAHSTEREALMSELKVLSYLgN 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 682 HPHILRLEGVVTKRKPIMIVTEFMENGALDAFLKEREDQ----------------------------------LAPG--- 724
Cdd:cd05104    98 HINIVNLLGACTVGGPTLVITEYCCYGDLLNFLRRKRDSficpkfedlaeaalyrnllhqremacdslneymdMKPSvsy 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 725 -------------------------------------QLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSD 767
Cdd:cd05104   178 vvptkadkrrgvrsgsyvdqdvtseileedelaldteDLLSFSYQVAKGMEFLASKNCIHRDLAARNILLTHGRITKICD 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 768 FGLTRLLDDfDGTYETQG-GKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMN-NQEVMKSIEEGYRL 845
Cdd:cd05104   258 FGLARDIRN-DSNYVVKGnARLPVKWMAPESIFECVYTFESDVWSYGILLWEIFSLGSSPYPGMPvDSKFYKMIKEGYRM 336
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 2038291632 846 PPPVDCPAPLYELMKNCWAYDRARRPHFLQLQAHLEQLL 884
Cdd:cd05104   337 DSPEFAPSEMYDIMRSCWDADPLKRPTFKQIVQLIEQQL 375
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
629-876 4.79e-41

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: 152.75  E-value: 4.79e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEV--YRGAlrfPSQD--CKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKR--KPIMIVT 702
Cdd:cd05080    11 DLGEGHFGKVslYCYD---PTNDgtGEMVAVKALKADCGPQHRSGWKQEIDILKTLYHENIVKYKGCCSEQggKSLQLIM 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 703 EFMENGALDAFLKEREDQLApgQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYE 782
Cdd:cd05080    88 EYVPLGSLRDYLPKHSIGLA--QLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAKAVPEGHEYYR 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 783 -TQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDkPY---------------GEMNNQEVMKSIEEGYRLP 846
Cdd:cd05080   166 vREDGDSPVFWYAPECLKEYKFYYASDVWSFGVTLYELLTHCD-SSqspptkflemigiaqGQMTVVRLIELLERGERLP 244
                         250       260       270
                  ....*....|....*....|....*....|
gi 2038291632 847 PPVDCPAPLYELMKNCWAYDRARRPHFLQL 876
Cdd:cd05080   245 CPDKCPQEVYHLMKNCWETEASFRPTFENL 274
SAM_EPH-A1 cd09542
SAM domain of EPH-A1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
912-974 8.51e-41

SAM domain of EPH-A1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A1 subfamily of the receptor tyrosine kinases is a C-terminal protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A1 receptors and appears to mediate cell-cell initiated signal transduction. Activation of these receptors leads to inhibition of cell spreading and migration in a RhoA-ROCK-dependent manner. EPH-A1 receptors are known to bind ILK (integrin-linked kinase) which is the mediator of interactions between integrin and the actin cytoskeleton. However SAM is not sufficient for this interaction; it rather plays an ancillary role. SAM domains of Eph-A1 receptors do not form homo/hetero dimers/oligomers. EphA1 gene was found expressed widely in differentiated epithelial cells. In a number of different malignant tumors EphA1 genes are downregulated. In breast carcinoma the downregulation is associated with invasive behavior of the cell.


Pssm-ID: 188941  Cd Length: 63  Bit Score: 143.99  E-value: 8.51e-41
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038291632 912 GIPYRSVSEWLESIRMKRYILHFRSAGLDTMECVLELTAEDLTQMGITLPGHQKRILCSIQGF 974
Cdd:cd09542     1 GIPYRSVSEWLESIRMKRYILHFRSAGLDTMECVLELTAEDLTQMGITLPGHQKRILCSIQGF 63
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
614-883 9.85e-41

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: 153.62  E-value: 9.85e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 614 DFAQELdptwLIVDTVIGEGEFGEVYR----GALRFPSqdCKTVAIKTLKDTSPDGQWWNFLREATIMGQF-NHPHILRL 688
Cdd:cd14207     3 EFARER----LKLGKSLGRGAFGKVVQasafGIKKSPT--CRVVAVKMLKEGATASEYKALMTELKILIHIgHHLNVVNL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 689 EGVVTKRK-PIMIVTEFMENGALDAFLKEREDQLAPGQ------------------------------------------ 725
Cdd:cd14207    77 LGACTKSGgPLMVIVEYCKYGNLSNYLKSKRDFFVTNKdtslqeelikekkeaeptggkkkrlesvtssesfassgfqed 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 726 -------------------------LVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRllDDF-DG 779
Cdd:cd14207   157 kslsdveeeeedsgdfykrpltmedLISYSFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLAR--DIYkNP 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 780 TYETQG-GKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPY-GEMNNQEVMKSIEEGYRLPPPVDCPAPLYE 857
Cdd:cd14207   235 DYVRKGdARLPLKWMAPESIFDKIYSTKSDVWSYGVLLWEIFSLGASPYpGVQIDEDFCSKLKEGIRMRAPEFATSEIYQ 314
                         330       340
                  ....*....|....*....|....*.
gi 2038291632 858 LMKNCWAYDRARRPHFLQLQAHLEQL 883
Cdd:cd14207   315 IMLDCWQGDPNERPRFSELVERLGDL 340
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
629-883 1.96e-40

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: 150.14  E-value: 1.96e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRfpsqdCKTVAIKTLK---DTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFM 705
Cdd:cd14148     1 IIGVGGFGKVYKGLWR-----GEEVAVKAARqdpDEDIAVTAENVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVMEYA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 706 ENGALDAFLKERedQLAPGQLVAMLLGIASGMNYLsgHN-----YVHRDLAARNILV-----NQNL---CCKVSDFGLTR 772
Cdd:cd14148    76 RGGALNRALAGK--KVPPHVLVNWAVQIARGMNYL--HNeaivpIIHRDLKSSNILIlepieNDDLsgkTLKITDFGLAR 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 773 LLDDFD-----GTYEtqggkipirWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSIE-EGYRLP 846
Cdd:cd14148   152 EWHKTTkmsaaGTYA---------WMAPEVIRLSLFSKSSDVWSFGVLLWELLT-GEVPYREIDALAVAYGVAmNKLTLP 221
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2038291632 847 PPVDCPAPLYELMKNCWAYDRARRPHFLQLQAHLEQL 883
Cdd:cd14148   222 IPSTCPEPFARLLEECWDPDPHGRPDFGSILKRLEDI 258
EphR_LBD_B1 cd10476
Ligand Binding Domain of Ephrin type-B Receptor 1; Ephrin receptors (EphRs) comprise the ...
29-203 2.25e-39

Ligand Binding Domain of Ephrin type-B Receptor 1; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EhpB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. Using EphB1 knockout-mice, EphB1 has been shown to be essential to the development of long-term potentiation (LTP), a cellular model of synaptic plasticity, learning and memory formation. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine 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).


Pssm-ID: 198444  Cd Length: 176  Bit Score: 144.04  E-value: 2.25e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632  29 TLMDTSKAQGELGWLLDPpEDGWSEVQQM-LNGTPLYMYQDCPVEESgDTNHWLRSNWIYRgEEASRVHVELQFTVRDCK 107
Cdd:cd10476     2 TLMDTRTATAELGWTANP-ASGWEEVSGYdENLNTIRTYQVCNVFEP-NQNNWLLTTFINR-RGAHRIYTEMRFTVRDCS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 108 SFPGGAGpmGCKETFNLLYMESDQDVGIQLR----RPLFQKVTTVAADQSFTIRDLASGAVKLNVERCSLGRLTHRGLYL 183
Cdd:cd10476    79 SLPNVPG--SCKETFNLYYYETDSVIATKKSafwtEAPYLKVDTIAADESFSQVDFGGRLMKVNTEVRSFGPLTRNGFYL 156
                         170       180
                  ....*....|....*....|
gi 2038291632 184 AFHNPGSCVALVSVRVFYQR 203
Cdd:cd10476   157 AFQDYGACMSLLSVRVFFKK 176
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
602-884 5.54e-39

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: 149.22  E-value: 5.54e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 602 LQAYE-------DPAQGALDFAQELDPTWLIVDTVIGEGEFGEVYRG-ALRFPSQD-CKTVAIKTLKDTSPDGQWWNFLR 672
Cdd:cd05106    11 IEAAEgnnytfiDPTQLPYNEKWEFPRDNLQFGKTLGAGAFGKVVEAtAFGLGKEDnVLRVAVKMLKASAHTDEREALMS 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 673 EATIMGQF-NHPHILRLEGVVTKRKPIMIVTEFMENGALDAFLKERED-------------------------------- 719
Cdd:cd05106    91 ELKILSHLgQHKNIVNLLGACTHGGPVLVITEYCCYGDLLNFLRKKAEtflnfvmalpeisetssdyknitlekkyirsd 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 720 ------------QLAPGQ-------------------------LVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLC 762
Cdd:cd05106   171 sgfssqgsdtyvEMRPVSssssqssdskdeedtedswpldlddLLRFSSQVAQGMDFLASKNCIHRDVAARNVLLTDGRV 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 763 CKVSDFGLTRLLDDfDGTYETQG-GKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPY-GEMNNQEVMKSIE 840
Cdd:cd05106   251 AKICDFGLARDIMN-DSNYVVKGnARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGKSPYpGILVNSKFYKMVK 329
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 2038291632 841 EGYRLPPPVDCPAPLYELMKNCWAYDRARRPHFLQLQAHLEQLL 884
Cdd:cd05106   330 RGYQMSRPDFAPPEIYSIMKMCWNLEPTERPTFSQISQLIQRQL 373
EphR_LBD_B4 cd10474
Ligand Binding Domain of Ephrin type-B Receptor 4; Ephrin receptors (EphRs) comprise the ...
27-203 5.98e-39

Ligand Binding Domain of Ephrin type-B Receptor 4; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EhpB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. EphB4 plays a role in osteoblast differentiation and has been linked to multiple myeloma. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine 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).


Pssm-ID: 198442  Cd Length: 180  Bit Score: 142.79  E-value: 5.98e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632  27 EVTLMDTSKAQGELGWLLDPPEDG-WSEVQQM-LNGTPLYMYQDCPVEESGDTNHWLRSNWIYRGEeASRVHVELQFTVR 104
Cdd:cd10474     1 EETLLNTKLETADLKWVTYPQVDGqWEELSGLdEEQHSVRTYEVCDAQRAGGQAHWLRTGWVPRRG-AVHVYATLRFTML 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 105 DCKSFPGGAgpMGCKETFNLLYMESDQDVGIQLRRPLFQ----KVTTVAADQSFTIRDLASGAVKLNVERCSLGRLTHRG 180
Cdd:cd10474    80 ECLSLPRAG--RSCKETFTVFYYESDADTATAHTPAWMEnpyiKVDTVAAEHLTRKRPGAEATGKVNVKTLRLGPLSKAG 157
                         170       180
                  ....*....|....*....|...
gi 2038291632 181 LYLAFHNPGSCVALVSVRVFYQR 203
Cdd:cd10474   158 FYLAFQDQGACMALLSLHLFYKK 180
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
626-905 6.71e-39

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 151.70  E-value: 6.71e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 626 VDTVIGEGEFGEVYRGalRFPSQDcKTVAIKTLKDTSPDGQWW--NFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTE 703
Cdd:COG0515    11 ILRLLGRGGMGVVYLA--RDLRLG-RPVALKVLRPELAADPEAreRFRREARALARLNHPNIVRVYDVGEEDGRPYLVME 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 704 FMENGALDAFLKEREdQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDfdgTYET 783
Cdd:COG0515    88 YVEGESLADLLRRRG-PLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGG---ATLT 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 784 QGGKIP--IRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSIEEGYRLPPPV---DCPAPLYEL 858
Cdd:COG0515   164 QTGTVVgtPGYMAPEQARGEPVDPRSDVYSLGVTLYELLT-GRPPFDGDSPAELLRAHLREPPPPPSElrpDLPPALDAI 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2038291632 859 MKNCWAYDRARRPH-FLQLQAHLEQLLTDPHSLRTIANFDPRVTLRLP 905
Cdd:COG0515   243 VLRALAKDPEERYQsAAELAAALRAVLRSLAAAAAAAAAAAAAAAAAA 290
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
630-884 2.98e-38

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: 143.35  E-value: 2.98e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGalRFPSQDcktVAIKTLKDTSPDGqwwNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGA 709
Cdd:cd14058     1 VGRGSFGVVCKA--RWRNQI---VAVKIIESESEKK---AFEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGGS 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 710 LDAFLKEREDQLA--PGQLVAMLLGIASGMNYLsgHNY-----VHRDLAARNIL-VNQNLCCKVSDFGLTRlldDFDgTY 781
Cdd:cd14058    73 LYNVLHGKEPKPIytAAHAMSWALQCAKGVAYL--HSMkpkalIHRDLKPPNLLlTNGGTVLKICDFGTAC---DIS-TH 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 782 ETQGgKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQ--EVMKSIEEGYRLPPPVDCPAPLYELM 859
Cdd:cd14058   147 MTNN-KGSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVIT-RRKPFDHIGGPafRIMWAVHNGERPPLIKNCPKPIESLM 224
                         250       260
                  ....*....|....*....|....*
gi 2038291632 860 KNCWAYDRARRPHFLQLQAHLEQLL 884
Cdd:cd14058   225 TRCWSKDPEKRPSMKEIVKIMSHLM 249
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
629-883 4.27e-38

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: 143.64  E-value: 4.27e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRfpSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENG 708
Cdd:cd14146     1 IIGVGGFGKVYRATWK--GQEVAVKAARQDPDEDIKATAESVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEFARGG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 ALDAFL--------KEREDQLAPGQLVAMLLGIASGMNYLSGHNYV---HRDLAARNILV-----NQNLC---CKVSDFG 769
Cdd:cd14146    79 TLNRALaaanaapgPRRARRIPPHILVNWAVQIARGMLYLHEEAVVpilHRDLKSSNILLlekieHDDICnktLKITDFG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 770 LTRLLD-----DFDGTYEtqggkipirWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSIE-EGY 843
Cdd:cd14146   159 LAREWHrttkmSAAGTYA---------WMAPEVIKSSLFSKGSDIWSYGVLLWELLT-GEVPYRGIDGLAVAYGVAvNKL 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2038291632 844 RLPPPVDCPAPLYELMKNCWAYDRARRPHFLQLqahLEQL 883
Cdd:cd14146   229 TLPIPSTCPEPFAKLMKECWEQDPHIRPSFALI---LEQL 265
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
624-883 4.93e-38

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: 143.25  E-value: 4.93e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 624 LIVDTVIGEGEFGEVYRGALRfpsqdCKTVAIKTLK-----DTSPDGQwwNFLREATIMGQFNHPHILRLEGVVTKRKPI 698
Cdd:cd14147     5 LRLEEVIGIGGFGKVYRGSWR-----GELVAVKAARqdpdeDISVTAE--SVRQEARLFAMLAHPNIIALKAVCLEEPNL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 699 MIVTEFMENGALDAFLKERedQLAPGQLVAMLLGIASGMNYLSGHNYV---HRDLAARNILVNQN--------LCCKVSD 767
Cdd:cd14147    78 CLVMEYAAGGPLSRALAGR--RVPPHVLVNWAVQIARGMHYLHCEALVpviHRDLKSNNILLLQPienddmehKTLKITD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 768 FGLTRLLDDFD-----GTYEtqggkipirWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSIE-E 841
Cdd:cd14147   156 FGLAREWHKTTqmsaaGTYA---------WMAPEVIKASTFSKGSDVWSFGVLLWELLT-GEVPYRGIDCLAVAYGVAvN 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2038291632 842 GYRLPPPVDCPAPLYELMKNCWAYDRARRPHFLQLQAHLEQL 883
Cdd:cd14147   226 KLTLPIPSTCPEPFAQLMADCWAQDPHRRPDFASILQQLEAL 267
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
618-885 3.49e-37

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: 140.95  E-value: 3.49e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 618 ELDPTWLIVDTVIGEGEFGEVYRGalrFPSQDckTVAIKTLK---DTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTK 694
Cdd:cd14145     2 EIDFSELVLEEIIGIGGFGKVYRA---IWIGD--EVAVKAARhdpDEDISQTIENVRQEAKLFAMLKHPNIIALRGVCLK 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 695 RKPIMIVTEFMENGALDAFLKERedQLAPGQLVAMLLGIASGMNYLsgHN-----YVHRDLAARNILVNQ--------NL 761
Cdd:cd14145    77 EPNLCLVMEFARGGPLNRVLSGK--RIPPDILVNWAVQIARGMNYL--HCeaivpVIHRDLKSSNILILEkvengdlsNK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 762 CCKVSDFGLTRLLD-----DFDGTYEtqggkipirWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVM 836
Cdd:cd14145   153 ILKITDFGLAREWHrttkmSAAGTYA---------WMAPEVIRSSMFSKGSDVWSYGVLLWELLT-GEVPFRGIDGLAVA 222
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2038291632 837 KSIE-EGYRLPPPVDCPAPLYELMKNCWAYDRARRPHFLQLqahLEQLLT 885
Cdd:cd14145   223 YGVAmNKLSLPIPSTCPEPFARLMEDCWNPDPHSRPPFTNI---LDQLTA 269
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
629-879 4.68e-37

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: 140.03  E-value: 4.68e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRgALRFPSQdcKTVAIKTLKDTSPDgQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENG 708
Cdd:cd05122     7 KIGKGGFGVVYK-ARHKKTG--QIVAIKKINLESKE-KKESILNEIAILKKCKHPNIVKYYGSYLKKDELWIVMEFCSGG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 ALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYETQGGKI 788
Cdd:cd05122    83 SLKDLLKNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQLSDGKTRNTFVGTPY 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 789 pirWTAPEAIAHRIFTTASDVWSFGIVMWEvLSFGDKPYGEMNNQEVMKSI--EEGYRLPPPVDCPAPLYELMKNCWAYD 866
Cdd:cd05122   163 ---WMAPEVIQGKPYGFKADIWSLGITAIE-MAEGKPPYSELPPMKALFLIatNGPPGLRNPKKWSKEFKDFLKKCLQKD 238
                         250
                  ....*....|...
gi 2038291632 867 RARRPHFLQLQAH 879
Cdd:cd05122   239 PEKRPTAEQLLKH 251
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
630-881 6.97e-37

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: 139.45  E-value: 6.97e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRfpsqdcKTVAIKTLKDTSP-DGQWWNFLREATIMGQFNHPHILRLEGVVTKRKpIMIVTEFMENG 708
Cdd:cd14062     1 IGSGSFGTVYKGRWH------GDVAVKKLNVTDPtPSQLQAFKNEVAVLRKTRHVNILLFMGYMTKPQ-LAIVTQWCEGS 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 ALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYETQGGKI 788
Cdd:cd14062    74 SLYKHLHVLETKFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLATVKTRWSGSQQFEQPTG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 789 PIRWTAPEAIahRI-----FTTASDVWSFGIVMWEVLSfGDKPYGEMNNQE-VMKSIEEGYrLPPPV-----DCPAPLYE 857
Cdd:cd14062   154 SILWMAPEVI--RMqdenpYSFQSDVYAFGIVLYELLT-GQLPYSHINNRDqILFMVGRGY-LRPDLskvrsDTPKALRR 229
                         250       260
                  ....*....|....*....|....
gi 2038291632 858 LMKNCWAYDRARRPHFLQLQAHLE 881
Cdd:cd14062   230 LMEDCIKFQRDERPLFPQILASLE 253
Pkinase pfam00069
Protein kinase domain;
624-879 6.69e-36

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 135.45  E-value: 6.69e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 624 LIVDTVIGEGEFGEVYRGALRfpsQDCKTVAIKTL-KDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVT 702
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHR---DTGKIVAIKKIkKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 703 EFMENGALDAFLKEREdQLAPGQLVAMLLGIASGMNYLSghnyvhrdlaarnilvnqnlcckvsdfgltrLLDDFDGTYE 782
Cdd:pfam00069  78 EYVEGGSLFDLLSEKG-AFSEREAKFIMKQILEGLESGS-------------------------------SLTTFVGTPW 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 783 tqggkipirWTAPEAIAHRIFTTASDVWSFGIVMWEVLsFGDKPYGEMNNQEVMKSI--EEGYRLPPPVDCPAPLYELMK 860
Cdd:pfam00069 126 ---------YMAPEVLGGNPYGPKVDVWSLGCILYELL-TGKPPFPGINGNEIYELIidQPYAFPELPSNLSEEAKDLLK 195
                         250
                  ....*....|....*....
gi 2038291632 861 NCWAYDRARRPHFLQLQAH 879
Cdd:pfam00069 196 KLLKKDPSKRLTATQALQH 214
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
623-879 1.01e-35

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: 136.11  E-value: 1.01e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 623 WLIVDTvIGEGEFGEVYRGalrfpsQDCKT---VAIKTL-KDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPI 698
Cdd:cd14003     2 YELGKT-LGEGSFGKVKLA------RHKLTgekVAIKIIdKSKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVIETENKI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 699 MIVTEFMENGAL------DAFLKEREDQLAPGQLVamllgiaSGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTR 772
Cdd:cd14003    75 YLVMEYASGGELfdyivnNGRLSEDEARRFFQQLI-------SAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSN 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 773 LLDDfDGTYETQGGKIPirWTAPEAIAHRIF-TTASDVWSFGIVMWeVLSFGDKPYGEMNNQEVMKSIEEG-YRLPPPVd 850
Cdd:cd14003   148 EFRG-GSLLKTFCGTPA--YAAPEVLLGRKYdGPKADVWSLGVILY-AMLTGYLPFDDDNDSKLFRKILKGkYPIPSHL- 222
                         250       260
                  ....*....|....*....|....*....
gi 2038291632 851 cPAPLYELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd14003   223 -SPDARDLIRRMLVVDPSKRITIEEILNH 250
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
630-880 2.39e-35

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: 134.93  E-value: 2.39e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRfpsQDCKTVAIKTLKDTSPDGqwwNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGA 709
Cdd:cd14065     1 LGKGFFGEVYKVTHR---ETGKVMVMKELKRFDEQR---SFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 710 LDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILV---NQNLCCKVSDFGLTRLLDDFDGTYETQGG 786
Cdd:cd14065    75 LEELLKSMDEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVreaNRGRNAVVADFGLAREMPDEKTKKPDRKK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 787 KIPI----RWTAPEAIAHRIFTTASDVWSFGIVMWEVLsfgdkpyGEMN-NQEVMKSIE------EGYRLPPPVDCPAPL 855
Cdd:cd14065   155 RLTVvgspYWMAPEMLRGESYDEKVDVFSFGIVLCEII-------GRVPaDPDYLPRTMdfgldvRAFRTLYVPDCPPSF 227
                         250       260
                  ....*....|....*....|....*
gi 2038291632 856 YELMKNCWAYDRARRPHFLQLQAHL 880
Cdd:cd14065   228 LPLAIRCCQLDPEKRPSFVELEHHL 252
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
629-879 6.24e-35

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: 134.19  E-value: 6.24e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGalrfpsQDCKT---VAIKTLKDTSPDGQWWNFL-REATIMGQFNHPHILRLEGVVTKRKPIMIVTEF 704
Cdd:cd06606     7 LLGKGSFGSVYLA------LNLDTgelMAVKEVELSGDSEEELEALeREIRILSSLKHPNIVRYLGTERTENTLNIFLEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 705 MENGALDAFLKE----REDQLApgQLVAMLLgiaSGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDfdgt 780
Cdd:cd06606    81 VPGGSLASLLKKfgklPEPVVR--KYTRQIL---EGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKRLAE---- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 781 YETQGGKIPIR----WTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQ-EVMKSIEEGYRLPP-PVDCPAP 854
Cdd:cd06606   152 IATGEGTKSLRgtpyWMAPEVIRGEGYGRAADIWSLGCTVIEMAT-GKPPWSELGNPvAALFKIGSSGEPPPiPEHLSEE 230
                         250       260
                  ....*....|....*....|....*
gi 2038291632 855 LYELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd06606   231 AKDFLRKCLQRDPKKRPTADELLQH 255
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
630-883 4.17e-34

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: 132.06  E-value: 4.17e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRfpsqdcKTVAIKTLKDTSPDG-QWWNFLREATIMGQFNHPHILRLEGVVTkRKPIMIVTEFMENG 708
Cdd:cd14150     8 IGTGSFGTVFRGKWH------GDVAVKILKVTEPTPeQLQAFKNEMQVLRKTRHVNILLFMGFMT-RPNFAIITQWCEGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 ALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYETQGGKI 788
Cdd:cd14150    81 SLYRHLHVTETRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLATVKTRWSGSQQVEQPSG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 789 PIRWTAPEAIAHR---IFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQ-EVMKSIEEGYrLPPPV-----DCPAPLYELM 859
Cdd:cd14150   161 SILWMAPEVIRMQdtnPYSFQSDVYAYGVVLYELMS-GTLPYSNINNRdQIIFMVGRGY-LSPDLsklssNCPKAMKRLL 238
                         250       260
                  ....*....|....*....|....
gi 2038291632 860 KNCWAYDRARRPHFLQLQAHLEQL 883
Cdd:cd14150   239 IDCLKFKREERPLFPQILVSIELL 262
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
630-871 5.69e-34

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: 131.56  E-value: 5.69e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALrFPSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGA 709
Cdd:cd05042     3 IGNGWFGKVLLGEI-YSGTSVAQVVVKELKASANPKEQDTFLKEGQPYRILQHPNILQCLGQCVEAIPYLLVMEFCDLGD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 710 LDAFLK-EREDQLAPGQ---LVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGL--TRLLDDFdgtYET 783
Cdd:cd05042    82 LKAYLRsEREHERGDSDtrtLQRMACEVAAGLAHLHKLNFVHSDLALRNCLLTSDLTVKIGDYGLahSRYKEDY---IET 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 784 QGGK-IPIRWTAPEAIA--HRIFTTA-----SDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSI--EEGYRLPPPvDCPA 853
Cdd:cd05042   159 DDKLwFPLRWTAPELVTefHDRLLVVdqtkySNIWSLGVTLWELFENGAQPYSNLSDLDVLAQVvrEQDTKLPKP-QLEL 237
                         250       260
                  ....*....|....*....|..
gi 2038291632 854 PL----YELMKNCWaYDRARRP 871
Cdd:cd05042   238 PYsdrwYEVLQFCW-LSPEQRP 258
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
631-876 6.65e-34

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: 131.06  E-value: 6.65e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 631 GEGEFGEVYRGALRFPSQDCKTVAIKTLKDTSPDGQWW--NFLREATIMGQFNHPHILRLEGVvTKRKPIMIVTEFMENG 708
Cdd:cd05037     8 GQGTFTNIYDGILREVGDGRVQEVEVLLKVLDSDHRDIseSFFETASLMSQISHKHLVKLYGV-CVADENIMVQEYVRYG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 ALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQN------LCCKVSDFGLTRLLddfdGTYE 782
Cdd:cd05037    87 PLDKYLRRMGNNVPLSWKLQVAKQLASALHYLEDKKLIHGNVRGRNILLAREgldgypPFIKLSDPGVPITV----LSRE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 783 TQGGKIPirWTAPEAI--AHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPvDCpAPLYELMK 860
Cdd:cd05037   163 ERVDRIP--WIAPECLrnLQANLTIAADKWSFGTTLWEICSGGEEPLSALSSQEKLQFYEDQHQLPAP-DC-AELAELIM 238
                         250
                  ....*....|....*.
gi 2038291632 861 NCWAYDRARRPHFLQL 876
Cdd:cd05037   239 QCWTYEPTKRPSFRAI 254
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
631-883 7.36e-34

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: 130.46  E-value: 7.36e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 631 GEGEFGEVYRGalRFPSQDcKTVAIKTLKDTSpdgqwwnflREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGAL 710
Cdd:cd14060     2 GGGSFGSVYRA--IWVSQD-KEVAVKKLLKIE---------KEAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGSL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 711 DAFLKERE-DQLAPGQLVAMLLGIASGMNYLSGH---NYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDfdGTYETQGG 786
Cdd:cd14060    70 FDYLNSNEsEEMDMDQIMTWATDIAKGMHYLHMEapvKVIHRDLKSRNVVIAADGVLKICDFGASRFHSH--TTHMSLVG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 787 KIPirWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVM-KSIEEGYRLPPPVDCPAPLYELMKNCWAY 865
Cdd:cd14060   148 TFP--WMAPEVIQSLPVSETCDTYSYGVVLWEMLT-REVPFKGLEGLQVAwLVVEKNERPTIPSSCPRSFAELMRRCWEA 224
                         250
                  ....*....|....*...
gi 2038291632 866 DRARRPHFLQLQAHLEQL 883
Cdd:cd14060   225 DVKERPSFKQIIGILESM 242
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
630-883 8.08e-34

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: 131.48  E-value: 8.08e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRfpsQDCKTVAIKTLKDTSPDGQWwNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGA 709
Cdd:cd14154     1 LGKGFFGQAIKVTHR---ETGEVMVMKELIRFDEEAQR-NFLKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGGT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 710 LDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDD-------FDGTYE 782
Cdd:cd14154    77 LKDVLKDMARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLARLIVEerlpsgnMSPSET 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 783 TQGGKIPIR-----------WTAPEAIAHRIFTTASDVWSFGIVMWEVLS--FGDKPYGEMNNQEVMKsiEEGYRLPPPV 849
Cdd:cd14154   157 LRHLKSPDRkkrytvvgnpyWMAPEMLNGRSYDEKVDIFSFGIVLCEIIGrvEADPDYLPRTKDFGLN--VDSFREKFCA 234
                         250       260       270
                  ....*....|....*....|....*....|....
gi 2038291632 850 DCPAPLYELMKNCWAYDRARRPHFLQLQAHLEQL 883
Cdd:cd14154   235 GCPPPFFKLAFLCCDLDPEKRPPFETLEEWLEAL 268
EphR_LBD_B6 cd10475
Ligand Binding Domain of Ephrin type-B Receptor 6; Ephrin receptors (EphRs) comprise the ...
27-201 9.02e-34

Ligand Binding Domain of Ephrin type-B Receptor 6; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EhpB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. EphB6, a kinase-defective member of this family, is downregulated in MDA-MB-231-breast cancer cells and myeloid cancers and upregulated in neuroblasoma and glioblastoma. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine 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).


Pssm-ID: 198443  Cd Length: 180  Bit Score: 128.12  E-value: 9.02e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632  27 EVTLMDTSKAQGELGWLLDPPeDGWSEV-----QQMLNGTplymYQDCPVEESG-DTNHWLRSNWIYRgEEASRVHVELQ 100
Cdd:cd10475     1 EEVLLDTTGETSEIGWLTYPP-GGWDEVsvlddQRRLTRT----FEVCNVAAQGpGQDNWLRTHFIER-RGAHRVHVRLH 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 101 FTVRDCKSFPGGAGPmgCKETFNLLYMESDQDVGIQ------LRRplFQKVTTVAADQSFTiRDLASGA--VKLNVERCS 172
Cdd:cd10475    75 FSVRDCASLGVPGGT--CRETFTLYYRQADEPDEPAdksewhEGP--WTKVDTIAADESFP-ASLGKGGqgLQMNVKERS 149
                         170       180
                  ....*....|....*....|....*....
gi 2038291632 173 LGRLTHRGLYLAFHNPGSCVALVSVRVFY 201
Cdd:cd10475   150 FGPLTQRGFYLAFQDSGACLSLVAVKVFF 178
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
618-893 9.56e-33

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: 128.61  E-value: 9.56e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 618 ELDPTWLIVDTVIGEGEFGEVYRGALRfpsqdcKTVAIKTLKDTSPD-GQWWNFLREATIMGQFNHPHILRLEGVVTKRK 696
Cdd:cd14149     8 EIEASEVMLSTRIGSGSFGTVYKGKWH------GDVAVKILKVVDPTpEQFQAFRNEVAVLRKTRHVNILLFMGYMTKDN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 697 pIMIVTEFMENGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDD 776
Cdd:cd14149    82 -LAIVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 777 FDGTYETQGGKIPIRWTAPEAIA---HRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQ-EVMKSIEEGYRLPPPV--- 849
Cdd:cd14149   161 WSGSQQVEQPTGSILWMAPEVIRmqdNNPFSFQSDVYSYGIVLYELMT-GELPYSHINNRdQIIFMVGRGYASPDLSkly 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2038291632 850 -DCPAPLYELMKNCWAYDRARRPHFLQLQAHLEQLltdPHSLRTI 893
Cdd:cd14149   240 kNCPKAMKRLVADCIKKVKEERPLFPQILSSIELL---QHSLPKI 281
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
630-863 1.21e-32

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: 127.80  E-value: 1.21e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRfPSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGA 709
Cdd:cd05087     5 IGHGWFGKVFLGEVN-SGLSSTQVVVKELKASASVQDQMQFLEEAQPYRALQHTNLLQCLAQCAEVTPYLLVMEFCPLGD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 710 LDAFLK--EREDQLAPGQLV--AMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRL--LDDFdgtYET 783
Cdd:cd05087    84 LKGYLRscRAAESMAPDPLTlqRMACEVACGLLHLHRNNFVHSDLALRNCLLTADLTVKIGDYGLSHCkyKEDY---FVT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 784 QGGK-IPIRWTAPEAI--AHRIF-----TTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSI--EEGYRLPPPvDCPA 853
Cdd:cd05087   161 ADQLwVPLRWIAPELVdeVHGNLlvvdqTKQSNVWSLGVTIWELFELGNQPYRHYSDRQVLTYTvrEQQLKLPKP-QLKL 239
                         250
                  ....*....|....
gi 2038291632 854 PL----YELMKNCW 863
Cdd:cd05087   240 SLaerwYEVMQFCW 253
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
630-871 2.35e-32

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: 126.57  E-value: 2.35e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGAlrfpsqDCKT---VAIKTLK-DTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFM 705
Cdd:cd06627     8 IGRGAFGSVYKGL------NLNTgefVAIKQISlEKIPKSDLKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYIILEYV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 706 ENGALDAFLKEREDqlAPGQLVAMLLG-IASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGL-TRLLDDFDGTYET 783
Cdd:cd06627    82 ENGSLASIIKKFGK--FPESLVAVYIYqVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVaTKLNEVEKDENSV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 784 QGGkiPiRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLYELMKNCW 863
Cdd:cd06627   160 VGT--P-YWMAPEVIEMSGVTTASDIWSVGCTVIELLT-GNPPYYDLQPMAALFRIVQDDHPPLPENISPELRDFLLQCF 235

                  ....*...
gi 2038291632 864 AYDRARRP 871
Cdd:cd06627   236 QKDPTLRP 243
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
630-883 2.49e-32

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: 127.10  E-value: 2.49e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRfpsqdcKTVAIKTLKDTSPDGQWWN-FLREATIMGQFNHPHILRLEGVVTKRKpIMIVTEFMENG 708
Cdd:cd14151    16 IGSGSFGTVYKGKWH------GDVAVKMLNVTAPTPQQLQaFKNEVGVLRKTRHVNILLFMGYSTKPQ-LAIVTQWCEGS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 ALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYETQGGKI 788
Cdd:cd14151    89 SLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFEQLSG 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 789 PIRWTAPEAIAHR---IFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQ-EVMKSIEEGYrLPPPV-----DCPAPLYELM 859
Cdd:cd14151   169 SILWMAPEVIRMQdknPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRdQIIFMVGRGY-LSPDLskvrsNCPKAMKRLM 246
                         250       260
                  ....*....|....*....|....
gi 2038291632 860 KNCWAYDRARRPHFLQLQAHLEQL 883
Cdd:cd14151   247 AECLKKKRDERPLFPQILASIELL 270
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
630-880 3.89e-32

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: 126.60  E-value: 3.89e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALrFPSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGA 709
Cdd:cd14206     5 IGNGWFGKVILGEI-FSDYTPAQVVVKELRVSAGPLEQRKFISEAQPYRSLQHPNILQCLGLCTETIPFLLIMEFCQLGD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 710 LDAFLK--EREDQLAPG-------QLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRllDDFDGT 780
Cdd:cd14206    84 LKRYLRaqRKADGMTPDlptrdlrTLQRMAYEITLGLLHLHKNNYIHSDLALRNCLLTSDLTVRIGDYGLSH--NNYKED 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 781 YETQGGK--IPIRWTAPEAIA--HRIF-----TTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSI--EEGYRLPPP- 848
Cdd:cd14206   162 YYLTPDRlwIPLRWVAPELLDelHGNLivvdqSKESNVWSLGVTIWELFEFGAQPYRHLSDEEVLTFVvrEQQMKLAKPr 241
                         250       260       270
                  ....*....|....*....|....*....|....
gi 2038291632 849 VDCPAP--LYELMKNCWaYDRARRPHFLQLQAHL 880
Cdd:cd14206   242 LKLPYAdyWYEIMQSCW-LPPSQRPSVEELHLQL 274
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
670-884 1.79e-31

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: 124.30  E-value: 1.79e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 670 FLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRD 749
Cdd:cd14221    37 FLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGTLRGIIKSMDSHYPWSQRVSFAKDIASGMAYLHSMNIIHRD 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 750 LAARNILVNQNLCCKVSDFGLTRLL-DDFDGTYETQGGKIPIR-----------WTAPEAIAHRIFTTASDVWSFGIVMW 817
Cdd:cd14221   117 LNSHNCLVRENKSVVVADFGLARLMvDEKTQPEGLRSLKKPDRkkrytvvgnpyWMAPEMINGRSYDEKVDVFSFGIVLC 196
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2038291632 818 EVLSF--GDKPYgemnnqeVMKSIEEGY-------RLPPPvDCPAPLYELMKNCWAYDRARRPHFLQLQAHLEQLL 884
Cdd:cd14221   197 EIIGRvnADPDY-------LPRTMDFGLnvrgfldRYCPP-NCPPSFFPIAVLCCDLDPEKRPSFSKLEHWLETLR 264
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
652-875 1.77e-30

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: 121.34  E-value: 1.77e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 652 TVAIK--TLKDTSPDGQwwnfLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGALDAFLKEREDQLAPGQLVAM 729
Cdd:cd13992    27 TVAIKhiTFSRTEKRTI----LQELNQLKELVHDNLNKFIGICINPPNIAVVTEYCTRGSLQDVLLNREIKMDWMFKSSF 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 730 LLGIASGMNYL-SGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDfDGTYETQGGKIPIR--WTAPEAI-----AHR 801
Cdd:cd13992   103 IKDIVKGMNYLhSSSIGYHGRLKSSNCLVDSRWVVKLTDFGLRNLLEE-QTNHQLDEDAQHKKllWTAPELLrgsllEVR 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 802 IfTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVD------CPAPLYELMKNCWAYDRARRPHFLQ 875
Cdd:cd13992   182 G-TQKGDVYSFAIILYEILFRSDPFALEREVAIVEKVISGGNKPFRPELavlldeFPPRLVLLVKQCWAENPEKRPSFKQ 260
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
628-887 5.94e-30

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: 119.62  E-value: 5.94e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 628 TVIGEGEFGEVYRGALRfpsQDCKTVAIKTLKDTSPDGQwwNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMEN 707
Cdd:cd06614     6 EKIGEGASGEVYKATDR---ATGKEVAIKKMRLRKQNKE--LIINEILIMKECKHPNIVDYYDSYLVGDELWVVMEYMDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGltrllddfdgtYETQGGK 787
Cdd:cd06614    81 GSLTDIITQNPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFG-----------FAAQLTK 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 788 I-PIR--------WTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSIEEGyrLPPPVDCPAPLYEL 858
Cdd:cd06614   150 EkSKRnsvvgtpyWMAPEVIKRKDYGPKVDIWSLGIMCIEMAE-GEPPYLEEPPLRALFLITTK--GIPPLKNPEKWSPE 226
                         250       260       270
                  ....*....|....*....|....*....|...
gi 2038291632 859 MKN----CWAYDRARRPHFlqlqahlEQLLTDP 887
Cdd:cd06614   227 FKDflnkCLVKDPEKRPSA-------EELLQHP 252
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
630-881 2.48e-29

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: 117.63  E-value: 2.48e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRfpsqdCKTVAIKTLKDT--SPDGQWWNFLREATIMGQFNHPHILRLEGV-VTKRKPIMIVTEFME 706
Cdd:cd14064     1 IGSGSFGKVYKGRCR-----NKIVAIKRYRANtyCSKSDVDMFCREVSILCRLNHPCVIQFVGAcLDDPSQFAIVTQYVS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 707 NGALDAFLKEREDQLAPGQLVAMLLGIASGMNYL--SGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDgtyETQ 784
Cdd:cd14064    76 GGSLFSLLHEQKRVIDLQSKLIIAVDVAKGMEYLhnLTQPIIHRDLNSHNILLYEDGHAVVADFGESRFLQSLD---EDN 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 785 GGKIP--IRWTAPEAIAHRI-FTTASDVWSFGIVMWEVLSfGDKPYGEMnnQEVMKSIEEGY---RLPPPVDCPAPLYEL 858
Cdd:cd14064   153 MTKQPgnLRWMAPEVFTQCTrYSIKADVFSYALCLWELLT-GEIPFAHL--KPAAAAADMAYhhiRPPIGYSIPKPISSL 229
                         250       260
                  ....*....|....*....|...
gi 2038291632 859 MKNCWAYDRARRPHFLQLQAHLE 881
Cdd:cd14064   230 LMRGWNAEPESRPSFVEIVALLE 252
PTKc_Aatyk2 cd05086
Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs ...
630-863 5.82e-29

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: 117.27  E-value: 5.82e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFPSQDCKTVaIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGA 709
Cdd:cd05086     5 IGNGWFGKVLLGEIYTGTSVARVV-VKELKASANPKEQDDFLQQGEPYYILQHPNILQCVGQCVEAIPYLLVFEFCDLGD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 710 LDAFLKEREDQLApGQLVAMLLG-----IASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGL--TRLLDDFDGTYE 782
Cdd:cd05086    84 LKTYLANQQEKLR-GDSQIMLLQrmaceIAAGLAHMHKHNFLHSDLALRNCYLTSDLTVKVGDYGIgfSRYKEDYIETDD 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 783 TQggKIPIRWTAPEAIAHRI-------FTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSI--EEGYRLPPP-VDCP 852
Cdd:cd05086   163 KK--YAPLRWTAPELVTSFQdgllaaeQTKYSNIWSLGVTLWELFENAAQPYSDLSDREVLNHVikERQVKLFKPhLEQP 240
                         250
                  ....*....|...
gi 2038291632 853 AP--LYELMKNCW 863
Cdd:cd05086   241 YSdrWYEVLQFCW 253
SAM_EPH-R cd09488
SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH ...
914-974 7.96e-29

SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH (erythropoietin-producing hepatocyte) family of receptor tyrosine kinases is a C-terminal signal transduction module located in the cytoplasmic region of these receptors. SAM appears to mediate cell-cell initiated signal transduction via binding proteins to a conserved tyrosine that is phosphorylated. In some cases the SAM domain mediates homodimerization/oligomerization and plays a role in the clustering process necessary for signaling. EPH kinases are the largest family of receptor tyrosine kinases. They are classified into two groups based on their abilities to bind ephrin-A and ephrin-B ligands. The EPH receptors are involved in regulation of cell movement, shape, and attachment during embryonic development; they control cell-cell interactions in the vascular, nervous, epithelial, and immune systems, and in many tumors. They are potential molecular markers for cancer diagnostics and potential targets for cancer therapy.


Pssm-ID: 188887  Cd Length: 61  Bit Score: 109.63  E-value: 7.96e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2038291632 914 PYRSVSEWLESIRMKRYILHFRSAGLDTMECVLELTAEDLTQMGITLPGHQKRILCSIQGF 974
Cdd:cd09488     1 AFRSVGEWLESIKMGRYKENFTAAGYTSLDAVAQMTAEDLTRLGVTLVGHQKKILNSIQAL 61
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
630-888 1.09e-28

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: 116.44  E-value: 1.09e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFPSQDCktvAIKTLKDTSPDGQWWN-FLREATIMGQFNHPHILRLEGVVtkRKPIMIVTEFMENG 708
Cdd:cd14025     4 VGSGGFGQVYKVRHKHWKTWL---AIKCPPSLHVDDSERMeLLEEAKKMEMAKFRHILPVYGIC--SEPVGLVMEYMETG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 ALDAFLKEredQLAPGQL-VAMLLGIASGMNYLSGHN--YVHRDLAARNILVNQNLCCKVSDFGLTR---LLDDFDGTYE 782
Cdd:cd14025    79 SLEKLLAS---EPLPWELrFRIIHETAVGMNFLHCMKppLLHLDLKPANILLDAHYHVKISDFGLAKwngLSHSHDLSRD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 783 TQGGKIPirWTAPEAI--AHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNN-QEVMKSIEEGYR--LPP-----PVDCP 852
Cdd:cd14025   156 GLRGTIA--YLPPERFkeKNRCPDTKHDVYSFAIVIWGILT-QKKPFAGENNiLHIMVKVVKGHRpsLSPiprqrPSECQ 232
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2038291632 853 ApLYELMKNCWAYDRARRPHFLQLQAHLEQLLTDPH 888
Cdd:cd14025   233 Q-MICLMKRCWDQDPRKRPTFQDITSETENLLSLLE 267
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
630-883 6.70e-28

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: 114.52  E-value: 6.70e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALrfpsqDCKTVAIKTLKDTS----PDGQWwNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFM 705
Cdd:cd14158    23 LGEGGFGVVFKGYI-----NDKNVAVKKLAAMVdistEDLTK-QFEQEIQVMAKCQHENLVELLGYSCDGPQLCLVYTYM 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 706 ENGALDAFLKEREDQLAPG--QLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYET 783
Cdd:cd14158    97 PNGSLLDRLACLNDTPPLSwhMRCKIAQGTANGINYLHENNHIHRDIKSANILLDETFVPKISDFGLARASEKFSQTIMT 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 784 QGGKIPIRWTAPEAIAHRIfTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSIE----------EGYRLPPPVDCPA 853
Cdd:cd14158   177 ERIVGTTAYMAPEALRGEI-TPKSDIFSFGVVLLEIIT-GLPPVDENRDPQLLLDIKeeiedeektiEDYVDKKMGDWDS 254
                         250       260       270
                  ....*....|....*....|....*....|....
gi 2038291632 854 P----LYELMKNCWAYDRARRPHFLQLQAHLEQL 883
Cdd:cd14158   255 TsieaMYSVASQCLNDKKNRRPDIAKVQQLLQEL 288
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
628-871 1.18e-27

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: 113.25  E-value: 1.18e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 628 TVIGEGEFGEVYRGALRfpsqdCKTVAIKTL----KDTSPDGQWWNFLREATImgqfNHPHILRL---EGVVTKRKPIMI 700
Cdd:cd13979     9 EPLGSGGFGSVYKATYK-----GETVAVKIVrrrrKNRASRQSFWAELNAARL----RHENIVRVlaaETGTDFASLGLI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 701 VTEFMENGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDgt 780
Cdd:cd13979    80 IMEYCGNGTLQQLIYEGSEPLPLAHRILISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCSVKLGEGN-- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 781 yETQGGKIPIRWT----APEAIAHRIFTTASDVWSFGIVMWEvLSFGDKPYGEMnNQEVMKSIeEGYRLPPPVDcpaPLY 856
Cdd:cd13979   158 -EVGTPRSHIGGTytyrAPELLKGERVTPKADIYSFGITLWQ-MLTRELPYAGL-RQHVLYAV-VAKDLRPDLS---GLE 230
                         250       260
                  ....*....|....*....|....
gi 2038291632 857 E---------LMKNCWAYDRARRP 871
Cdd:cd13979   231 DsefgqrlrsLISRCWSAQPAERP 254
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
630-879 2.63e-27

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: 112.26  E-value: 2.63e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYrgaLRFPSQDCKTVAIKTLK---------DTSPDGQWWNFL----REATIMGQFNHPHILRLEGVV---T 693
Cdd:cd14008     1 LGRGSFGKVK---LALDTETGQLYAIKIFNksrlrkrreGKNDRGKIKNALddvrREIAIMKKLDHPNIVRLYEVIddpE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 694 KRKpIMIVTEFMENGALDAFL-KEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTR 772
Cdd:cd14008    78 SDK-LYLVLEYCEGGPVMELDsGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFGVSE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 773 LLDDFDGTYETQGGkipirwT----APEAIA--HRIFTT-ASDVWSFGIVMWeVLSFGDKPYGEMNNQEVMKSI-EEGYR 844
Cdd:cd14008   157 MFEDGNDTLQKTAG------TpaflAPELCDgdSKTYSGkAADIWALGVTLY-CLVFGRLPFNGDNILELYEAIqNQNDE 229
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2038291632 845 LPPPVDCPAPLYELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd14008   230 FPIPPELSPELKDLLRRMLEKDPEKRITLKEIKEH 264
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
630-884 2.73e-27

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: 112.70  E-value: 2.73e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGAlrfpSQDCKT-VAIKTLKDTSP--DGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFME 706
Cdd:cd14026     5 LSRGAFGTVSRAR----HADWRVtVAIKCLKLDSPvgDSERNCLLKEAEILHKARFSYILPILGICNEPEFLGIVTEYMT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 707 NGALDAFLKERED--QLAPGQLVAMLLGIASGMNYLsgHNY----VHRDLAARNILVNQNLCCKVSDFGLT--RLLDDFD 778
Cdd:cd14026    81 NGSLNELLHEKDIypDVAWPLRLRILYEIALGVNYL--HNMspplLHHDLKTQNILLDGEFHVKIADFGLSkwRQLSISQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 779 GTYET---QGGKIPirWTAPEAIAHRIFTTAS---DVWSFGIVMWEVLSfGDKPYGEMNNQ-EVMKSIEEGYRL-----P 846
Cdd:cd14026   159 SRSSKsapEGGTII--YMPPEEYEPSQKRRASvkhDIYSYAIIMWEVLS-RKIPFEEVTNPlQIMYSVSQGHRPdtgedS 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2038291632 847 PPVDCP--APLYELMKNCWAYDRARRPHFLQLQAHLEQLL 884
Cdd:cd14026   236 LPVDIPhrATLINLIESGWAQNPDERPSFLKCLIELEPVL 275
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
629-883 9.60e-27

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: 111.21  E-value: 9.60e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRfpsqdCKTVAIKTLkdTSPDGQWWNflREA----TIMgqFNHPHILRL-------EGVVTKrkp 697
Cdd:cd14056     2 TIGKGRYGEVWLGKYR-----GEKVAVKIF--SSRDEDSWF--RETeiyqTVM--LRHENILGFiaadiksTGSWTQ--- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 698 IMIVTEFMENGALDAFLKEREdqLAPGQLVAMLLGIASGMNYLsgHNYV----------HRDLAARNILVNQNLCCKVSD 767
Cdd:cd14056    68 LWLITEYHEHGSLYDYLQRNT--LDTEEALRLAYSAASGLAHL--HTEIvgtqgkpaiaHRDLKSKNILVKRDGTCCIAD 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 768 FGLTRllddfdgTYETQGGKIPI---------RWTAPEAIAHRIFTT------ASDVWSFGIVMWEVL----SFGDK--- 825
Cdd:cd14056   144 LGLAV-------RYDSDTNTIDIppnprvgtkRYMAPEVLDDSINPKsfesfkMADIYSFGLVLWEIArrceIGGIAeey 216
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2038291632 826 --PYGEM----NNQEVMKSIEEGYRLPPPVD-------CPAPLYELMKNCWAYDRARRPHFLQLQAHLEQL 883
Cdd:cd14056   217 qlPYFGMvpsdPSFEEMRKVVCVEKLRPPIPnrwksdpVLRSMVKLMQECWSENPHARLTALRVKKTLAKL 287
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
630-820 1.10e-26

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: 111.03  E-value: 1.10e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGalrFPSQDCKTVAIKTLK-DTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENG 708
Cdd:cd07829     7 LGEGTYGVVYKA---KDKKTGEIVALKKIRlDNEEEGIPSTALREISLLKELKHPNIVKLLDVIHTENKLYLVFEYCDQD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 aLDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLddfdgtyetqggKI 788
Cdd:cd07829    84 -LKKYLDKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGLARAF------------GI 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2038291632 789 PIR---------W-TAPEAIAH-RIFTTASDVWSFGIVMWEVL 820
Cdd:cd07829   151 PLRtythevvtlWyRAPEILLGsKHYSTAVDIWSVGCIFAELI 193
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
633-873 1.18e-26

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: 110.28  E-value: 1.18e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 633 GEFGEVYRGALRFPSQdcktVAIKTLKdTSPDGQWWN--FLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGAL 710
Cdd:cd14027     4 GGFGKVSLCFHRTQGL----VVLKTVY-TGPNCIEHNeaLLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKGNL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 711 DAFLKEREDQLA-PGQLVamlLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGL-------------TRLLDD 776
Cdd:cd14027    79 MHVLKKVSVPLSvKGRII---LEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLasfkmwskltkeeHNEQRE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 777 FDGTYETQGGKipIRWTAPEAI--AHRIFTTASDVWSFGIVMWEVLSfGDKPYGE-MNNQEVMKSIEEGYR-----LPPp 848
Cdd:cd14027   156 VDGTAKKNAGT--LYYMAPEHLndVNAKPTEKSDVYSFAIVLWAIFA-NKEPYENaINEDQIIMCIKSGNRpdvddITE- 231
                         250       260
                  ....*....|....*....|....*
gi 2038291632 849 vDCPAPLYELMKNCWAYDRARRPHF 873
Cdd:cd14027   232 -YCPREIIDLMKLCWEANPEARPTF 255
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
625-849 1.49e-26

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: 109.87  E-value: 1.49e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 625 IVDTVIGEGEFGEVYRGALRfpsQDCKTVAIKTL-KDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTE 703
Cdd:cd05117     3 ELGKVLGRGSFGVVRLAVHK---KTGEEYAVKIIdKKKLKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 704 FMENGALDAFLKER----EDQLApgQLVAMLLgiaSGMNYLSGHNYVHRDLAARNILV---NQNLCCKVSDFGLTRLLDD 776
Cdd:cd05117    80 LCTGGELFDRIVKKgsfsEREAA--KIMKQIL---SAVAYLHSQGIVHRDLKPENILLaskDPDSPIKIIDFGLAKIFEE 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038291632 777 FDGTYETQGgkipirwT----APEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSIEEG-YRLPPPV 849
Cdd:cd05117   155 GEKLKTVCG-------TpyyvAPEVLKGKGYGKKCDIWSLGVILYILLC-GYPPFYGETEQELFEKILKGkYSFDSPE 224
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
630-829 1.52e-26

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: 110.28  E-value: 1.52e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALrfpsQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGA 709
Cdd:cd14664     1 IGRGGAGTVYKGVM----PNGTLVAVKRLKGEGTQGGDHGFQAEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPNGS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 710 LDAFLKEREDQLAPGQLVA---MLLGIASGMNYLSGH---NYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDfDGTYET 783
Cdd:cd14664    77 LGELLHSRPESQPPLDWETrqrIALGSARGLAYLHHDcspLIIHRDVKSNNILLDEEFEAHVADFGLAKLMDD-KDSHVM 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2038291632 784 QGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGE 829
Cdd:cd14664   156 SSVAGSYGYIAPEYAYTGKVSEKSDVYSYGVVLLELIT-GKRPFDE 200
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
624-883 4.55e-26

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: 108.59  E-value: 4.55e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 624 LIVDTVIGEGEFGEVYRGALRfpsqdcKTVAIKTLK-DTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVT 702
Cdd:cd14063     2 LEIKEVIGKGRFGRVHRGRWH------GDVAIKLLNiDYLNEEQLEAFKEEVAAYKNTRHDNLVLFMGACMDPPHLAIVT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 703 EFMENGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQnlcCKV--SDFGLTRlLDDFDGT 780
Cdd:cd14063    76 SLCKGRTLYSLIHERKEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLEN---GRVviTDFGLFS-LSGLLQP 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 781 YETQGG-KIPIRWT---APEAI-AHRI---------FTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSIEEGYRLP 846
Cdd:cd14063   152 GRREDTlVIPNGWLcylAPEIIrALSPdldfeeslpFTKASDVYAFGTVWYELLA-GRWPFKEQPAESIIWQVGCGKKQS 230
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2038291632 847 PP-VDCPAPLYELMKNCWAYDRARRPHFLQLQAHLEQL 883
Cdd:cd14063   231 LSqLDIGREVKDILMQCWAYDPEKRPTFSDLLRMLERL 268
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
626-848 6.50e-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: 107.74  E-value: 6.50e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 626 VDTVIGEGEFGEVYRGALRfpsQDCKTVAIKTLkdtSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFM 705
Cdd:cd06612     7 ILEKLGEGSYGSVYKAIHK---ETGQVVAIKVV---PVEEDLQEIIKEISILKQCDSPYIVKYYGSYFKNTDLWIVMEYC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 706 ENGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDfdgTYETQG 785
Cdd:cd06612    81 GAGSVSDIMKITNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQLTD---TMAKRN 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2038291632 786 GKI--PIrWTAPEAIAHRIFTTASDVWSFGIVMWEvLSFGDKPYGEMNNQEVMKSIEegyRLPPP 848
Cdd:cd06612   158 TVIgtPF-WMAPEVIQEIGYNNKADIWSLGITAIE-MAEGKPPYSDIHPMRAIFMIP---NKPPP 217
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
630-884 1.15e-25

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: 107.18  E-value: 1.15e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFPSQdckTVAIKTLKDTSPDGqwwNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGA 709
Cdd:cd14155     1 IGSGFFSEVYKVRHRTSGQ---VMALKMNTLSSNRA---NMLREVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGGN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 710 LDAFLKEREdQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILV---NQNLCCKVSDFGLTRLLDDfdgtYETQGG 786
Cdd:cd14155    75 LEQLLDSNE-PLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIkrdENGYTAVVGDFGLAEKIPD----YSDGKE 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 787 KIPI----RWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPvDCPAPLYELMKNC 862
Cdd:cd14155   150 KLAVvgspYWMAPEVLRGEPYNEKADVFSYGIILCEIIARIQADPDYLPRTEDFGLDYDAFQHMVG-DCPPDFLQLAFNC 228
                         250       260
                  ....*....|....*....|..
gi 2038291632 863 WAYDRARRPHFLQLQAHLEQLL 884
Cdd:cd14155   229 CNMDPKSRPSFHDIVKTLEEIL 250
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
669-883 2.13e-25

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: 106.95  E-value: 2.13e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 669 NFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGALDAFLKErEDQLAPGQLVAMLLGIASGMNYLSGHNYVHR 748
Cdd:cd14222    36 TFLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGTLKDFLRA-DDPFPWQQKVSFAKGIASGMAYLHSMSIIHR 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 749 DLAARNILVNQNLCCKVSDFGLTRLL---------------------DDFDGTYETQGGKIpirWTAPEAIAHRIFTTAS 807
Cdd:cd14222   115 DLNSHNCLIKLDKTVVVADFGLSRLIveekkkpppdkpttkkrtlrkNDRKKRYTVVGNPY---WMAPEMLNGKSYDEKV 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 808 DVWSFGIVMWEVLSfgdKPYGEMNNqeVMKSIEEGYRLPP------PVDCPAPLYELMKNCWAYDRARRPHFLQLQAHLE 881
Cdd:cd14222   192 DIFSFGIVLCEIIG---QVYADPDC--LPRTLDFGLNVRLfwekfvPKDCPPAFFPLAAICCRLEPDSRPAFSKLEDSFE 266

                  ..
gi 2038291632 882 QL 883
Cdd:cd14222   267 AL 268
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
629-871 2.23e-25

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: 106.39  E-value: 2.23e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRgALRfpSQDCKTVAIKT--LKDTSPDGQWwNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFME 706
Cdd:cd08215     7 VIGKGSFGSAYL-VRR--KSDGKLYVLKEidLSNMSEKERE-EALNEVKLLSKLKHPNIVKYYESFEENGKLCIVMEYAD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 707 NGALDAFLKEREDQ---LAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYET 783
Cdd:cd08215    83 GGDLAQKIKKQKKKgqpFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISKVLESTTDLAKT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 784 QGGkipirwT----APEAIAHRIFTTASDVWSFGIVMWEVLSFgDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLYELM 859
Cdd:cd08215   163 VVG------TpyylSPELCENKPYNYKSDIWALGCVLYELCTL-KHPFEANNLPALVYKIVKGQYPPIPSQYSSELRDLV 235
                         250
                  ....*....|..
gi 2038291632 860 KNCWAYDRARRP 871
Cdd:cd08215   236 NSMLQKDPEKRP 247
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
630-871 2.57e-25

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: 106.35  E-value: 2.57e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRgalrfpSQDCKTVA---IKTLKDTS-----PDgQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIV 701
Cdd:cd08222     8 LGSGNFGTVYL------VSDLKATAdeeLKVLKEISvgelqPD-ETVDANREAKLLSKLDHPAIVKFHDSFVEKESFCIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 702 TEFMENGALDAFLKE---REDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLcCKVSDFGLTRLL---- 774
Cdd:cd08222    81 TEYCEGGDLDDKISEykkSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLKNNV-IKVGDFGISRILmgts 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 775 ---DDFDGT-YetqggkipirWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEmNNQEVMKSIEEGyRLPPPVD 850
Cdd:cd08222   160 dlaTTFTGTpY----------YMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAFDGQ-NLLSVMYKIVEG-ETPSLPD 227
                         250       260
                  ....*....|....*....|..
gi 2038291632 851 C-PAPLYELMKNCWAYDRARRP 871
Cdd:cd08222   228 KySKELNAIYSRMLNKDPALRP 249
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
629-827 2.74e-25

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: 105.80  E-value: 2.74e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRFPSQdckTVAIK-TLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMEn 707
Cdd:cd14002     8 LIGEGSFGKVYKGRRKYTGQ---VVALKfIPKRGKSEKELRNLRQEIEILRKLNHPNIIEMLDSFETKKEFVVVTEYAQ- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GAL------DAFLKEREDQLAPGQLVamllgiaSGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTR-------LL 774
Cdd:cd14002    84 GELfqiledDGTLPEEEVRSIAKQLV-------SALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFARamscntlVL 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2038291632 775 DDFDGTyetqggkiPIrWTAPEAIAHRIFTTASDVWSFGIVMWEvLSFGDKPY 827
Cdd:cd14002   157 TSIKGT--------PL-YMAPELVQEQPYDHTADLWSLGCILYE-LFVGQPPF 199
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
630-853 3.73e-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: 105.38  E-value: 3.73e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFPSQDC--KTVAIKTLKDTSPDgqwwNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMEN 707
Cdd:cd14009     1 IGRGSFATVWKGRHKQTGEVVaiKEISRKKLNKKLQE----NLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GALDAFLKERedQLAPGQLVAMLLG-IASGMNYLSGHNYVHRDLAARNILV---NQNLCCKVSDFGLTRLLDDFdGTYET 783
Cdd:cd14009    77 GDLSQYIRKR--GRLPEAVARHFMQqLASGLKFLRSKNIIHRDLKPQNLLLstsGDDPVLKIADFGFARSLQPA-SMAET 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 784 QGGKiPIrWTAPEAIAHRIFTTASDVWSFGIVMWEVLsFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPA 853
Cdd:cd14009   154 LCGS-PL-YMAPEILQFQKYDAKADLWSVGAILFEML-VGKPPFRGSNHVQLLRNIERSDAVIPFPIAAQ 220
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
617-879 5.04e-25

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: 105.94  E-value: 5.04e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 617 QELDPTWlIVDTVIGEGEFGEVyrgALRFPSQDCKTVAIKTLKD-------TSPDGQWWNFLREATIMGQFNHPHILRLE 689
Cdd:cd14084     2 KELRKKY-IMSRTLGSGACGEV---KLAYDKSTCKKVAIKIINKrkftigsRREINKPRNIETEIEILKKLSHPCIIKIE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 690 GVVTKRKPIMIVTEFMENGAL----DAFLKEREDQlapGQLVA--MLLGIasgmNYLSGHNYVHRDLAARNILV---NQN 760
Cdd:cd14084    78 DFFDAEDDYYIVLELMEGGELfdrvVSNKRLKEAI---CKLYFyqMLLAV----KYLHSNGIIHRDLKPENVLLssqEEE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 761 LCCKVSDFGLTRLLDDfDGTYETQGGKipIRWTAPEAIAH---RIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMK 837
Cdd:cd14084   151 CLIKITDFGLSKILGE-TSLMKTLCGT--PTYLAPEVLRSfgtEGYTRAVDCWSLGVILFICLS-GYPPFSEEYTQMSLK 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2038291632 838 -SIEEG-YRLPPP----VDCPAPLyeLMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd14084   227 eQILSGkYTFIPKawknVSEEAKD--LVKKMLVVDPSRRPSIEEALEH 272
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
630-879 7.56e-25

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: 105.52  E-value: 7.56e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGalrFPSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENG- 708
Cdd:cd06640    12 IGKGSFGEVFKG---IDNRTQQVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIMEYLGGGs 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 ALDAFLKEREDQLapgQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYETQGGKi 788
Cdd:cd06640    89 ALDLLRAGPFDEF---QIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRNTFVGT- 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 789 PIrWTAPEAIAHRIFTTASDVWSFGIVMWEvLSFGDKPYGEMNNQEVMKSIEegyRLPPPV---DCPAPLYELMKNCWAY 865
Cdd:cd06640   165 PF-WMAPEVIQQSAYDSKADIWSLGITAIE-LAKGEPPNSDMHPMRVLFLIP---KNNPPTlvgDFSKPFKEFIDACLNK 239
                         250
                  ....*....|....
gi 2038291632 866 DRARRPHFLQLQAH 879
Cdd:cd06640   240 DPSFRPTAKELLKH 253
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
630-870 1.75e-24

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: 103.62  E-value: 1.75e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFPSqdcKTVAIKTL-KDTSPDGQWWNFL-REATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMEN 707
Cdd:cd14073     9 LGKGTYGKVKLAIERATG---REVAIKSIkKDKIEDEQDMVRIrREIEIMSSLNHPHIIRIYEVFENKDKIVIVMEYASG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GALDAFLKEREdQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDfDGTYETQGGK 787
Cdd:cd14073    86 GELYDYISERR-RLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLSNLYSK-DKLLQTFCGS 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 788 iPIrWTAPEAIAHRIFTTAS-DVWSFGIVMWeVLSFGDKPYGEMNNQEVMKSIEEG-YRLPPPvdcPAPLYELMKNCWAY 865
Cdd:cd14073   164 -PL-YASPEIVNGTPYQGPEvDCWSLGVLLY-TLVYGTMPFDGSDFKRLVKQISSGdYREPTQ---PSDASGLIRWMLTV 237

                  ....*
gi 2038291632 866 DRARR 870
Cdd:cd14073   238 NPKRR 242
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
617-879 2.19e-24

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: 104.34  E-value: 2.19e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 617 QELDP--TWLIVDTvIGEGEFGEVYRGAlrfpSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTK 694
Cdd:cd06644     6 RDLDPneVWEIIGE-LGDGAFGKVYKAK----NKETGALAAAKVIETKSEEELEDYMVEIEILATCNHPYIVKLLGAFYW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 695 RKPIMIVTEFMENGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLT--- 771
Cdd:cd06644    81 DGKLWIMIEFCPGGAVDAIMLELDRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSakn 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 772 ----RLLDDFDGTyetqggkiPIrWTAPEAIAHRIFTTA-----SDVWSFGIVMWEVLSFgDKPYGEMNNQEVMKSIEEG 842
Cdd:cd06644   161 vktlQRRDSFIGT--------PY-WMAPEVVMCETMKDTpydykADIWSLGITLIEMAQI-EPPHHELNPMRVLLKIAKS 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2038291632 843 YrlPPPVDCPAP----LYELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd06644   231 E--PPTLSQPSKwsmeFRDFLKTALDKHPETRPSAAQLLEH 269
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
630-879 2.52e-24

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: 103.32  E-value: 2.52e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRgalrfpSQDCKT---VAIK-----TLKDTSPDGQwwnFLREATIMGQFNHPHILRLEGVVTKRKPIMIV 701
Cdd:cd14007     8 LGKGKFGNVYL------AREKKSgfiVALKvisksQLQKSGLEHQ---LRREIEIQSHLRHPNILRLYGYFEDKKRIYLI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 702 TEFMENGALDAFLKeREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDD----- 776
Cdd:cd14007    79 LEYAPNGELYKELK-KQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWSVHAPSnrrkt 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 777 FDGTYEtqggkipirWTAPEAIAHRIFTTASDVWSFGIVMWEVLsFGDKPYGEMNNQEVMKSIEEG-YRLPPPVDCPApl 855
Cdd:cd14007   158 FCGTLD---------YLPPEMVEGKEYDYKVDIWSLGVLCYELL-VGKPPFESKSHQETYKRIQNVdIKFPSSVSPEA-- 225
                         250       260
                  ....*....|....*....|....
gi 2038291632 856 YELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd14007   226 KDLISKLLQKDPSKRLSLEQVLNH 249
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
630-820 5.07e-24

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: 103.42  E-value: 5.07e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGalrfpsQDCKT---VAIKTLKDtspdGQWW------NF--LREATIMGQFNHPHILRLEGVVTKRKPI 698
Cdd:cd07841     8 LGEGTYAVVYKA------RDKETgriVAIKKIKL----GERKeakdgiNFtaLREIKLLQELKHPNIIGLLDVFGHKSNI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 699 MIVTEFMEnGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFD 778
Cdd:cd07841    78 NLVFEFME-TDLEKVIKDKSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLARSFGSPN 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2038291632 779 GTYETQggkIPIRW-TAPEAI-AHRIFTTASDVWSFGIVMWEVL 820
Cdd:cd07841   157 RKMTHQ---VVTRWyRAPELLfGARHYGVGVDMWSVGCIFAELL 197
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
630-821 6.12e-24

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: 103.03  E-value: 6.12e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFPSqdcKTVAIKTLK-DTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKP------IMIVT 702
Cdd:cd07840     7 IGEGTYGQVYKARNKKTG---ELVALKKIRmENEKEGFPITAIREIKLLQKLDHPNVVRLKEIVTSKGSakykgsIYMVF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 703 EFMENGaLDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLD-DFDGTY 781
Cdd:cd07840    84 EYMDHD-LTGLLDNPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGLARPYTkENNADY 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2038291632 782 ETqggKIPIRW-TAPEAIAH-RIFTTASDVWSFGIVMWEVLS 821
Cdd:cd07840   163 TN---RVITLWyRPPELLLGaTRYGPEVDMWSVGCILAELFT 201
PTK_Jak2_rpt1 cd05078
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely ...
624-873 7.38e-24

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: 101.95  E-value: 7.38e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 624 LIVDTVIGEGEFGEVYRGALR----FPSQDCKTVAIKTLkDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIM 699
Cdd:cd05078     1 LIFNESLGQGTFTKIFKGIRRevgdYGQLHETEVLLKVL-DKAHRNYSESFFEAASMMSQLSHKHLVLNYGVCVCGDENI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 700 IVTEFMENGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNL--------CCKVSDFGLT 771
Cdd:cd05078    80 LVQEYVKFGSLDTYLKKNKNCINILWKLEVAKQLAWAMHFLEEKTLVHGNVCAKNILLIREEdrktgnppFIKLSDPGIS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 772 RLLDDFDGTYEtqggKIPirWTAPEAIAH-RIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVd 850
Cdd:cd05078   160 ITVLPKDILLE----RIP--WVPPECIENpKNLSLATDKWSFGTTLWEICSGGDKPLSALDSQRKLQFYEDRHQLPAPK- 232
                         250       260
                  ....*....|....*....|...
gi 2038291632 851 cPAPLYELMKNCWAYDRARRPHF 873
Cdd:cd05078   233 -WTELANLINNCMDYEPDHRPSF 254
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
630-876 9.53e-24

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: 101.72  E-value: 9.53e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRgALRfpSQDCKTVAIKTLKDTSPDGQWWN-FLREATIMGQFNHPHILR-LEGVVTKRKpIMIVTEFMEN 707
Cdd:cd08529     8 LGKGSFGVVYK-VVR--KVDGRVYALKQIDISRMSRKMREeAIDEARVLSKLNSPYVIKyYDSFVDKGK-LNIVMEYAEN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GALDAFLK-EREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYETQGG 786
Cdd:cd08529    84 GDLHSLIKsQRGRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAKILSDTTNFAQTIVG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 787 KiPIrWTAPEAIAHRIFTTASDVWSFGIVMWEvLSFGDKPYgEMNNQ-EVMKSIEEGYRLPPPVDCPAPLYELMKNCWAY 865
Cdd:cd08529   164 T-PY-YLSPELCEDKPYNEKSDVWALGCVLYE-LCTGKHPF-EAQNQgALILKIVRGKYPPISASYSQDLSQLIDSCLTK 239
                         250
                  ....*....|.
gi 2038291632 866 DRARRPHFLQL 876
Cdd:cd08529   240 DYRQRPDTTEL 250
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
623-879 1.37e-23

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: 102.03  E-value: 1.37e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 623 WLIVDTvIGEGEFGEVYRGAlrfpSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVT 702
Cdd:cd06643     7 WEIVGE-LGDGAFGKVYKAQ----NKETGILAAAKVIDTKSEEELEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 703 EFMENGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGL----TRLL---D 775
Cdd:cd06643    82 EFCAGGAVDAVMLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVsaknTRTLqrrD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 776 DFDGTyetqggkiPIrWTAPEAI-----AHRIFTTASDVWSFGIVMWEVLSFgDKPYGEMNNQEVMKSIEEGYrlPPPVD 850
Cdd:cd06643   162 SFIGT--------PY-WMAPEVVmcetsKDRPYDYKADVWSLGVTLIEMAQI-EPPHHELNPMRVLLKIAKSE--PPTLA 229
                         250       260       270
                  ....*....|....*....|....*....|...
gi 2038291632 851 CP----APLYELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd06643   230 QPsrwsPEFKDFLRKCLEKNVDARWTTSQLLQH 262
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
629-848 2.03e-23

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: 101.17  E-value: 2.03e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRFPSQdckTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENG 708
Cdd:cd06609     8 RIGKGSFGEVYKGIDKRTNQ---VVAIKVIDLEEAEDEIEDIQQEIQFLSQCDSPYITKYYGSFLKGSKLWIIMEYCGGG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 ALDAFLKE---REDQLApgqlvAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFG----LTRLL---DDFD 778
Cdd:cd06609    85 SVLDLLKPgplDETYIA-----FILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGvsgqLTSTMskrNTFV 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 779 GTyetqggkiPIrWTAPEAIAHRIFTTASDVWSFGIVMWEvLSFGDKPYGEMNNQEVMKSIEegyRLPPP 848
Cdd:cd06609   160 GT--------PF-WMAPEVIKQSGYDEKADIWSLGITAIE-LAKGEPPLSDLHPMRVLFLIP---KNNPP 216
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
619-879 2.28e-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: 100.97  E-value: 2.28e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 619 LDPT--WLIVDTvIGEGEFGEVYRGALRFPSQdcktVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRK 696
Cdd:cd06611     1 VNPNdiWEIIGE-LGDGAFGKVYKAQHKETGL----FAAAKIIQIESEEELEDFMVEIDILSECKHPNIVGLYEAYFYEN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 697 PIMIVTEFMENGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLL-- 774
Cdd:cd06611    76 KLWILIEFCDGGALDSIMLELERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSAKNks 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 775 -----DDFDGTyetqggkiPiRWTAPEAIAHRIFTTA-----SDVWSFGIVMWEvLSFGDKPYGEMNNQEVMKSIEEGYr 844
Cdd:cd06611   156 tlqkrDTFIGT--------P-YWMAPEVVACETFKDNpydykADIWSLGITLIE-LAQMEPPHHELNPMRVLLKILKSE- 224
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2038291632 845 lPPPVDCP----APLYELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd06611   225 -PPTLDQPskwsSSFNDFLKSCLVKDPDDRPTAAELLKH 262
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
911-975 2.51e-23

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 93.87  E-value: 2.51e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2038291632 911 DGIPYRSVSEWLESIRMKRYILHFRsAGLDTMECVLELTAEDLTQMGITLPGHQKRILCSIQGFK 975
Cdd:pfam00536   1 DGWSVEDVGEWLESIGLGQYIDSFR-AGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRLK 64
SAM_EPH-A2 cd09543
SAM domain of EPH-A2 family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of ...
911-976 2.57e-23

SAM domain of EPH-A2 family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A2 subfamily of receptor tyrosine kinases is a C-terminal protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A2 receptors and appears to mediate cell-cell initiated signal transduction. For example, SAM domain of EPH-A2 receptors interacts with SAM domain of Ship2 proteins (SH2 containing phosphoinositide 5-phosphotase-2) forming heterodimers; such recruitment of Ship2 by EPH-A2 attenuates the positive signal for receptor endocytosis. Eph-A2 is found overexpressed in many types of human cancer, including breast, prostate, lung and colon cancer. High level of expression could induce cancer progression by a variety of mechanisms and could be used as a novel tag for cancer immunotherapy. EPH-A2 receptors are attractive targets for drag design.


Pssm-ID: 188942  Cd Length: 70  Bit Score: 94.13  E-value: 2.57e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2038291632 911 DGIPYRSVSEWLESIRMKRYILHFRSAGLDTMECVLELTAEDLTQMGITLPGHQKRILCSIQGFKD 976
Cdd:cd09543     1 EGVPFRTVAEWLESIKMQQYTEHFMAAGYNSIDKVLQMTQEDIKHIGVRLPGHQKRIAYSILGLKE 66
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
630-879 2.58e-23

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: 100.92  E-value: 2.58e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGaLRFPSQdcKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGA 709
Cdd:cd06641    12 IGKGSFGEVFKG-IDNRTQ--KVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYLGGGS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 710 ldaflkeREDQLAPG-----QLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDD-------F 777
Cdd:cd06641    89 -------ALDLLEPGpldetQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDtqikrn*F 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 778 DGTyetqggkiPIrWTAPEAIAHRIFTTASDVWSFGIVMWEvLSFGDKPYGEMNNQEVMKSIEEGyrlPPPV---DCPAP 854
Cdd:cd06641   162 VGT--------PF-WMAPEVIKQSAYDSKADIWSLGITAIE-LARGEPPHSELHPMKVLFLIPKN---NPPTlegNYSKP 228
                         250       260
                  ....*....|....*....|....*
gi 2038291632 855 LYELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd06641   229 LKEFVEACLNKEPSFRPTAKELLKH 253
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
630-879 2.95e-23

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: 100.90  E-value: 2.95e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGalrFPSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGA 709
Cdd:cd06642    12 IGKGSFGEVYKG---IDNRTKEVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYITRYYGSYLKGTKLWIIMEYLGGGS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 710 LDAFLKEreDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYETQGGKiP 789
Cdd:cd06642    89 ALDLLKP--GPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRNTFVGT-P 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 790 IrWTAPEAIAHRIFTTASDVWSFGIVMWEvLSFGDKPYGEMNNQEVMKSIEEGYrlPPPVDC--PAPLYELMKNCWAYDR 867
Cdd:cd06642   166 F-WMAPEVIKQSAYDFKADIWSLGITAIE-LAKGEPPNSDLHPMRVLFLIPKNS--PPTLEGqhSKPFKEFVEACLNKDP 241
                         250
                  ....*....|..
gi 2038291632 868 ARRPHFLQLQAH 879
Cdd:cd06642   242 RFRPTAKELLKH 253
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
628-879 3.41e-23

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: 100.36  E-value: 3.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 628 TVIGEGEFGEVYRGALRfpsQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMEN 707
Cdd:cd06623     7 KVLGQGSSGVVYKVRHK---PTGKIYALKKIHVDGDEEFRKQLLRELKTLRSCESPYVVKCYGAFYKEGEISIVLEYMDG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GALDAFLKER----EDQLApgqLVA--MLLGIAsgmnYL-SGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDD-FDG 779
Cdd:cd06623    84 GSLADLLKKVgkipEPVLA---YIArqILKGLD----YLhTKRHIIHRDIKPSNLLINSKGEVKIADFGISKVLENtLDQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 780 TYETQGgkipirwTA----PEAIAHRIFTTASDVWSFGIVMWEvLSFGDKPY---GEMNNQEVMKSI--EEGYRLpPPVD 850
Cdd:cd06623   157 CNTFVG-------TVtymsPERIQGESYSYAADIWSLGLTLLE-CALGKFPFlppGQPSFFELMQAIcdGPPPSL-PAEE 227
                         250       260
                  ....*....|....*....|....*....
gi 2038291632 851 CPAPLYELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd06623   228 FSPEFRDFISACLQKDPKKRPSAAELLQH 256
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
629-874 4.58e-23

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: 100.48  E-value: 4.58e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALrfpsqDCKTVAIKTLKDTspDGQWWNFLREATIMGQFNHPHIL-------RLEGVVTKrkpIMIV 701
Cdd:cd14053     2 IKARGRFGAVWKAQY-----LNRLVAVKIFPLQ--EKQSWLTEREIYSLPGMKHENILqfigaekHGESLEAE---YWLI 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 702 TEFMENGALDAFLKEREDQLapGQLVAMLLGIASGMNYL----------SGHNYVHRDLAARNILVNQNLCCKVSDFGLT 771
Cdd:cd14053    72 TEFHERGSLCDYLKGNVISW--NELCKIAESMARGLAYLhedipatnggHKPSIAHRDFKSKNVLLKSDLTACIADFGLA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 772 RLLDDFDGTYETQGGKIPIRWTAPE----AIAhriFTTAS----DVWSFGIVMWEVLS---FGDKPYGEmnnqevmksie 840
Cdd:cd14053   150 LKFEPGKSCGDTHGQVGTRRYMAPEvlegAIN---FTRDAflriDMYAMGLVLWELLSrcsVHDGPVDE----------- 215
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2038291632 841 egYRLPPPVDC-PAPLYELMKNCWAyDRARRPHFL 874
Cdd:cd14053   216 --YQLPFEEEVgQHPTLEDMQECVV-HKKLRPQIR 247
PTK_Jak3_rpt1 cd14208
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is ...
630-873 7.70e-23

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: 99.21  E-value: 7.70e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFPSQD--CKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMiVTEFMEN 707
Cdd:cd14208     7 LGKGSFTKIYRGLRTDEEDDerCETEVLLKVMDPTHGNCQESFLEAASIMSQISHKHLVLLHGVCVGKDSIM-VQEFVCH 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GALDAFLKER--EDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQN------LCCKVSDFGLT-RLLDDfd 778
Cdd:cd14208    86 GALDLYLKKQqqKGPVAISWKLQVVKQLAYALNYLEDKQLVHGNVSAKKVLLSREgdkgspPFIKLSDPGVSiKVLDE-- 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 779 gtyETQGGKIPirWTAPEAIAH-RIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVdcPAPLYE 857
Cdd:cd14208   164 ---ELLAERIP--WVAPECLSDpQNLALEADKWGFGATLWEIFSGGHMPLSALDPSKKLQFYNDRKQLPAPH--WIELAS 236
                         250
                  ....*....|....*.
gi 2038291632 858 LMKNCWAYDRARRPHF 873
Cdd:cd14208   237 LIQQCMSYNPLLRPSF 252
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
630-821 8.28e-23

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: 99.99  E-value: 8.28e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGalrfpsQDCKT---VAIKTLK-DTSPDGQWWNFLREATIMGQFNHPHILRLEGVV--TKRKPIMIVTE 703
Cdd:cd07843    13 IEEGTYGVVYRA------RDKKTgeiVALKKLKmEKEKEGFPITSLREINILLKLQHPNIVTVKEVVvgSNLDKIYMVME 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 704 FMENgALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYeT 783
Cdd:cd07843    87 YVEH-DLKSLMETMKQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGLAREYGSPLKPY-T 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2038291632 784 QggKIPIRW-TAPEAI-AHRIFTTASDVWSFGIVMWEVLS 821
Cdd:cd07843   165 Q--LVVTLWyRAPELLlGAKEYSTAIDMWSVGCIFAELLT 202
PTK_Jak1_rpt1 cd05077
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely ...
630-873 1.16e-22

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: 98.86  E-value: 1.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFPSQDCK---------TVAIKTLKDTSPDGQWwNFLREATIMGQFNHPHILRLEGVVTKRKPIMI 700
Cdd:cd05077     7 LGRGTRTQIYAGILNYKDDDEDegysyekeiKVILKVLDPSHRDISL-AFFETASMMRQVSHKHIVLLYGVCVRDVENIM 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 701 VTEFMENGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQ----NLC---CKVSDFG--LT 771
Cdd:cd05077    86 VEEFVEFGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNILLARegidGECgpfIKLSDPGipIT 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 772 RLlddfdgTYETQGGKIPirWTAPEAIA-HRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPvD 850
Cdd:cd05077   166 VL------SRQECVERIP--WIAPECVEdSKNLSIAADKWSFGTTLWEICYNGEIPLKDKTLAEKERFYEGQCMLVTP-S 236
                         250       260
                  ....*....|....*....|...
gi 2038291632 851 CPApLYELMKNCWAYDRARRPHF 873
Cdd:cd05077   237 CKE-LADLMTHCMNYDPNQRPFF 258
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
630-879 2.30e-22

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: 98.37  E-value: 2.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFPSQdckTVAIKTLKDTSPDGQWWNFLREATIMGQFN-HPHILRLEGVVTKRKPIMIVTEFMENG 708
Cdd:cd07830     7 LGDGTFGSVYLARNKETGE---LVAIKKMKKKFYSWEECMNLREVKSLRKLNeHPNIVKLKEVFRENDELYFVFEYMEGN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 ALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLD------DFDGTye 782
Cdd:cd07830    84 LYQLMKDRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLAREIRsrppytDYVST-- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 783 tqggkipiRW-TAPEAI-AHRIFTTASDVWSFGIVMWEVLSFgdKP-----------------YGEMNNQ------EVMK 837
Cdd:cd07830   162 --------RWyRAPEILlRSTSYSSPVDIWALGCIMAELYTL--RPlfpgsseidqlykicsvLGTPTKQdwpegyKLAS 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2038291632 838 SIeeGYRLP--PPV-------DCPAPLYELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd07830   232 KL--GFRFPqfAPTslhqlipNASPEAIDLIKDMLRWDPKKRPTASQALQH 280
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
630-861 2.75e-22

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: 97.33  E-value: 2.75e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRfpsqDCKTVAIKTL-KDTSPDGQ-WWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMEN 707
Cdd:cd14161    11 LGKGTYGRVKKARDS----SGRLVAIKSIrKDRIKDEQdLLHIRREIEIMSSLNHPHIISVYEVFENSSKIVIVMEYASR 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GALDAFLKEREdQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDfDGTYETQGGK 787
Cdd:cd14161    87 GDLYDYISERQ-RLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLSNLYNQ-DKFLQTYCGS 164
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038291632 788 iPIrWTAPEAIAHRIFTTAS-DVWSFGIVMWeVLSFGDKPYGEMNNQEVMKSIEEG-YRLPP-PVD-CPAPLYELMKN 861
Cdd:cd14161   165 -PL-YASPEIVNGRPYIGPEvDSWSLGVLLY-ILVHGTMPFDGHDYKILVKQISSGaYREPTkPSDaCGLIRWLLMVN 239
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
629-879 2.87e-22

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: 96.92  E-value: 2.87e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGalrfpsQDCKT---VAIKTLKdtsPDGQWWNF-LREATIMGQFN----HPHILRLEGVVTKRKP--I 698
Cdd:cd05118     6 KIGEGAFGTVWLA------RDKVTgekVAIKKIK---NDFRHPKAaLREIKLLKHLNdvegHPNIVKLLDVFEHRGGnhL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 699 MIVTEFMENGALDaFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLC-CKVSDFGLTRLLDDF 777
Cdd:cd05118    77 CLVFELMGMNLYE-LIKDYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLELGqLKLADFGLARSFTSP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 778 DGTyetqgGKIPIRW-TAPEAI-AHRIFTTASDVWSFGIVMWEVLS----FGDKpygemNNQEVMKSIEEgyRLPPPvdc 851
Cdd:cd05118   156 PYT-----PYVATRWyRAPEVLlGAKPYGSSIDIWSLGCILAELLTgrplFPGD-----SEVDQLAKIVR--LLGTP--- 220
                         250       260
                  ....*....|....*....|....*...
gi 2038291632 852 paPLYELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd05118   221 --EALDLLSKMLKYDPAKRITASQALAH 246
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
626-826 3.89e-22

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: 98.16  E-value: 3.89e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 626 VDTVIGEGEFGEVYRGALRfpsQDCKTVAIK-TLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVV-------TKRKP 697
Cdd:cd07866    12 ILGKLGEGTFGEVYKARQI---KTGRVVALKkILMHNEKDGFPITALREIKILKKLKHPNVVPLIDMAverpdksKRKRG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 698 IM-IVTEFMENGaLDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDD 776
Cdd:cd07866    89 SVyMVTPYMDHD-LSGLLENPSVKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADFGLARPYDG 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 777 --FDGTYETQGGK------IPIRW-TAPEAIAH-RIFTTASDVWSFGIVMWEVlsFGDKP 826
Cdd:cd07866   168 ppPNPKGGGGGGTrkytnlVVTRWyRPPELLLGeRRYTTAVDIWGIGCVFAEM--FTRRP 225
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
629-847 4.02e-22

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: 96.70  E-value: 4.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGAlrfPSQDCKTVAIKTL-----KDTSPDGQwwnFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTE 703
Cdd:cd14663     7 TLGEGTFAKVKFAR---NTKTGESVAIKIIdkeqvAREGMVEQ---IKREIAIMKLLRHPNIVELHEVMATKTKIFFVME 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 704 FMENGAL------DAFLKEREDQLAPGQLVamllgiaSGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDF 777
Cdd:cd14663    81 LVTGGELfskiakNGRLKEDKARKYFQQLI-------DAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSALSEQF 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038291632 778 --DGTYETQGGKiPiRWTAPEAIAHRIFTTA-SDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSIEEG-YRLPP 847
Cdd:cd14663   154 rqDGLLHTTCGT-P-NYVAPEVLARRGYDGAkADIWSCGVILFVLLA-GYLPFDDENLMALYRKIMKGeFEYPR 224
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
629-879 4.56e-22

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: 97.03  E-value: 4.56e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRfPSQdcKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENG 708
Cdd:cd06605     8 ELGEGNGGVVSKVRHR-PSG--QIMAVKVIRLEIDEALQKQILRELDVLHKCNSPYIVGFYGAFYSEGDISICMEYMDGG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 ALDAFLKER----EDQLApgqlvAMLLGIASGMNYL-SGHNYVHRDLAARNILVNQNLCCKVSDFGL-TRLLDD----FD 778
Cdd:cd06605    85 SLDKILKEVgripERILG-----KIAVAVVKGLIYLhEKHKIIHRDVKPSNILVNSRGQVKLCDFGVsGQLVDSlaktFV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 779 GTYEtqggkipirWTAPEAIAHRIFTTASDVWSFGIVMWEvLSFGDKPY------GEMNNQEVMKSIEEGyrlPPPV--- 849
Cdd:cd06605   160 GTRS---------YMAPERISGGKYTVKSDIWSLGLSLVE-LATGRFPYpppnakPSMMIFELLSYIVDE---PPPLlps 226
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2038291632 850 -DCPAPLYELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd06605   227 gKFSPDFQDFVSQCLQKDPTERPSYKELMEH 257
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
625-879 4.75e-22

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: 96.87  E-value: 4.75e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 625 IVDTVIGEGEFGEVYRgALRFPSQDCKTVAIKTL-KDTSPDGQWWNFL-REATIMGQFNHPHILRLEGVVTKRKPIMIVT 702
Cdd:cd14080     3 RLGKTIGEGSYSKVKL-AEYTKSGLKEKVACKIIdKKKAPKDFLEKFLpRELEILRKLRHPNIIQVYSIFERGSKVFIFM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 703 EFMENGALDAFLKER----EDQLApgqlvAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLL--DD 776
Cdd:cd14080    82 EYAEHGDLLEYIQKRgalsESQAR-----IWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGFARLCpdDD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 777 FDGTYETQGGKIPirWTAPEAIAHRIFT-TASDVWSFGIVMWeVLSFGDKPYGEMNNQEVMKS-IEEGYRLPPPVDCPAP 854
Cdd:cd14080   157 GDVLSKTFCGSAA--YAAPEILQGIPYDpKKYDIWSLGVILY-IMLCGSMPFDDSNIKKMLKDqQNRKVRFPSSVKKLSP 233
                         250       260
                  ....*....|....*....|....*.
gi 2038291632 855 -LYELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd14080   234 eCKDLIDQLLEPDPTKRATIEEILNH 259
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
629-879 5.23e-22

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: 96.83  E-value: 5.23e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGalrFPSQDCKTVAIKTLKDTSPDGQWWN--------FLREATIMGQFNHPHILRLEGVVTKRKPIMI 700
Cdd:cd06628     7 LIGSGSFGSVYLG---MNASSGELMAVKQVELPSVSAENKDrkksmldaLQREIALLRELQHENIVQYLGSSSDANHLNI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 701 VTEFMENGALDAFLK---EREDQLapgqLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLdDF 777
Cdd:cd06628    84 FLEYVPGGSVATLLNnygAFEESL----VRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISKKL-EA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 778 DGTYETQGGKIP-----IRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSIEEGYRLPPPVDCP 852
Cdd:cd06628   159 NSLSTKNNGARPslqgsVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLT-GTHPFPDCTQMQAIFKIGENASPTIPSNIS 237
                         250       260
                  ....*....|....*....|....*..
gi 2038291632 853 APLYELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd06628   238 SEARDFLEKTFEIDHNKRPTADELLKH 264
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
630-879 5.73e-22

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: 96.60  E-value: 5.73e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGA------------LRFpsQDCKTVAIKTLKDtspdgqwwnflrEATIMGQFNHPHILRLEGVVTKRKP 697
Cdd:cd06626     8 IGEGTFGKVYTAVnldtgelmamkeIRF--QDNDPKTIKEIAD------------EMKVLEGLDHPNLVRYYGVEVHREE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 698 IMIVTEFMENGALDAFLK--EREDQLAPGQLVAMLLgiaSGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLD 775
Cdd:cd06626    74 VYIFMEYCQEGTLEELLRhgRILDEAVIRVYTLQLL---EGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAVKLK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 776 DFDGTY---ETQGGKIPIRWTAPEAIAHRIFT---TASDVWSFGIVMWEVLSfGDKPYGEMNNQ-EVMKSIEEGYR--LP 846
Cdd:cd06626   151 NNTTTMapgEVNSLVGTPAYMAPEVITGNKGEghgRAADIWSLGCVVLEMAT-GKRPWSELDNEwAIMYHVGMGHKppIP 229
                         250       260       270
                  ....*....|....*....|....*....|...
gi 2038291632 847 PPVDCPAPLYELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd06626   230 DSLQLSPEGKDFLSRCLESDPKKRPTASELLDH 262
PTK_Tyk2_rpt1 cd05076
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; Tyk2 is ...
670-874 6.07e-22

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: 96.90  E-value: 6.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 670 FLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRD 749
Cdd:cd05076    62 FFETASLMSQVSHTHLVFVHGVCVRGSENIMVEEFVEHGPLDVWLRKEKGHVPMAWKFVVARQLASALSYLENKNLVHGN 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 750 LAARNILV-------NQNLCCKVSD--FGLTRLlddfdgTYETQGGKIPirWTAPEAIAH-RIFTTASDVWSFGIVMWEV 819
Cdd:cd05076   142 VCAKNILLarlgleeGTSPFIKLSDpgVGLGVL------SREERVERIP--WIAPECVPGgNSLSTAADKWGFGATLLEI 213
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2038291632 820 LSFGDKPYGEMNNQEVMKSIEEGYRLPPPvDCPApLYELMKNCWAYDRARRPHFL 874
Cdd:cd05076   214 CFNGEAPLQSRTPSEKERFYQRQHRLPEP-SCPE-LATLISQCLTYEPTQRPSFR 266
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
630-819 9.62e-22

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: 96.34  E-value: 9.62e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRgaLRFPSQDCKTVAIKTLK-DTSPDGQWWNFLREATIMGQF---NHPHILRLEGVVTKRKPIMIVTEFM 705
Cdd:cd14052     8 IGSGEFSQVYK--VSERVPTGKVYAVKKLKpNYAGAKDRLRRLEEVSILRELtldGHDNIVQLIDSWEYHGHLYIQTELC 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 706 ENGALDAFLKEREDQ--LAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGL-TRLLDDFDgtYE 782
Cdd:cd14052    86 ENGSLDVFLSELGLLgrLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMaTVWPLIRG--IE 163
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2038291632 783 TQGGKIPIrwtAPEAIAHRIFTTASDVWSFGIVMWEV 819
Cdd:cd14052   164 REGDREYI---APEILSEHMYDKPADIFSLGLILLEA 197
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
630-887 9.88e-22

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: 95.70  E-value: 9.88e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFPSQD--CKTVAIKTLKDTspdGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMEN 707
Cdd:cd14099     9 LGKGGFAKCYEVTDMSTGKVyaGKVVPKSSLTKP---KQREKLKSEIKIHRSLKHPNIVKFHDCFEDEENVYILLELCSN 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GALDAFLKEREdQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGL-TRLLDDFD------GT 780
Cdd:cd14099    86 GSLMELLKRRK-ALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLaARLEYDGErkktlcGT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 781 yetqggkiPiRWTAPEAIA----HrifTTASDVWSFGIVMWEVLsFGDKPYGEMNNQEVMKSIEEG-YRLPPPVDCPAPL 855
Cdd:cd14099   165 --------P-NYIAPEVLEkkkgH---SFEVDIWSLGVILYTLL-VGKPPFETSDVKETYKRIKKNeYSFPSHLSISDEA 231
                         250       260       270
                  ....*....|....*....|....*....|..
gi 2038291632 856 YELMKNCWAYDRARRPhflqlqaHLEQLLTDP 887
Cdd:cd14099   232 KDLIRSMLQPDPTKRP-------SLDEILSHP 256
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
630-879 1.29e-21

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: 95.55  E-value: 1.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGalrFPSQDCKTVAIKTLKDTSPDGQWWNFL----REATIMGQFNHPHILRLEGVVTKRKPIMIVTEFM 705
Cdd:cd06632     8 LGSGSFGSVYEG---FNGDTGDFFAVKEVSLVDDDKKSRESVkqleQEIALLSKLRHPNIVQYYGTEREEDNLYIFLEYV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 706 ENGALDAFLKeREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYETQG 785
Cdd:cd06632    85 PGGSIHKLLQ-RYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKHVEAFSFAKSFKG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 786 GKIpirWTAPEAIA--HRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAP-LYELMKNC 862
Cdd:cd06632   164 SPY---WMAPEVIMqkNSGYGLAVDIWSLGCTVLEMAT-GKPPWSQYEGVAAIFKIGNSGELPPIPDHLSPdAKDFIRLC 239
                         250
                  ....*....|....*..
gi 2038291632 863 WAYDRARRPHFLQLQAH 879
Cdd:cd06632   240 LQRDPEDRPTASQLLEH 256
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
630-879 1.65e-21

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: 95.95  E-value: 1.65e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRfpsQDCKTVAIKT-LKDTSPDGQWwNFLREATIMGQFNHPHILRLEGVVTKRKP--IMIVTEFME 706
Cdd:cd06621     9 LGEGAGGSVTKCRLR---NTKTIFALKTiTTDPNPDVQK-QILRELEINKSCASPYIVKYYGAFLDEQDssIGIAMEYCE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 707 NGALDAFLKE---REDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLT-RLLDDFDGTYE 782
Cdd:cd06621    85 GGSLDSIYKKvkkKGGRIGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGVSgELVNSLAGTFT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 783 -TQggkipiRWTAPEAIAHRIFTTASDVWSFGIVMWEVLS--FGDKPYGEMNNQ--EVMKSIeegYRLPPP--VDCPA-- 853
Cdd:cd06621   165 gTS------YYMAPERIQGGPYSITSDVWSLGLTLLEVAQnrFPFPPEGEPPLGpiELLSYI---VNMPNPelKDEPEng 235
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2038291632 854 -----PLYELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd06621   236 ikwseSFKDFIEKCLEKDGTRRPGPWQMLAH 266
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
630-879 5.00e-21

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: 94.31  E-value: 5.00e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGalrFPSQDCKTVAIKtLKDTSPDgqwW------NF----LREATIMGQFNHPHILRLEGVVT-KRKPI 698
Cdd:cd13990     8 LGKGGFSEVYKA---FDLVEQRYVACK-IHQLNKD---WseekkqNYikhaLREYEIHKSLDHPRIVKLYDVFEiDTDSF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 699 MIVTEFMENGALDAFLK------EREDQLapgqlvaMLLGIASGMNYLSGHN--YVHRDLAARNILVNQN---LCCKVSD 767
Cdd:cd13990    81 CTVLEYCDGNDLDFYLKqhksipEREARS-------IIMQVVSALKYLNEIKppIIHYDLKPGNILLHSGnvsGEIKITD 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 768 FGLTRLLDDFD-------------GTYETQGGKIPIRWTAPEAIAHRIfttasDVWSFGIVMWEVLsFGDKPYGEMNNQE 834
Cdd:cd13990   154 FGLSKIMDDESynsdgmeltsqgaGTYWYLPPECFVVGKTPPKISSKV-----DVWSVGVIFYQML-YGRKPFGHNQSQE 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2038291632 835 -------VMKSIEEGYRLPPPVDCPAPlyELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd13990   228 aileentILKATEVEFPSKPVVSSEAK--DFIRRCLTYRKEDRPDVLQLAND 277
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
630-827 5.26e-21

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: 93.51  E-value: 5.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRgALRfPSQDCKTVAIK-----TLKDTSPDgqwwNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEF 704
Cdd:cd14121     3 LGSGTYATVYK-AYR-KSGAREVVAVKcvsksSLNKASTE----NLLTEIELLKKLKHPHIVELKDFQWDEEHIYLIMEY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 705 MENGALDAFLKEREdQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILV--NQNLCCKVSDFGLTRLLDDFDGTYE 782
Cdd:cd14121    77 CSGGDLSRFIRSRR-TLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLssRYNPVLKLADFGFAQHLKPNDEAHS 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2038291632 783 TQGGkiPIrWTAPEAIAHRIFTTASDVWSFGIVMWEVLsFGDKPY 827
Cdd:cd14121   156 LRGS--PL-YMAPEMILKKKYDARVDLWSVGVILYECL-FGRAPF 196
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
625-846 5.42e-21

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: 93.49  E-value: 5.42e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 625 IVDTVIGEGEFGEVYRGALRFPSQdckTVAIKTL---KDTSPDGQWwNFLREATIMGQFNHPHILRLEGVVTKRKPIMIV 701
Cdd:cd14079     5 ILGKTLGVGSFGKVKLAEHELTGH---KVAVKILnrqKIKSLDMEE-KIRREIQILKLFRHPHIIRLYEVIETPTDIFMV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 702 TEFMENGALDAFLKEReDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDdfDGTY 781
Cdd:cd14079    81 MEYVSGGELFDYIVQK-GRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLSNIMR--DGEF 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038291632 782 -ETQGGKiPiRWTAPEAIAHRIFTTAS-DVWSFGIVMWeVLSFGDKPYGEMNNQEVMKSIEEG-YRLP 846
Cdd:cd14079   158 lKTSCGS-P-NYAAPEVISGKLYAGPEvDVWSCGVILY-ALLCGSLPFDDEHIPNLFKKIKSGiYTIP 222
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
629-879 7.89e-21

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: 93.26  E-value: 7.89e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYrgaLRFPSQDCKTVAIKTLK-DTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMEN 707
Cdd:cd08220     7 VVGRGAYGTVY---LCRRKDDNKLVIIKQIPvEQMTKEERQAALNEVKVLSMLHHPNIIEYYESFLEDKALMIVMEYAPG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GALDAFLKEREDQL-APGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQN-LCCKVSDFGLTRLLDDFDGTYETQG 785
Cdd:cd08220    84 GTLFEYIQQRKGSLlSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKrTVVKIGDFGISKILSSKSKAYTVVG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 786 GKIPIrwtAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKsIEEGYRLPPPVDCPAPLYELMKNCWAY 865
Cdd:cd08220   164 TPCYI---SPELCEGKPYNQKSDIWALGCVLYELASLKRAFEAANLPALVLK-IMRGTFAPISDRYSEELRHLILSMLHL 239
                         250
                  ....*....|....
gi 2038291632 866 DRARRPHFLQLQAH 879
Cdd:cd08220   240 DPNKRPTLSEIMAQ 253
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
630-879 8.22e-21

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: 92.83  E-value: 8.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRgaLRFPSQDCKTVAIKTLKDTSPDGQWWNFLRE---ATIMGQfnHPHILRLEGVVTKRKPIMIVTEFME 706
Cdd:cd13997     8 IGSGSFSEVFK--VRSKVDGCLYAVKKSKKPFRGPKERARALREveaHAALGQ--HPNIVRYYSSWEEGGHLYIQMELCE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 707 NGALDAFLKE--REDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYETQ 784
Cdd:cd13997    84 NGSLQDALEElsPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLATRLETSGDVEEGD 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 785 GgkipiRWTAPEAIA-HRIFTTASDVWSFGIVMWEVLSFGDKPygemNNQEVMKSIEEGYRLPPPVDC-PAPLYELMKNC 862
Cdd:cd13997   164 S-----RYLAPELLNeNYTHLPKADIFSLGVTVYEAATGEPLP----RNGQQWQQLRQGKLPLPPGLVlSQELTRLLKVM 234
                         250
                  ....*....|....*..
gi 2038291632 863 WAYDRARRPHFLQLQAH 879
Cdd:cd13997   235 LDPDPTRRPTADQLLAH 251
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
649-883 9.12e-21

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: 93.38  E-value: 9.12e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 649 DCKTVAIKTLKDTSpdgqwwnFLREATI------MGQFNHPHILRLEGVVTKRKPIMIVTEFMENGALDAFLKEREDQLA 722
Cdd:cd14045    29 DGRTVAIKKIAKKS-------FTLSKRIrkevkqVRELDHPNLCKFIGGCIEVPNVAIITEYCPKGSLNDVLLNEDIPLN 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 723 PGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDfDGTYETQGGKIPIR--WTAPEAIAH 800
Cdd:cd14045   102 WGFRFSFATDIARGMAYLHQHKIYHGRLKSSNCVIDDRWVCKIADYGLTTYRKE-DGSENASGYQQRLMqvYLPPENHSN 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 801 RIF--TTASDVWSFGIVMWEVLSFGDKPygemnnQEVMKSIEEGYRLPPP----------VDCPAPLYELMKNCWAYDRA 868
Cdd:cd14045   181 TDTepTQATDVYSYAIILLEIATRNDPV------PEDDYSLDEAWCPPLPelisgktensCPCPADYVELIRRCRKNNPA 254
                         250
                  ....*....|....*
gi 2038291632 869 RRPHFLQLQAHLEQL 883
Cdd:cd14045   255 QRPTFEQIKKTLHKI 269
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
630-879 1.07e-20

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: 93.27  E-value: 1.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRgALRFPSQdcKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKP-IMIVTEFMENG 708
Cdd:cd06620    13 LGAGNGGSVSK-VLHIPTG--TIMAKKVIHIDAKSSVRKQILRELQILHECHSPYIVSFYGAFLNENNnIIICMEYMDCG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 ALDAFLKEReDQLAPGQLVAMLLGIASGMNYL-SGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLL-----DDFDGTYE 782
Cdd:cd06620    90 SLDKILKKK-GPFPEEVLGKIAVAVLEGLTYLyNVHRIIHRDIKPSNILVNSKGQIKLCDFGVSGELinsiaDTFVGTST 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 783 tqggkipirWTAPEAIAHRIFTTASDVWSFGIVMWEvLSFGDKPYGEMNNQ-----------EVMKSI--EEGYRLPPPV 849
Cdd:cd06620   169 ---------YMSPERIQGGKYSVKSDVWSLGLSIIE-LALGEFPFAGSNDDddgyngpmgilDLLQRIvnEPPPRLPKDR 238
                         250       260       270
                  ....*....|....*....|....*....|
gi 2038291632 850 DCPAPLYELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd06620   239 IFPKDLRDFVDRCLLKDPRERPSPQLLLDH 268
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
629-870 1.21e-20

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: 93.27  E-value: 1.21e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRFpsqdcKTVAIKTLkdtsPDGQWWNFLREATIMGQFN--HPHILRL----EGVVTKRKPIMIVT 702
Cdd:cd13998     2 VIGKGRFGEVWKASLKN-----EPVAVKIF----SSRDKQSWFREKEIYRTPMlkHENILQFiaadERDTALRTELWLVT 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 703 EFMENGALDAFLkeREDQLAPGQLVAMLLGIASGMNYL-------SGHN--YVHRDLAARNILVNQNLCCKVSDFGLTRL 773
Cdd:cd13998    73 AFHPNGSL*DYL--SLHTIDWVSLCRLALSVARGLAHLhseipgcTQGKpaIAHRDLKSKNILVKNDGTCCIADFGLAVR 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 774 LDDFDGT--YETQGGKIPIRWTAPEAIAHRI-FTTAS-----DVWSFGIVMWEVLS-----FG-----DKPYGEMNNQ-- 833
Cdd:cd13998   151 LSPSTGEedNANNGQVGTKRYMAPEVLEGAInLRDFEsfkrvDIYAMGLVLWEMASrctdlFGiveeyKPPFYSEVPNhp 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2038291632 834 --EVMKSIEEGYRLPPPV-----DCPA--PLYELMKNCWAYDRARR 870
Cdd:cd13998   231 sfEDMQEVVVRDKQRPNIpnrwlSHPGlqSLAETIEECWDHDAEAR 276
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
630-883 1.40e-20

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: 92.20  E-value: 1.40e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGAlrfPSQDCKTVAIKTLKDtspDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGA 709
Cdd:cd14156     1 IGSGFFSKVYKVT---HGATGKVMVVKIYKN---DVDQHKIVREISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGC 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 710 LDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQN---LCCKVSDFGLTRLLDDFDgtyetqgG 786
Cdd:cd14156    75 LEELLAREELPLSWREKVELACDISRGMVYLHSKNIYHRDLNSKNCLIRVTprgREAVVTDFGLAREVGEMP-------A 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 787 KIPIR---------WTAPEAIAHRIFTTASDVWSFGIVMWEVLsfGDKPygemNNQEVMKSIEE------GYRLPPPvDC 851
Cdd:cd14156   148 NDPERklslvgsafWMAPEMLRGEPYDRKVDVFSFGIVLCEIL--ARIP----ADPEVLPRTGDfgldvqAFKEMVP-GC 220
                         250       260       270
                  ....*....|....*....|....*....|..
gi 2038291632 852 PAPLYELMKNCWAYDRARRPHFLQLQAHLEQL 883
Cdd:cd14156   221 PEPFLDLAASCCRMDAFKRPSFAELLDELEDI 252
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
620-879 2.31e-20

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: 92.37  E-value: 2.31e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 620 DP--TWLIVDtVIGEGEFGEVYRGALRfpsQDCKTVAIKTLkDTSPDGQWwNFLREATIMGQF-NHPHILRLEGVVTKRK 696
Cdd:cd06608     3 DPagIFELVE-VIGEGTYGKVYKARHK---KTGQLAAIKIM-DIIEDEEE-EIKLEINILRKFsNHPNIATFYGAFIKKD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 697 P------IMIVTEFMENGALDAFLKE--REDQLAPGQLVAMLL-GIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSD 767
Cdd:cd06608    77 PpggddqLWLVMEYCGGGSVTDLVKGlrKKGKRLKEEWIAYILrETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 768 FGLTRLLDDFDGTYETQGGKiPIrWTAPEAIA-----HRIFTTASDVWSFGIVMWEvLSFGDKPYGEMNNQEVMKSIEeg 842
Cdd:cd06608   157 FGVSAQLDSTLGRRNTFIGT-PY-WMAPEVIAcdqqpDASYDARCDVWSLGITAIE-LADGKPPLCDMHPMRALFKIP-- 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2038291632 843 yRLPPP-VDCPAP----LYELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd06608   232 -RNPPPtLKSPEKwskeFNDFISECLIKNYEQRPFTEELLEH 272
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
625-879 4.48e-20

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: 91.00  E-value: 4.48e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 625 IVDTVIGEGEFGEV---YRGALRFpsqdckTVAIKTL-KDTSPDGQWWNFL-REATIMGQFNHPHILRL-EGVVTKRKPI 698
Cdd:cd14165     4 ILGINLGEGSYAKVksaYSERLKC------NVAIKIIdKKKAPDDFVEKFLpRELEILARLNHKSIIKTyEIFETSDGKV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 699 MIVTEFMENGALDAFLKERedqLAPGQLVA--MLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTR-LLD 775
Cdd:cd14165    78 YIVMELGVQGDLLEFIKLR---GALPEDVArkMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKrCLR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 776 DFDGTY---ETQGGKIPirWTAPEAIAHRIFT-TASDVWSFGIVMWeVLSFGDKPYGEMNNQEVMK-SIEEGYRLPPPVD 850
Cdd:cd14165   155 DENGRIvlsKTFCGSAA--YAAPEVLQGIPYDpRIYDIWSLGVILY-IMVCGSMPYDDSNVKKMLKiQKEHRVRFPRSKN 231
                         250       260
                  ....*....|....*....|....*....
gi 2038291632 851 CPAPLYELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd14165   232 LTSECKDLIYRLLQPDVSQRLCIDEVLSH 260
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
911-976 5.46e-20

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 84.65  E-value: 5.46e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2038291632  911 DGIPYRSVSEWLESIRMKRYILHFRSAGLDTMECVLELTAEDLTQMGITLPGHQKRILCSIQGFKD 976
Cdd:smart00454   2 SQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLKE 67
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
629-879 5.99e-20

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: 90.88  E-value: 5.99e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRgALRFPSQDckTVAIKTLK----DTSPDgqwwNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEF 704
Cdd:cd06610     8 VIGSGATAVVYA-AYCLPKKE--KVAIKRIDlekcQTSMD----ELRKEIQAMSQCNHPNVVSYYTSFVVGDELWLVMPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 705 MENGALDAFLKER--EDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLddFDGTYE 782
Cdd:cd06610    81 LSGGSLLDIMKSSypRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVSASL--ATGGDR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 783 TQGGKIPIR----WTAPEAIA-HRIFTTASDVWSFGIVMWEvLSFGDKPYGEMNNQEV-MKSIEEGyrlPPPVD------ 850
Cdd:cd06610   159 TRKVRKTFVgtpcWMAPEVMEqVRGYDFKADIWSFGITAIE-LATGAAPYSKYPPMKVlMLTLQND---PPSLEtgadyk 234
                         250       260       270
                  ....*....|....*....|....*....|
gi 2038291632 851 -CPAPLYELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd06610   235 kYSKSFRKMISLCLQKDPSKRPTAEELLKH 264
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
630-820 6.69e-20

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: 91.66  E-value: 6.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGalrfpsQDCKT---VAIKTLK-DTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRK--PIMIVTE 703
Cdd:cd07845    15 IGEGTYGIVYRA------RDTTSgeiVALKKVRmDNERDGIPISSLREITLLLNLRHPNIVELKEVVVGKHldSIFLVME 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 704 FMENGaLDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYET 783
Cdd:cd07845    89 YCEQD-LASLLDNMPTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGLARTYGLPAKPMTP 167
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2038291632 784 qggKIPIRW-TAPEAI-AHRIFTTASDVWSFGIVMWEVL 820
Cdd:cd07845   168 ---KVVTLWyRAPELLlGCTTYTTAIDMWAVGCILAELL 203
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
625-826 6.69e-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: 90.62  E-value: 6.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 625 IVDTVIGEGEFGEVYRG--ALRFPSQDCKTVAIKTLK--DTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMI 700
Cdd:cd14076     4 ILGRTLGEGEFGKVKLGwpLPKANHRSGVQVAIKLIRrdTQQENCQTSKIMREINILKGLTHPNIVRLLDVLKTKKYIGI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 701 VTEFMENGAL------DAFLKEREDQLAPGQLVamllgiaSGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLL 774
Cdd:cd14076    84 VLEFVSGGELfdyilaRRRLKDSVACRLFAQLI-------SGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANTF 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2038291632 775 DDFDGTYETQGGKIPIrWTAPEAIAHRIFTTAS--DVWSFGIVMWEVLS----FGDKP 826
Cdd:cd14076   157 DHFNGDLMSTSCGSPC-YAAPELVVSDSMYAGRkaDIWSCGVILYAMLAgylpFDDDP 213
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
626-846 7.68e-20

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: 90.14  E-value: 7.68e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 626 VDTVIGEGEFGEVYRGALRFpsqdCKT-VAIKTLKDTSPDGQwwNF---LREATIMGQFNHPHILRLEGVVTKRKPIMIV 701
Cdd:cd14071     4 IERTIGKGNFAVVKLARHRI----TKTeVAIKIIDKSQLDEE--NLkkiYREVQIMKMLNHPHIIKLYQVMETKDMLYLV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 702 TEFMENGALDAFLKeREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDfDGTY 781
Cdd:cd14071    78 TEYASNGEIFDYLA-QHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFSNFFKP-GELL 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038291632 782 ETQGGKIPirWTAPEAIAHRIFTTAS-DVWSFGIVMWeVLSFGDKPYGEMNNQEVMKSIEEG-YRLP 846
Cdd:cd14071   156 KTWCGSPP--YAAPEVFEGKEYEGPQlDIWSLGVVLY-VLVCGALPFDGSTLQTLRDRVLSGrFRIP 219
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
630-886 8.03e-20

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: 90.27  E-value: 8.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVyRGALRFPSQdcKTVAIKTLKDTS-PDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENG 708
Cdd:cd14072     8 IGKGNFAKV-KLARHVLTG--REVAIKIIDKTQlNPSSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEYASGG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 ALDAFL------KEREDQLAPGQLVamllgiaSGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTrllDDFdgtye 782
Cdd:cd14072    85 EVFDYLvahgrmKEKEARAKFRQIV-------SAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFS---NEF----- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 783 TQGGKIPIRWTAPEAIAHRIFTTAS------DVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSIEEG-YRLP--PPVDCPa 853
Cdd:cd14072   150 TPGNKLDTFCGSPPYAAPELFQGKKydgpevDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGkYRIPfyMSTDCE- 227
                         250       260       270
                  ....*....|....*....|....*....|...
gi 2038291632 854 plyELMKNCWAYDRARRphflqlqAHLEQLLTD 886
Cdd:cd14072   228 ---NLLKKFLVLNPSKR-------GTLEQIMKD 250
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
630-826 8.50e-20

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: 91.04  E-value: 8.50e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRfpsqdcKTV-AIKTLKDTSpDGQW----WNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEF 704
Cdd:cd14159     1 IGEGGFGCVYQAVMR------NTEyAVKRLKEDS-ELDWsvvkNSFLTEVEKLSRFRHPNIVDLAGYSAQQGNYCLIYVY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 705 MENGALDAFLKERED--QLAPGQLVAMLLGIASGMNYLsgHNY----VHRDLAARNILVNQNLCCKVSDFGLTRLlddfd 778
Cdd:cd14159    74 LPNGSLEDRLHCQVScpCLSWSQRLHVLLGTARAIQYL--HSDspslIHGDVKSSNILLDAALNPKLGDFGLARF----- 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2038291632 779 GTYETQGGKI-------PIRWT----APEAIAHRIFTTASDVWSFGIVMWEVLSfGDKP 826
Cdd:cd14159   147 SRRPKQPGMSstlartqTVRGTlaylPEEYVKTGTLSVEIDVYSFGVVLLELLT-GRRA 204
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
630-821 9.48e-20

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: 90.64  E-value: 9.48e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRfpsQDCKTVAIKTLK-DTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENG 708
Cdd:cd07860     8 IGEGTYGVVYKARNK---LTGEVVALKKIRlDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFLHQD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 aldafLKEREDQLAPG-----QLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYET 783
Cdd:cd07860    85 -----LKKFMDASALTgiplpLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYTH 159
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2038291632 784 QggKIPIRWTAPEA-IAHRIFTTASDVWSFGIVMWEVLS 821
Cdd:cd07860   160 E--VVTLWYRAPEIlLGCKYYSTAVDIWSLGCIFAEMVT 196
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
623-851 1.02e-19

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: 89.62  E-value: 1.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 623 WLIVDTvIGEGEFGEVYrgaLRFPSQDCKTVAIKTLKDT--SPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMI 700
Cdd:cd14081     3 YRLGKT-LGKGQTGLVK---LAKHCVTGQKVAIKIVNKEklSKESVLMKVEREIAIMKLIEHPNVLKLYDVYENKKYLYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 701 VTEFMENGAL-DAFLKERedQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRlLDDFDG 779
Cdd:cd14081    79 VLEYVSGGELfDYLVKKG--RLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMAS-LQPEGS 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2038291632 780 TYETQGGKiPiRWTAPEAIAHRIFT-TASDVWSFGIVMWeVLSFGDKPYGEMNNQEVMKSIEEG-YRLPP--PVDC 851
Cdd:cd14081   156 LLETSCGS-P-HYACPEVIKGEKYDgRKADIWSCGVILY-ALLVGALPFDDDNLRQLLEKVKRGvFHIPHfiSPDA 228
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
630-842 2.08e-19

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: 89.14  E-value: 2.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRfpsQDCKTVAIKTLkDTSPDGQWWNFL--REATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMEN 707
Cdd:cd14097     9 LGQGSFGVVIEATHK---ETQTKWAIKKI-NREKAGSSAVKLleREVDILKHVNHAHIIHLEEVFETPKRMYLVMELCED 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GALDAFLkEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILV-------NQNLCCKVSDFGLT-----RLLD 775
Cdd:cd14097    85 GELKELL-LRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVkssiidnNDKLNIKVTDFGLSvqkygLGED 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038291632 776 DFDGTYETqggkiPIrWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSIEEG 842
Cdd:cd14097   164 MLQETCGT-----PI-YMAPEVISAHGYSQQCDIWSIGVIMYMLLC-GEPPFVAKSEEKLFEEIRKG 223
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
625-846 3.65e-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: 88.12  E-value: 3.65e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 625 IVDTVIGEGEFGEVYRGalrFPSQDCKTVAIKTL-KDTSPDGQWWNFL-REATIMGQFNHPHILRLEGVVTKRKPIMIVT 702
Cdd:cd14162     3 IVGKTLGHGSYAVVKKA---YSTKHKCKVAIKIVsKKKAPEDYLQKFLpREIEVIKGLKHPNLICFYEAIETTSRVYIIM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 703 EFMENGAL------DAFLKEREDQLAPGQLVAmllgiasGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRlldd 776
Cdd:cd14162    80 ELAENGDLldyirkNGALPEPQARRWFRQLVA-------GVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFAR---- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 777 fdGTYETQGGKIPIRWT--------APE---AIAHRIFttASDVWSFGIVMWEVLsFGDKPYGEMNNQEVMKSIEEGYRL 845
Cdd:cd14162   149 --GVMKTKDGKPKLSETycgsyayaSPEilrGIPYDPF--LSDIWSMGVVLYTMV-YGRLPFDDSNLKVLLKQVQRRVVF 223

                  .
gi 2038291632 846 P 846
Cdd:cd14162   224 P 224
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
679-879 5.48e-19

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: 87.80  E-value: 5.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 679 QFNHPHILRLEGVVTKRKP------IMIVTEFMENGALDAFLkEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAA 752
Cdd:cd14012    54 KLRHPNLVSYLAFSIERRGrsdgwkVYLLTEYAPGGSLSELL-DSVGSVPLDTARRWTLQLLEALEYLHRNGVVHKSLHA 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 753 RNILVNQNLC---CKVSDFGLTRLLDDFDgtyeTQGGKI---PIRWTAPEAIA-HRIFTTASDVWSFGIVMWEvLSFGdk 825
Cdd:cd14012   133 GNVLLDRDAGtgiVKLTDYSLGKTLLDMC----SRGSLDefkQTYWLPPELAQgSKSPTRKTDVWDLGLLFLQ-MLFG-- 205
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2038291632 826 pygemnnQEVMKSIEEGYRLPPPVDCPAPLYELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd14012   206 -------LDVLEKYTSPNPVLVSLDLSASLQDFLSKCLSLDPKKRPTALELLPH 252
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
629-879 5.93e-19

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: 88.53  E-value: 5.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRFPSQdckTVAIKTLKDTSPDGQWWNF-LREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMEN 707
Cdd:cd07833     8 VVGEGAYGVVLKCRNKATGE---IVAIKKFKESEDDEDVKKTaLREVKVLRQLRHENIVNLKEAFRRKGRLYLVFEYVER 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GALDaFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLddfdgtyeTQGGK 787
Cdd:cd07833    85 TLLE-LLEASPGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFARAL--------TARPA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 788 IPI------RW-TAPEA-IAHRIFTTASDVWSFGIVMWEVLS----F-GD----------KPYGEMN------------- 831
Cdd:cd07833   156 SPLtdyvatRWyRAPELlVGDTNYGKPVDVWAIGCIMAELLDgeplFpGDsdidqlyliqKCLGPLPpshqelfssnprf 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2038291632 832 ------NQEVMKSIEEGYrlppPVDCPAPLYELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd07833   236 agvafpEPSQPESLERRY----PGKVSSPALDFLKACLRMDPKERLTCDELLQH 285
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
639-883 5.94e-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: 88.04  E-value: 5.94e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 639 YRGALrfpsqdcktVAIKTLKDTSPDGQWwNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGALDAFLkERE 718
Cdd:cd14042    28 YKGNL---------VAIKKVNKKRIDLTR-EVLKELKHMRDLQHDNLTRFIGACVDPPNICILTEYCPKGSLQDIL-ENE 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 719 D-QLAPGQLVAMLLGIASGMNYLsgHNYV---HRDLAARNILVNQNLCCKVSDFGLTRL---LDDFDGTYETQGGKIpir 791
Cdd:cd14042    97 DiKLDWMFRYSLIHDIVKGMHYL--HDSEiksHGNLKSSNCVVDSRFVLKITDFGLHSFrsgQEPPDDSHAYYAKLL--- 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 792 WTAPEAIAHRIF----TTASDVWSFGIVMWEVLS----FGDKPYGEMNNQEVMKSIEEGYRLP-----PPVDCPAPLYEL 858
Cdd:cd14042   172 WTAPELLRDPNPpppgTQKGDVYSFGIILQEIATrqgpFYEEGPDLSPKEIIKKKVRNGEKPPfrpslDELECPDEVLSL 251
                         250       260
                  ....*....|....*....|....*
gi 2038291632 859 MKNCWAYDRARRPHFLQLQAHLEQL 883
Cdd:cd14042   252 MQRCWAEDPEERPDFSTLRNKLKKL 276
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
629-876 6.09e-19

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: 88.05  E-value: 6.09e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRFPSQDCKTVAIKTLKDTSPDGQWWNFLR---------------EATIMGQFNHPHILRLEGVVT 693
Cdd:cd14000     1 LLGDGGFGSVYRASYKGEPVAVKIFNKHTSSNFANVPADTMLRHlratdamknfrllrqELTVLSHLHHPSIVYLLGIGI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 694 KrkPIMIVTEFMENGALDAFLKEREDQLAPgqLVAML-----LGIASGMNYLSGHNYVHRDLAARNILV-----NQNLCC 763
Cdd:cd14000    81 H--PLMLVLELAPLGSLDHLLQQDSRSFAS--LGRTLqqriaLQVADGLRYLHSAMIIYRDLKSHNVLVwtlypNSAIII 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 764 KVSDFGLTRllDDFDGTYETQGGKIPIRwtAPEAIAHR-IFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEeg 842
Cdd:cd14000   157 KIADYGISR--QCCRMGAKGSEGTPGFR--APEIARGNvIYNEKVDVFSFGMLLYEILSGGAPMVGHLKFPNEFDIHG-- 230
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2038291632 843 yRLPPPV---DC--PAPLYELMKNCWAYDRARRPHFLQL 876
Cdd:cd14000   231 -GLRPPLkqyECapWPEVEVLMKKCWKENPQQRPTAVTV 268
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
630-879 7.96e-19

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: 87.44  E-value: 7.96e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRgALRFPSQD---CKTVAI-KTLKDTSPDGQ--WWNFLR-EATIMGQFNHPHILRLEGVVTKRKPIMIVT 702
Cdd:cd06629     9 IGKGTYGRVYL-AMNATTGEmlaVKQVELpKTSSDRADSRQktVVDALKsEIDTLKDLDHPNIVQYLGFEETEDYFSIFL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 703 EFMENGALDAFLKE----REDqlapgqLVAMLLG-IASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDF 777
Cdd:cd06629    88 EYVPGGSIGSCLRKygkfEED------LVRFFTRqILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGISKKSDDI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 778 DGTYETQGGKIPIRWTAPEAI--AHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSIEEGYRLPP-PVDC--P 852
Cdd:cd06629   162 YGNNGATSMQGSVFWMAPEVIhsQGQGYSAKVDIWSLGCVVLEMLA-GRRPWSDDEAIAAMFKLGNKRSAPPvPEDVnlS 240
                         250       260
                  ....*....|....*....|....*..
gi 2038291632 853 APLYELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd06629   241 PEALDFLNACFAIDPRDRPTAAELLSH 267
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
630-852 8.43e-19

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: 88.17  E-value: 8.43e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGalRFPSQDCKTVAIKTLK-DTSPDGQWWNFLREATIMGQ---FNHPHILRLEGVVT-----KRKPIMI 700
Cdd:cd07862     9 IGEGAYGKVFKA--RDLKNGGRFVALKRVRvQTGEEGMPLSTIREVAVLRHletFEHPNVVRLFDVCTvsrtdRETKLTL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 701 VTEFMENGaLDAFLKEREDQLAPGQLVA-MLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLlddFDG 779
Cdd:cd07862    87 VFEHVDQD-LTTYLDKVPEPGVPTETIKdMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLARI---YSF 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038291632 780 TYETQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVlsFGDKPYGEMNNQ-EVMKSIEEGYRLPPPVDCP 852
Cdd:cd07862   163 QMALTSVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEM--FRRKPLFRGSSDvDQLGKILDVIGLPGEEDWP 234
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
630-821 1.19e-18

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: 87.25  E-value: 1.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFPSQDCKTvaIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGA 709
Cdd:cd14160     1 IGEGEIFEVYRVRIGNRSYAVKL--FKQEKKMQWKKHWKRFLSELEVLLLFQHPNILELAAYFTETEKFCLVYPYMQNGT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 710 L-DAFLKEREDQLAPGQL-VAMLLGIASGMNYLsgHN-----YVHRDLAARNILVNQNLCCKVSDFGLTRL---LDDFDG 779
Cdd:cd14160    79 LfDRLQCHGVTKPLSWHErINILIGIAKAIHYL--HNsqpctVICGNISSANILLDDQMQPKLTDFALAHFrphLEDQSC 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2038291632 780 TYETQGGKIPIRWTAPEA-IAHRIFTTASDVWSFGIVMWEVLS 821
Cdd:cd14160   157 TINMTTALHKHLWYMPEEyIRQGKLSVKTDVYSFGIVIMEVLT 199
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
630-818 1.20e-18

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: 87.33  E-value: 1.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRfpsQDCKTVAIKTLK-DTSPDGQWWNFLREATIMGQ---FNHPHILRL----EGVVTKRK-PIMI 700
Cdd:cd07838     7 IGEGAYGTVYKARDL---QDGRFVALKKVRvPLSEEGIPLSTIREIALLKQlesFEHPNVVRLldvcHGPRTDRElKLTL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 701 VTEFMENGaLDAFL-KEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRllddfdg 779
Cdd:cd07838    84 VFEHVDQD-LATYLdKCPKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADFGLAR------- 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2038291632 780 TYETQGGKIPIRWT----APEAIAHRIFTTASDVWSFGIVMWE 818
Cdd:cd07838   156 IYSFEMALTSVVVTlwyrAPEVLLQSSYATPVDMWSVGCIFAE 198
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
628-883 1.25e-18

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: 86.39  E-value: 1.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 628 TVIGEGEFGEVYRGalRFPSQDcktVAIKTLK--DTSPDGQWwNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFM 705
Cdd:cd14057     1 TKINETHSGELWKG--RWQGND---IVAKILKvrDVTTRISR-DFNEEYPRLRIFSHPNVLPVLGACNSPPNLVVISQYM 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 706 ENGALDAFLKERE----DQlapGQLVAMLLGIASGMNYL-SGHNYVHR-DLAARNILVNQNLCCKVSdfgltrlLDDFDG 779
Cdd:cd14057    75 PYGSLYNVLHEGTgvvvDQ---SQAVKFALDIARGMAFLhTLEPLIPRhHLNSKHVMIDEDMTARIN-------MADVKF 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 780 TYETQGGKIPIRWTAPEAIAHR---IFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEV-MKSIEEGYRLPPPVDCPAPL 855
Cdd:cd14057   145 SFQEPGKMYNPAWMAPEALQKKpedINRRSADMWSFAILLWELVT-REVPFADLSNMEIgMKIALEGLRVTIPPGISPHM 223
                         250       260
                  ....*....|....*....|....*...
gi 2038291632 856 YELMKNCWAYDRARRPHFLQLQAHLEQL 883
Cdd:cd14057   224 CKLMKICMNEDPGKRPKFDMIVPILEKM 251
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
626-821 1.41e-18

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 88.28  E-value: 1.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 626 VDTVIGEGEFGEVYRGalrFPSQDCKTVAIKTLK------DTSPDGQW-----WNF--LREATIMGQFNHPHILRLEGVV 692
Cdd:PTZ00024   13 KGAHLGEGTYGKVEKA---YDTLTGKIVAIKKVKiieisnDVTKDRQLvgmcgIHFttLRELKIMNEIKHENIMGLVDVY 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 693 TKRKPIMIVTEFMEnGALDAFLkEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTR 772
Cdd:PTZ00024   90 VEGDFINLVMDIMA-SDLKKVV-DRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGLAR 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038291632 773 --LLDDFDGTYETQGGKIPIR----------WTAPEAI--AHRiFTTASDVWSFGIVMWEVLS 821
Cdd:PTZ00024  168 ryGYPPYSDTLSKDETMQRREemtskvvtlwYRAPELLmgAEK-YHFAVDMWSVGCIFAELLT 229
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
630-839 1.88e-18

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: 86.77  E-value: 1.88e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFPSQdckTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGa 709
Cdd:cd07836     8 LGEGTYATVYKGRNRTTGE---IVALKEIHLDAEEGTPSTAIREISLMKELKHENIVRLHDVIHTENKLMLVFEYMDKD- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 710 LDAFLKEREDQ--LAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRlldDFDGTYETQGGK 787
Cdd:cd07836    84 LKKYMDTHGVRgaLDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLAR---AFGIPVNTFSNE 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2038291632 788 IPIRW-TAPEAI-AHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSI 839
Cdd:cd07836   161 VVTLWyRAPDVLlGSRTYSTSIDIWSVGCIMAEMIT-GRPLFPGTNNEDQLLKI 213
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
629-821 2.06e-18

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: 87.03  E-value: 2.06e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALrfpsqDCKTVAIKTLkdtsPDGQWWNFLREATIMGQF--NHPHILRLegVVTKRKPI-------M 699
Cdd:cd14054     2 LIGQGRYGTVWKGSL-----DERPVAVKVF----PARHRQNFQNEKDIYELPlmEHSNILRF--IGADERPTadgrmeyL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 700 IVTEFMENGALDAFLkeREDQLAPGQLVAMLLGIASGMNYL-----SGHNY----VHRDLAARNILVNQNLCCKVSDFGL 770
Cdd:cd14054    71 LVLEYAPKGSLCSYL--RENTLDWMSSCRMALSLTRGLAYLhtdlrRGDQYkpaiAHRDLNSRNVLVKADGSCVICDFGL 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2038291632 771 ---TRLLDDFDGTYETQGGKIP-----IRWTAPE----AIAHRIFTTA---SDVWSFGIVMWEVLS 821
Cdd:cd14054   149 amvLRGSSLVRGRPGAAENASIsevgtLRYMAPEvlegAVNLRDCESAlkqVDVYALGLVLWEIAM 214
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
626-827 2.14e-18

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: 86.07  E-value: 2.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 626 VDTVIGEGEFGEVYRGALRFPSQDcktVAIKTL--KDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTE 703
Cdd:cd14186     5 VLNLLGKGSFACVYRARSLHTGLE---VAIKMIdkKAMQKAGMVQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLVLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 704 FMENGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYET 783
Cdd:cd14186    82 MCHNGEMSRYLKNRKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLKMPHEKHFT 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2038291632 784 QGGKiPiRWTAPEAIAHRIFTTASDVWSFGIVMWEVLsFGDKPY 827
Cdd:cd14186   162 MCGT-P-NYISPEIATRSAHGLESDVWSLGCMFYTLL-VGRPPF 202
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
623-842 2.27e-18

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: 86.35  E-value: 2.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 623 WLIVDTvIGEGEFGEVYRGALRfpsQDCKTVAIKTLKDTSPDGQWWNF--------------LREATIMGQFNHPHILRL 688
Cdd:cd14077     3 WEFVKT-IGAGSMGKVKLAKHI---RTGEKCAIKIIPRASNAGLKKERekrlekeisrdirtIREAALSSLLNHPHICRL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 689 EGVVTKRKPIMIVTEFMENGALDAFL----KEREDQlapGQLVAMllGIASGMNYLSGHNYVHRDLAARNILVNQNLCCK 764
Cdd:cd14077    79 RDFLRTPNHYYMLFEYVDGGQLLDYIishgKLKEKQ---ARKFAR--QIASALDYLHRNSIVHRDLKIENILISKSGNIK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 765 VSDFGLT------RLLDDFDGTyetqggkipIRWTAPEAIAHRIFTTAS-DVWSFGIVMWeVLSFGDKPYGEMNNQEVMK 837
Cdd:cd14077   154 IIDFGLSnlydprRLLRTFCGS---------LYFAAPELLQAQPYTGPEvDVWSFGVVLY-VLVCGKVPFDDENMPALHA 223

                  ....*
gi 2038291632 838 SIEEG 842
Cdd:cd14077   224 KIKKG 228
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
630-879 2.34e-18

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: 85.77  E-value: 2.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVyRGALrfpsqDCKT---VAIKTLKDTS----PDGqWWNFLREATIMGQFNHPHILRLEGVVT---KRKPIM 699
Cdd:cd14119     1 LGEGSYGKV-KEVL-----DTETlcrRAVKILKKRKlrriPNG-EANVKREIQILRRLNHRNVIKLVDVLYneeKQKLYM 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 700 ivteFME--NGALDAFLKERED-QLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDD 776
Cdd:cd14119    74 ----VMEycVGGLQEMLDSAPDkRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVAEALDL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 777 FDGTYE---TQGGkiPiRWTAPE-AIAHRIFT-TASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSIEEG-YRLPPpvD 850
Cdd:cd14119   150 FAEDDTcttSQGS--P-AFQPPEiANGQDSFSgFKVDIWSAGVTLYNMTT-GKYPFEGDNIYKLFENIGKGeYTIPD--D 223
                         250       260
                  ....*....|....*....|....*....
gi 2038291632 851 CPAPLYELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd14119   224 VDPDLQDLLRGMLEKDPEKRFTIEQIRQH 252
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
629-883 2.70e-18

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: 86.34  E-value: 2.70e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRfpsqdCKTVAIKTLkdTSPDGQWWnfLREA----TIMgqFNHPHIL-------RLEGVVTKrkp 697
Cdd:cd14143     2 SIGKGRFGEVWRGRWR-----GEDVAVKIF--SSREERSW--FREAeiyqTVM--LRHENILgfiaadnKDNGTWTQ--- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 698 IMIVTEFMENGALDAFLKERedQLAPGQLVAMLLGIASGMNYLsgHNYV----------HRDLAARNILVNQNLCCKVSD 767
Cdd:cd14143    68 LWLVSDYHEHGSLFDYLNRY--TVTVEGMIKLALSIASGLAHL--HMEIvgtqgkpaiaHRDLKSKNILVKKNGTCCIAD 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 768 FGLTRLLDDFDGTYETQ-----GGKipiRWTAPEAIAHRIFTTA------SDVWSFGIVMWEV---LSFGDK------PY 827
Cdd:cd14143   144 LGLAVRHDSATDTIDIApnhrvGTK---RYMAPEVLDDTINMKHfesfkrADIYALGLVFWEIarrCSIGGIhedyqlPY 220
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038291632 828 GEM----NNQEVMKSI--EEGYRLPPP-----VDCPAPLYELMKNCWAYDRARRPHFLQLQAHLEQL 883
Cdd:cd14143   221 YDLvpsdPSIEEMRKVvcEQKLRPNIPnrwqsCEALRVMAKIMRECWYANGAARLTALRIKKTLSQL 287
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
627-879 3.21e-18

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: 85.35  E-value: 3.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 627 DTVIGEGEFGEVYRGalrFPSQDCKTVA---IKTLKDTSPDGQwwNFLREATIMGQFNHPHILRLEG--VVTKRKPIMIV 701
Cdd:cd13983     6 NEVLGRGSFKTVYRA---FDTEEGIEVAwneIKLRKLPKAERQ--RFKQEIEILKSLKHPNIIKFYDswESKSKKEVIFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 702 TEFMENGALDAFLKeREDQLAPGQLVAMLLGIASGMNYLSGHNY--VHRDLAARNILVNQNL-CCKVSDFGL-TRLLDDF 777
Cdd:cd13983    81 TELMTSGTLKQYLK-RFKRLKLKVIKSWCRQILEGLNYLHTRDPpiIHRDLKCDNIFINGNTgEVKIGDLGLaTLLRQSF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 778 D----GTYEtqggkipirWTAPEAIAHRiFTTASDVWSFGIVMWEVLSfGDKPYGE-MNNQEVMKSIEEGYrlpPP---- 848
Cdd:cd13983   160 AksviGTPE---------FMAPEMYEEH-YDEKVDIYAFGMCLLEMAT-GEYPYSEcTNAAQIYKKVTSGI---KPesls 225
                         250       260       270
                  ....*....|....*....|....*....|..
gi 2038291632 849 -VDCPaPLYELMKNCWAyDRARRPHFLQLQAH 879
Cdd:cd13983   226 kVKDP-ELKDFIEKCLK-PPDERPSARELLEH 255
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
628-869 3.33e-18

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: 86.28  E-value: 3.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 628 TVIGEGEFGEVYRGALRF-PSQDCKTVAIKTLkdTSPDGQWWNFLREATIMGQFNHPHILRL----EGVVTKRKPIMIVT 702
Cdd:cd14055     1 KLVGKGRFAEVWKAKLKQnASGQYETVAVKIF--PYEEYASWKNEKDIFTDASLKHENILQFltaeERGVGLDRQYWLIT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 703 EFMENGALDAFLKERedQLAPGQLVAMLLGIASGMNYLSGHNY---------VHRDLAARNILVNQNLCCKVSDFGLTRL 773
Cdd:cd14055    79 AYHENGSLQDYLTRH--ILSWEDLCKMAGSLARGLAHLHSDRTpcgrpkipiAHRDLKSSNILVKNDGTCVLADFGLALR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 774 LDDFDGTYE-TQGGKI-PIRWTAPEAIAHRIFTT------ASDVWSFGIVMWEVLS--------------FGDKpYGEMN 831
Cdd:cd14055   157 LDPSLSVDElANSGQVgTARYMAPEALESRVNLEdlesfkQIDVYSMALVLWEMASrceasgevkpyelpFGSK-VRERP 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2038291632 832 NQEVMKSIEEGYRLPPPVdcPAP---------LYELMKNCWAYD-RAR 869
Cdd:cd14055   236 CVESMKDLVLRDRGRPEI--PDSwlthqgmcvLCDTITECWDHDpEAR 281
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
624-847 4.19e-18

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: 85.73  E-value: 4.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 624 LIVDTVIGEGEFGEVYRGALRFPSqdcKTVAIKTLkDTSpdgqwwnFL----------REATIMGQFNHPHILRLEGVVT 693
Cdd:cd05581     3 FKFGKPLGEGSYSTVVLAKEKETG---KEYAIKVL-DKR-------HIikekkvkyvtIEKEVLSRLAHPGIVKLYYTFQ 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 694 KRKPIMIVTEFMENGALDAFLK------EREDQLAPGQLVamllgiaSGMNYLSGHNYVHRDLAARNILVNQNLCCKVSD 767
Cdd:cd05581    72 DESKLYFVLEYAPNGDLLEYIRkygsldEKCTRFYTAEIV-------LALEYLHSKGIIHRDLKPENILLDEDMHIKITD 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 768 FGLTRLLDD------FDGTYETQGGKIPIR---------WTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNN 832
Cdd:cd05581   145 FGTAKVLGPdsspesTKGDADSQIAYNQARaasfvgtaeYVSPELLNEKPAGKSSDLWALGCIIYQMLT-GKPPFRGSNE 223
                         250
                  ....*....|....*.
gi 2038291632 833 QEVMKSIEEG-YRLPP 847
Cdd:cd05581   224 YLTFQKIVKLeYEFPE 239
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
629-839 4.99e-18

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: 86.30  E-value: 4.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRFPSQDCKTVAIKTLKDTSPDGQwwNFLR---EATIMGQFNHPHILRLEGVVTKRKPIMIVTEFM 705
Cdd:cd05582     2 VLGQGSFGKVFLVRKITGPDAGTLYAMKVLKKATLKVR--DRVRtkmERDILADVNHPFIVKLHYAFQTEGKLYLILDFL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 706 ENGalDAFLKEREDQLAPGQLVAMLLG-IASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTR-LLDDFDGTYET 783
Cdd:cd05582    80 RGG--DLFTRLSKEVMFTEEDVKFYLAeLALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKeSIDHEKKAYSF 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2038291632 784 QGgkiPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSI 839
Cdd:cd05582   158 CG---TVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GSLPFQGKDRKETMTMI 209
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
625-879 5.81e-18

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: 84.75  E-value: 5.81e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 625 IVDTVIGEGEFGEVYRgALRFpsQDCKTVAIKTLKDTS-PDGQWWNFLREATIMGQFNHPHILRL-EGVVTKRKpIMIVT 702
Cdd:cd08530     3 KVLKKLGKGSYGSVYK-VKRL--SDNQVYALKEVNLGSlSQKEREDSVNEIRLLASVNHPNIIRYkEAFLDGNR-LCIVM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 703 EFMENGALDAFLKEREDQ--LAPGQLV-AMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDdfDG 779
Cdd:cd08530    79 EYAPFGDLSKLISKRKKKrrLFPEDDIwRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGISKVLK--KN 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 780 TYETQGGKiPIrWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGdKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLYELM 859
Cdd:cd08530   157 LAKTQIGT-PL-YAAPEVWKGRPYDYKSDIWSLGCLLYEMATFR-PPFEARTMQELRYKVCRGKFPPIPPVYSQDLQQII 233
                         250       260
                  ....*....|....*....|
gi 2038291632 860 KNCWAYDRARRPHFLQLQAH 879
Cdd:cd08530   234 RSLLQVNPKKRPSCDKLLQS 253
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
623-829 6.91e-18

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: 84.69  E-value: 6.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 623 WLIVDTvIGEGEFGEVYRGALRFPSqdcKTVAIKTLKDTSPDGQWWNFLR-EATIMGQFNHPHILRLEGVVtKRKPIM-I 700
Cdd:cd14069     3 WDLVQT-LGEGAFGEVFLAVNRNTE---EAVAVKFVDMKRAPGDCPENIKkEVCIQKMLSHKNVVRFYGHR-REGEFQyL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 701 VTEFMENGAL------DAFLKEREDQLAPGQLVamllgiaSGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLT--- 771
Cdd:cd14069    78 FLEYASGGELfdkiepDVGMPEDVAQFYFQQLM-------AGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLAtvf 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2038291632 772 ------RLLDDFDGTyetqggkIPirWTAPEAIAHRIF-TTASDVWSFGIVMWEVLSfGDKPYGE 829
Cdd:cd14069   151 rykgkeRLLNKMCGT-------LP--YVAPELLAKKKYrAEPVDVWSCGIVLFAMLA-GELPWDQ 205
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
629-876 7.39e-18

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: 84.23  E-value: 7.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRfpSQDcktVAIKTL-KDTSpdgqwWNFLR-EATIMGQFNHPHILRLEGVVTKrkPIMIVTEFME 706
Cdd:cd14068     1 LLGDGGFGSVYRAVYR--GED---VAVKIFnKHTS-----FRLLRqELVVLSHLHHPSLVALLAAGTA--PRMLVMELAP 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 707 NGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILV-----NQNLCCKVSDFGLTRLLDDFD-GT 780
Cdd:cd14068    69 KGSLDALLQQDNASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLftlypNCAIIAKIADYGIAQYCCRMGiKT 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 781 YETQGGkipirWTAPE-AIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPV---DC-PAPL 855
Cdd:cd14068   149 SEGTPG-----FRAPEvARGNVIYNQQADVYSFGLLLYDILTCGERIVEGLKFPNEFDELAIQGKLPDPVkeyGCaPWPG 223
                         250       260
                  ....*....|....*....|..
gi 2038291632 856 YE-LMKNCWAYDRARRPHFLQL 876
Cdd:cd14068   224 VEaLIKDCLKENPQCRPTSAQV 245
SAM_EPH-B4 cd09554
SAM domain of EPH-B4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
917-975 8.21e-18

SAM domain of EPH-B4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B4 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B4 receptors and appears to mediate cell-cell initiated signal transduction. EPH-B4 protein kinase performs kinase-dependent and kinase-independent functions. These receptors play a role in the regular vascular system development during embryogenesis. They were found overexpressed in a variety of cancers, including carcinoma of the head and neck, ovarian cancer, bladder cancer, and downregulated in bone myeloma. Thus, EphB4 is a potential biomarker and a target for drug design.


Pssm-ID: 188953  Cd Length: 67  Bit Score: 78.37  E-value: 8.21e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2038291632 917 SVSEWLESIRMKRYILHFRSAGLDTMECVLELTAEDLTQMGITLPGHQKRILCSIQGFK 975
Cdd:cd09554     5 SVGEWLRAIKMERYEDSFLQAGFTTFQLVSQISTEDLLRMGVTLAGHQKKILSSIQAMG 63
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
630-822 1.19e-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: 84.25  E-value: 1.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRfpsQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFN-HPHILRLEGVVTKRKP--IMIVTEFME 706
Cdd:cd07831     7 IGEGTFSEVLKAQSR---KTGKYYAIKCMKKHFKSLEQVNNLREIQALRRLSpHPNILRLIEVLFDRKTgrLALVFELMD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 707 nGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNlCCKVSDFGLTRllddfdGTYETQ-- 784
Cdd:cd07831    84 -MNLYELIKGRKRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDD-ILKLADFGSCR------GIYSKPpy 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2038291632 785 GGKIPIRW-TAPEAI-AHRIFTTASDVWSFGIVMWEVLSF 822
Cdd:cd07831   156 TEYISTRWyRAPECLlTDGYYGPKMDIWAVGCVFFEILSL 195
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
630-861 1.26e-17

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: 83.54  E-value: 1.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVyrgALRFPSQDCKTVAIKTLKDTSPDGQWWNFL-REATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENG 708
Cdd:cd14075    10 LGSGNFSQV---KLGIHQLTKEKVAIKILDKTKLDQKTQRLLsREISSMEKLHHPNIIRLYEVVETLSKLHLVMEYASGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 AL------DAFLKEREDQLAPGQLVamllgiaSGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDfDGTYE 782
Cdd:cd14075    87 ELytkistEGKLSESEAKPLFAQIV-------SAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGFSTHAKR-GETLN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 783 TQGGKIPirWTAPEaiahrIFTTAS------DVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSIEEG-YRLPPPVdcPAPL 855
Cdd:cd14075   159 TFCGSPP--YAAPE-----LFKDEHyigiyvDIWALGVLLYFMVT-GVMPFRAETVAKLKKCILEGtYTIPSYV--SEPC 228

                  ....*.
gi 2038291632 856 YELMKN 861
Cdd:cd14075   229 QELIRG 234
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
629-887 1.37e-17

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: 84.47  E-value: 1.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRgalrfpSQDCKTVAIKTLKDTSPDGQWWNF----LREATIMGQFNHPHILRLEGVVTKRKPIM----- 699
Cdd:cd07864    14 IIGEGTYGQVYK------AKDKDTGELVALKKVRLDNEKEGFpitaIREIKILRQLNHRSVVNLKEIVTDKQDALdfkkd 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 700 -----IVTEFMENGaLDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLL 774
Cdd:cd07864    88 kgafyLVFEYMDHD-LMGLLESGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLADFGLARLY 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 775 DDFDGTYETQggKIPIRWTAPEA--IAHRIFTTASDVWSFGIVMWEVlsFGDKPYGEMNNQevMKSIEEGYRL---PPPV 849
Cdd:cd07864   167 NSEESRPYTN--KVITLWYRPPEllLGEERYGPAIDVWSCGCILGEL--FTKKPIFQANQE--LAQLELISRLcgsPCPA 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2038291632 850 DCP----APLYELMKNCWAYDRARRPHFLQLQAH----LEQLLT-DP 887
Cdd:cd07864   241 VWPdvikLPYFNTMKPKKQYRRRLREEFSFIPTPaldlLDHMLTlDP 287
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
628-879 1.38e-17

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: 83.76  E-value: 1.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 628 TVIGEGEFGEVyrgALRFPSQDCKTVAIKTL--KDTSPDGQWWNFLREATIMGQFNHPHILRL-EGVVTKRKPIMIVtef 704
Cdd:cd14164     6 TTIGEGSFSKV---KLATSQKYCCKVAIKIVdrRRASPDFVQKFLPRELSILRRVNHPNIVQMfECIEVANGRLYIV--- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 705 MENGALDAFLKEREDQLAPGQLV-AMLLGIASGMNYLSGHNYVHRDLAARNILVN-QNLCCKVSDFGLTRLLDDFDGTYE 782
Cdd:cd14164    80 MEAAATDLLQKIQEVHHIPKDLArDMFAQMVGAVNYLHDMNIVHRDLKCENILLSaDDRKIKIADFGFARFVEDYPELST 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 783 TQGGKIPirWTAPEAIAHRIFTTAS-DVWSFGIVMWeVLSFGDKPYGEmNNQEVMKSIEEGYRLPPPVDCPAPLYELMKN 861
Cdd:cd14164   160 TFCGSRA--YTPPEVILGTPYDPKKyDVWSLGVVLY-VMVTGTMPFDE-TNVRRLRLQQRGVLYPSGVALEEPCRALIRT 235
                         250
                  ....*....|....*...
gi 2038291632 862 CWAYDRARRPHFLQLQAH 879
Cdd:cd14164   236 LLQFNPSTRPSIQQVAGN 253
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
626-820 1.78e-17

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: 84.88  E-value: 1.78e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 626 VDTVIGEGEFGEVYRGalrFPSQDCKTVAIKTLKDTspdgqwwnF---------LREATIMGQFNHPHILRLEGVVTKRK 696
Cdd:cd07834     4 LLKPIGSGAYGVVCSA---YDKRTGRKVAIKKISNV--------FddlidakriLREIKILRHLKHENIIGLLDILRPPS 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 697 P-----IMIVTEFMENGaLDAFLKEREDqLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLT 771
Cdd:cd07834    73 PeefndVYIVTELMETD-LHKVIKSPQP-LTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFGLA 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2038291632 772 RLLD-DFDGTYETQGgkIPIRW-TAPEAI--AHRiFTTASDVWSFGIVMWEVL 820
Cdd:cd07834   151 RGVDpDEDKGFLTEY--VVTRWyRAPELLlsSKK-YTKAIDIWSVGCIFAELL 200
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
629-879 3.34e-17

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: 83.32  E-value: 3.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRFPSQdckTVAIK-TLKDTspdgqwwNFL-REATIMGQFNHPHILRLEG-----VVTKRKPIM-I 700
Cdd:cd14137    11 VIGSGSFGVVYQAKLLETGE---VVAIKkVLQDK-------RYKnRELQIMRRLKHPNIVKLKYffyssGEKKDEVYLnL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 701 VTEFM-ENgaLDAFLKEREDQlapGQLVAMLL------GIASGMNYLSGHNYVHRDLAARNILVNQNLC-CKVSDFGLTR 772
Cdd:cd14137    81 VMEYMpET--LYRVIRHYSKN---KQTIPIIYvklysyQLFRGLAYLHSLGICHRDIKPQNLLVDPETGvLKLCDFGSAK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 773 LLDDFDG--TYetqggkIPIR-WTAPEAIAH-RIFTTASDVWSFGIVMWEVLSfgDKPY--GEMNNQ---EVMK-----S 838
Cdd:cd14137   156 RLVPGEPnvSY------ICSRyYRAPELIFGaTDYTTAIDIWSAGCVLAELLL--GQPLfpGESSVDqlvEIIKvlgtpT 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 839 IEE---------GYRLP----------PPVDCPAPLYELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd14137   228 REQikamnpnytEFKFPqikphpwekvFPKRTPPDAIDLLSKILVYNPSKRLTALEALAH 287
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
626-879 4.74e-17

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: 81.97  E-value: 4.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 626 VDTVIGEGEFGEVYRGALRfpsQDCKTVAIKTLKDTSPDGQWW-NFLREATIMGQFN-HPHILRLEGVVTKRKPIMIVTE 703
Cdd:cd14050     5 ILSKLGEGSFGEVFKVRSR---EDGKLYAVKRSRSRFRGEKDRkRKLEEVERHEKLGeHPNCVRFIKAWEEKGILYIQTE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 704 fMENGALDAFLkEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYET 783
Cdd:cd14050    82 -LCDTSLQQYC-EETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLVVELDKEDIHDAQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 784 QGGKipiRWTAPEAIaHRIFTTASDVWSFGIVMWEVLSFGDKP-YGEMNNQevmksIEEGYrLPPPV--DCPAPLYELMK 860
Cdd:cd14050   160 EGDP---RYMAPELL-QGSFTKAADIFSLGITILELACNLELPsGGDGWHQ-----LRQGY-LPEEFtaGLSPELRSIIK 229
                         250
                  ....*....|....*....
gi 2038291632 861 NCWAYDRARRPHFLQLQAH 879
Cdd:cd14050   230 LMMDPDPERRPTAEDLLAL 248
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
630-820 5.18e-17

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: 82.76  E-value: 5.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRfpsQDCKTVAIKTLK-DTSPDGQWWNFLREATIMGQFN-HPHILRLEGVVTKRKPIMIVTEFMEN 707
Cdd:cd07832     8 IGEGAHGIVFKAKDR---ETGETVALKKVAlRKLEGGIPNQALREIKALQACQgHPYVVKLRDVFPHGTGFVLVFEYMLS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GaLDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLL-DDFDGTYETQgg 786
Cdd:cd07832    85 S-LSEVLRDEERPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLARLFsEEDPRLYSHQ-- 161
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2038291632 787 kIPIRW-TAPEAI-AHRIFTTASDVWSFGIVMWEVL 820
Cdd:cd07832   162 -VATRWyRAPELLyGSRKYDEGVDLWAVGCIFAELL 196
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
672-879 6.83e-17

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: 81.60  E-value: 6.83e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 672 REATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGALDAFLKEREDQLAPgQLVAMLLGIASGMNYLSGHNYVHRDLA 751
Cdd:cd14188    50 KEIELHRILHHKHVVQFYHYFEDKENIYILLEYCSRRSMAHILKARKVLTEP-EVRYYLRQIVSGLKYLHEQEILHRDLK 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 752 ARNILVNQNLCCKVSDFGLTRLLDDFDGTYETQGGKiPiRWTAPEAIAHRIFTTASDVWSFGIVMWEVLsFGDKPYGEMN 831
Cdd:cd14188   129 LGNFFINENMELKVGDFGLAARLEPLEHRRRTICGT-P-NYLSPEVLNKQGHGCESDIWALGCVMYTML-LGRPPFETTN 205
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2038291632 832 NQEVMKSIEEG-YRLPPPVDCPAPlyELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd14188   206 LKETYRCIREArYSLPSSLLAPAK--HLIASMLSKNPEDRPSLDEIIRH 252
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
606-841 6.84e-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: 82.78  E-value: 6.84e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 606 EDPAQGALDFAQelDPTWLIVDT-VIGEGEFGEVYRGAlrfPSQDCKTVAIKTL----KDTSPdgQWWNFLREATIMGQF 680
Cdd:cd06633     6 KDPEIADLFYKD--DPEEIFVDLhEIGHGSFGAVYFAT---NSHTNEVVAIKKMsysgKQTNE--KWQDIIKEVKFLQQL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 681 NHPHILRLEGVVTKRKPIMIVTEFMENGALDaFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQN 760
Cdd:cd06633    79 KHPNTIEYKGCYLKDHTAWLVMEYCLGSASD-LLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 761 LCCKVSDFGLTRLL---DDFDGTyetqggkiPIrWTAPE---AIAHRIFTTASDVWSFGIVMWEvLSFGDKPYGEMNNQE 834
Cdd:cd06633   158 GQVKLADFGSASIAspaNSFVGT--------PY-WMAPEvilAMDEGQYDGKVDIWSLGITCIE-LAERKPPLFNMNAMS 227

                  ....*..
gi 2038291632 835 VMKSIEE 841
Cdd:cd06633   228 ALYHIAQ 234
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
629-871 7.47e-17

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: 81.33  E-value: 7.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYrgaLRFPSQDCKTVAIKTLK-DTSPDGQWWNFLREATIMGQFNHPHILRL-EGVVTKRKPIMIVTEFME 706
Cdd:cd08223     7 VIGKGSYGEVW---LVRHKRDRKQYVIKKLNlKNASKRERKAAEQEAKLLSKLKHPNIVSYkESFEGEDGFLYIVMGFCE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 707 NGALDAFLKEREDQLAP-GQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYETQG 785
Cdd:cd08223    84 GGDLYTRLKEQKGVLLEeRQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARVLESSSDMATTLI 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 786 GKiPIrWTAPEAIAHRIFTTASDVWSFGIVMWEVLS----FGDKpygEMNNqeVMKSIEEGyRLPP-PVDCPAPLYELMK 860
Cdd:cd08223   164 GT-PY-YMSPELFSNKPYNHKSDVWALGCCVYEMATlkhaFNAK---DMNS--LVYKILEG-KLPPmPKQYSPELGELIK 235
                         250
                  ....*....|.
gi 2038291632 861 NCWAYDRARRP 871
Cdd:cd08223   236 AMLHQDPEKRP 246
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
630-818 8.05e-17

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: 81.95  E-value: 8.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFPSQdckTVAIKTLK-DTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFmeng 708
Cdd:cd07835     7 IGEGTYGVVYKARDKLTGE---IVALKKIRlETEDEGVPSTAIREISLLKELNHPNIVRLLDVVHSENKLYLVFEF---- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 aLDAFLKEREDQLAPGQLVAMLLG-----IASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDdfdgtyet 783
Cdd:cd07835    80 -LDLDLKKYMDSSPLTGLDPPLIKsylyqLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLARAFG-------- 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2038291632 784 qggkIPIR---------W-TAPEA-IAHRIFTTASDVWSFGIVMWE 818
Cdd:cd07835   151 ----VPVRtythevvtlWyRAPEIlLGSKHYSTPVDIWSVGCIFAE 192
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
629-890 9.46e-17

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A splice variant of TLK1, called TLK1B, is expressed in the presence of double strand breaks (DSBs). It lacks the N-terminal part of TLK1, but is expected to phosphorylate the same substrates. TLK1/1B interacts with Rad9, which is critical in DNA damage-activated checkpoint response, and plays a role in the repair of linearized DNA with incompatible ends. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. The TLK1 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: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 82.03  E-value: 9.46e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRgALRFPSQDCKTVAIKTLKDTSPDGQWWNF----LREATIMGQFNHPHILRLEGVVT-KRKPIMIVTE 703
Cdd:cd14040    13 LLGRGGFSEVYK-AFDLYEQRYAAVKIHQLNKSWRDEKKENYhkhaCREYRIHKELDHPRIVKLYDYFSlDTDTFCTVLE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 704 FMENGALDAFLKEREdQLAPGQLVAMLLGIASGMNYLSGHN--YVHRDLAARNILVNQNLCC---KVSDFGLTRLLDD-- 776
Cdd:cd14040    92 YCEGNDLDFYLKQHK-LMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACgeiKITDFGLSKIMDDds 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 777 --FDGTYETQGGKIPIRWTAPEAIA----HRIFTTASDVWSFGIVMWEVLsFGDKPYGEMNNQE-------VMKSIEEGY 843
Cdd:cd14040   171 ygVDGMDLTSQGAGTYWYLPPECFVvgkePPKISNKVDVWSVGVIFFQCL-YGRKPFGHNQSQQdilqentILKATEVQF 249
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2038291632 844 RLPPPVDCPAPLYelMKNCWAYDRARRphflqlqAHLEQLLTDPHSL 890
Cdd:cd14040   250 PVKPVVSNEAKAF--IRRCLAYRKEDR-------FDVHQLASDPYLL 287
SAM_EPH-A5 cd09546
SAM domain of EPH-A5 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
915-975 9.62e-17

SAM domain of EPH-A5 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A5 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A5 receptors and appears to mediate cell-cell initiated signal transduction. Eph-A5 gene is almost exclusively expressed in the nervous system. Murine EPH-A5 receptors participate in axon guidance during embryogenesis and play a role in the adult synaptic plasticity, particularly in neuron-target interactions in multiple neural circuits. Additionally EPH-A5 receptors and its ligand ephrin A5 regulate dopaminergic axon outgrowth and influence the formation of the midbrain dopaminergic pathways. EphA5 gene expression was found decreased in a few different breast cancer cell lines, thus it might be a potential molecular marker for breast cancer carcinogenesis and progression.


Pssm-ID: 188945  Cd Length: 66  Bit Score: 75.35  E-value: 9.62e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2038291632 915 YRSVSEWLESIRMKRYILHFRSAGLDTMECVLELTAEDLTQMGITLPGHQKRILCSIQGFK 975
Cdd:cd09546     3 YRSVGEWLEAIKMGRYTEIFMENGYSSMDAVAQVTLEDLRRLGVTLVGHQKKIMNSIQEMR 63
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
620-879 1.08e-16

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: 81.60  E-value: 1.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 620 DP--TWLIVDTvIGEGEFGEVYRgalRFPSQDCKTVAIKTLK-----DTSPDGQWwNFLREATimgqfNHPHILRLEGVV 692
Cdd:cd06638    15 DPsdTWEIIET-IGKGTYGKVFK---VLNKKNGSKAAVKILDpihdiDEEIEAEY-NILKALS-----DHPNVVKFYGMY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 693 TKRK-----PIMIVTEFMENGAL----DAFLKEREDQLAPgqLVAMLLGIA-SGMNYLSGHNYVHRDLAARNILVNQNLC 762
Cdd:cd06638    85 YKKDvkngdQLWLVLELCNGGSVtdlvKGFLKRGERMEEP--IIAYILHEAlMGLQHLHVNKTIHRDVKGNNILLTTEGG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 763 CKVSDFGLTRLLDDFDGTYETQGGKiPIrWTAPEAIA-----HRIFTTASDVWSFGIVMWEvLSFGDKPYGEMNNqevMK 837
Cdd:cd06638   163 VKLVDFGVSAQLTSTRLRRNTSVGT-PF-WMAPEVIAceqqlDSTYDARCDVWSLGITAIE-LGDGDPPLADLHP---MR 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2038291632 838 SIEEGYRLPPPVDCPAPLY-----ELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd06638   237 ALFKIPRNPPPTLHQPELWsnefnDFIRKCLTKDYEKRPTVSDLLQH 283
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
620-879 1.10e-16

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: 81.58  E-value: 1.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 620 DP--TWLIVDTvIGEGEFGEVYRGALRfpsQDCKTVAIKTLKDTSPDGQW----WNFLREATimgqfNHPHILRLEGVVT 693
Cdd:cd06639    19 DPsdTWDIIET-IGKGTYGKVYKVTNK---KDGSLAAVKILDPISDVDEEieaeYNILRSLP-----NHPNVVKFYGMFY 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 694 KRK-----PIMIVTEFMENGALDAFLK---EREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKV 765
Cdd:cd06639    90 KADqyvggQLWLVLELCNGGSVTELVKgllKCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKL 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 766 SDFGLTRLLDDFDGTYETQGGKiPIrWTAPEAIA-----HRIFTTASDVWSFGIVMWEvLSFGDKPYGEMNNQEVMKSIE 840
Cdd:cd06639   170 VDFGVSAQLTSARLRRNTSVGT-PF-WMAPEVIAceqqyDYSYDARCDVWSLGITAIE-LADGDPPLFDMHPVKALFKIP 246
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2038291632 841 egyRLPPPVD------CPApLYELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd06639   247 ---RNPPPTLlnpekwCRG-FSHFISQCLIKDFEKRPSVTHLLEH 287
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
630-821 1.26e-16

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: 81.31  E-value: 1.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFPSQdckTVAIKTLKDTSPD-GQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFmeng 708
Cdd:cd07861     8 IGEGTYGVVYKGRNKKTGQ---IVAMKKIRLESEEeGVPSTAIREISLLKELQHPNIVCLEDVLMQENRLYLVFEF---- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 aLDAFLKEREDQLAPGQ-LVAMLLG-----IASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDdfdgtye 782
Cdd:cd07861    81 -LSMDLKKYLDSLPKGKyMDAELVKsylyqILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLARAFG------- 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2038291632 783 tqggkIPIR----------WTAPEAI--AHRiFTTASDVWSFGIVMWEVLS 821
Cdd:cd07861   153 -----IPVRvythevvtlwYRAPEVLlgSPR-YSTPVDIWSIGTIFAEMAT 197
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
629-853 1.54e-16

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: 80.36  E-value: 1.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGAlrfPSQDCKTVAIKTLKDT--SPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFME 706
Cdd:cd14189     8 LLGKGGFARCYEMT---DLATNKTYAVKVIPHSrvAKPHQREKIVNEIELHRDLHHKHVVKFSHHFEDAENIYIFLELCS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 707 NGALDAFLKEREDQLAPgQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYETQGG 786
Cdd:cd14189    85 RKSLAHIWKARHTLLEP-EVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAARLEPPEQRKKTICG 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038291632 787 KiPiRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSIEE-GYRLPPPVDCPA 853
Cdd:cd14189   164 T-P-NYLAPEVLLRQGHGPESDVWSLGCVMYTLLC-GNPPFETLDLKETYRCIKQvKYTLPASLSLPA 228
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
630-819 1.54e-16

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: 81.33  E-value: 1.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALrfpsQDcKTVAIKTLkdTSPDGQWWnfLREA----TIMgqFNHPHILRLEGV-VTKRKP---IMIV 701
Cdd:cd14142    13 IGKGRYGEVWRGQW----QG-ESVAVKIF--SSRDEKSW--FRETeiynTVL--LRHENILGFIASdMTSRNSctqLWLI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 702 TEFMENGALDAFLKEREdqLAPGQLVAMLLGIASGMNYLSGHNY--------VHRDLAARNILVNQNLCCKVSDFGL--- 770
Cdd:cd14142    82 THYHENGSLYDYLQRTT--LDHQEMLRLALSAASGLVHLHTEIFgtqgkpaiAHRDLKSKNILVKSNGQCCIADLGLavt 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2038291632 771 -TRLLDDFD-GTYETQGGKipiRWTAPEAIAHRIFTTA------SDVWSFGIVMWEV 819
Cdd:cd14142   160 hSQETNQLDvGNNPRVGTK---RYMAPEVLDETINTDCfesykrVDIYAFGLVLWEV 213
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
629-839 1.55e-16

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: 80.98  E-value: 1.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGaLRFPSQdcKTVAIKTLKDTSPDGQWWNFLREATIMGQFNH---PHILRLEGVVTKRKPIMIVTEFM 705
Cdd:cd06917     8 LVGRGSYGAVYRG-YHVKTG--RVVALKVLNLDTDDDDVSDIQKEVALLSQLKLgqpKNIIKYYGSYLKGPSLWIIMDYC 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 706 ENGALDAFLKeredqlaPGQLVAMLLGIAS-----GMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGT 780
Cdd:cd06917    85 EGGSIRTLMR-------AGPIAERYIAVIMrevlvALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASLNQNSSK 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 781 YETQGGKiPIrWTAPEAIAH-RIFTTASDVWSFGIVMWEvLSFGDKPYGEmnnQEVMKSI 839
Cdd:cd06917   158 RSTFVGT-PY-WMAPEVITEgKYYDTKADIWSLGITTYE-MATGNPPYSD---VDALRAV 211
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
629-820 1.65e-16

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: 80.80  E-value: 1.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRFpsqDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENG 708
Cdd:cd13996    13 LLGSGGFGSVYKVRNKV---DGVTYAIKKIRLTEKSSASEKVLREVKALAKLNHPNIVRYYTAWVEEPPLYIQMELCEGG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 ALDAFLKEREDQLAPGQLVA--MLLGIASGMNYLSGHNYVHRDLAARNILVNQN-LCCKVSDFGLTRLLDDF-------- 777
Cdd:cd13996    90 TLRDWIDRRNSSSKNDRKLAleLFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDdLQVKIGDFGLATSIGNQkrelnnln 169
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2038291632 778 ------DGTYETQGGKipIRWTAPEAIAHRIFTTASDVWSFGIVMWEVL 820
Cdd:cd13996   170 nnnngnTSNNSVGIGT--PLYASPEQLDGENYNEKADIYSLGIILFEML 216
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
630-883 1.76e-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: 80.98  E-value: 1.76e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRfpsqdCKTVAIKTLKdTSPDGQWwnfLREATIMGQ--FNHPHIL-------RLEGVVTKrkpIMI 700
Cdd:cd14144     3 VGKGRYGEVWKGKWR-----GEKVAVKIFF-TTEEASW---FRETEIYQTvlMRHENILgfiaadiKGTGSWTQ---LYL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 701 VTEFMENGALDAFLkeREDQLAPGQLVAMLLGIASGMNYLSGHNY--------VHRDLAARNILVNQNLCCKVSDFGLT- 771
Cdd:cd14144    71 ITDYHENGSLYDFL--RGNTLDTQSMLKLAYSAACGLAHLHTEIFgtqgkpaiAHRDIKSKNILVKKNGTCCIADLGLAv 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 772 RLLDDFDGTYETQGGKIPI-RWTAPEAIAHRI-------FTTAsDVWSFGIVMWEV----LSFG-----DKPYGEM---- 830
Cdd:cd14144   149 KFISETNEVDLPPNTRVGTkRYMAPEVLDESLnrnhfdaYKMA-DMYSFGLVLWEIarrcISGGiveeyQLPYYDAvpsd 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 831 NNQEVMKSIEEGYRLPPPV-------DCPAPLYELMKNCWAYDRARRPHFLQLQAHLEQL 883
Cdd:cd14144   228 PSYEDMRRVVCVERRRPSIpnrwssdEVLRTMSKLMSECWAHNPAARLTALRVKKTLGKL 287
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
630-831 2.12e-16

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: 80.19  E-value: 2.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYrgaLRFPSQDCKTVAIKTLKDTSPDGQ--WWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMEN 707
Cdd:cd06607     9 IGHGSFGAVY---YARNKRTSEVVAIKKMSYSGKQSTekWQDIIKEVKFLRQLRHPNTIEYKGCYLREHTAWLVMEYCLG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GALDAF--LKE--REDQLApgqlvAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLD---DFDGT 780
Cdd:cd06607    86 SASDIVevHKKplQEVEIA-----AICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFGSASLVCpanSFVGT 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2038291632 781 yetqggkiPIrWTAPE---AIAHRIFTTASDVWSFGIVMWEvLSFGDKPYGEMN 831
Cdd:cd06607   161 --------PY-WMAPEvilAMDEGQYDGKVDVWSLGITCIE-LAERKPPLFNMN 204
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
630-842 2.13e-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: 79.96  E-value: 2.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRgalrfpsqdC------KTVAIKTLKDTSPDgQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTE 703
Cdd:cd14103     1 LGRGKFGTVYR---------CvekatgKELAAKFIKCRKAK-DREDVRNEIEIMNQLRHPRLLQLYDAFETPREMVLVME 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 704 FMENGAL-------DAFLKEREdqlapgqlVAMLL-GIASGMNYLSGHNYVHRDLAARNIL-VNQN-LCCKVSDFGLTRL 773
Cdd:cd14103    71 YVAGGELfervvddDFELTERD--------CILFMrQICEGVQYMHKQGILHLDLKPENILcVSRTgNQIKIIDFGLARK 142
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2038291632 774 LDDFD------GTYEtqggkipirWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPY-GEmNNQEVMKSIEEG 842
Cdd:cd14103   143 YDPDKklkvlfGTPE---------FVAPEVVNYEPISYATDMWSVGVICYVLLS-GLSPFmGD-NDAETLANVTRA 207
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
673-879 2.40e-16

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: 80.18  E-value: 2.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 673 EATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGAL-DAFLKER--EDQLApgqlvAMLLGIASGMNYLSGHNYVHRD 749
Cdd:cd06648    54 EVVIMRDYQHPNIVEMYSSYLVGDELWVVMEFLEGGALtDIVTHTRmnEEQIA-----TVCRAVLKALSFLHSQGVIHRD 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 750 LAARNILVNQNLCCKVSDFGLTRLLDDfdgtyetqggKIPIR--------WTAPEAIAHRIFTTASDVWSFGIVMWEVLS 821
Cdd:cd06648   129 IKSDSILLTSDGRVKLSDFGFCAQVSK----------EVPRRkslvgtpyWMAPEVISRLPYGTEVDIWSLGIMVIEMVD 198
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2038291632 822 fGDKPYGEMNNQEVMKSIEEgyRLPP----PVDCPAPLYELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd06648   199 -GEPPYFNEPPLQAMKRIRD--NEPPklknLHKVSPRLRSFLDRMLVRDPAQRATAAELLNH 257
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
618-821 2.61e-16

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: 81.20  E-value: 2.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 618 ELDPTWLIVDtVIGEGEFGEVYrGALRFPSQDckTVAIKTLkdtSPdgqwwnF---------LREATIMGQFNHPHILRL 688
Cdd:cd07849     2 DVGPRYQNLS-YIGEGAYGMVC-SAVHKPTGQ--KVAIKKI---SP------FehqtyclrtLREIKILLRFKHENIIGI 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 689 EGVVTKR-----KPIMIVTEFMENgalDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCC 763
Cdd:cd07849    69 LDIQRPPtfesfKDVYIVQELMET---DLYKLIKTQHLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDL 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 764 KVSDFGLTRLLDDFDGTYETQGGKIPIRW-TAPE-AIAHRIFTTASDVWSFGIVMWEVLS 821
Cdd:cd07849   146 KICDFGLARIADPEHDHTGFLTEYVATRWyRAPEiMLNSKGYTKAIDIWSVGCILAEMLS 205
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
630-814 3.02e-16

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: 79.66  E-value: 3.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRgALRFPSQDckTVAIKTLKdTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGA 709
Cdd:cd06613     8 IGSGTYGDVYK-ARNIATGE--LAAVKVIK-LEPGDDFEIIQQEISMLKECRHPNIVAYFGSYLRRDKLWIVMEYCGGGS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 710 LDAFLKE----REDQLAPGQLVAMLlgiasGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDD-------FD 778
Cdd:cd06613    84 LQDIYQVtgplSELQIAYVCRETLK-----GLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSAQLTAtiakrksFI 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2038291632 779 GT-YetqggkipirWTAPEAIAHR---IFTTASDVWSFGI 814
Cdd:cd06613   159 GTpY----------WMAPEVAAVErkgGYDGKCDIWALGI 188
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
700-876 3.23e-16

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: 79.76  E-value: 3.23e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 700 IVTEFMENGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLlddfdg 779
Cdd:cd14043    73 IVSEHCSRGSLEDLLRNDDMKLDWMFKSSLLLDLIKGMRYLHHRGIVHGRLKSRNCVVDGRFVLKITDYGYNEI------ 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 780 tYETQGGKIPIR------WTAPE-----AIAHRIfTTASDVWSFGIVMWEVLSFGdKPYG--EMNNQEVMKSIeegyRLP 846
Cdd:cd14043   147 -LEAQNLPLPEPapeellWTAPEllrdpRLERRG-TFPGDVFSFAIIMQEVIVRG-APYCmlGLSPEEIIEKV----RSP 219
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2038291632 847 PPVDCP------APL--YELMKNCWAYDRARRPHFLQL 876
Cdd:cd14043   220 PPLCRPsvsmdqAPLecIQLMKQCWSEAPERRPTFDQI 257
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
672-839 3.26e-16

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: 80.06  E-value: 3.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 672 REATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGALDAFLKEREdQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLA 751
Cdd:cd14194    57 REVSILKEIQHPNVITLHEVYENKTDVILILELVAGGELFDFLAEKE-SLTEEEATEFLKQILNGVYYLHSLQIAHFDLK 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 752 ARNI-LVNQNLC---CKVSDFGLTRLLD---DFDGTYETQggkipiRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGD 824
Cdd:cd14194   136 PENImLLDRNVPkprIKIIDFGLAHKIDfgnEFKNIFGTP------EFVAPEIVNYEPLGLEADMWSIGVITYILLS-GA 208
                         170
                  ....*....|....*
gi 2038291632 825 KPYGEMNNQEVMKSI 839
Cdd:cd14194   209 SPFLGDTKQETLANV 223
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
629-846 3.47e-16

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: 79.62  E-value: 3.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRFPSQDCktvAIKTLKDTS-PDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMEN 707
Cdd:cd08225     7 KIGEGSFGKIYLAKAKSDSEHC---VIKEIDLTKmPVKEKEASKKEVILLAKMKHPNIVTFFASFQENGRLFIVMEYCDG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GAL-DAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQN-LCCKVSDFGLTRLLDDFDGTYETQG 785
Cdd:cd08225    84 GDLmKRINRQRGVLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNgMVAKLGDFGIARQLNDSMELAYTCV 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2038291632 786 GKiPIrWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFgDKPYGEMNNQEVMKSIEEGYRLP 846
Cdd:cd08225   164 GT-PY-YLSPEICQNRPYNNKTDIWSLGCVLYELCTL-KHPFEGNNLHQLVLKICQGYFAP 221
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
630-879 4.44e-16

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: 79.10  E-value: 4.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYrgALRFPSQDcKTVAIKTLKDTS--PDGQWWNFLREATIMGQFNHPHILRLEGVV-TKRKPIMiVTEFME 706
Cdd:cd05123     1 LGKGSFGKVL--LVRKKDTG-KLYAMKVLRKKEiiKRKEVEHTLNERNILERVNHPFIVKLHYAFqTEEKLYL-VLDYVP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 707 NGALDAFLKER----EDqlapgqlVAMLLG--IASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFD-- 778
Cdd:cd05123    77 GGELFSHLSKEgrfpEE-------RARFYAaeIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELSSDGdr 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 779 -----GTYEtqggkipirWTAPEAIAHRIFTTASDVWSFGIVMWEVLsFGDKPYGEMNNQEVMKSIEEG-YRLPPPVDCP 852
Cdd:cd05123   150 tytfcGTPE---------YLAPEVLLGKGYGKAVDWWSLGVLLYEML-TGKPPFYAENRKEIYEKILKSpLKFPEYVSPE 219
                         250       260       270
                  ....*....|....*....|....*....|
gi 2038291632 853 AplYELMKNCWAYDRARRPHFL---QLQAH 879
Cdd:cd05123   220 A--KSLISGLLQKDPTKRLGSGgaeEIKAH 247
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
600-879 4.49e-16

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: 79.67  E-value: 4.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 600 VDLQAYEDPAqGALDFAQeldptwlivdtVIGEGEFGEVYRGalrfpsQDCKT---VAIKTLKDTSPDGQwwNFLREATI 676
Cdd:cd06636     6 IDLSALRDPA-GIFELVE-----------VVGNGTYGQVYKG------RHVKTgqlAAIKVMDVTEDEEE--EIKLEINM 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 677 MGQFNH-PHILRLEGVVTKRKP------IMIVTEFMENGALDAFLKEREDQLAPGQLVAMLL-GIASGMNYLSGHNYVHR 748
Cdd:cd06636    66 LKKYSHhRNIATYYGAFIKKSPpghddqLWLVMEFCGAGSVTDLVKNTKGNALKEDWIAYICrEILRGLAHLHAHKVIHR 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 749 DLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYETQGGKiPIrWTAPEAIA-----HRIFTTASDVWSFGIVMWEvLSFG 823
Cdd:cd06636   146 DIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRRNTFIGT-PY-WMAPEVIAcdenpDATYDYRSDIWSLGITAIE-MAEG 222
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 824 DKPYGEMNNQEVMKSIEegyRLPPP----VDCPAPLYELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd06636   223 APPLCDMHPMRALFLIP---RNPPPklksKKWSKKFIDFIEGCLVKNYLSRPSTEQLLKH 279
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
629-827 4.68e-16

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: 79.54  E-value: 4.68e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRgALRFPSQdcKTVAIKTLK-DTSPDGQWwNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMEN 707
Cdd:cd06619     8 ILGHGNGGTVYK-AYHLLTR--RILAVKVIPlDITVELQK-QIMSELEILYKCDSPYIIGFYGAFFVENRISICTEFMDG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GALDAFLKEREDQLApgqlvAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGL-TRLLDDFDGTYETQGG 786
Cdd:cd06619    84 GSLDVYRKIPEHVLG-----RIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVsTQLVNSIAKTYVGTNA 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2038291632 787 kipirWTAPEAIAHRIFTTASDVWSFGIVMWEvLSFGDKPY 827
Cdd:cd06619   159 -----YMAPERISGEQYGIHSDVWSLGISFME-LALGRFPY 193
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
626-871 4.75e-16

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: 79.24  E-value: 4.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 626 VDTVIGEGEFGEVYRGALRfpsQDCKTVAIKTLK--DTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTE 703
Cdd:cd08224     4 IEKKIGKGQFSVVYRARCL---LDGRLVALKKVQifEMMDAKARQDCLKEIDLLQQLNHPNIIKYLASFIENNELNIVLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 704 FMENGALDAFLKEREDQLAP---GQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDdfDGT 780
Cdd:cd08224    81 LADAGDLSRLIKHFKKQKRLipeRTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGLGRFFS--SKT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 781 YETQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGE-MNNQEVMKSIEEGYRLPPPVDC-PAPLYEL 858
Cdd:cd08224   159 TAAHSLVGTPYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFYGEkMNLYSLCKKIEKCEYPPLPADLySQELRDL 238
                         250
                  ....*....|...
gi 2038291632 859 MKNCWAYDRARRP 871
Cdd:cd08224   239 VAACIQPDPEKRP 251
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
917-975 5.26e-16

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 73.07  E-value: 5.26e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2038291632 917 SVSEWLESIRMKRYILHFRSAGLDTMECVLELTAEDLTQMGITLPGHQKRILCSIQGFK 975
Cdd:pfam07647   8 SVADWLRSIGLEQYTDNFRDQGITGAELLLRLTLEDLKRLGITSVGHRRKILKKIQELK 66
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
625-850 5.96e-16

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: 79.06  E-value: 5.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 625 IVDTViGEGEFGEVYRGALRfpsQDCKTVAIK-------TLKDTSPDGqwwnFLREATIMGQFNHPHILRLEGVVTKRKP 697
Cdd:cd14098     4 IIDRL-GSGTFAEVKKAVEV---ETGKMRAIKqivkrkvAGNDKNLQL----FQREINILKSLEHPGIVRLIDWYEDDQH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 698 IMIVTEFMENGALDAFLKER----EDQLAPgqlvaMLLGIASGMNYLSGHNYVHRDLAARNILVNQN--LCCKVSDFGLT 771
Cdd:cd14098    76 IYLVMEYVEGGDLMDFIMAWgaipEQHARE-----LTKQILEAMAYTHSMGITHRDLKPENILITQDdpVIVKISDFGLA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 772 R------LLDDFDGTyetqggkipIRWTAPEAIAHR------IFTTASDVWSFGIVMWeVLSFGDKPYGEMNNQEVMKSI 839
Cdd:cd14098   151 KvihtgtFLVTFCGT---------MAYLAPEILMSKeqnlqgGYSNLVDMWSVGCLVY-VMLTGALPFDGSSQLPVEKRI 220
                         250
                  ....*....|..
gi 2038291632 840 EEG-YRLPPPVD 850
Cdd:cd14098   221 RKGrYTQPPLVD 232
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
630-879 6.98e-16

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: 79.12  E-value: 6.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRgALRFPSQdcKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGA 709
Cdd:cd06622     9 LGKGNYGSVYK-VLHRPTG--VTMAMKEIRLELDESKFNQIIMELDILHKAVSPYIVDFYGAFFIEGAVYMCMEYMDAGS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 710 LDAFLKE--REDQLAPGQLVAMLLGIASGMNYL-SGHNYVHRDLAARNILVNQNLCCKVSDFGLTrllddfdGTYETQGG 786
Cdd:cd06622    86 LDKLYAGgvATEGIPEDVLRRITYAVVKGLKFLkEEHNIIHRDVKPTNVLVNGNGQVKLCDFGVS-------GNLVASLA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 787 KIPI---RWTAPEAI------AHRIFTTASDVWSFGIVMWEvLSFGDKPYGEMNNQEV---MKSIEEGY--RLPPPVDCP 852
Cdd:cd06622   159 KTNIgcqSYMAPERIksggpnQNPTYTVQSDVWSLGLSILE-MALGRYPYPPETYANIfaqLSAIVDGDppTLPSGYSDD 237
                         250       260
                  ....*....|....*....|....*..
gi 2038291632 853 AplYELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd06622   238 A--QDFVAKCLNKIPNRRPTYAQLLEH 262
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
626-871 7.18e-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: 79.30  E-value: 7.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 626 VDTVIGEGEFGEVYRGALRFpsqDCKTVAIKTLK--DTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTE 703
Cdd:cd08229    28 IEKKIGRGQFSEVYRATCLL---DGVPVALKKVQifDLMDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVLE 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 704 FMENGALDAFLK--EREDQLAPGQLV-AMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGT 780
Cdd:cd08229   105 LADAGDLSRMIKhfKKQKRLIPEKTVwKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKTTA 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 781 YETQGGKiPIrWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGE-MNNQEVMKSIEEGYRLPPPVD-CPAPLYEL 858
Cdd:cd08229   185 AHSLVGT-PY-YMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDkMNLYSLCKKIEQCDYPPLPSDhYSEELRQL 262
                         250
                  ....*....|...
gi 2038291632 859 MKNCWAYDRARRP 871
Cdd:cd08229   263 VNMCINPDPEKRP 275
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
606-841 7.42e-16

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: 79.71  E-value: 7.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 606 EDPAQGALDFAQelDPTWLIVD-TVIGEGEFGEVYRgalrfpSQDCKTVAIKTLKDTSPDGQ-----WWNFLREATIMGQ 679
Cdd:cd06635    10 KDPDIAELFFKE--DPEKLFSDlREIGHGSFGAVYF------ARDVRTSEVVAIKKMSYSGKqsnekWQDIIKEVKFLQR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 680 FNHPHILRLEGVVTKRKPIMIVTEFMENGALDaFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQ 759
Cdd:cd06635    82 IKHPNSIEYKGCYLREHTAWLVMEYCLGSASD-LLEVHKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 760 NLCCKVSDFGLTRLL---DDFDGTyetqggkiPIrWTAPE---AIAHRIFTTASDVWSFGIVMWEvLSFGDKPYGEMNNQ 833
Cdd:cd06635   161 PGQVKLADFGSASIAspaNSFVGT--------PY-WMAPEvilAMDEGQYDGKVDVWSLGITCIE-LAERKPPLFNMNAM 230

                  ....*...
gi 2038291632 834 EVMKSIEE 841
Cdd:cd06635   231 SALYHIAQ 238
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
629-893 8.52e-16

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; 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 TLK2 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: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 79.33  E-value: 8.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRgALRFPSQDCKTVAIKTLKDTSPDGQWWNF----LREATIMGQFNHPHILRLEGVVT-KRKPIMIVTE 703
Cdd:cd14041    13 LLGRGGFSEVYK-AFDLTEQRYVAVKIHQLNKNWRDEKKENYhkhaCREYRIHKELDHPRIVKLYDYFSlDTDSFCTVLE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 704 FMENGALDAFLKEREdQLAPGQLVAMLLGIASGMNYLSGHN--YVHRDLAARNILVNQNLCC---KVSDFGLTRLLDD-- 776
Cdd:cd14041    92 YCEGNDLDFYLKQHK-LMSEKEARSIIMQIVNALKYLNEIKppIIHYDLKPGNILLVNGTACgeiKITDFGLSKIMDDds 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 777 ---FDGTYETQGGKIPIRWTAPEAIA----HRIFTTASDVWSFGIVMWEVLsFGDKPYGEMNNQE-------VMKSIEeg 842
Cdd:cd14041   171 ynsVDGMELTSQGAGTYWYLPPECFVvgkePPKISNKVDVWSVGVIFYQCL-YGRKPFGHNQSQQdilqentILKATE-- 247
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2038291632 843 YRLPPPVDCPAPLYELMKNCWAYDRARRphflqlqAHLEQLLTDPHSLRTI 893
Cdd:cd14041   248 VQFPPKPVVTPEAKAFIRRCLAYRKEDR-------IDVQQLACDPYLLPHI 291
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
630-827 1.07e-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: 78.85  E-value: 1.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVyrgaLRFPSQDC-KTVAIKTLK-DTSPD--GQWwnfLREATIMGQFNHPHILR-------LEGVVTKRKPI 698
Cdd:cd14038     2 LGTGGFGNV----LRWINQETgEQVAIKQCRqELSPKnrERW---CLEIQIMKRLNHPNVVAardvpegLQKLAPNDLPL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 699 MIVtEFMENGALDAFLKERED--QLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVN---QNLCCKVSDFGLTRL 773
Cdd:cd14038    75 LAM-EYCQGGDLRKYLNQFENccGLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQqgeQRLIHKIIDLGYAKE 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 774 LD------DFDGTyetqggkipIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPY 827
Cdd:cd14038   154 LDqgslctSFVGT---------LQYLAPELLEQQKYTVTVDYWSFGTLAFECIT-GFRPF 203
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
630-879 1.20e-15

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: 78.56  E-value: 1.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRgALRFPSQdcKTVAIKTLKDTSPDGQWWNFLREA-TIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENg 708
Cdd:cd06616    14 IGRGAFGTVNK-MLHKPSG--TIMAVKRIRSTVDEKEQKRLLMDLdVVMRSSDCPYIVKFYGALFREGDCWICMELMDI- 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 ALDAFLK---EREDQLAPGQLVAML-LGIASGMNYL-SGHNYVHRDLAARNILVNQNLCCKVSDFGLT-RLLDDFDGTYE 782
Cdd:cd06616    90 SLDKFYKyvyEVLDSVIPEEILGKIaVATVKALNYLkEELKIIHRDVKPSNILLDRNGNIKLCDFGISgQLVDSIAKTRD 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 783 TqgGKIPirWTAPEAIAHRIFTTA----SDVWSFGIVMWEVlSFGDKPYGEMNN-----QEVMKSieegyrlPPPVDCPA 853
Cdd:cd06616   170 A--GCRP--YMAPERIDPSASRDGydvrSDVWSLGITLYEV-ATGKFPYPKWNSvfdqlTQVVKG-------DPPILSNS 237
                         250       260       270
                  ....*....|....*....|....*....|...
gi 2038291632 854 PLYEL---MKN----CWAYDRARRPHFLQLQAH 879
Cdd:cd06616   238 EEREFspsFVNfvnlCLIKDESKRPKYKELLKH 270
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
629-887 1.30e-15

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: 78.22  E-value: 1.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGalrfpsQDCKT---VAIKTLKDTSpDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFM 705
Cdd:cd06624    15 VLGKGTFGVVYAA------RDLSTqvrIAIKEIPERD-SREVQPLHEEIALHSRLSHKNIVQYLGSVSEDGFFKIFMEQV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 706 ENGALDAFLKEREDQLAPGQLVAMLLG--IASGMNYLSGHNYVHRDLAARNILVNQ-NLCCKVSDFGLTRLLDDFDGTYE 782
Cdd:cd06624    88 PGGSLSALLRSKWGPLKDNENTIGYYTkqILEGLKYLHDNKIVHRDIKGDNVLVNTySGVVKISDFGTSKRLAGINPCTE 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 783 TQGGKipIRWTAPEAIAH--RIFTTASDVWSFGIVMWEvLSFGDKPYGEMNN-QEVMKSIeeG-YRLPPPVdcPAPLYEL 858
Cdd:cd06624   168 TFTGT--LQYMAPEVIDKgqRGYGPPADIWSLGCTIIE-MATGKPPFIELGEpQAAMFKV--GmFKIHPEI--PESLSEE 240
                         250       260       270
                  ....*....|....*....|....*....|...
gi 2038291632 859 MKN----CWAYDRARRPhflqlQAHleQLLTDP 887
Cdd:cd06624   241 AKSfilrCFEPDPDKRA-----TAS--DLLQDP 266
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
630-826 1.35e-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: 78.24  E-value: 1.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRfpsQDCKTVAIKTLK-DTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENG 708
Cdd:cd07839     8 IGEGTYGTVFKAKNR---ETHEIVALKRVRlDDDDEGVPSSALREICLLKELKHKNIVRLYDVLHSDKKLTLVFEYCDQD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 aLDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDdfdgtyetqggkI 788
Cdd:cd07839    85 -LKKYFDSCNGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARAFG------------I 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2038291632 789 PIR---------WTAPEAI--AHRIFTTASDVWSFGIVMWEvLSFGDKP 826
Cdd:cd07839   152 PVRcysaevvtlWYRPPDVlfGAKLYSTSIDMWSAGCIFAE-LANAGRP 199
SAM_EPH-A7 cd09548
SAM domain of EPH-A7 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
915-972 1.52e-15

SAM domain of EPH-A7 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A7 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A7 receptors and appears to mediate cell-cell initiated signal transduction. EphA7 was found expressed in human embryonic stem (ES) cells, neural tissues, kidney vasculature. EphA7 knockout mice show decrease in cortical progenitor cell death at mid-neurogenesis and significant increase in cortical size. EphA7 may be involved in the pathogenesis and development of different cancers; in particular, EphA7 was found upregulated in glioblastoma and downregulated in colorectal cancer and gastric cancer. Thus, it is a potential molecular marker and/or therapy target for these types of cancers.


Pssm-ID: 188947  Cd Length: 70  Bit Score: 71.98  E-value: 1.52e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2038291632 915 YRSVSEWLESIRMKRYILHFRSAGLDTMECVLELTAEDLTQMGITLPGHQKRILCSIQ 972
Cdd:cd09548     7 FCSVGEWLEAIKMERYKDNFTAAGYNSLESVARMTIEDVMSLGITLVGHQKKIMSSIQ 64
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
607-841 1.59e-15

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: 78.53  E-value: 1.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 607 DPAQGALDFAQelDPTWLIVD-TVIGEGEFGEVYRgalrfpSQDCKTVAIKTLKDTSPDGQ-----WWNFLREATIMGQF 680
Cdd:cd06634     1 DPEVAELFFKD--DPEKLFSDlREIGHGSFGAVYF------ARDVRNNEVVAIKKMSYSGKqsnekWQDIIKEVKFLQKL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 681 NHPHILRLEGVVTKRKPIMIVTEFMENGALDaFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQN 760
Cdd:cd06634    73 RHPNTIEYRGCYLREHTAWLVMEYCLGSASD-LLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEP 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 761 LCCKVSDFGLTRLL---DDFDGTyetqggkiPIrWTAPE---AIAHRIFTTASDVWSFGIVMWEvLSFGDKPYGEMNNQE 834
Cdd:cd06634   152 GLVKLGDFGSASIMapaNSFVGT--------PY-WMAPEvilAMDEGQYDGKVDVWSLGITCIE-LAERKPPLFNMNAMS 221

                  ....*..
gi 2038291632 835 VMKSIEE 841
Cdd:cd06634   222 ALYHIAQ 228
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
629-879 1.81e-15

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: 77.48  E-value: 1.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGalrFPSQD----CKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEF 704
Cdd:cd06631     8 VLGKGAYGTVYCG---LTSTGqliaVKQVELDTSDKEKAEKEYEKLQEEVDLLKTLKHVNIVGYLGTCLEDNVVSIFMEF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 705 MENGALDAFLKeREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTR------------ 772
Cdd:cd06631    85 VPGGSIASILA-RFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGCAKrlcinlssgsqs 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 773 -LLDDFDGT-YetqggkipirWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSIEEGYRLPP--P 848
Cdd:cd06631   164 qLLKSMRGTpY----------WMAPEVINETGHGRKSDIWSIGCTVFEMAT-GKPPWADMNPMAAIFAIGSGRKPVPrlP 232
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2038291632 849 VDCPAPLYELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd06631   233 DKFSPEARDFVHACLTRDQDERPSAEQLLKH 263
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
630-883 1.84e-15

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: 77.70  E-value: 1.84e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGalRFPSQdcktVAIKTLK-DTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENG 708
Cdd:cd14152     8 IGQGRWGKVHRG--RWHGE----VAIRLLEiDGNNQDHLKLFKKEVMNYRQTRHENVVLFMGACMHPPHLAIITSFCKGR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 ALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCkVSDFGLTRLLDDF-DGTYETQgGK 787
Cdd:cd14152    82 TLYSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFGLFGISGVVqEGRRENE-LK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 788 IPIRWT---APEaIAHRI----------FTTASDVWSFGIVmWEVLSFGDKPYGEMNNQEVMKSIEEG---YRLPPPVDC 851
Cdd:cd14152   160 LPHDWLcylAPE-IVREMtpgkdedclpFSKAADVYAFGTI-WYELQARDWPLKNQPAEALIWQIGSGegmKQVLTTISL 237
                         250       260       270
                  ....*....|....*....|....*....|..
gi 2038291632 852 PAPLYELMKNCWAYDRARRPHFLQLQAHLEQL 883
Cdd:cd14152   238 GKEVTEILSACWAFDLEERPSFTLLMDMLEKL 269
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
624-870 1.91e-15

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: 78.00  E-value: 1.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 624 LIVDTvIGEGEFGEVYRgALRFPSQdcKTVAIKTLK--DTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIV 701
Cdd:cd05580     4 EFLKT-LGTGSFGRVRL-VKHKDSG--KYYALKILKkaKIIKLKQVEHVLNEKRILSEVRHPFIVNLLGSFQDDRNLYMV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 702 TEFMENGALDAFLkeREDQLAPGQlVAMLLG--IASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDdfDG 779
Cdd:cd05580    80 MEYVPGGELFSLL--RRSGRFPND-VAKFYAaeVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAKRVK--DR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 780 TYETQGgkIPiRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSIEEG-YRLPPPVDCPAplYEL 858
Cdd:cd05580   155 TYTLCG--TP-EYLAPEIILSKGHGKAVDWWALGILIYEMLA-GYPPFFDENPMKIYEKILEGkIRFPSFFDPDA--KDL 228
                         250
                  ....*....|..
gi 2038291632 859 MKNCWAYDRARR 870
Cdd:cd05580   229 IKRLLVVDLTKR 240
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
629-839 1.91e-15

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: 77.38  E-value: 1.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVyrgALRFPSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENG 708
Cdd:cd14167    10 VLGTGAFSEV---VLAEEKRTQKLVAIKCIAKKALEGKETSIENEIAVLHKIKHPNIVALDDIYESGGHLYLIMQLVSGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 AL------DAFLKEREdqlaPGQLVAMLLgiaSGMNYLSGHNYVHRDLAARNIL---VNQNLCCKVSDFGLTRLLDDfdG 779
Cdd:cd14167    87 ELfdriveKGFYTERD----ASKLIFQIL---DAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGLSKIEGS--G 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 780 TYETQGGKIPiRWTAPEAIAHRIFTTASDVWSFGIVMWeVLSFGDKPYGEMNNQEVMKSI 839
Cdd:cd14167   158 SVMSTACGTP-GYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDAKLFEQI 215
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
672-839 1.93e-15

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: 77.69  E-value: 1.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 672 REATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGALDAFLKEREdQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLA 751
Cdd:cd14196    57 REVSILRQVLHPNIITLHDVYENRTDVVLILELVSGGELFDFLAQKE-SLSEEEATSFIKQILDGVNYLHTKKIAHFDLK 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 752 ARNI-LVNQNLC---CKVSDFGLTRLLDD---FDGTYETQggkipiRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGD 824
Cdd:cd14196   136 PENImLLDKNIPiphIKLIDFGLAHEIEDgveFKNIFGTP------EFVAPEIVNYEPLGLEADMWSIGVITYILLS-GA 208
                         170
                  ....*....|....*
gi 2038291632 825 KPYGEMNNQEVMKSI 839
Cdd:cd14196   209 SPFLGDTKQETLANI 223
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
630-826 2.27e-15

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: 77.70  E-value: 2.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRfpsQDCKTVAIKTLK-DTSPDGQWWNFLREATIMG---QFNHPHILRLEGV-VTKRKPIMI-VTE 703
Cdd:cd07863     8 IGVGAYGTVYKARDP---HSGHFVALKSVRvQTNEDGLPLSTVREVALLKrleAFDHPNIVRLMDVcATSRTDRETkVTL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 704 FMENgaLDAFLKEREDQLAPGQLVA-----MLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLlddfd 778
Cdd:cd07863    85 VFEH--VDQDLRTYLDKVPPPGLPAetikdLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLARI----- 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2038291632 779 gtYETQGGKIPIRWT----APEAIAHRIFTTASDVWSFGIVMWEVlsFGDKP 826
Cdd:cd07863   158 --YSCQMALTPVVVTlwyrAPEVLLQSTYATPVDMWSVGCIFAEM--FRRKP 205
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
629-843 2.34e-15

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: 77.73  E-value: 2.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRFPSqdcKTVAIKTLKdTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENG 708
Cdd:cd14166    10 VLGSGAFSEVYLVKQRSTG---KLYALKCIK-KSPLSRDSSLENEIAVLKRIKHENIVTLEDIYESTTHYYLVMQLVSGG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 AL-DAFLK-----EREDQLAPGQLVamllgiaSGMNYLSGHNYVHRDLAARNILV---NQNLCCKVSDFGLTRLLDDfdG 779
Cdd:cd14166    86 ELfDRILErgvytEKDASRVINQVL-------SAVKYLHENGIVHRDLKPENLLYltpDENSKIMITDFGLSKMEQN--G 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038291632 780 TYETQGGKiPiRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSIEEGY 843
Cdd:cd14166   157 IMSTACGT-P-GYVAPEVLAQKPYSKAVDCWSIGVITYILLC-GYPPFYEETESRLFEKIKEGY 217
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
629-859 2.79e-15

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: 76.97  E-value: 2.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGalRFPSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENG 708
Cdd:cd14202     9 LIGHGAFAVVFKG--RHKEKHDLEVAVKCINKKNLAKSQTLLGKEIKILKELKHENIVALYDFQEIANSVYLVMEYCNGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 ALDAFLKEREdQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVN---------QNLCCKVSDFGLTRLLDDfDG 779
Cdd:cd14202    87 DLADYLHTMR-TLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSysggrksnpNNIRIKIADFGFARYLQN-NM 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 780 TYETQGGKiPIrWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSIEEGYRLPP--PVDCPAPLYE 857
Cdd:cd14202   165 MAATLCGS-PM-YMAPEVIMSQHYDAKADLWSIGTIIYQCLT-GKAPFQASSPQDLRLFYEKNKSLSPniPRETSSHLRQ 241

                  ..
gi 2038291632 858 LM 859
Cdd:cd14202   242 LL 243
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
630-848 2.80e-15

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: 76.54  E-value: 2.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRgalrfpsqdC------KTVAIKTLKDTSPDGQwwNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTE 703
Cdd:cd14006     1 LGRGRFGVVKR---------CiekatgREFAAKFIPKRDKKKE--AVLREISILNQLQHPRIIQLHEAYESPTELVLILE 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 704 FMENGALDAFLKEREdQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILV-----NQnlcCKVSDFGLTRLLDD-- 776
Cdd:cd14006    70 LCSGGELLDRLAERG-SLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLadrpsPQ---IKIIDFGLARKLNPge 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038291632 777 ----FDGTYETQggkipirwtAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSIEEG-YRLPPP 848
Cdd:cd14006   146 elkeIFGTPEFV---------APEIVNGEPVSLATDMWSIGVLTYVLLS-GLSPFLGEDDQETLANISACrVDFSEE 212
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
630-827 3.00e-15

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: 77.49  E-value: 3.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVyrgaLRFPSQDC-KTVAIKTLK-DTSPDGQ----WWNflrEATIMGQFNHPHILR-------LEGVVTKRK 696
Cdd:cd13989     1 LGSGGFGYV----TLWKHQDTgEYVAIKKCRqELSPSDKnrerWCL---EVQIMKKLNHPNVVSardvppeLEKLSPNDL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 697 PIMIVtEFMENGALDAFLKEREDQ--LAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNIL---VNQNLCCKVSDFGLT 771
Cdd:cd13989    74 PLLAM-EYCSGGDLRKVLNQPENCcgLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVlqqGGGRVIYKLIDLGYA 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2038291632 772 RLLDD------FDGTYEtqggkipirWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPY 827
Cdd:cd13989   153 KELDQgslctsFVGTLQ---------YLAPELFESKKYTCTVDYWSFGTLAFECIT-GYRPF 204
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
626-871 3.16e-15

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: 76.99  E-value: 3.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 626 VDTVIGEGEFGEVYRGALRFpsqDCKTVAIKTLK--DTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTE 703
Cdd:cd08228     6 IEKKIGRGQFSEVYRATCLL---DRKPVALKKVQifEMMDAKARQDCVKEIDLLKQLNHPNVIKYLDSFIEDNELNIVLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 704 FMENGALDAFLK--EREDQLAPGQLV-AMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGT 780
Cdd:cd08228    83 LADAGDLSQMIKyfKKQKRLIPERTVwKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKTTA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 781 YETQGGKiPIrWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGE-MNNQEVMKSIEEGYRLPPPVD-CPAPLYEL 858
Cdd:cd08228   163 AHSLVGT-PY-YMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDkMNLFSLCQKIEQCDYPPLPTEhYSEKLREL 240
                         250
                  ....*....|...
gi 2038291632 859 MKNCWAYDRARRP 871
Cdd:cd08228   241 VSMCIYPDPDQRP 253
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
629-879 3.41e-15

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: 76.63  E-value: 3.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYrgaLRFPSQDCKTVAIKTL------KDTSPDGQwwNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVT 702
Cdd:cd06625     7 LLGQGAFGQVY---LCYDADTGRELAVKQVeidpinTEASKEVK--ALECEIQLLKNLQHERIVQYYGCLQDEKSLSIFM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 703 EFMENGALDAFLKeredqlAPGQLVAMLLG-----IASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDdf 777
Cdd:cd06625    82 EYMPGGSVKDEIK------AYGALTENVTRkytrqILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGASKRLQ-- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 778 dgTYETQGGKIPIR----WTAPEAIAHRIFTTASDVWSFGIVMWEVLSfgDKPygEMNNQEVMKSI------EEGYRLPP 847
Cdd:cd06625   154 --TICSSTGMKSVTgtpyWMSPEVINGEGYGRKADIWSVGCTVVEMLT--TKP--PWAEFEPMAAIfkiatqPTNPQLPP 227
                         250       260       270
                  ....*....|....*....|....*....|..
gi 2038291632 848 PVDCPAplYELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd06625   228 HVSEDA--RDFLSLIFVRNKKQRPSAEELLSH 257
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
672-839 3.78e-15

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: 76.76  E-value: 3.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 672 REATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGALDAFLKEREdQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLA 751
Cdd:cd14105    57 REVSILRQVLHPNIITLHDVFENKTDVVLILELVAGGELFDFLAEKE-SLSEEEATEFLKQILDGVNYLHTKNIAHFDLK 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 752 ARNI-LVNQNLC---CKVSDFGLTRLLDD---FDGTYETQggkipiRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGD 824
Cdd:cd14105   136 PENImLLDKNVPiprIKLIDFGLAHKIEDgneFKNIFGTP------EFVAPEIVNYEPLGLEADMWSIGVITYILLS-GA 208
                         170
                  ....*....|....*
gi 2038291632 825 KPYGEMNNQEVMKSI 839
Cdd:cd14105   209 SPFLGDTKQETLANI 223
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
630-820 3.89e-15

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: 76.92  E-value: 3.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFPSQdckTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGa 709
Cdd:cd07870     8 LGEGSYATVYKGISRINGQ---LVALKVISMKTEEGVPFTAIREASLLKGLKHANIVLLHDIIHTKETLTFVFEYMHTD- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 710 LDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYETQggKIP 789
Cdd:cd07870    84 LAQYMIQHPGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLARAKSIPSQTYSSE--VVT 161
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2038291632 790 IRWTAPEAIAHRI-FTTASDVWSFGIVMWEVL 820
Cdd:cd07870   162 LWYRPPDVLLGATdYSSALDIWGAGCIFIEML 193
TM_EphA1 cd12841
Transmembrane domain of Ephrin Receptor A1 Protein Tyrosine Kinase; Ephrin receptors (EphRs) ...
536-568 3.92e-15

Transmembrane domain of Ephrin Receptor A1 Protein Tyrosine Kinase; Ephrin receptors (EphRs) comprise the largest subfamily of receptor PTKs, and are classified into two classes (EphA and EphB), corresponding 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. EphA1 has been associated with late-onset Alzheimer's disease and certain cancers such as colorectal and gastric carcinomas. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a single-span transmembrane (TM) domain, 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 TM domain mediates dimerization.


Pssm-ID: 214014  Cd Length: 38  Bit Score: 69.70  E-value: 3.92e-15
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2038291632 536 SPPVSRSLTGGEIVAIIFGVLLGIALLIGIYVF 568
Cdd:cd12841     1 SPPVSRGLTGGEIVAIIFGLLLGVALLLGILVF 33
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
625-875 4.36e-15

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: 76.39  E-value: 4.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 625 IVDTVIGEGEFGEVYRGaLRFPSQDckTVAIKTL-KDTSPDGQWW--NFLREATIMGQFNHPHILRLEGVVTKRKPIMIV 701
Cdd:cd14070     5 LIGRKLGEGSFAKVREG-LHAVTGE--KVAIKVIdKKKAKKDSYVtkNLRREGRIQQMIRHPNITQLLDILETENSYYLV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 702 TEFMENGAL------DAFLKEREDQLAPGQLVamllgiaSGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLT---R 772
Cdd:cd14070    82 MELCPGGNLmhriydKKRLEEREARRYIRQLV-------SAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSncaG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 773 LLDDFDGTYeTQGGKIPirWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYG--EMNNQEVMKSIEEGYRLPPPVD 850
Cdd:cd14070   155 ILGYSDPFS-TQCGSPA--YAAPELLARKKYGPKVDVWSIGVNMYAMLT-GTLPFTvePFSLRALHQKMVDKEMNPLPTD 230
                         250       260
                  ....*....|....*....|....*
gi 2038291632 851 CPAPLYELMKNCWAYDRARRPHFLQ 875
Cdd:cd14070   231 LSPGAISFLRSLLEPDPLKRPNIKQ 255
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
630-818 5.31e-15

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: 77.02  E-value: 5.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFPSQdckTVAIK-TLKDTSPDGQWWNFLREATIMGQFNHPHILRL-EGVVTKRKP-------IMI 700
Cdd:cd07865    20 IGQGTFGEVFKARHRKTGQ---IVALKkVLMENEKEGFPITALREIKILQLLKHENVVNLiEICRTKATPynrykgsIYL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 701 VTEFMENGaLDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRllddfdgT 780
Cdd:cd07865    97 VFEFCEHD-LAGLLSNKNVKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGVLKLADFGLAR-------A 168
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2038291632 781 YETQGGKIPIRWT---------APE-AIAHRIFTTASDVWSFGIVMWE 818
Cdd:cd07865   169 FSLAKNSQPNRYTnrvvtlwyrPPElLLGERDYGPPIDMWGAGCIMAE 216
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
630-842 5.88e-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: 75.98  E-value: 5.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFPSqdcKTVAIKTLKDTSPDG--QWWNFLREATI-MGQFNHPHILRLEGVVTKRKPIMIVTEFME 706
Cdd:cd05611     4 ISKGAFGSVYLAKKRSTG---DYFAIKVLKKSDMIAknQVTNVKAERAImMIQGESPYVAKLYYSFQSKDYLYLVMEYLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 707 NGALDAFLKER---EDQLAPGQLVAMLLGIasgmNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLL------DDF 777
Cdd:cd05611    81 GGDCASLIKTLgglPEDWAKQYIAEVVLGV----EDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSRNGlekrhnKKF 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2038291632 778 DGTYEtqggkipirWTAPEAIAHRIFTTASDVWSFGIVMWEVLsFGDKPYGEMNNQEVMKSIEEG 842
Cdd:cd05611   157 VGTPD---------YLAPETILGVGDDKMSDWWSLGCVIFEFL-FGYPPFHAETPDAVFDNILSR 211
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
629-871 6.85e-15

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: 75.78  E-value: 6.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGevyRGALRFPSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENG 708
Cdd:cd08219     7 VVGEGSFG---RALLVQHVNSDQKYAMKEIRLPKSSSAVEDSRKEAVLLAKMKHPNIVAFKESFEADGHLYIVMEYCDGG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 ALDAFLKEREDQLAPGQLV-AMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDD---FDGTYETQ 784
Cdd:cd08219    84 DLMQKIKLQRGKLFPEDTIlQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLTSpgaYACTYVGT 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 785 GGKIPirwtaPEAIAHRIFTTASDVWSFGIVMWEVLSFgDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLYELMKNCWA 864
Cdd:cd08219   164 PYYVP-----PEIWENMPYNNKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQGSYKPLPSHYSYELRSLIKQMFK 237

                  ....*..
gi 2038291632 865 YDRARRP 871
Cdd:cd08219   238 RNPRSRP 244
SAM_EPH-A4 cd09545
SAM domain of EPH-A4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
917-973 8.17e-15

SAM domain of EPH-A4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A4 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A4 receptors and appears to mediate cell-cell initiated signal transduction. SAM domains of EPH-A4 receptors can form homodimers. EPH-A4 receptors bind ligands such as erphirin A1, A4, A5. They are known to interact with a number of different proteins, including meltrin beta metalloprotease, Cdk5, and EFS2alpha, however SAM domain doesn't participate in these interactions. EPH-A4 receptors are involved in regulation of corticospinal tract formation, in pathway controlling voluntary movements, in formation of motor neurons, and in axon guidance (SAM domain is not required for axon guidance or for EPH-A4 kinase signaling). In Xenopus embryos EPH-A4 induces loss of cell adhesion, ventro-lateral protrusions, and severely expanded posterior structures. Mutations in SAM domain conserved tyrosine (Y928F) enhance the ability of EPH-A4 to induce these phenotypes, thus supporting the idea that the SAM domain may negatively regulate some aspects of EPH-A4 activity. EphA4 gene was found overexpressed in a number of different cancers including human gastric cancer, colorectal cancer, and pancreatic ductal adenocarcinoma. It is likely to be a promising molecular target for the cancer therapy.


Pssm-ID: 188944  Cd Length: 71  Bit Score: 69.98  E-value: 8.17e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2038291632 917 SVSEWLESIRMKRYILHFRSAGLDTMECVLELTAEDLTQMGITLPGHQKRILCSIQG 973
Cdd:cd09545     5 SVDDWLQAIKMERYKDNFTAAGYTTLEAVVHMNQDDLARIGISAIAHQNKILSSVQG 61
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
630-880 9.39e-15

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: 75.61  E-value: 9.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFpsqDCKTVAIKTLKDTSPdgqwwNFLREATIMGQFNHPHILRLEGV----------------VT 693
Cdd:cd14047    14 IGSGGFGQVFKAKHRI---DGKTYAIKRVKLNNE-----KAEREVKALAKLDHPNIVRYNGCwdgfdydpetsssnssRS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 694 KRKPIMIVTEFMENGALDAFLKERE-DQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTR 772
Cdd:cd14047    86 KTKCLFIQMEFCEKGTLESWIEKRNgEKLDKVLALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGKVKIGDFGLVT 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 773 LLddfDGTYETQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKpygEMNNQEVMKSIEEGyRLPPPVDCP 852
Cdd:cd14047   166 SL---KNDGKRTKSKGTLSYMSPEQISSQDYGKEVDIYALGLILFELLHVCDS---AFEKSKFWTDLRNG-ILPDIFDKR 238
                         250       260
                  ....*....|....*....|....*....
gi 2038291632 853 APLYE-LMKNCWAYDRARRPHFLQLQAHL 880
Cdd:cd14047   239 YKIEKtIIKKMLSKKPEDRPNASEILRTL 267
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
629-883 1.06e-14

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: 75.43  E-value: 1.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGalRFPSQdcktVAIKTLK-DTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMEN 707
Cdd:cd14153     7 LIGKGRFGQVYHG--RWHGE----VAIRLIDiERDNEEQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNqNLCCKVSDFGLTRLLDDFDGTYETQGGK 787
Cdd:cd14153    81 RTLYSVVRDAKVVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLFTISGVLQAGRREDKLR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 788 IPIRWT---APEAIaHRI----------FTTASDVWSFGIVmWEVLSFGDKPYGEMNNQEVMKSIEEGYR-LPPPVDCPA 853
Cdd:cd14153   160 IQSGWLchlAPEII-RQLspeteedklpFSKHSDVFAFGTI-WYELHAREWPFKTQPAEAIIWQVGSGMKpNLSQIGMGK 237
                         250       260       270
                  ....*....|....*....|....*....|
gi 2038291632 854 PLYELMKNCWAYDRARRPHFLQLQAHLEQL 883
Cdd:cd14153   238 EISDILLFCWAYEQEERPTFSKLMEMLEKL 267
SAM_EPH-A8 cd09550
SAM domain of EPH-A8 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
916-972 1.15e-14

SAM domain of EPH-A8 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A8 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A8 receptors and appears to mediate cell-cell initiated signal transduction. EPH-A8 receptors are involved in ligand dependent (ephirin A2, A3, A5) regulation of cell adhesion and migration, and in ligand independent regulation of neurite outgrowth in neuronal cells. They perform signaling in kinase dependent and kinase independent manner. EPH-A8 receptors are known to interact with a number of different proteins including PI 3-kinase and AIDA1-like subfamily SAM repeat domain containing proteins. However other domains (not SAM) of EPH-A8 receptors are involved in these interactions.


Pssm-ID: 188949  Cd Length: 65  Bit Score: 69.51  E-value: 1.15e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2038291632 916 RSVSEWLESIRMKRYILHFRSAGLDTMECVLELTAEDLTQMGITLPGHQKRILCSIQ 972
Cdd:cd09550     3 LSVDDWLDSIKMGRYKDHFAAGGYSSLGMVMRMNIEDIRRLGITLMGHQKKILTSIQ 59
SAM_EPH-B3 cd09553
SAM domain of EPH-B3 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
911-975 1.30e-14

SAM domain of EPH-B3 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B3 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B3 receptors and appears to mediate cell-cell initiated signal transduction. EPH-B3 receptor protein kinase performs kinase-dependent and kinase-independent functions. It is known to be involved in thymus morphogenesis, in regulation of cell adhesion and migration. Also EphB3 controls cell positioning and ordered migration in the intestinal epithelium and plays a role in the regulation of adult retinal ganglion cell axon plasticity after optic nerve injury. In some experimental models overexpression of EphB3 enhances cell/cell contacts and suppresses colon tumor growth.


Pssm-ID: 188952  Cd Length: 69  Bit Score: 69.29  E-value: 1.30e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2038291632 911 DGIPYRSVSEWLESIRMKRYILHFRSAGLDTMECVLELTAEDLTQMGITLPGHQKRILCSIQGFK 975
Cdd:cd09553     2 DYTTFTTVGDWLDAIKMGRYKENFVSAGFASFDLVAQMTAEDLLRIGVTLAGHQKKILSSIQDMR 66
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
630-821 1.39e-14

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 75.62  E-value: 1.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFPSQdckTVAIKTLK-DTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFmeng 708
Cdd:PLN00009   10 IGEGTYGVVYKARDRVTNE---TIALKKIRlEQEDEGVPSTAIREISLLKEMQHGNIVRLQDVVHSEKRLYLVFEY---- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 aLDAFLKEREDQLA-----PGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQ-NLCCKVSDFGLTRLLDdfdgtye 782
Cdd:PLN00009   83 -LDLDLKKHMDSSPdfaknPRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRrTNALKLADFGLARAFG------- 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2038291632 783 tqggkIPIR----------WTAPEA-IAHRIFTTASDVWSFGIVMWEVLS 821
Cdd:PLN00009  155 -----IPVRtfthevvtlwYRAPEIlLGSRHYSTPVDIWSVGCIFAEMVN 199
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
630-883 1.41e-14

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: 75.46  E-value: 1.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRfpsqdCKTVAIKTLKdTSPDGQWWnflREATIMGQ--FNHPHILRLEGVVTK----RKPIMIVTE 703
Cdd:cd14220     3 IGKGRYGEVWMGKWR-----GEKVAVKVFF-TTEEASWF---RETEIYQTvlMRHENILGFIAADIKgtgsWTQLYLITD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 704 FMENGALDAFLKERedQLAPGQLVAMLLGIASGMNYLSGHNY--------VHRDLAARNILVNQNLCCKVSDFGLTRLLD 775
Cdd:cd14220    74 YHENGSLYDFLKCT--TLDTRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGTCCIADLGLAVKFN 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 776 DfdgtyETQGGKIPI-------RWTAPEAI------AHRIFTTASDVWSFGIVMWE---------VLSFGDKPYGEM--- 830
Cdd:cd14220   152 S-----DTNEVDVPLntrvgtkRYMAPEVLdeslnkNHFQAYIMADIYSFGLIIWEmarrcvtggIVEEYQLPYYDMvps 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2038291632 831 -NNQEVMKSIEEGYRLPPPV-------DCPAPLYELMKNCWAYDRARRPHFLQLQAHLEQL 883
Cdd:cd14220   227 dPSYEDMREVVCVKRLRPTVsnrwnsdECLRAVLKLMSECWAHNPASRLTALRIKKTLAKM 287
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
630-885 2.09e-14

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: 74.64  E-value: 2.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYrgaLRFPSQDCKTVAIKTLKDTSPDGQWwNFLREATIMGQFNHPHILRLE--GVVTKR---KPIMIVTEF 704
Cdd:cd13986     8 LGEGGFSFVY---LVEDLSTGRLYALKKILCHSKEDVK-EAMREIENYRLFNHPNILRLLdsQIVKEAggkKEVYLLLPY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 705 MENGAL-DAF--LKEREDQLAPGQLVAMLLGIASGMNYLSGHN---YVHRDLAARNILVNQNLCCKVSDFG--------- 769
Cdd:cd13986    84 YKRGSLqDEIerRLVKGTFFPEDRILHIFLGICRGLKAMHEPElvpYAHRDIKPGNVLLSEDDEPILMDLGsmnpariei 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 770 ----LTRLLDDFDgtyeTQGGKIPirWTAPE---AIAHRIFTTASDVWSFGIVMWEVLsFGDKPYgEMNNQE---VMKSI 839
Cdd:cd13986   164 egrrEALALQDWA----AEHCTMP--YRAPElfdVKSHCTIDEKTDIWSLGCTLYALM-YGESPF-ERIFQKgdsLALAV 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2038291632 840 EEG-YRLPPPVDCPAPLYELMKNCWAYDRARRPHFLQLQAHLEQLLT 885
Cdd:cd13986   236 LSGnYSFPDNSRYSEELHQLVKSMLVVNPAERPSIDDLLSRVHDLIP 282
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
630-821 2.15e-14

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: 74.72  E-value: 2.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFPSQdckTVAIKTLKDTSPDGQWWNF-LREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENG 708
Cdd:cd07847     9 IGEGSYGVVFKCRNRETGQ---IVAIKKFVESEDDPVIKKIaLREIRMLKQLKHPNLVNLIEVFRRKRKLHLVFEYCDHT 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 ALDAfLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYETQggkI 788
Cdd:cd07847    86 VLNE-LEKNPRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFARILTGPGDDYTDY---V 161
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2038291632 789 PIRW-TAPEAIAHRI-FTTASDVWSFGIVMWEVLS 821
Cdd:cd07847   162 ATRWyRAPELLVGDTqYGPPVDVWAIGCVFAELLT 196
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
629-879 2.31e-14

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: 74.76  E-value: 2.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRFPSQdckTVAIKTLKDTSPDGQwwNFLREATIMGQFNH-PHILRLEGVVTKRKP------IMIV 701
Cdd:cd06637    13 LVGNGTYGQVYKGRHVKTGQ---LAAIKVMDVTGDEEE--EIKQEINMLKKYSHhRNIATYYGAFIKKNPpgmddqLWLV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 702 TEFMENGALDAFLKEREDQLAPGQLVAMLL-GIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGT 780
Cdd:cd06637    88 MEFCGAGSVTDLIKNTKGNTLKEEWIAYICrEILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGR 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 781 YETQGGKiPIrWTAPEAIA-----HRIFTTASDVWSFGIVMWEvLSFGDKPYGEMNNQEVMKSIEegyRLPPP----VDC 851
Cdd:cd06637   168 RNTFIGT-PY-WMAPEVIAcdenpDATYDFKSDLWSLGITAIE-MAEGAPPLCDMHPMRALFLIP---RNPAPrlksKKW 241
                         250       260
                  ....*....|....*....|....*...
gi 2038291632 852 PAPLYELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd06637   242 SKKFQSFIESCLVKNHSQRPSTEQLMKH 269
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
627-848 3.02e-14

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: 73.99  E-value: 3.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 627 DTVIGEGEFGEVYRGALRfpsQDCKTVAIKTL-KDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFM 705
Cdd:cd14082     8 DEVLGSGQFGIVYGGKHR---KTGRDVAIKVIdKLRFPTKQESQLRNEVAILQQLSHPGVVNLECMFETPERVFVVMEKL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 706 ENGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQN-------LCckvsDFGLTRLLddfd 778
Cdd:cd14082    85 HGDMLEMILSSEKGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAepfpqvkLC----DFGFARII---- 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038291632 779 gtyetqgGKIPIR--------WTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEmnNQEVMKSIEEGYRLPPP 848
Cdd:cd14082   157 -------GEKSFRrsvvgtpaYLAPEVLRNKGYNRSLDMWSVGVIIYVSLS-GTFPFNE--DEDINDQIQNAAFMYPP 224
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
629-879 3.15e-14

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: 73.73  E-value: 3.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRgALRFPSQdcKTVAIKTL---KDTSPDGQwwNFLREATIMGQFNHPHILRLEG--VVTKRKPIMIVTE 703
Cdd:cd08217     7 TIGKGSFGTVRK-VRRKSDG--KILVWKEIdygKMSEKEKQ--QLVSEVNILRELKHPNIVRYYDriVDRANTTLYIVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 704 FMENGALDAFLK--EREDQLAPGQLV-----AMLLGIASGMNYLSGHNYV-HRDLAARNILVNQNLCCKVSDFGLTRLLD 775
Cdd:cd08217    82 YCEGGDLAQLIKkcKKENQYIPEEFIwkiftQLLLALYECHNRSVGGGKIlHRDLKPANIFLDSDNNVKLGDFGLARVLS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 776 D-------FDGTyetqggkiPIRWtAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSIEEGYRLPPP 848
Cdd:cd08217   162 HdssfaktYVGT--------PYYM-SPELLNEQSYDEKSDIWSLGCLIYELCA-LHPPFQAANQLELAKKIKEGKFPRIP 231
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2038291632 849 VDCPAPLYELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd08217   232 SRYSSELNEVIKSMLNVDPDKRPSVEELLQL 262
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
630-859 3.77e-14

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: 73.56  E-value: 3.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGalRFPSQDCKTVAIKTLKDTSPdGQWWNFL-REATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENG 708
Cdd:cd14120     1 IGHGAFAVVFKG--RHRKKPDLPVAIKCITKKNL-SKSQNLLgKEIKILKELSHENVVALLDCQETSSSVYLVMEYCNGG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 ALDAFLKER----EDQLApgqlvAMLLGIASGMNYLSGHNYVHRDLAARNILVNQN---------LCCKVSDFGLTRLLD 775
Cdd:cd14120    78 DLADYLQAKgtlsEDTIR-----VFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNsgrkpspndIRLKIADFGFARFLQ 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 776 DFDGTYETQGGKIpirWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSIEEGYRLPP--PVDCPA 853
Cdd:cd14120   153 DGMMAATLCGSPM---YMAPEVIMSLQYDAKADLWSIGTIVYQCLT-GKAPFQAQTPQELKAFYEKNANLRPniPSGTSP 228

                  ....*.
gi 2038291632 854 PLYELM 859
Cdd:cd14120   229 ALKDLL 234
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
671-861 3.79e-14

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: 74.39  E-value: 3.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 671 LREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGALDAFLKEredqlaPGQLVAMLLG-----IASGMNYL-SGHN 744
Cdd:cd06615    47 IRELKVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQVLKK------AGRIPENILGkisiaVLRGLTYLrEKHK 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 745 YVHRDLAARNILVNQNLCCKVSDFGLTRLLDD-----FDGTYEtqggkipirWTAPEAIAHRIFTTASDVWSFGIVMWEv 819
Cdd:cd06615   121 IMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDsmansFVGTRS---------YMSPERLQGTHYTVQSDIWSLGLSLVE- 190
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2038291632 820 LSFGDKP--------YGEMNNQEVMKSIEEGYRLPP---PVDCPAPL--YELMKN 861
Cdd:cd06615   191 MAIGRYPipppdakeLEAMFGRPVSEGEAKESHRPVsghPPDSPRPMaiFELLDY 245
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
626-839 3.87e-14

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: 73.50  E-value: 3.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 626 VDTVIGEGEFGEVYRgalRFPSQDCKTVAIKTLKDTSPDGQWwNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFM 705
Cdd:cd14191     6 IEERLGSGKFGQVFR---LVEKKTKKVWAGKFFKAYSAKEKE-NIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEMV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 706 ENGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNIL-VNQN-LCCKVSDFGLTRLLDDfDGTYET 783
Cdd:cd14191    82 SGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTgTKIKLIDFGLARRLEN-AGSLKV 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2038291632 784 QGGKiPiRWTAPEAIAHRIFTTASDVWSFGIVMWeVLSFGDKPYGEMNNQEVMKSI 839
Cdd:cd14191   161 LFGT-P-EFVAPEVINYEPIGYATDMWSIGVICY-ILVSGLSPFMGDNDNETLANV 213
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
629-839 3.99e-14

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: 73.46  E-value: 3.99e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRFPSQD--CKTVAIKTLKDTSpdgqwwNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFME 706
Cdd:cd14192    11 VLGGGRFGQVHKCTELSTGLTlaAKIIKVKGAKERE------EVKNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 707 NGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNIL-VNQN-LCCKVSDFGLTR-------LLDDF 777
Cdd:cd14192    85 GGELFDRITDESYQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILcVNSTgNQIKIIDFGLARrykprekLKVNF 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2038291632 778 dGTYEtqggkipirWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSI 839
Cdd:cd14192   165 -GTPE---------FLAPEVVNYDFVSFPTDMWSVGVITYMLLS-GLSPFLGETDAETMNNI 215
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
630-851 4.49e-14

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: 73.40  E-value: 4.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGalrfpsQDCKT---VAIKTLK--DTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEF 704
Cdd:cd05579     1 ISRGAYGRVYLA------KKKSTgdlYAIKVIKkrDMIRKNQVDSVLAERNILSQAQNPFVVKLYYSFQGKKNLYLVMEY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 705 MENGALDAFLK------EREDQLAPGQLVAMLlgiasgmNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTR--LLDD 776
Cdd:cd05579    75 LPGGDLYSLLEnvgaldEDVARIYIAEIVLAL-------EYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSKvgLVRR 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 777 FDGTYETQGGKIPIR-----------WTAPEAIAHRIFTTASDVWSFGIVMWEVLsFGDKPYGEMNNQEVMKSIEEGyRL 845
Cdd:cd05579   148 QIKLSIQKKSNGAPEkedrrivgtpdYLAPEILLGQGHGKTVDWWSLGVILYEFL-VGIPPFHAETPEEIFQNILNG-KI 225

                  ....*.
gi 2038291632 846 PPPVDC 851
Cdd:cd05579   226 EWPEDP 231
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
629-827 4.67e-14

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: 73.06  E-value: 4.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVY---------RGALRFPS-QDC-KTVAIKtlkdtspdgqwwNFLREATIMGQFNHPHILRLEGVVTKRKP 697
Cdd:cd05578     7 VIGKGSFGKVCivqkkdtkkMFAMKYMNkQKCiEKDSVR------------NVLNELEILQELEHPFLVNLWYSFQDEED 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 698 IMIVTEFMENGALDAFLkEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDF 777
Cdd:cd05578    75 MYMVVDLLLGGDLRYHL-QQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIATKLTDG 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2038291632 778 DGTYETQGGKIpirWTAPEAIAHRIFTTASDVWSFGIVMWEVLsFGDKPY 827
Cdd:cd05578   154 TLATSTSGTKP---YMAPEVFMRAGYSFAVDWWSLGVTAYEML-RGKRPY 199
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
620-848 4.86e-14

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: 73.87  E-value: 4.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 620 DPTWLIVDTV-IGEGEFGEVyrgALRFPSQDCKTVAIKTLkDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPI 698
Cdd:cd06659    18 DPRQLLENYVkIGEGSTGVV---CIAREKHSGRQVAVKMM-DLRKQQRRELLFNEVVIMRDYQHPNVVEMYKSYLVGEEL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 699 MIVTEFMENGALDAFLKERedQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDfd 778
Cdd:cd06659    94 WVLMEYLQGGALTDIVSQT--RLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGFCAQISK-- 169
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038291632 779 gtyetqggKIPIR--------WTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSIEEGyrlPPP 848
Cdd:cd06659   170 --------DVPKRkslvgtpyWMAPEVISRCPYGTEVDIWSLGIMVIEMVD-GEPPYFSDSPVQAMKRLRDS---PPP 235
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
673-879 4.91e-14

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: 73.23  E-value: 4.91e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 673 EATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGALdAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAA 752
Cdd:cd06630    53 EIRMMARLNHPNIVRMLGATQHKSHFNIFVEWMAGGSV-ASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKG 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 753 RNILVN---QNLccKVSDFGLT-RLLDDFDGTYETQGGKI-PIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPY 827
Cdd:cd06630   132 ANLLVDstgQRL--RIADFGAAaRLASKGTGAGEFQGQLLgTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMAT-AKPPW 208
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2038291632 828 GEMNNQEVMKSIeegYRL-----PPPV-DCPAP-LYELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd06630   209 NAEKISNHLALI---FKIasattPPPIpEHLSPgLRDVTLRCLELQPEDRPPARELLKH 264
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
630-879 5.18e-14

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 74.47  E-value: 5.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRgALRFPSQdcKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGA 709
Cdd:PLN00034   82 IGSGAGGTVYK-VIHRPTG--RLYALKVIYGNHEDTVRRQICREIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGS 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 710 LDAFLKEREDQLAPgqlVAMllGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDD-FDGTYETQGgki 788
Cdd:PLN00034  159 LEGTHIADEQFLAD---VAR--QILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRILAQtMDPCNSSVG--- 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 789 PIRWTAPEaiahRIFTT---------ASDVWSFGIVMWEvLSFGDKPYGeMNNQ----EVMKSIeeGYRLPP--PVDCPA 853
Cdd:PLN00034  231 TIAYMSPE----RINTDlnhgaydgyAGDIWSLGVSILE-FYLGRFPFG-VGRQgdwaSLMCAI--CMSQPPeaPATASR 302
                         250       260
                  ....*....|....*....|....*.
gi 2038291632 854 PLYELMKNCWAYDRARRPHFLQLQAH 879
Cdd:PLN00034  303 EFRHFISCCLQREPAKRWSAMQLLQH 328
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
681-871 5.31e-14

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: 73.46  E-value: 5.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 681 NHPHILRLEGVVTKRKPIMIVTEFMEnGALDAFLK---EREDQLAPG-QLVAMLLGIASGMNYLSGHNYVHRDLAARNIL 756
Cdd:cd13982    53 EHPNVIRYFCTEKDRQFLYIALELCA-ASLQDLVEsprESKLFLRPGlEPVRLLRQIASGLAHLHSLNIVHRDLKPQNIL 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 757 VNQ-----NLCCKVSDFGLTRLLDDFDGTY-ETQGGKIPIRWTAPEAI----AHRIfTTASDVWSFGIVMWEVLSFGDKP 826
Cdd:cd13982   132 ISTpnahgNVRAMISDFGLCKKLDVGRSSFsRRSGVAGTSGWIAPEMLsgstKRRQ-TRAVDIFSLGCVFYYVLSGGSHP 210
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2038291632 827 YGEMNNQE--VMKSIEEGYRLPPPVDCPAPLYELMKNCWAYDRARRP 871
Cdd:cd13982   211 FGDKLEREanILKGKYSLDKLLSLGEHGPEAQDLIERMIDFDPEKRP 257
SAM_EPH-B1 cd09551
SAM domain of EPH-B1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
915-975 5.56e-14

SAM domain of EPH-B1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B1 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH- B1 receptors. In human vascular endothelial cells it appears to mediate cell-cell initiated signal transduction via the binding of the adaptor protein GRB10 (growth factor) through its SH2 domain to a conserved tyrosine that is phosphorylated. EPH-B1 receptors play a role in neurogenesis, in particular in regulation of proliferation and migration of neural progenitors in the hippocampus and in corneal neovascularization; they are involved in converting the crossed retinal projection to ipsilateral retinal projection. They may be potential targets in angiogenesis-related disorders.


Pssm-ID: 188950  Cd Length: 68  Bit Score: 67.76  E-value: 5.56e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2038291632 915 YRSVSEWLESIRMKRYILHFRSAGLDTMECVLELTAEDLTQMGITLPGHQKRILCSIQGFK 975
Cdd:cd09551     6 FTSVEDWLSAIKMSQYRDNFLSSGFTSLQLVAQMTSEDLLRIGVTLAGHQKKILNSIQSMR 66
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
622-821 6.57e-14

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: 73.50  E-value: 6.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 622 TWLIVDTvIGEGEFGEVYRGALRFPSQdckTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIV 701
Cdd:cd07873     3 TYIKLDK-LGEGTYATVYKGRSKLTDN---LVALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIIHTEKSLTLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 702 TEFmengaLDAFLKEREDQLapGQLVAM------LLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLD 775
Cdd:cd07873    79 FEY-----LDKDLKQYLDDC--GNSINMhnvklfLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKS 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2038291632 776 DFDGTYETQggkIPIRWTAPEAI--AHRIFTTASDVWSFGIVMWEVLS 821
Cdd:cd07873   152 IPTKTYSNE---VVTLWYRPPDIllGSTDYSTQIDMWGVGCIFYEMST 196
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
630-854 6.85e-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: 73.10  E-value: 6.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVY----RGALRFpsqdcktVAIKTLKDTSPDG--QWWNFLREatimgqFNHPHILRLEGVVTKRKPIMIVTE 703
Cdd:cd14010     8 IGRGKHSVVYkgrrKGTIEF-------VAIKCVDKSKRPEvlNEVRLTHE------LKHPNVLKFYEWYETSNHLWLVVE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 704 FMENGALDAFLkeREDQLAPGQLVAML-LGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDD------ 776
Cdd:cd14010    75 YCTGGDLETLL--RQDGNLPESSVRKFgRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLARREGEilkelf 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 777 --FDGTYETQGGKIPIR------WTAPEAIAHRIFTTASDVWSFGIVMWEvLSFGDKPYGEMNNQEVMKSI--EEGYRLP 846
Cdd:cd14010   153 gqFSDEGNVNKVSKKQAkrgtpyYMAPELFQGGVHSFASDLWALGCVLYE-MFTGKPPFVAESFTELVEKIlnEDPPPPP 231

                  ....*...
gi 2038291632 847 PPVDCPAP 854
Cdd:cd14010   232 PKVSSKPS 239
PK_GC-C cd14044
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain ...
643-885 7.05e-14

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: 73.00  E-value: 7.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 643 LRFPSQDCKTVAIKTLKDTspDGqwwNFLREATI----MGQFNHPHILRLEGVVTKRKPIMIVTEFMENGALDAFLKER- 717
Cdd:cd14044    24 LRQGKYDKKVVILKDLKNN--EG---NFTEKQKIelnkLLQIDYYNLTKFYGTVKLDTMIFGVIEYCERGSLRDVLNDKi 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 718 ---EDQLAPGQL-VAMLLGIASGMNYL-SGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDdfdgtyetqggkiPIR- 791
Cdd:cd14044    99 sypDGTFMDWEFkISVMYDIAKGMSYLhSSKTEVHGRLKSTNCVVDSRMVVKITDFGCNSILP-------------PSKd 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 792 -WTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGE-----------MNNQEVMKSIEEGYRLPPPVDCPAPLYELM 859
Cdd:cd14044   166 lWTAPEHLRQAGTSQKGDVYSYGIIAQEIILRKETFYTAacsdrkekiyrVQNPKGMKPFRPDLNLESAGEREREVYGLV 245
                         250       260
                  ....*....|....*....|....*.
gi 2038291632 860 KNCWAYDRARRPHFLQLQAHLEQLLT 885
Cdd:cd14044   246 KNCWEEDPEKRPDFKKIENTLAKIFS 271
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
629-879 7.54e-14

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: 73.23  E-value: 7.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRFPSQdckTVAIKTLKDtSPDGQWWN--FLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFME 706
Cdd:cd07846     8 LVGEGSYGMVMKCRHKETGQ---IVAIKKFLE-SEDDKMVKkiAMREIKMLKQLRHENLVNLIEVFRRKKRWYLVFEFVD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 707 NGALDAfLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLddfDGTYETQGG 786
Cdd:cd07846    84 HTVLDD-LEKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTL---AAPGEVYTD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 787 KIPIRW-TAPEAIAHRI-FTTASDVWSFGIVMWEVLS----F-GD----------KPYGE--MNNQEVMKS--IEEGYRL 845
Cdd:cd07846   160 YVATRWyRAPELLVGDTkYGKAVDVWAVGCLVTEMLTgeplFpGDsdidqlyhiiKCLGNliPRHQELFQKnpLFAGVRL 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2038291632 846 pPPVDCPAPL-----------YELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd07846   240 -PEVKEVEPLerrypklsgvvIDLAKKCLHIDPDKRPSCSELLHH 283
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
630-839 8.71e-14

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: 72.64  E-value: 8.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYrgaLRFPSQDCKTVAIKTLK-----DTspdGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEF 704
Cdd:cd05572     1 LGVGGFGRVE---LVQLKSKGRTFALKCVKkrhivQT---RQQEHIFSEKEILEECNSPFIVKLYRTFKDKKYLYMLMEY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 705 MENGALDAFLKERedqlapGQL--------VAMllgIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDD 776
Cdd:cd05572    75 CLGGELWTILRDR------GLFdeytarfyTAC---VVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKKLGS 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2038291632 777 FDGTYETQGgkIPiRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQ--EVMKSI 839
Cdd:cd05572   146 GRKTWTFCG--TP-EYVAPEIILNKGYDFSVDYWSLGILLYELLT-GRPPFGGDDEDpmKIYNII 206
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
630-820 9.37e-14

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: 73.19  E-value: 9.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFpsqDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGa 709
Cdd:cd07869    13 LGEGSYATVYKGKSKV---NGKLVALKVIRLQEEEGTPFTAIREASLLKGLKHANIVLLHDIIHTKETLTLVFEYVHTD- 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 710 LDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYETQggkIP 789
Cdd:cd07869    89 LCQYMDKHPGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARAKSVPSHTYSNE---VV 165
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2038291632 790 IRWTAPEAI--AHRIFTTASDVWSFGIVMWEVL 820
Cdd:cd07869   166 TLWYRPPDVllGSTEYSTCLDMWGVGCIFVEMI 198
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
628-827 1.05e-13

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: 72.38  E-value: 1.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 628 TVIGEGEFGEVYRgALRfpSQDCKTVAIKTLKDTSPDGQWWN------FLREATIMGQF-NHPHILRLEGVVTKRKPIMI 700
Cdd:cd13993     6 SPIGEGAYGVVYL-AVD--LRTGRKYAIKCLYKSGPNSKDGNdfqklpQLREIDLHRRVsRHPNIITLHDVFETEVAIYI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 701 VTEFMENGalDAFLKEREDQLAPGQLVAM---LLGIASGMNYLSGHNYVHRDLAARNILVNQN-LCCKVSDFGLTRlldd 776
Cdd:cd13993    83 VLEYCPNG--DLFEAITENRIYVGKTELIknvFLQLIDAVKHCHSLGIYHRDIKPENILLSQDeGTVKLCDFGLAT---- 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2038291632 777 fDGTYETQGGKIPIRWTAPEAI-----AHRIFTTAS-DVWSFGIVMWEVLsFGDKPY 827
Cdd:cd13993   157 -TEKISMDFGVGSEFYMAPECFdevgrSLKGYPCAAgDIWSLGIILLNLT-FGRNPW 211
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
626-887 1.10e-13

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: 72.37  E-value: 1.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 626 VDTVIGEGEFGEVYRGALRfpsQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFM 705
Cdd:cd14184     5 IGKVIGDGNFAVVKECVER---STGKEFALKIIDKAKCCGKEHLIENEVSILRRVKHPNIIMLIEEMDTPAELYLVMELV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 706 ENGAL-DAFLKEREDQLAPGQlvAMLLGIASGMNYLSGHNYVHRDLAARNILV----NQNLCCKVSDFGLTRLLDdfdGT 780
Cdd:cd14184    82 KGGDLfDAITSSTKYTERDAS--AMVYNLASALKYLHGLCIVHRDIKPENLLVceypDGTKSLKLGDFGLATVVE---GP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 781 YETQGGKiPIrWTAPEAIAHRIFTTASDVWSFGIVMWeVLSFGDKPYGEMNN--QEVMKSIEEGYrlpppVDCPAPLYEL 858
Cdd:cd14184   157 LYTVCGT-PT-YVAPEIIAETGYGLKVDIWAAGVITY-ILLCGFPPFRSENNlqEDLFDQILLGK-----LEFPSPYWDN 228
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2038291632 859 MKncwayDRARRPHFLQLQAHLE------QLLTDP 887
Cdd:cd14184   229 IT-----DSAKELISHMLQVNVEarytaeQILSHP 258
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
671-848 1.13e-13

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: 72.39  E-value: 1.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 671 LREATIMGQFN-HPHILRLEGVVTKRKPIMIVTEFMENGALDAFLKEREdQLAPGQLVAMLLGIASGMNYLSGHNYVHRD 749
Cdd:cd14093    56 RREIEILRQVSgHPNIIELHDVFESPTFIFLVFELCRKGELFDYLTEVV-TLSEKKTRRIMRQLFEAVEFLHSLNIVHRD 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 750 LAARNILVNQNLCCKVSDFGLTRLLDDFDGTYE---TQGgkipirWTAPEAIAHRIFTTAS------DVWSFGIVMWEVL 820
Cdd:cd14093   135 LKPENILLDDNLNVKISDFGFATRLDEGEKLRElcgTPG------YLAPEVLKCSMYDNAPgygkevDMWACGVIMYTLL 208
                         170       180
                  ....*....|....*....|....*....
gi 2038291632 821 SfGDKPYGEMNNQEVMKSIEEG-YRLPPP 848
Cdd:cd14093   209 A-GCPPFWHRKQMVMLRNIMEGkYEFGSP 236
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
629-859 1.44e-13

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: 71.96  E-value: 1.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGalRFPSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENG 708
Cdd:cd14201    13 LVGHGAFAVVFKG--RHRKKTDWEVAIKSINKKNLSKSQILLGKEIKILKELQHENIVALYDVQEMPNSVFLVMEYCNGG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 ALDAFLKEReDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVN---------QNLCCKVSDFGLTRLLDDFDG 779
Cdd:cd14201    91 DLADYLQAK-GTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSyasrkkssvSGIRIKIADFGFARYLQSNMM 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 780 TYETQGGKIpirWTAPEAIAHRIFTTASDVWSFGIVMWEVLsFGDKPYGEMNNQEVMKSIEEGYRLPP--PVDCPAPLYE 857
Cdd:cd14201   170 AATLCGSPM---YMAPEVIMSQHYDAKADLWSIGTVIYQCL-VGKPPFQANSPQDLRMFYEKNKNLQPsiPRETSPYLAD 245

                  ..
gi 2038291632 858 LM 859
Cdd:cd14201   246 LL 247
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
673-882 1.74e-13

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: 72.05  E-value: 1.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 673 EATIMGQFNHPHILRLEGVVT-KRKPIMIVTEFME---NGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLsgHN---Y 745
Cdd:cd14001    55 EAKILKSLNHPNIVGFRAFTKsEDGSLCLAMEYGGkslNDLIEERYEAGLGPFPAATILKVALSIARALEYL--HNekkI 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 746 VHRDLAARNILVNQNL-CCKVSDFGLTRLLD-----DFDGTYETQGGKIpirWTAPEAI-AHRIFTTASDVWSFGIVMWE 818
Cdd:cd14001   133 LHGDIKSGNVLIKGDFeSVKLCDFGVSLPLTenlevDSDPKAQYVGTEP---WKAKEALeEGGVITDKADIFAYGLVLWE 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 819 VLSFgDKPYGEMNNQEVM---KSIEE------------GYRLPPPVDCPAPLY----ELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd14001   210 MMTL-SVPHLNLLDIEDDdedESFDEdeedeeayygtlGTRPALNLGELDDSYqkviELFYACTQEDPKDRPSAAHIVEA 288

                  ...
gi 2038291632 880 LEQ 882
Cdd:cd14001   289 LEA 291
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
627-821 2.33e-13

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: 72.85  E-value: 2.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 627 DTVIGEGEFGEVYrgALRFPsQDCKTVAIKTLKDTspdgqWWNF------LREATIMGQFNHPHILRLEGVVTKRKP--- 697
Cdd:cd07853     5 DRPIGYGAFGVVW--SVTDP-RDGKRVALKKMPNV-----FQNLvsckrvFRELKMLCFFKHDNVLSALDILQPPHIdpf 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 698 --IMIVTEFMENGALDAFLkeREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLD 775
Cdd:cd07853    77 eeIYVVTELMQSDLHKIIV--SPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLARVEE 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2038291632 776 DFDGTYETQgGKIPIRWTAPEAI-AHRIFTTASDVWSFGIVMWEVLS 821
Cdd:cd07853   155 PDESKHMTQ-EVVTQYYRAPEILmGSRHYTSAVDIWSVGCIFAELLG 200
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
611-848 2.44e-13

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: 71.54  E-value: 2.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 611 GALDFAQELDPTwlivdTVIGEGEFGEVYRGALRFPSQDcktVAIKTLKDT----SPdgQWWNFLREAT-----IMGQF- 680
Cdd:cd14181     4 GAKEFYQKYDPK-----EVIGRGVSSVVRRCVHRHTGQE---FAVKIIEVTaerlSP--EQLEEVRSSTlkeihILRQVs 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 681 NHPHILRLEGVVTKRKPIMIVTEFMENGALDAFLKEREdQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQN 760
Cdd:cd14181    74 GHPSIITLIDSYESSTFIFLVFDLMRRGELFDYLTEKV-TLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQ 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 761 LCCKVSDFGLTRLLDDFDGTYETQGGKipiRWTAPEAI------AHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQE 834
Cdd:cd14181   153 LHIKLSDFGFSCHLEPGEKLRELCGTP---GYLAPEILkcsmdeTHPGYGKEVDLWACGVILFTLLA-GSPPFWHRRQML 228
                         250
                  ....*....|....*
gi 2038291632 835 VMKSIEEG-YRLPPP 848
Cdd:cd14181   229 MLRMIMEGrYQFSSP 243
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
630-848 2.66e-13

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: 71.18  E-value: 2.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVyRGALRFPSQDCKTVAIKTLK---DTSPDGQWWN-FLREATIMGQFNHPHILR-LEGVVTKRKPIMIVTEF 704
Cdd:cd13994     1 IGKGATSVV-RIVTKKNPRSGVLYAVKEYRrrdDESKRKDYVKrLTSEYIISSKLHHPNIVKvLDLCQDLHGKWCLVMEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 705 MENGALDAFLKEReDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLT-RLLDDFDGTYET 783
Cdd:cd13994    80 CPGGDLFTLIEKA-DSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTAeVFGMPAEKESPM 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 784 QGGKI-PIRWTAPEAiahriFT------TASDVWSFGIVM---------WEVLSFGDKPYgemnnQEVMKSIEEGYRLPP 847
Cdd:cd13994   159 SAGLCgSEPYMAPEV-----FTsgsydgRAVDVWSCGIVLfalftgrfpWRSAKKSDSAY-----KAYEKSGDFTNGPYE 228

                  .
gi 2038291632 848 P 848
Cdd:cd13994   229 P 229
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
628-875 3.48e-13

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: 71.15  E-value: 3.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 628 TVIGEGEFGEVYRGALRFPSQDCK-------TVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKrkPIMI 700
Cdd:cd14067     8 TVIYRARYQGQPVAVKRFHIKKCKkrtdgsaDTMLKHLRAADAMKNFSEFRQEASMLHSLQHPCIVYLIGISIH--PLCF 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 701 VTEFMENGALDAFLKE--REDQLAP-GQLVAMLLG--IASGMNYLSGHNYVHRDLAARNILV-----NQNLCCKVSDFGL 770
Cdd:cd14067    86 ALELAPLGSLNTVLEEnhKGSSFMPlGHMLTFKIAyqIAAGLAYLHKKNIIFCDLKSDNILVwsldvQEHINIKLSDYGI 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 771 TRllDDF-DGTYETQGGKipiRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSIEEGYRlpPPV 849
Cdd:cd14067   166 SR--QSFhEGALGVEGTP---GYQAPEIRPRIVYDEKVDMFSYGMVLYELLS-GQRPSLGHHQLQIAKKLSKGIR--PVL 237
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2038291632 850 DCPAP-----LYELMKNCWAYDRARRPHFLQ 875
Cdd:cd14067   238 GQPEEvqffrLQALMMECWDTKPEKRPLACS 268
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
630-879 3.60e-13

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: 71.25  E-value: 3.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFPSqdcKTVAIKTLKDTSPDGQWWNFLREATIMGQ-FNHPHILRLEGVVTKRKPIMIVTEFMENg 708
Cdd:cd06618    23 IGSGTCGQVYKMRHKKTG---HVMAVKQMRRSGNKEENKRILMDLDVVLKsHDCPYIVKCYGYFITDSDVFICMELMST- 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 ALDAFLKeREDQLAPGQLVA-MLLGIASGMNYL-SGHNYVHRDLAARNILVNQNLCCKVSDFGLT-RLLDDFDGTyeTQG 785
Cdd:cd06618    99 CLDKLLK-RIQGPIPEDILGkMTVSIVKALHYLkEKHGVIHRDVKPSNILLDESGNVKLCDFGISgRLVDSKAKT--RSA 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 786 GKIPirWTAPEAI---AHRIFTTASDVWSFGIVMWEvLSFGDKPYGEMNNQ-EVMKSI--EEGYRLPPPVDCPAPLYELM 859
Cdd:cd06618   176 GCAA--YMAPERIdppDNPKYDIRADVWSLGISLVE-LATGQFPYRNCKTEfEVLTKIlnEEPPSLPPNEGFSPDFCSFV 252
                         250       260
                  ....*....|....*....|
gi 2038291632 860 KNCWAYDRARRPHFLQLQAH 879
Cdd:cd06618   253 DLCLTKDHRYRPKYRELLQH 272
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
629-819 3.69e-13

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: 71.18  E-value: 3.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRfpsQDCKTVAIKTLKDTSPDGQW-WNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMEN 707
Cdd:cd07848     8 VVGEGAYGVVLKCRHK---ETKEIVAIKKFKDSEENEEVkETTLRELKMLRTLKQENIVELKEAFRRRGKLYLVFEYVEK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GALDaFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDdfDGTYETQGGK 787
Cdd:cd07848    85 NMLE-LLEEMPNGVPPEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNLS--EGSNANYTEY 161
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2038291632 788 IPIRW-TAPEAIAHRIFTTASDVWSFGIVMWEV 819
Cdd:cd07848   162 VATRWyRSPELLLGAPYGKAVDMWSVGCILGEL 194
SAM_EPH-B6 cd09555
SAM domain of EPH-B6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
902-972 3.78e-13

SAM domain of EPH-B6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B6 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B6 receptors and appears to mediate cell-cell initiated signal transduction. Receptors of this type are highly expressed in embryo and adult nervous system, in thymus and also in T-cells. They are involved in regulation of cell adhesion and migration. (EPH-B6 receptor is unusual; it fails to show catalytic activity due to alteration in kinase domain). EPH-B6 may be considered as a biomarker in some types of tumors; EPH-B6 activates MAP kinase signaling in lung adenocarcinoma, suppresses metastasis formation in non-small cell lung cancer, and slows invasiveness in some breast cancer cell lines.


Pssm-ID: 188954  Cd Length: 69  Bit Score: 65.34  E-value: 3.78e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2038291632 902 LRLPSLSgsdgipyrSVSEWLESIRMKRYILHFRSAGLDTMECVLELTAEDLTQMGITLPGHQKRILCSIQ 972
Cdd:cd09555     1 LDFPCLD--------SPQAWLSAIGLECYQDNFSKFGLCTFSDVAQLSLEDLPALGITLAGHQKKLLHHIQ 63
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
607-849 4.26e-13

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: 70.84  E-value: 4.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 607 DPAQGALDFAQeldptwlivdtvIGEGEFGEVyrgALRFPSQDCKTVAIKTLkDTSPDGQWWNFLREATIMGQFNHPHIL 686
Cdd:cd06658    19 DPREYLDSFIK------------IGEGSTGIV---CIATEKHTGKQVAVKKM-DLRKQQRRELLFNEVVIMRDYHHENVV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 687 RLEGVVTKRKPIMIVTEFMENGALDAFLKEreDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVS 766
Cdd:cd06658    83 DMYNSYLVGDELWVVMEFLEGGALTDIVTH--TRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 767 DFGLTRLLDDfdgtyetqggKIPIR--------WTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKS 838
Cdd:cd06658   161 DFGFCAQVSK----------EVPKRkslvgtpyWMAPEVISRLPYGTEVDIWSLGIMVIEMID-GEPPYFNEPPLQAMRR 229
                         250
                  ....*....|.
gi 2038291632 839 IEEGyrLPPPV 849
Cdd:cd06658   230 IRDN--LPPRV 238
SAM_EPH-A6 cd09547
SAM domain of EPH-A6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
917-975 4.65e-13

SAM domain of EPH-A6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A6 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A6 receptors and appears to mediate cell-cell initiated signal transduction. Eph-A6 gene is preferentially expressed in the nervous system. EPH-A6 receptors are involved in primate retina vascular and axon guidance, and in neural circuits responsible for learning and memory. EphA6 gene was significantly down regulated in colorectal cancer and in malignant melanomas. It is a potential molecular marker for these cancers.


Pssm-ID: 188946  Cd Length: 64  Bit Score: 64.91  E-value: 4.65e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2038291632 917 SVSEWLESIRMKRYILHFRSAGLDTMECVLELTAEDLTQMGITLPGHQKRILCSIQGFK 975
Cdd:cd09547     5 TVSDWLDSIKMGQYKNNFMAAGFTTLDMVSRMTIDDIRRIGVTLIGHQRRIVSSIQTLR 63
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
672-839 4.84e-13

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: 70.42  E-value: 4.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 672 REATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGALDAFLKEREdQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLA 751
Cdd:cd14195    57 REVNILREIQHPNIITLHDIFENKTDVVLILELVSGGELFDFLAEKE-SLTEEEATQFLKQILDGVHYLHSKRIAHFDLK 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 752 ARNI-LVNQNLC---CKVSDFGLTRLL---DDFDGTYETQggkipiRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGD 824
Cdd:cd14195   136 PENImLLDKNVPnprIKLIDFGIAHKIeagNEFKNIFGTP------EFVAPEIVNYEPLGLEADMWSIGVITYILLS-GA 208
                         170
                  ....*....|....*
gi 2038291632 825 KPYGEMNNQEVMKSI 839
Cdd:cd14195   209 SPFLGETKQETLTNI 223
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
623-879 4.95e-13

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: 70.52  E-value: 4.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 623 WLIVDTVIGEGEFGEVYRGalrFPSQDCKTVAIKTLKDTS-PDGQWWNFLREATIMGQFNHPHILRL----EGVVTKRKP 697
Cdd:cd14031    11 FLKFDIELGRGAFKTVYKG---LDTETWVEVAWCELQDRKlTKAEQQRFKEEAEMLKGLQHPNIVRFydswESVLKGKKC 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 698 IMIVTEFMENGALDAFLKeREDQLAPGQLVAMLLGIASGMNYLSGHN--YVHRDLAARNILVN-QNLCCKVSDFGLTRLL 774
Cdd:cd14031    88 IVLVTELMTSGTLKTYLK-RFKVMKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLATLM 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 775 ddfdgtyETQGGKIPI---RWTAPEAIAHRiFTTASDVWSFGIVMWEvLSFGDKPYGEMNN-QEVMKSIEEGYRLPPPVD 850
Cdd:cd14031   167 -------RTSFAKSVIgtpEFMAPEMYEEH-YDESVDVYAFGMCMLE-MATSEYPYSECQNaAQIYRKVTSGIKPASFNK 237
                         250       260       270
                  ....*....|....*....|....*....|
gi 2038291632 851 CPAP-LYELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd14031   238 VTDPeVKEIIEGCIRQNKSERLSIKDLLNH 267
SAM_EPH-B2 cd09552
SAM domain of EPH-B2 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
915-972 5.38e-13

SAM domain of EPH-B2 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B2 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B2 receptors and appears to mediate cell-cell initiated signal transduction. SAM domains of this subfamily form homodimers/oligomers (in head-to-head/tail-to-tail orientation); apparently such clustering is necessary for signaling. EPH-B2 receptor is involved in regulation of synaptic function; it is needed for normal vestibular function, proper formation of anterior commissure, control of cell positioning, and ordered migration in the intestinal epithelium. EPH-B2 plays a tumor suppressor role in colorectal cancer. It was found to be downregulated in gastric cancer and thus may be a negative biomarker for it.


Pssm-ID: 188951  Cd Length: 71  Bit Score: 65.03  E-value: 5.38e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2038291632 915 YRSVSEWLESIRMKRYILHFRSAGLDTMECVLELTAEDLTQMGITLPGHQKRILCSIQ 972
Cdd:cd09552     6 FSTVDEWLDAIKMGQYKESFANAGFTSFDVVSQMTMEDILRVGVTLAGHQKKILNSIQ 63
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
681-841 6.99e-13

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: 69.95  E-value: 6.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 681 NHPHILRLEGVVTKRKPIMIVTEFMENGAL-DAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNIL--- 756
Cdd:cd14198    66 SNPRVVNLHEVYETTSEIILILEYAAGGEIfNLCVPDLAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILlss 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 757 VNQNLCCKVSDFGLTRLLDDFDGTYETQGGKipiRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVM 836
Cdd:cd14198   146 IYPLGDIKIVDFGMSRKIGHACELREIMGTP---EYLAPEILNYDPITTATDMWNIGVIAYMLLT-HESPFVGEDNQETF 221

                  ....*
gi 2038291632 837 KSIEE 841
Cdd:cd14198   222 LNISQ 226
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
629-896 7.36e-13

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: 70.02  E-value: 7.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRFPSQDCktvAIKTLKDtSPDGQwwnflREATIMGQFNH-PHILRL----EGVVTKRKPIMIVTE 703
Cdd:cd14172    11 VLGLGVNGKVLECFHRRTGQKC---ALKLLYD-SPKAR-----REVEHHWRASGgPHIVHIldvyENMHHGKRCLLIIME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 704 FMENGALDAFLKEREDQ-LAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILV---NQNLCCKVSDFGLTRllddfdG 779
Cdd:cd14172    82 CMEGGELFSRIQERGDQaFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYtskEKDAVLKLTDFGFAK------E 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 780 TYETQGGKIPIR---WTAPEAIAHRIFTTASDVWSFGIVMWeVLSFGDKPYGEMNNQEVMKSIEEGYRLPPpvdcpaplY 856
Cdd:cd14172   156 TTVQNALQTPCYtpyYVAPEVLGPEKYDKSCDMWSLGVIMY-ILLCGFPPFYSNTGQAISPGMKRRIRMGQ--------Y 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2038291632 857 ELMKNCWA--YDRARrphflQLQAHLeqLLTDPHSLRTIANF 896
Cdd:cd14172   227 GFPNPEWAevSEEAK-----QLIRHL--LKTDPTERMTITQF 261
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
626-821 7.87e-13

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: 70.97  E-value: 7.87e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 626 VDTVIGEGEFGEVYRGALRFPSQdckTVAIKTLKDT---SPDGQwwNFLREATIMGQFNHPHILRLEGVV---TKR--KP 697
Cdd:cd07859     4 IQEVIGKGSYGVVCSAIDTHTGE---KVAIKKINDVfehVSDAT--RILREIKLLRLLRHPDIVEIKHIMlppSRRefKD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 698 IMIVTEFMENGaLDAFLKEREDqLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDF 777
Cdd:cd07859    79 IYVVFELMESD-LHQVIKANDD-LTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGLARVAFND 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2038291632 778 DGTYETQGGKIPIRW-TAPEAIAHRI--FTTASDVWSFGIVMWEVLS 821
Cdd:cd07859   157 TPTAIFWTDYVATRWyRAPELCGSFFskYTPAIDIWSIGCIFAEVLT 203
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
917-972 8.83e-13

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 63.80  E-value: 8.83e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2038291632 917 SVSEWLESIRMKRYILHFRSAGLDtMECVLELTAEDLTQMGITLPGHQKRILCSIQ 972
Cdd:cd09487     1 DVAEWLESLGLEQYADLFRKNEID-GDALLLLTDEDLKELGITSPGHRKKILRAIQ 55
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
630-870 9.60e-13

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: 69.77  E-value: 9.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFPSQDC--KTVAIKTLKDTSpdgQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMEN 707
Cdd:cd05612     9 IGTGTFGRVHLVRDRISEHYYalKVMAIPEVIRLK---QEQHVHNEKRVLKEVSHPFIIRLFWTEHDQRFLYMLMEYVPG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GALDAFLKEREdQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDD----FDGTYEt 783
Cdd:cd05612    86 GELFSYLRNSG-RFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAKKLRDrtwtLCGTPE- 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 784 qggkipirWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSIEEG-YRLPPPVDCPAPlyELMKNC 862
Cdd:cd05612   164 --------YLAPEVIQSKGHNKAVDWWALGILIYEMLV-GYPPFFDDNPFGIYEKILAGkLEFPRHLDLYAK--DLIKKL 232

                  ....*...
gi 2038291632 863 WAYDRARR 870
Cdd:cd05612   233 LVVDRTRR 240
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
630-879 1.04e-12

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: 69.76  E-value: 1.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRgaLRFPSQDcKTVAIKTLKDTSPDGQWWNFLREATI-MGQFNHPHILRLEGVVTKRKPIMIVTEFMENg 708
Cdd:cd06617     9 LGRGAYGVVDK--MRHVPTG-TIMAVKRIRATVNSQEQKRLLMDLDIsMRSVDCPYTVTFYGALFREGDVWICMEVMDT- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 ALDAFLKE--REDQLAPGQLVA-MLLGIASGMNYL-SGHNYVHRDLAARNILVNQNLCCKVSDFGLT-RLLDDFDGTyeT 783
Cdd:cd06617    85 SLDKFYKKvyDKGLTIPEDILGkIAVSIVKALEYLhSKLSVIHRDVKPSNVLINRNGQVKLCDFGISgYLVDSVAKT--I 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 784 QGGKIPirWTAPEAI----AHRIFTTASDVWSFGIVMWEvLSFGDKPYGEMNNQ-EVMKSIEEGyrlPPPvDCPAPLYEL 858
Cdd:cd06617   163 DAGCKP--YMAPERInpelNQKGYDVKSDVWSLGITMIE-LATGRFPYDSWKTPfQQLKQVVEE---PSP-QLPAEKFSP 235
                         250       260
                  ....*....|....*....|....*.
gi 2038291632 859 -----MKNCWAYDRARRPHFLQLQAH 879
Cdd:cd06617   236 efqdfVNKCLKKNYKERPNYPELLQH 261
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
614-841 1.07e-12

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: 69.50  E-value: 1.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 614 DFAQELdptwlivdtviGEGEFGEVYRGALRFPSqdcKTVAIKTLKDTSPDGQWWNflREATIMGQFNHPHILRLEGVVT 693
Cdd:cd14104     3 MIAEEL-----------GRGQFGIVHRCVETSSK---KTYMAKFVKVKGADQVLVK--KEISILNIARHRNILRLHESFE 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 694 KRKPIMIVTEFMENGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILvnqnlCC-------KVS 766
Cdd:cd14104    67 SHEELVMIFEFISGVDIFERITTARFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENII-----YCtrrgsyiKII 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 767 DFGLTRLLddfdgtyeTQGGKIPIRWTAPEAIA-----HRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSIEE 841
Cdd:cd14104   142 EFGQSRQL--------KPGDKFRLQYTSAEFYApevhqHESVSTATDMWSLGCLVYVLLS-GINPFEAETNQQTIENIRN 212
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
630-878 1.17e-12

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: 69.45  E-value: 1.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRgaLRFPSQDCKTVAIKTLKDTSP---------DGQWWNFLREATIMG-QFNHPHILRLEGVVTKRKPIM 699
Cdd:cd08528     8 LGSGAFGCVYK--VRKKSNGQTLLALKEINMTNPafgrteqerDKSVGDIISEVNIIKeQLRHPNIVRYYKTFLENDRLY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 700 IVTEFMENGAL-DAF--LKEREDQLAPGQLVAMLLGIASGMNYLSGHN-YVHRDLAARNILVNQNLCCKVSDFGLTRLLD 775
Cdd:cd08528    86 IVMELIEGAPLgEHFssLKEKNEHFTEDRIWNIFVQMVLALRYLHKEKqIVHRDLKPNNIMLGEDDKVTITDFGLAKQKG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 776 DFDGTYETQGGKipIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPL 855
Cdd:cd08528   166 PESSKMTSVVGT--ILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPFYSTNMLTLATKIVEAEYEPLPEGMYSDDI 243
                         250       260
                  ....*....|....*....|...
gi 2038291632 856 YELMKNCWAYDRARRPHFLQLQA 878
Cdd:cd08528   244 TFVIRSCLTPDPEARPDIVEVSS 266
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
630-840 1.31e-12

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: 69.15  E-value: 1.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFPSQDCKTVAIKTLKDTSPDgqwwNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGA 709
Cdd:cd14114    10 LGTGAFGVVHRCTERATGNNFAAKFIMTPHESDKE----TVRKEIQIMNQLHHPKLINLHDAFEDDNEMVLILEFLSGGE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 710 LDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNIL--VNQNLCCKVSDFGLTRLLDDFDGTYETQGGK 787
Cdd:cd14114    86 LFERIAAEHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMctTKRSNEVKLIDFGLATHLDPKESVKVTTGTA 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2038291632 788 ipiRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSIE 840
Cdd:cd14114   166 ---EFAAPEIVEREPVGFYTDMWAVGVLSYVLLS-GLSPFAGENDDETLRNVK 214
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
630-879 1.33e-12

Catalytic domain of testis-specific serine/threonine kinase 3 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. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. Its mRNA levels is low at birth, increases at puberty, and remains high throughout adulthood. The TSSK3-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: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 68.86  E-value: 1.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGalrFPSQDCKTVAIKTL-KDTSPDGQWWNFL-REATIMGQFNHPHILRL-EGVVTKRKPIMIVTEFME 706
Cdd:cd14163     8 IGEGTYSKVKEA---FSKKHQRKVAIKIIdKSGGPEEFIQRFLpRELQIVERLDHKNIIHVyEMLESADGKIYLVMELAE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 707 NG-ALDAFLKEreDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVnQNLCCKVSDFGLTRLLDDfDGTYETQG 785
Cdd:cd14163    85 DGdVFDCVLHG--GPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALL-QGFTLKLTDFGFAKQLPK-GGRELSQT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 786 GKIPIRWTAPE---AIAHRifTTASDVWSFGIVMWeVLSFGDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLYELMKNC 862
Cdd:cd14163   161 FCGSTAYAAPEvlqGVPHD--SRKGDIWSMGVVLY-VMLCAQLPFDDTDIPKMLCQQQKGVSLPGHLGVSRTCQDLLKRL 237
                         250
                  ....*....|....*..
gi 2038291632 863 WAYDRARRPHFLQLQAH 879
Cdd:cd14163   238 LEPDMVLRPSIEEVSWH 254
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
630-821 1.40e-12

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: 69.64  E-value: 1.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFPSQdckTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFmenga 709
Cdd:cd07872    14 LGEGTYATVFKGRSKLTEN---LVALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIVHTDKSLTLVFEY----- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 710 LDAFLKEREDQLapGQLVAM------LLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYET 783
Cdd:cd07872    86 LDKDLKQYMDDC--GNIMSMhnvkifLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKSVPTKTYSN 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2038291632 784 QggkIPIRWTAPEAI--AHRIFTTASDVWSFGIVMWEVLS 821
Cdd:cd07872   164 E---VVTLWYRPPDVllGSSEYSTQIDMWGVGCIFFEMAS 200
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
625-842 1.63e-12

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: 69.29  E-value: 1.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 625 IVDTVIGEGEFGEVYRGALRFPSQDcktVAIKTLKDTSPDGQwwnflREATIMGQF-NHPHILRLEGVVTKRKPIMIVTE 703
Cdd:cd14175     4 VVKETIGVGSYSVCKRCVHKATNME---YAVKVIDKSKRDPS-----EEIEILLRYgQHPNIITLKDVYDDGKHVYLVTE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 704 FMENGAL------DAFLKEREDQlapgqlvAMLLGIASGMNYLSGHNYVHRDLAARNIL-VNQN---LCCKVSDFGLTRL 773
Cdd:cd14175    76 LMRGGELldkilrQKFFSEREAS-------SVLHTICKTVEYLHSQGVVHRDLKPSNILyVDESgnpESLRICDFGFAKQ 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2038291632 774 LDDFDGTYETQGgkIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYG---EMNNQEVMKSIEEG 842
Cdd:cd14175   149 LRAENGLLMTPC--YTANFVAPEVLKRQGYDEGCDIWSLGILLYTMLA-GYTPFAngpSDTPEEILTRIGSG 217
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
630-871 1.69e-12

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: 68.68  E-value: 1.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGevyRGALRFPSQDCKTVAIKTLKDT--SPDGQWwNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMEN 707
Cdd:cd08218     8 IGEGSFG---KALLVKSKEDGKQYVIKEINISkmSPKERE-ESRKEVAVLSKMKHPNIVQYQESFEENGNLYIVMDYCDG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GALDAFLKEREDQLAP-GQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDfdgTYETQGG 786
Cdd:cd08218    84 GDLYKRINAQRGVLFPeDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARVLNS---TVELART 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 787 KIPI-RWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDK-PYGEMNNQeVMKSIEEGYrlPP-PVDCPAPLYELMKNCW 863
Cdd:cd08218   161 CIGTpYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAfEAGNMKNL-VLKIIRGSY--PPvPSRYSYDLRSLVSQLF 237

                  ....*...
gi 2038291632 864 AYDRARRP 871
Cdd:cd08218   238 KRNPRDRP 245
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
630-889 1.78e-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: 69.37  E-value: 1.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFPSQDcktVAIKTLK-DTSPDGQWwnFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENG 708
Cdd:cd06656    27 IGQGASGTVYTAIDIATGQE---VAIKQMNlQQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGG 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 ALDAFLKEreDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYETQGGKi 788
Cdd:cd06656   102 SLTDVVTE--TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGT- 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 789 PIrWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSIEEG--YRLPPPVDCPAPLYELMKNCWAYD 866
Cdd:cd06656   179 PY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPYLNENPLRALYLIATNgtPELQNPERLSAVFRDFLNRCLEMD 256
                         250       260
                  ....*....|....*....|...
gi 2038291632 867 RARRPHFLQLQAHLEQLLTDPHS 889
Cdd:cd06656   257 VDRRGSAKELLQHPFLKLAKPLS 279
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
625-832 1.80e-12

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: 68.45  E-value: 1.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 625 IVDTVIGEGEFGEVYRGalrfpsQDCKT---VAIKTLKDtSPDgqwwnFLR----EATIM------GQFNHPHILRLEGV 691
Cdd:cd14133     2 EVLEVLGKGTFGQVVKC------YDLLTgeeVALKIIKN-NKD-----YLDqsldEIRLLellnkkDKADKYHIVRLKDV 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 692 VTKRKPIMIVTEFMENGALDaFLKE-REDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCC--KVSDF 768
Cdd:cd14133    70 FYFKNHLCIVFELLSQNLYE-FLKQnKFQYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSRCqiKIIDF 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 769 GLTRLLDDFDGTYetqggkIPIR-WTAPEAIAHRIFTTASDVWSFGIVMWE-----VLSFGDKPYGEMNN 832
Cdd:cd14133   149 GSSCFLTQRLYSY------IQSRyYRAPEVILGLPYDEKIDMWSLGCILAElytgePLFPGASEVDQLAR 212
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
630-827 1.81e-12

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: 69.18  E-value: 1.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRgalrFPSQDC-KTVAIKT--LKDTSPDGQWWNflREATIMGQFNHPHILRLEGVVTKRKPI-----MIV 701
Cdd:cd14039     1 LGTGGFGNVCL----YQNQETgEKIAIKScrLELSVKNKDRWC--HEIQIMKKLNHPNVVKACDVPEEMNFLvndvpLLA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 702 TEFMENGALDAFLKERED--QLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNIL---VNQNLCCKVSDFGLTRLLD- 775
Cdd:cd14039    75 MEYCSGGDLRKLLNKPENccGLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVlqeINGKIVHKIIDLGYAKDLDq 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2038291632 776 -----DFDGTyetqggkipIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPY 827
Cdd:cd14039   155 gslctSFVGT---------LQYLAPELFENKSYTVTVDYWSFGTMVFECIA-GFRPF 201
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
630-821 1.84e-12

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: 68.88  E-value: 1.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFPSQdckTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFmenga 709
Cdd:cd07871    13 LGEGTYATVFKGRSKLTEN---LVALKEIRLEHEEGAPCTAIREVSLLKNLKHANIVTLHDIIHTERCLTLVFEY----- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 710 LDAFLKEREDQLapGQLVAM------LLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYET 783
Cdd:cd07871    85 LDSDLKQYLDNC--GNLMSMhnvkifMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLARAKSVPTKTYSN 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2038291632 784 QggkIPIRWTAPEAI--AHRIFTTASDVWSFGIVMWEVLS 821
Cdd:cd07871   163 E---VVTLWYRPPDVllGSTEYSTPIDMWGVGCILYEMAT 199
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
630-847 1.85e-12

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: 68.56  E-value: 1.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFPSQdckTVAIK-----TLKDTSPDGQwwnflREATIMGQFNHPHILRLEGVVTKRKPIMIVTEF 704
Cdd:cd14078    11 IGSGGFAKVKLATHILTGE---KVAIKimdkkALGDDLPRVK-----TEIEALKNLSHQHICRLYHVIETDNKIFMVLEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 705 MENGALDAFLKEReDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGL-TRLLDDFDGTYET 783
Cdd:cd14078    83 CPGGELFDYIVAK-DRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLcAKPKGGMDHHLET 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2038291632 784 QGGKiPIrWTAPEAIAHRIFTTA-SDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSIEEG-YRLPP 847
Cdd:cd14078   162 CCGS-PA-YAAPELIQGKPYIGSeADVWSMGVLLYALLC-GFLPFDDDNVMALYRKIQSGkYEEPE 224
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
683-841 2.06e-12

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: 68.42  E-value: 2.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 683 PHILRLEGVVTKRKPIMIVTEFMENGAL-DAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNL 761
Cdd:cd14197    69 PWVINLHEVYETASEMILVLEYAAGGEIfNQCVADREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSES 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 762 C---CKVSDFGLTRLLDDFDGTYETQGGKipiRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKS 838
Cdd:cd14197   149 PlgdIKIVDFGLSRILKNSEELREIMGTP---EYVAPEILSYEPISTATDMWSIGVLAYVMLT-GISPFLGDDKQETFLN 224

                  ...
gi 2038291632 839 IEE 841
Cdd:cd14197   225 ISQ 227
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
659-822 2.09e-12

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 69.90  E-value: 2.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 659 KDTSPD------GQWWNFLREATIMGQFNHPHILRLEGVVTkRKPI--MIVTEFmeNGALDAFLKEREDQLAPGQLVAML 730
Cdd:PHA03209   87 KPGQPDpvvlkiGQKGTTLIEAMLLQNVNHPSVIRMKDTLV-SGAItcMVLPHY--SSDLYTYLTKRSRPLPIDQALIIE 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 731 LGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRL----LDDFD--GTYETQggkipirwtAPEAIAHRIFT 804
Cdd:PHA03209  164 KQILEGLRYLHAQRIIHRDVKTENIFINDVDQVCIGDLGAAQFpvvaPAFLGlaGTVETN---------APEVLARDKYN 234
                         170
                  ....*....|....*...
gi 2038291632 805 TASDVWSFGIVMWEVLSF 822
Cdd:PHA03209  235 SKADIWSAGIVLFEMLAY 252
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
623-879 2.16e-12

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: 68.49  E-value: 2.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 623 WLIVDTVIGEGEFGEVYRGALRFPSQDCKTVAIKTLKDTSPDGQwwNFLREATIMGQFNHPHILRL----EGVVTKRKPI 698
Cdd:cd14033     2 FLKFNIEIGRGSFKTVYRGLDTETTVEVAWCELQTRKLSKGERQ--RFSEEVEMLKGLQHPNIVRFydswKSTVRGHKCI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 699 MIVTEFMENGALDAFLKeREDQLAPGQLVAMLLGIASGMNYLSGHN--YVHRDLAARNILVN-QNLCCKVSDFGLTRL-- 773
Cdd:cd14033    80 ILVTELMTSGTLKTYLK-RFREMKLKLLQRWSRQILKGLHFLHSRCppILHRDLKCDNIFITgPTGSVKIGDLGLATLkr 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 774 ---LDDFDGTYEtqggkipirWTAPEAIAHRiFTTASDVWSFGIVMWEvLSFGDKPYGEMNN-QEVMKSIEEGYRLPPPV 849
Cdd:cd14033   159 asfAKSVIGTPE---------FMAPEMYEEK-YDEAVDVYAFGMCILE-MATSEYPYSECQNaAQIYRKVTSGIKPDSFY 227
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2038291632 850 DCPAP-LYELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd14033   228 KVKVPeLKEIIEGCIRTDKDERFTIQDLLEH 258
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
618-820 2.22e-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: 69.32  E-value: 2.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 618 ELDPTWLIVDTvIGEGEFGEVYRgALRFPSQdcKTVAIK----------TLKDTspdgqwwnfLREATIMGQFNHPH--- 684
Cdd:cd07855     2 DVGDRYEPIET-IGSGAYGVVCS-AIDTKSG--QKVAIKkipnafdvvtTAKRT---------LRELKILRHFKHDNiia 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 685 ---ILRLEGVVTKRKPIMIVTEFMENgalDAFLKEREDQLAPGQLVAMLLG-IASGMNYLSGHNYVHRDLAARNILVNQN 760
Cdd:cd07855    69 irdILRPKVPYADFKDVYVVLDLMES---DLHHIIHSDQPLTLEHIRYFLYqLLRGLKYIHSANVIHRDLKPSNLLVNEN 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2038291632 761 LCCKVSDFGLTRLLDDFD---GTYETQggKIPIRW-TAPEAI--AHRiFTTASDVWSFGIVMWEVL 820
Cdd:cd07855   146 CELKIGDFGMARGLCTSPeehKYFMTE--YVATRWyRAPELMlsLPE-YTQAIDMWSVGCIFAEML 208
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
671-854 3.95e-12

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: 68.54  E-value: 3.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 671 LREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGALDAFLKEredqlaPGQLVAMLLGIAS-----GMNYL-SGHN 744
Cdd:cd06650    51 IRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQVLKK------AGRIPEQILGKVSiavikGLTYLrEKHK 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 745 YVHRDLAARNILVNQNLCCKVSDFGLT-RLLDDFDGTYetqggkIPIR-WTAPEAIAHRIFTTASDVWSFGIVMWEvLSF 822
Cdd:cd06650   125 IMHRDVKPSNILVNSRGEIKLCDFGVSgQLIDSMANSF------VGTRsYMSPERLQGTHYSVQSDIWSMGLSLVE-MAV 197
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2038291632 823 GDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAP 854
Cdd:cd06650   198 GRYPIPPPDAKELELMFGCQVEGDAAETPPRP 229
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
630-849 5.43e-12

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: 67.29  E-value: 5.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYrgaLRFPSQDCKTVAIKTL--KDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMEN 707
Cdd:cd14116    13 LGKGKFGNVY---LAREKQSKFILALKVLfkAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GALDAFLkEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGL-----TRLLDDFDGTYE 782
Cdd:cd14116    90 GTVYREL-QKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWsvhapSSRRTTLCGTLD 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038291632 783 tqggkipirWTAPEAIAHRIFTTASDVWSFGIVMWEVLsFGDKPYGEMNNQEVMKSIEE-GYRLPPPV 849
Cdd:cd14116   169 ---------YLPPEMIEGRMHDEKVDLWSLGVLCYEFL-VGKPPFEANTYQETYKRISRvEFTFPDFV 226
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
672-876 5.58e-12

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: 67.73  E-value: 5.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 672 REATIMGQFNHPHILR-LEGVVTKRKPIMIVTEFMEnGALDAFLKERED------QLAPGQL-----VAMLLGIASGMNY 739
Cdd:cd14011    51 RGVKQLTRLRHPRILTvQHPLEESRESLAFATEPVF-ASLANVLGERDNmpspppELQDYKLydveiKYGLLQISEALSF 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 740 LsgHN---YVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYETQGGKIPIR---------WTAPEAIAHRIFTTAS 807
Cdd:cd14011   130 L--HNdvkLVHGNICPESVVINSNGEWKLAGFDFCISSEQATDQFPYFREYDPNLpplaqpnlnYLAPEYILSKTCDPAS 207
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2038291632 808 DVWSFGIVMWEVLSFGDKPYGEMNNQ---EVMKSIEEGYRLPPPVDCPAPLYELMKNCWAYDRARRPHFLQL 876
Cdd:cd14011   208 DMFSLGVLIYAIYNKGKPLFDCVNNLlsyKKNSNQLRQLSLSLLEKVPEELRDHVKTLLNVTPEVRPDAEQL 279
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
630-847 6.38e-12

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: 67.36  E-value: 6.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRfpsQDCKTVAIKTLkDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGA 709
Cdd:cd06657    28 IGEGSTGIVCIATVK---SSGKLVAVKKM-DLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGA 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 710 LDAFLKEreDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDfdgtyETQGGKIP 789
Cdd:cd06657   104 LTDIVTH--TRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSK-----EVPRRKSL 176
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2038291632 790 I---RWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSIEEgyRLPP 847
Cdd:cd06657   177 VgtpYWMAPELISRLPYGPEVDIWSLGIMVIEMVD-GEPPYFNEPPLKAMKMIRD--NLPP 234
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
628-834 6.65e-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: 66.99  E-value: 6.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 628 TVIGEGEFGEVYRGALRFPSQDcktVAIKTLK------DTSPDgqwwnFLRE-ATIMGQFNHPHILRLEGVVTKRKPIMI 700
Cdd:cd14106    14 TPLGRGKFAVVRKCIHKETGKE---YAAKFLRkrrrgqDCRNE-----ILHEiAVLELCKDCPRVVNLHEVYETRSELIL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 701 VTEFMENGALDAFLkEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCC---KVSDFGLTRLLDDF 777
Cdd:cd14106    86 ILELAAGGELQTLL-DEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEFPLgdiKLCDFGISRVIGEG 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2038291632 778 DGTYETQGgkiPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQE 834
Cdd:cd14106   165 EEIREILG---TPDYVAPEILSYEPISLATDMWSIGVLTYVLLT-GHSPFGGDDKQE 217
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
682-842 9.35e-12

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: 67.74  E-value: 9.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 682 HPHILRLEGVVTKRKPIMIVTEFMENGAL------DAFLKEREDQlapgqlvAMLLGIASGMNYLSGHNYVHRDLAARNI 755
Cdd:cd14176    72 HPNIITLKDVYDDGKYVYVVTELMKGGELldkilrQKFFSEREAS-------AVLFTITKTVEYLHAQGVVHRDLKPSNI 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 756 L-VNQN---LCCKVSDFGLTRLLDDFDGTYETQGgkIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYG--- 828
Cdd:cd14176   145 LyVDESgnpESIRICDFGFAKQLRAENGLLMTPC--YTANFVAPEVLERQGYDAACDIWSLGVLLYTMLT-GYTPFAngp 221
                         170
                  ....*....|....
gi 2038291632 829 EMNNQEVMKSIEEG 842
Cdd:cd14176   222 DDTPEEILARIGSG 235
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
629-848 9.58e-12

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: 66.19  E-value: 9.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRFPSqdcKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENG 708
Cdd:cd14095     7 VIGDGNFAVVKECRDKATD---KEYALKIIDKAKCKGKEHMIENEVAILRRVKHPNIVQLIEEYDTDTELYLVMELVKGG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 AL-DAFLKERedQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQN----LCCKVSDFGL----TRLLDDFDG 779
Cdd:cd14095    84 DLfDAITSST--KFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHedgsKSLKLADFGLatevKEPLFTVCG 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2038291632 780 TyetqggkiPIrWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPY-GEMNNQEVM-KSIEEG-YRLPPP 848
Cdd:cd14095   162 T--------PT-YVAPEILAETGYGLKVDIWAAGVITYILLC-GFPPFrSPDRDQEELfDLILAGeFEFLSP 223
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
630-821 9.99e-12

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: 67.31  E-value: 9.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRgALRFPSQDCKTVAIKTLKDTSPDGQWWNF--LREATIMGQFNHPHILRLEGVV--TKRKPIMIVTEFM 705
Cdd:cd07842     8 IGRGTYGRVYK-AKRKNGKDGKEYAIKKFKGDKEQYTGISQsaCREIALLRELKHENVVSLVEVFleHADKSVYLLFDYA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 706 ENGALDAFLKERE---DQLAPGQLVAMLLGIASGMNYLsgH-NYV-HRDLAARNILV----NQNLCCKVSDFGLTRLLD- 775
Cdd:cd07842    87 EHDLWQIIKFHRQakrVSIPPSMVKSLLWQILNGIHYL--HsNWVlHRDLKPANILVmgegPERGVVKIGDLGLARLFNa 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2038291632 776 ------DFDGTYETqggkipIRWTAPEAI-AHRIFTTASDVWSFGIVMWEVLS 821
Cdd:cd07842   165 plkplaDLDPVVVT------IWYRAPELLlGARHYTKAIDIWAIGCIFAELLT 211
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
626-836 1.07e-11

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: 66.56  E-value: 1.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 626 VDTVIGEGEFGEVYRGALRfpSQDcKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFM 705
Cdd:cd14183    10 VGRTIGDGNFAVVKECVER--STG-REYALKIINKSKCRGKEHMIQNEVSILRRVKHPNIVLLIEEMDMPTELYLVMELV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 706 ENGAL-DAFLKEreDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNL----CCKVSDFGLTRLLDdfdGT 780
Cdd:cd14183    87 KGGDLfDAITST--NKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEHQdgskSLKLGDFGLATVVD---GP 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2038291632 781 YETQGGKiPIrWTAPEAIAHRIFTTASDVWSFGIVMWeVLSFGDKPY-GEMNNQEVM 836
Cdd:cd14183   162 LYTVCGT-PT-YVAPEIIAETGYGLKVDIWAAGVITY-ILLCGFPPFrGSGDDQEVL 215
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
629-853 1.07e-11

Catalytic domain of Yeast Protein Kinase 1-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 proteins with similarity to the AGC STKs, Saccharomyces cerevisiae YPK1 and Schizosaccharomyces pombe Gad8p. YPK1 is required for cell growth and acts as a downstream kinase in the sphingolipid-mediated signaling pathway of yeast. It also plays a role in efficient endocytosis and in the maintenance of cell wall integrity. Gad8p is a downstream target of Tor1p, the fission yeast homolog of mTOR. It plays a role in cell growth and sexual development. The YPK1-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: 270737 [Multi-domain]  Cd Length: 313  Bit Score: 67.21  E-value: 1.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRFPSqdcKTVAIKTLKDTS--PDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFME 706
Cdd:cd05585     1 VIGKGSFGKVMQVRKKDTS---RIYALKTIRKAHivSRSEVTHTLAERTVLAQVDCPFIVPLKFSFQSPEKLYLVLAFIN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 707 NGALDAFLKE--REDQLAPGQLVAMLLgiaSGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRL-------LDDF 777
Cdd:cd05585    78 GGELFHHLQRegRFDLSRARFYTAELL---CALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLCKLnmkdddkTNTF 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038291632 778 DGTYEtqggkipirWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSI-EEGYRLPPPVDCPA 853
Cdd:cd05585   155 CGTPE---------YLAPELLLGHGYTKAVDWWTLGVLLYEMLT-GLPPFYDENTNEMYRKIlQEPLRFPDGFDRDA 221
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
630-879 1.09e-11

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: 66.10  E-value: 1.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFPSQDcktVAIKTLK-DTSPDGQWwnFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENG 708
Cdd:cd06647    15 IGQGASGTVYTAIDVATGQE---VAIKQMNlQQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 ALDAFLKEreDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYETQGGKi 788
Cdd:cd06647    90 SLTDVVTE--TCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGT- 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 789 PIrWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSIEEGYR--LPPPVDCPAPLYELMKNCWAYD 866
Cdd:cd06647   167 PY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPYLNENPLRALYLIATNGTpeLQNPEKLSAIFRDFLNRCLEMD 244
                         250
                  ....*....|...
gi 2038291632 867 RARRPHFLQLQAH 879
Cdd:cd06647   245 VEKRGSAKELLQH 257
EphA2_TM pfam14575
Ephrin type-A receptor 2 transmembrane domain; Epha2_TM represents the left-handed dimer ...
548-621 1.09e-11

Ephrin type-A receptor 2 transmembrane domain; Epha2_TM represents the left-handed dimer transmembrane domain of of EphA2 receptor. This domain oligomerises and is important for the active signalling process.


Pssm-ID: 464211  Cd Length: 72  Bit Score: 61.08  E-value: 1.09e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038291632 548 IVAIIFGVLLGIALLIGIYVFRSRRGQRQRQQRqreraTNVDREDKL---WLKPYVDLQAYEDPAQGALDFAQELDP 621
Cdd:pfam14575   1 VVASVAGGLVLLLVVGVVLIRRRRCCGRKKSQD-----DDEEEFHQYkppGRKTYIDPHTYEDPNQAVLEFAKEIDA 72
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
630-879 1.11e-11

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: 66.67  E-value: 1.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFPSQDcktVAIKTLK-DTSPDGQWwnFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENG 708
Cdd:cd06654    28 IGQGASGTVYTAMDVATGQE---VAIRQMNlQQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGG 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 ALDAFLKEreDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYETQGGKi 788
Cdd:cd06654   103 SLTDVVTE--TCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGT- 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 789 PIrWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSIEEG--YRLPPPVDCPAPLYELMKNCWAYD 866
Cdd:cd06654   180 PY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMIE-GEPPYLNENPLRALYLIATNgtPELQNPEKLSAIFRDFLNRCLEMD 257
                         250
                  ....*....|...
gi 2038291632 867 RARRPHFLQLQAH 879
Cdd:cd06654   258 VEKRGSAKELLQH 270
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
615-823 1.21e-11

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: 66.44  E-value: 1.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 615 FAQELDPTwlivdTVIGEGEFGEVYRGalRFPSQDCkTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTK 694
Cdd:cd14048     4 FLTDFEPI-----QCLGRGGFGVVFEA--KNKVDDC-NYAVKRIRLPNNELAREKVLREVRALAKLDHPGIVRYFNAWLE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 695 RKP-----------IMIVTEFMENGALDAFL---KEREDQlAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQN 760
Cdd:cd14048    76 RPPegwqekmdevyLYIQMQLCRKENLKDWMnrrCTMESR-ELFVCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLD 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038291632 761 LCCKVSDFGLTRLLDDFD---------GTYETQGGKIPIR-WTAPEAIAHRIFTTASDVWSFGIVMWEVL-SFG 823
Cdd:cd14048   155 DVVKVGDFGLVTAMDQGEpeqtvltpmPAYAKHTGQVGTRlYMSPEQIHGNQYSEKVDIFALGLILFELIySFS 228
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
630-879 1.22e-11

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: 66.08  E-value: 1.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRgaLRFPsqDCKTVAIKTLKDTSPDGQWWN-FLREATIMGQFNH-PHILRLEG--VVTKRKPIMIVtefM 705
Cdd:cd14131     9 LGKGGSSKVYK--VLNP--KKKIYALKRVDLEGADEQTLQsYKNEIELLKKLKGsDRIIQLYDyeVTDEDDYLYMV---M 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 706 ENGALD--AFLKEREDQLAPGQLVA-----MLLGIasgmNYLSGHNYVHRDLAARN-ILVNQNLccKVSDFGLTRLLDDf 777
Cdd:cd14131    82 ECGEIDlaTILKKKRPKPIDPNFIRyywkqMLEAV----HTIHEEGIVHSDLKPANfLLVKGRL--KLIDFGIAKAIQN- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 778 DGTY---ETQGGKIpiRWTAPEAIAHRIFTT----------ASDVWSFGIVMWEVLsFGDKPYGEMNN--QEVMKSIEEG 842
Cdd:cd14131   155 DTTSivrDSQVGTL--NYMSPEAIKDTSASGegkpkskigrPSDVWSLGCILYQMV-YGKTPFQHITNpiAKLQAIIDPN 231
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2038291632 843 YRLPPPVDCPAPLYELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd14131   232 HEIEFPDIPNPDLIDVMKRCLQRDPKKRPSIPELLNH 268
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
628-820 1.31e-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: 1.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 628 TVIGEGEFGEVYRgalrfpSQDCKT---VAIKTL----------KDTspdgqwwnfLREATIMGQFNHPHILRLEGVVTK 694
Cdd:cd07851    21 SPVGSGAYGQVCS------AFDTKTgrkVAIKKLsrpfqsaihaKRT---------YRELRLLKHMKHENVIGLLDVFTP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 695 RKPIM------IVTEFMenGA-LDAFLKERedQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSD 767
Cdd:cd07851    86 ASSLEdfqdvyLVTHLM--GAdLNNIVKCQ--KLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILD 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2038291632 768 FGLTRLLDDFDGTYetqggkIPIRW-TAPEAIAHRI-FTTASDVWSFGIVMWEVL 820
Cdd:cd07851   162 FGLARHTDDEMTGY------VATRWyRAPEIMLNWMhYNQTVDIWSVGCIMAELL 210
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
630-839 1.36e-11

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: 66.75  E-value: 1.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFPSQdckTVAIKTLKDTS----PDGQwwnfLREATIMGQFNHPHILRL----EGVVTKRKpiMIV 701
Cdd:cd13988     1 LGQGATANVFRGRHKKTGD---LYAVKVFNNLSfmrpLDVQ----MREFEVLKKLNHKNIVKLfaieEELTTRHK--VLV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 702 TEFMENGALDAFLKEREDQ--LAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNIL--VNQNLCC--KVSDFGLTRLLD 775
Cdd:cd13988    72 MELCPCGSLYTVLEEPSNAygLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMrvIGEDGQSvyKLTDFGAARELE 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2038291632 776 DFD------GTYETQGGKIPIRWTAPEAIaHRIFTTASDVWSFGIVMWEV----LSFgdKPYGE-MNNQEVMKSI 839
Cdd:cd13988   152 DDEqfvslyGTEEYLHPDMYERAVLRKDH-QKKYGATVDLWSIGVTFYHAatgsLPF--RPFEGpRRNKEVMYKI 223
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
630-843 1.67e-11

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: 66.12  E-value: 1.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFPSQDCktvAIKTLKDTSPDGQwwnflREATIMGQF-NHPHILRLEGVVTKRKPIMIVTEFMENG 708
Cdd:cd14091     8 IGKGSYSVCKRCIHKATGKEY---AVKIIDKSKRDPS-----EEIEILLRYgQHPNIITLRDVYDDGNSVYLVTELLRGG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 AL------DAFLKEREDQlapgqlvAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLC----CKVSDFGLTRLLDDFD 778
Cdd:cd14091    80 ELldrilrQKFFSEREAS-------AVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGdpesLRICDFGFAKQLRAEN 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2038291632 779 GTYETqggkiPI---RWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNN---QEVMKSIEEGY 843
Cdd:cd14091   153 GLLMT-----PCytaNFVAPEVLKKQGYDAACDIWSLGVLLYTMLA-GYTPFASGPNdtpEVILARIGSGK 217
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
630-843 1.84e-11

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: 65.92  E-value: 1.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFPSQdcKTVAIKTLKDTSPDG------QWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTE 703
Cdd:cd14096     9 IGEGAFSNVYKAVPLRNTG--KPVAIKVVRKADLSSdnlkgsSRANILKEVQIMKRLSHPNIVKLLDFQESDEYYYIVLE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 704 FMENGALdaFlkeredqlapGQLVAM-----------LLGIASGMNYLSGHNYVHRDLAARNILV--------------- 757
Cdd:cd14096    87 LADGGEI--F----------HQIVRLtyfsedlsrhvITQVASAVKYLHEIGVVHRDIKPENLLFepipfipsivklrka 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 758 ---NQNL---------------CCKVSDFGLTRLLddFDGTYETQGGKipIRWTAPEAIAHRIFTTASDVWSFGIVMWEV 819
Cdd:cd14096   155 dddETKVdegefipgvggggigIVKLADFGLSKQV--WDSNTKTPCGT--VGYTAPEVVKDERYSKKVDMWALGCVLYTL 230
                         250       260
                  ....*....|....*....|....
gi 2038291632 820 LSfGDKPYGEMNNQEVMKSIEEGY 843
Cdd:cd14096   231 LC-GFPPFYDESIETLTEKISRGD 253
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
647-819 1.92e-11

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 66.94  E-value: 1.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 647 SQDCKTVAIKTlkdtspdGQWWNFLREATIMGQFNHPHILRLEGVVTKRK-PIMIVTEFMENgaLDAFLKEREdQLAPGQ 725
Cdd:PHA03212  114 NKTCEHVVIKA-------GQRGGTATEAHILRAINHPSIIQLKGTFTYNKfTCLILPRYKTD--LYCYLAAKR-NIAICD 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 726 LVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQ--NLCckVSDFGLTRLLDDFDGT-YETQGGKIPIrwTAPEAIAHRI 802
Cdd:PHA03212  184 ILAIERSVLRAIQYLHENRIIHRDIKAENIFINHpgDVC--LGDFGAACFPVDINANkYYGWAGTIAT--NAPELLARDP 259
                         170
                  ....*....|....*..
gi 2038291632 803 FTTASDVWSFGIVMWEV 819
Cdd:PHA03212  260 YGPAVDIWSAGIVLFEM 276
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
629-887 2.37e-11

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: 65.10  E-value: 2.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRfpsQDCKTVAIKTLKDTSPDGQWWNFLR-------EATIMGQFN---HPHILRLEGVVTKRKPI 698
Cdd:cd14004     7 EMGEGAYGQVNLAIYK---SKGKEVVIKFIFKERILVDTWVRDRklgtvplEIHILDTLNkrsHPNIVKLLDFFEDDEFY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 699 MIVTEFMENGaLDAF--------LKEREDQLAPGQLVAmllgiasGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGL 770
Cdd:cd14004    84 YLVMEKHGSG-MDLFdfierkpnMDEKEAKYIFRQVAD-------AVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFGS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 771 TRLL-----DDFDGTyetqggkipIRWTAPEAIA-HRIFTTASDVWSFGIVMWeVLSFGDKPYGEMnnQEVMKSieegyR 844
Cdd:cd14004   156 AAYIksgpfDTFVGT---------IDYAAPEVLRgNPYGGKEQDIWALGVLLY-TLVFKENPFYNI--EEILEA-----D 218
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 2038291632 845 LPPPVDCPAPLYELMKNCWAYDRARRPhflqlqaHLEQLLTDP 887
Cdd:cd14004   219 LRIPYAVSEDLIDLISRMLNRDVGDRP-------TIEELLTDP 254
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
629-848 2.44e-11

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: 65.35  E-value: 2.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGAlrfPSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENG 708
Cdd:cd14185     7 TIGDGNFAVVKECR---HWNENQEYAMKIIDKSKLKGKEDMIESEILIIKSLSHPNIVKLFEVYETEKEIYLILEYVRGG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 AL-DAFLKERedQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQN----LCCKVSDFGLTRLLddfDGTYET 783
Cdd:cd14185    84 DLfDAIIESV--KFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQHNpdksTTLKLADFGLAKYV---TGPIFT 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038291632 784 QGGKiPIrWTAPEAIAHRIFTTASDVWSFGIVMWeVLSFGDKPY--GEMNNQEVMKSIEEG-YRLPPP 848
Cdd:cd14185   159 VCGT-PT-YVAPEILSEKGYGLEVDMWAAGVILY-ILLCGFPPFrsPERDQEELFQIIQLGhYEFLPP 223
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
672-842 2.46e-11

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: 65.30  E-value: 2.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 672 REATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGAL--DAFLK----EREDQLAPGQLVamllgiaSGMNYLSGHNY 745
Cdd:cd14107    47 QERDILARLSHRRLTCLLDQFETRKTLILILELCSSEELldRLFLKgvvtEAEVKLYIQQVL-------EGIGYLHGMNI 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 746 VHRDLAARNILV----NQNLccKVSDFGLTRLLDDFDGTYETQGGKipiRWTAPEAIAHRIFTTASDVWSFGIVMWEVLS 821
Cdd:cd14107   120 LHLDIKPDNILMvsptREDI--KICDFGFAQEITPSEHQFSKYGSP---EFVAPEIVHQEPVSAATDIWALGVIAYLSLT 194
                         170       180
                  ....*....|....*....|.
gi 2038291632 822 FGDKPYGEmNNQEVMKSIEEG 842
Cdd:cd14107   195 CHSPFAGE-NDRATLLNVAEG 214
STKc_IRAK2 cd14157
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; ...
630-821 2.56e-11

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; 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. IRAK2 plays a role in mediating NFkB activation by TLR3, TLR4, and TLR8. It is specifically targeted by the viral protein A52, which is important for virulence, to inhibit all IL-1/TLR pathways, indicating that IRAK2 has a predominant role in NFkB activation. It is redundant with IRAK1 in early signaling but is critical for late and sustained activation. The IRAK2 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: 271059 [Multi-domain]  Cd Length: 289  Bit Score: 65.63  E-value: 2.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGalrfpSQDCKTVAIKTLKDT--SPDGQWWNFLR-EATIMGQFNHPHILRLEGVVTKRKPIMIVTEFME 706
Cdd:cd14157     1 ISEGTFADIYKG-----YRHGKQYVIKRLKETecESPKSTERFFQtEVQICFRCCHPNILPLLGFCVESDCHCLIYPYMP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 707 NGALDAFLKEREDQ--LAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLtRLLDDFDGTYETQ 784
Cdd:cd14157    76 NGSLQDRLQQQGGShpLPWEQRLSISLGLLKAVQHLHNFGILHGNIKSSNVLLDGNLLPKLGHSGL-RLCPVDKKSVYTM 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2038291632 785 GGKIPIRWTAP----EAIAHRIFTTASDVWSFGIVMWEVLS 821
Cdd:cd14157   155 MKTKVLQISLAylpeDFVRHGQLTEKVDIFSCGVVLAEILT 195
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
630-820 2.59e-11

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: 66.06  E-value: 2.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFPSQdckTVAIKTL-KDTSPDGQWWNFLREATIMGQFNHPHILRLEGV-VTKRKPIMIVTEFMEN 707
Cdd:cd07856    18 VGMGAFGLVCSARDQLTGQ---NVAVKKImKPFSTPVLAKRTYRELKLLKHLRHENIISLSDIfISPLEDIYFVTELLGT 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GaLDAFLKER--EDQLAPgqlvAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDdfdgtyETQG 785
Cdd:cd07856    95 D-LHRLLTSRplEKQFIQ----YFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLARIQD------PQMT 163
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2038291632 786 GKIPIR-WTAPE-AIAHRIFTTASDVWSFGIVMWEVL 820
Cdd:cd07856   164 GYVSTRyYRAPEiMLTWQKYDVEVDIWSAGCIFAEML 200
SAM_caskin1,2_repeat2 cd09498
SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 ...
917-976 2.62e-11

SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 proteins is a protein-protein interaction domain. Caskin has two tandem SAM domains. Caskin protein is known to interact with membrane-associated guanylate kinase CASK, and may play a role in neural development, synaptic protein targeting, and regulation of gene expression.


Pssm-ID: 188897  Cd Length: 71  Bit Score: 60.00  E-value: 2.62e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 917 SVSEWLESIRMKRYILHFRSAGLDTMECVLELTAEDLTQMGITLPGHQKRILCSIQGFKD 976
Cdd:cd09498     9 DLLEWLSLLGLPQYHKVLVENGYDSIDFVTDLTWEDLQDIGITKLGHQKKLMLAIKKLKD 68
SAM_EPH-A10 cd09549
SAM domain of EPH-A10 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
915-975 2.66e-11

SAM domain of EPH-A10 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A10 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A10 receptors and appears to mediate cell-cell initiated signal transduction. It was found preferentially expressed in the testis. EphA10 may be involved in the pathogenesis and development of prostate carcinoma and lymphocytic leukemia. It is a potential molecular marker and/or therapy target for these types of cancers.


Pssm-ID: 188948  Cd Length: 70  Bit Score: 59.88  E-value: 2.66e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2038291632 915 YRSVSEWLESIRMKRYILHFRSAGLDTMECVLELTAEDLTQMGITLPGHQKRILCSIQGFK 975
Cdd:cd09549     7 FGSVGEWLEALDLCRYKDNFAAAGYGSLEAVARMTAQDVLSLGITSLEHQELLLAGIQALR 67
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
629-832 2.79e-11

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: 64.94  E-value: 2.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVY-----RGALRFPSqdcKTVAIKTLKDTSpdgqwwNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTE 703
Cdd:cd14190    11 VLGGGKFGKVHtctekRTGLKLAA---KVINKQNSKDKE------MVLLEIQVMNQLNHRNLIQLYEAIETPNEIVLFME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 704 FMENGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNIL-VNQN-LCCKVSDFGLTR-------LL 774
Cdd:cd14190    82 YVEGGELFERIVDEDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILcVNRTgHQVKIIDFGLARrynprekLK 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038291632 775 DDFdGTYEtqggkipirWTAPEAIAHRIFTTASDVWSFGIVMWEVLS-----FGDKPYGEMNN 832
Cdd:cd14190   162 VNF-GTPE---------FLSPEVVNYDQVSFPTDMWSMGVITYMLLSglspfLGDDDTETLNN 214
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
626-829 3.08e-11

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 67.13  E-value: 3.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 626 VDTVIGEGEFGEVYRGalrfpsQDCK---TVAIKTLK-DTSPDGqwwNFL----REATIMGQFNHPHILRL------EGV 691
Cdd:NF033483   11 IGERIGRGGMAEVYLA------KDTRldrDVAVKVLRpDLARDP---EFVarfrREAQSAASLSHPNIVSVydvgedGGI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 692 VtkrkpiMIVTEFMENGALDAFLKEREdQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLT 771
Cdd:NF033483   82 P------YIVMEYVDGRTLKDYIREHG-PLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIA 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2038291632 772 RLLddfDGTYETQGGKI--PIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPY-GE 829
Cdd:NF033483  155 RAL---SSTTMTQTNSVlgTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLT-GRPPFdGD 211
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
630-819 3.22e-11

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: 65.24  E-value: 3.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRfpsQDCKTVAIK-TLKDTSPDGQWWNFLREATIMGQFNH-PHILRL---EGVVTKRKPIM-IVTE 703
Cdd:cd07837     9 IGEGTYGKVYKARDK---NTGKLVALKkTRLEMEEEGVPSTALREVSLLQMLSQsIYIVRLldvEHVEENGKPLLyLVFE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 704 FMENGA---LDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVN-QNLCCKVSDFGLTRLlddFDG 779
Cdd:cd07837    86 YLDTDLkkfIDSYGRGPHNPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDkQKGLLKIADLGLGRA---FTI 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2038291632 780 TYETQGGKIPIRW-TAPEAI---AHriFTTASDVWSFGIVMWEV 819
Cdd:cd07837   163 PIKSYTHEIVTLWyRAPEVLlgsTH--YSTPVDMWSVGCIFAEM 204
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
682-842 3.35e-11

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: 65.42  E-value: 3.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 682 HPHILRLEGVVTKRKPIMIVTEFMENGAL-DAFLKERedQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQN 760
Cdd:cd14178    56 HPNIITLKDVYDDGKFVYLVMELMRGGELlDRILRQK--CFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYMDE 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 761 L----CCKVSDFGLTRLLDDFDGTYETQGgkIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYG---EMNNQ 833
Cdd:cd14178   134 SgnpeSIRICDFGFAKQLRAENGLLMTPC--YTANFVAPEVLKRQGYDAACDIWSLGILLYTMLA-GFTPFAngpDDTPE 210

                  ....*....
gi 2038291632 834 EVMKSIEEG 842
Cdd:cd14178   211 EILARIGSG 219
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
629-901 3.48e-11

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: 65.75  E-value: 3.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVyrgALRFPSQDCKTVAIKTLKDTSPdgqwWNFLREATIMGQFN-------HPHILRLEGVVTKRKPIMIV 701
Cdd:cd05604     3 VIGKGSFGKV---LLAKRKRDGKYYAVKVLQKKVI----LNRKEQKHIMAERNvllknvkHPFLVGLHYSFQTTDKLYFV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 702 TEFMENGALdAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTR-------LL 774
Cdd:cd05604    76 LDFVNGGEL-FFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCKegisnsdTT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 775 DDFDGTYEtqggkipirWTAPEAIAHRIFTTASDVWSFGIVMWEVLsFGDKPYGEMNNQEVMKSI-EEGYRLPPPVDCPA 853
Cdd:cd05604   155 TTFCGTPE---------YLAPEVIRKQPYDNTVDWWCLGSVLYEML-YGLPPFYCRDTAEMYENIlHKPLVLRPGISLTA 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038291632 854 plYELMKNCWAYDRARR----PHFLQLQAH-----------LEQLLT---DPH--SLRTIANFDPRVT 901
Cdd:cd05604   225 --WSILEELLEKDRQLRlgakEDFLEIKNHpffesinwtdlVQKKIPppfNPNvnGPDDISNFDAEFT 290
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
626-848 4.04e-11

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: 65.14  E-value: 4.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 626 VDTVIGEGEFGEVYRGALRFPSQDCKTVAIKTLKDTSPDGQwwNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFM 705
Cdd:cd14086     5 LKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSARDHQ--KLEREARICRLLKHPNIVRLHDSISEEGFHYLVFDLV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 706 ENGALDAFLKERE-----DQLAPGQLvamllgIASGMNYLSGHNYVHRDLAARNILV---NQNLCCKVSDFGLTRLLDD- 776
Cdd:cd14086    83 TGGELFEDIVAREfyseaDASHCIQQ------ILESVNHCHQNGIVHRDLKPENLLLaskSKGAAVKLADFGLAIEVQGd 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2038291632 777 ------FDGTYEtqggkipirWTAPEAIAHRIFTTASDVWSFGIVMWeVLSFGDKPYGEMNNQEVMKSIEEG-YRLPPP 848
Cdd:cd14086   157 qqawfgFAGTPG---------YLSPEVLRKDPYGKPVDIWACGVILY-ILLVGYPPFWDEDQHRLYAQIKAGaYDYPSP 225
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
627-842 4.55e-11

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: 65.06  E-value: 4.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 627 DTVIGEGEFgEVYRGALRFPSQDCKTVAIKTLKDTSpdgqwwNFLREATIMGQFN-HPHILRLEGVVTKRKPIMIVTEFM 705
Cdd:cd14179    12 DKPLGEGSF-SICRKCLHKKTNQEYAVKIVSKRMEA------NTQREIAALKLCEgHPNIVKLHEVYHDQLHTFLVMELL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 706 ENGALDAFLKEREdQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILV---NQNLCCKVSDFGLTRLLDDfdgtyE 782
Cdd:cd14179    85 KGGELLERIKKKQ-HFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFtdeSDNSEIKIIDFGFARLKPP-----D 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 783 TQGGKIP---IRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNN-------QEVMKSIEEG 842
Cdd:cd14179   159 NQPLKTPcftLHYAAPELLNYNGYDESCDLWSLGVILYTMLS-GQVPFQCHDKsltctsaEEIMKKIKQG 227
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
630-870 4.69e-11

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 65.39  E-value: 4.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGalRFPSQDCKTVAIKTLKDTS--PDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMEN 707
Cdd:PTZ00426   38 LGTGSFGRVILA--TYKNEDFPPVAIKRFEKSKiiKQKQVDHVFSERKILNYINHPFCVNLYGSFKDESYLYLVLEFVIG 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GALDAFLkeREDQLAPGQLVAMLLG-IASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDdfDGTYETQGG 786
Cdd:PTZ00426  116 GEFFTFL--RRNKRFPNDVGCFYAAqIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGFAKVVD--TRTYTLCGT 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 787 KipiRWTAPEAIAHRIFTTASDVWSFGIVMWEVLsFGDKPYGEMNNQEVMKSIEEGYRLPPPV---DCPaplyELMKNCW 863
Cdd:PTZ00426  192 P---EYIAPEILLNVGHGKAADWWTLGIFIYEIL-VGCPPFYANEPLLIYQKILEGIIYFPKFldnNCK----HLMKKLL 263

                  ....*..
gi 2038291632 864 AYDRARR 870
Cdd:PTZ00426  264 SHDLTKR 270
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
671-826 5.22e-11

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: 65.07  E-value: 5.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 671 LREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGALDAFLKERedQLAPGQLVAML-LGIASGMNYL-SGHNYVHR 748
Cdd:cd06649    51 IRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQVLKEA--KRIPEEILGKVsIAVLRGLAYLrEKHQIMHR 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 749 DLAARNILVNQNLCCKVSDFGLT-RLLDDFDGTYetqggkIPIR-WTAPEAIAHRIFTTASDVWSFGIVMWEvLSFGDKP 826
Cdd:cd06649   129 DVKPSNILVNSRGEIKLCDFGVSgQLIDSMANSF------VGTRsYMSPERLQGTHYSVQSDIWSMGLSLVE-LAIGRYP 201
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
629-880 5.33e-11

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: 65.42  E-value: 5.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRfpsQDCKTVAIKTLKDTSpdgqwwnFLR---EATIMGQFN-------HPHILRLEGVVTKRKPI 698
Cdd:cd05602    14 VIGKGSFGKVLLARHK---SDEKFYAVKVLQKKA-------ILKkkeEKHIMSERNvllknvkHPFLVGLHFSFQTTDKL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 699 MIVTEFMENGALDAFLKEREDQLAP-GQLVAMllGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDF 777
Cdd:cd05602    84 YFVLDYINGGELFYHLQRERCFLEPrARFYAA--EIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENIEP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 778 DGTYETQGGKiPiRWTAPEAIAHRIFTTASDVWSFGIVMWEVLsFGDKPYGEMNNQEVMKSI-EEGYRLPPPVDCPAplY 856
Cdd:cd05602   162 NGTTSTFCGT-P-EYLAPEVLHKQPYDRTVDWWCLGAVLYEML-YGLPPFYSRNTAEMYDNIlNKPLQLKPNITNSA--R 236
                         250       260
                  ....*....|....*....|....*...
gi 2038291632 857 ELMKNCWAYDRARR----PHFLQLQAHL 880
Cdd:cd05602   237 HLLEGLLQKDRTKRlgakDDFTEIKNHI 264
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
626-831 5.39e-11

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: 65.02  E-value: 5.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 626 VDTVIGEGEFGEVYrgaLRFPSQDCKTVAIKTLK--DTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTE 703
Cdd:cd05601     5 VKNVIGRGHFGEVQ---VVKEKATGDIYAMKVLKksETLAQEEVSFFEEERDIMAKANSPWITKLQYAFQDSENLYLVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 704 FMENGALDAFLKEREDQLAPGQ----LVAMLLGIASgmnyLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDfDG 779
Cdd:cd05601    82 YHPGGDLLSLLSRYDDIFEESMarfyLAELVLAIHS----LHSMGYVHRDIKPENILIDRTGHIKLADFGSAAKLSS-DK 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038291632 780 TYETqggKIPIrwTAPEAIAHRIFTTAS-----------DVWSFGIVMWEVLsFGDKPYGEMN 831
Cdd:cd05601   157 TVTS---KMPV--GTPDYIAPEVLTSMNggskgtygvecDWWSLGIVAYEML-YGKTPFTEDT 213
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
629-770 5.47e-11

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: 64.31  E-value: 5.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVY--RGALrfpsqDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFME 706
Cdd:cd14046    13 VLGKGAFGQVVkvRNKL-----DGRYYAIKKIKLRSESKNNSRILREVMLLSRLNHQHVVRYYQAWIERANLYIQMEYCE 87
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038291632 707 NGAL----DAFLKEREDQLApgqlvAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGL 770
Cdd:cd14046    88 KSTLrdliDSGLFQDTDRLW-----RLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGL 150
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
630-889 6.48e-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: 64.36  E-value: 6.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFPSQDcktVAIKTLK-DTSPDGQWwnFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENG 708
Cdd:cd06655    27 IGQGASGTVFTAIDVATGQE---VAIKQINlQKQPKKEL--IINEILVMKELKNPNIVNFLDSFLVGDELFVVMEYLAGG 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 ALDAFLKEreDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYETQGGKi 788
Cdd:cd06655   102 SLTDVVTE--TCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCAQITPEQSKRSTMVGT- 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 789 PIrWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSIEEGYrlPPPVDCP---APLY-ELMKNCWA 864
Cdd:cd06655   179 PY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPYLNENPLRALYLIATNG--TPELQNPeklSPIFrDFLNRCLE 254
                         250       260
                  ....*....|....*....|....*
gi 2038291632 865 YDRARRPHFLQLQAHLEQLLTDPHS 889
Cdd:cd06655   255 MDVEKRGSAKELLQHPFLKLAKPLS 279
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
671-826 6.71e-11

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: 64.73  E-value: 6.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 671 LREATIMGQF-NHPHILRL--EGVVTKRK--PIMIVTEFMEnGALDAFLKErEDQLAPGQLVAMLLGIASGMNYLSGHNY 745
Cdd:cd07857    49 LRELKLLRHFrGHKNITCLydMDIVFPGNfnELYLYEELME-ADLHQIIRS-GQPLTDAHFQSFIYQILCGLKYIHSANV 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 746 VHRDLAARNILVNQNLCCKVSDFGLTRLLDdfDGTYETQG---GKIPIRW-TAPE-AIAHRIFTTASDVWSFGIVMWEVL 820
Cdd:cd07857   127 LHRDLKPGNLLVNADCELKICDFGLARGFS--ENPGENAGfmtEYVATRWyRAPEiMLSFQSYTKAIDVWSVGCILAELL 204

                  ....*.
gi 2038291632 821 sfGDKP 826
Cdd:cd07857   205 --GRKP 208
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
628-883 6.79e-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: 64.69  E-value: 6.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 628 TVIGEGEFGEVYRGALRfpsqdCKTVAIKTLKdTSPDGQWWnflREATIMGQ--FNHPHILRLEGVVTKRK----PIMIV 701
Cdd:cd14219    11 KQIGKGRYGEVWMGKWR-----GEKVAVKVFF-TTEEASWF---RETEIYQTvlMRHENILGFIAADIKGTgswtQLYLI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 702 TEFMENGALDAFLKEreDQLAPGQLVAMLLGIASGMNYLSGHNY--------VHRDLAARNILVNQNLCCKVSDFGL-TR 772
Cdd:cd14219    82 TDYHENGSLYDYLKS--TTLDTKAMLKLAYSSVSGLCHLHTEIFstqgkpaiAHRDLKSKNILVKKNGTCCIADLGLaVK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 773 LLDDfdgtyeTQGGKIPI-------RWTAPEAI------AHRIFTTASDVWSFGIVMWEV----LSFG-----DKPYGEM 830
Cdd:cd14219   160 FISD------TNEVDIPPntrvgtkRYMPPEVLdeslnrNHFQSYIMADMYSFGLILWEVarrcVSGGiveeyQLPYHDL 233
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038291632 831 ----NNQEVMKSIEEGYRLPPPV-------DCPAPLYELMKNCWAYDRARRPHFLQLQAHLEQL 883
Cdd:cd14219   234 vpsdPSYEDMREIVCIKRLRPSFpnrwssdECLRQMGKLMTECWAHNPASRLTALRVKKTLAKM 297
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
615-848 7.79e-11

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: 63.78  E-value: 7.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 615 FAQELDPTwlivdTVIGEGeFGEVYRGALRFPSqdCKTVAIKTLkDTSPDG----QWWNFLREAT-----IMGQFN-HPH 684
Cdd:cd14182     1 FYEKYEPK-----EILGRG-VSSVVRRCIHKPT--RQEYAVKII-DITGGGsfspEEVQELREATlkeidILRKVSgHPN 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 685 ILRLEGVVTKRKPIMIVTEFMENGALDAFLKEREdQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCK 764
Cdd:cd14182    72 IIQLKDTYETNTFFFLVFDLMKKGELFDYLTEKV-TLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 765 VSDFGLTRLLDDFDGTYETQGGKipiRWTAPEAIA------HRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKS 838
Cdd:cd14182   151 LTDFGFSCQLDPGEKLREVCGTP---GYLAPEIIEcsmddnHPGYGKEVDMWSTGVIMYTLLA-GSPPFWHRKQMLMLRM 226
                         250
                  ....*....|.
gi 2038291632 839 IEEG-YRLPPP 848
Cdd:cd14182   227 IMSGnYQFGSP 237
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
676-842 9.00e-11

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: 63.88  E-value: 9.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 676 IMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGAL-DAFLKERedQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARN 754
Cdd:cd14177    51 LMRYGQHPNIITLKDVYDDGRYVYLVTELMKGGELlDRILRQK--FFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSN 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 755 ILVNQNL----CCKVSDFGLTRLLDDFDGTYETQGgkIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEM 830
Cdd:cd14177   129 ILYMDDSanadSIRICDFGFAKQLRGENGLLLTPC--YTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLA-GYTPFANG 205
                         170
                  ....*....|....*
gi 2038291632 831 NN---QEVMKSIEEG 842
Cdd:cd14177   206 PNdtpEEILLRIGSG 220
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
629-879 9.65e-11

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: 63.51  E-value: 9.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYrgaLRFPSQDCKTVAIKTLK---DTSPDGQWWNFLR-EATIMGQFNHPHILRLEGVVT--KRKPIMIVT 702
Cdd:cd06653     9 LLGRGAFGEVY---LCYDADTGRELAVKQVPfdpDSQETSKEVNALEcEIQLLKNLRHDRIVQYYGCLRdpEEKKLSIFV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 703 EFMENGALdaflkerEDQL-APGQLVAMLL-----GIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDD 776
Cdd:cd06653    86 EYMPGGSV-------KDQLkAYGALTENVTrrytrQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRIQT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 777 F--DGTYETQGGKIPIrWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMnnqEVMKSI------EEGYRLPPP 848
Cdd:cd06653   159 IcmSGTGIKSVTGTPY-WMSPEVISGEGYGRKADVWSVACTVVEMLT-EKPPWAEY---EAMAAIfkiatqPTKPQLPDG 233
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2038291632 849 VDcpAPLYELMKNCWaYDRARRPHFLQLQAH 879
Cdd:cd06653   234 VS--DACRDFLRQIF-VEEKRRPTAEFLLRH 261
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
615-821 1.03e-10

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: 64.29  E-value: 1.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 615 FAQELDPT-WLIVD-----TVIGEGEFGEVYRGalrFPSQDCKTVAIKTL----------KDTspdgqwwnfLREATIMG 678
Cdd:cd07877     4 YRQELNKTiWEVPEryqnlSPVGSGAYGSVCAA---FDTKTGLRVAVKKLsrpfqsiihaKRT---------YRELRLLK 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 679 QFNHPHILRLEGVVTKRKP------IMIVTEFMenGA-LDAFLKERedQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLA 751
Cdd:cd07877    72 HMKHENVIGLLDVFTPARSleefndVYLVTHLM--GAdLNNIVKCQ--KLTDDHVQFLIYQILRGLKYIHSADIIHRDLK 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2038291632 752 ARNILVNQNLCCKVSDFGLTRLLDDfdgtyeTQGGKIPIRW-TAPEAIAHRI-FTTASDVWSFGIVMWEVLS 821
Cdd:cd07877   148 PSNLAVNEDCELKILDFGLARHTDD------EMTGYVATRWyRAPEIMLNWMhYNQTVDIWSVGCIMAELLT 213
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
630-820 1.11e-10

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: 64.12  E-value: 1.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRfpsQDCKTVAIKTLKDT---SPDGQwwNFLREATIMGQFN-HPHILRLEGVV--TKRKPIMIVTE 703
Cdd:cd07852    15 LGKGAYGIVWKAIDK---KTGEVVALKKIFDAfrnATDAQ--RTFREIMFLQELNdHPNIIKLLNVIraENDKDIYLVFE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 704 FMENGaLDA-----FLKEREDQLAPGQLVAMLLGIASGmnylsghNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFD 778
Cdd:cd07852    90 YMETD-LHAviranILEDIHKQYIMYQLLKALKYLHSG-------GVIHRDLKPSNILLNSDCRVKLADFGLARSLSQLE 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2038291632 779 gtyetQGGKIPI-------RW-TAPEA-IAHRIFTTASDVWSFGIVMWEVL 820
Cdd:cd07852   162 -----EDDENPVltdyvatRWyRAPEIlLGSTRYTKGVDMWSVGCILGEML 207
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
630-870 1.16e-10

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: 63.34  E-value: 1.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRfpsQDCKTVAIKTL--KDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMEN 707
Cdd:cd14117    14 LGKGKFGNVYLAREK---QSKFIVALKVLfkSQIEKEGVEHQLRREIEIQSHLRHPNILRLYNYFHDRKRIYLILEYAPR 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GALDAFLkEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFG-------LTRllddfdgt 780
Cdd:cd14117    91 GELYKEL-QKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGwsvhapsLRR-------- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 781 yETQGGKIPirWTAPEAIAHRIFTTASDVWSFGIVMWEVLsFGDKPYGEMNNQEVMKSIEE-GYRLPPPVDCPA------ 853
Cdd:cd14117   162 -RTMCGTLD--YLPPEMIEGRTHDEKVDLWCIGVLCYELL-VGMPPFESASHTETYRRIVKvDLKFPPFLSDGSrdlisk 237
                         250       260
                  ....*....|....*....|....*..
gi 2038291632 854 ----------PLYELMKNCWAYDRARR 870
Cdd:cd14117   238 llryhpserlPLKGVMEHPWVKANSRR 264
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
627-839 1.18e-10

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: 63.01  E-value: 1.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 627 DTVIGEGEFGEVYRgalrfpsqdCK------TVAIKTLKDTSPDgQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMI 700
Cdd:cd14193     9 EEILGGGRFGQVHK---------CEekssglKLAAKIIKARSQK-EKEEVKNEIEVMNQLNHANLIQLYDAFESRNDIVL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 701 VTEFMENGALDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNIL-VNQNLC-CKVSDFGLTR------ 772
Cdd:cd14193    79 VMEYVDGGELFDRIIDENYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILcVSREANqVKIIDFGLARrykpre 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038291632 773 -LLDDFdGTYEtqggkipirWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSI 839
Cdd:cd14193   159 kLRVNF-GTPE---------FLAPEVVNYEFVSFPTDMWSLGVIAYMLLS-GLSPFLGEDDNETLNNI 215
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
673-886 1.32e-10

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: 63.03  E-value: 1.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 673 EATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGALDAFLKEREDQLAPgQLVAMLLGIASGMNYLSGHNYVHRDLAA 752
Cdd:cd14187    57 EIAIHRSLAHQHVVGFHGFFEDNDFVYVVLELCRRRSLLELHKRRKALTEP-EARYYLRQIILGCQYLHRNRVIHRDLKL 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 753 RNILVNQNLCCKVSDFGLTRLLdDFDGTYETQGGKIPiRWTAPEAIAHRIFTTASDVWSFGIVMWEVLsFGDKPYGEMNN 832
Cdd:cd14187   136 GNLFLNDDMEVKIGDFGLATKV-EYDGERKKTLCGTP-NYIAPEVLSKKGHSFEVDIWSIGCIMYTLL-VGKPPFETSCL 212
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2038291632 833 QEVMKSIEEG-YRLPPPVDCPAPlyELMKNCWAYDRARRPhflqlqaHLEQLLTD 886
Cdd:cd14187   213 KETYLRIKKNeYSIPKHINPVAA--SLIQKMLQTDPTARP-------TINELLND 258
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
619-821 1.34e-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: 63.71  E-value: 1.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 619 LDPTWLIVDtVIGEGEFGEVYRGALRFPSQDCKTVAIKTLKDTSPDGQWWNFL-REATIMGQFNHPHILRLEGVVTKRKP 697
Cdd:cd14094     1 FEDVYELCE-VIGKGPFSVVRRCIHRETGQQFAVKIVDVAKFTSSPGLSTEDLkREASICHMLKHPHIVELLETYSSDGM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 698 IMIVTEFMENGALDAFLKEREDQ-LAPGQLVA--MLLGIASGMNYLSGHNYVHRDLAARNIL---VNQNLCCKVSDFGLT 771
Cdd:cd14094    80 LYMVFEFMDGADLCFEIVKRADAgFVYSEAVAshYMRQILEALRYCHDNNIIHRDVKPHCVLlasKENSAPVKLGGFGVA 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2038291632 772 RLLDdfDGTYETQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLS 821
Cdd:cd14094   160 IQLG--ESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLS 207
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
630-839 1.37e-10

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: 63.37  E-value: 1.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVyRGALRFPSQdcKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGA 709
Cdd:cd14169    11 LGEGAFSEV-VLAQERGSQ--RLVALKCIPKKALRGKEAMVENEIAVLRRINHENIVSLEDIYESPTHLYLAMELVTGGE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 710 LDAFLKER--EDQLAPGQLVAMLLGiasGMNYLSGHNYVHRDLAARNILVN---QNLCCKVSDFGLTRLLDDfdGTYETQ 784
Cdd:cd14169    88 LFDRIIERgsYTEKDASQLIGQVLQ---AVKYLHQLGIVHRDLKPENLLYAtpfEDSKIMISDFGLSKIEAQ--GMLSTA 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2038291632 785 GGKiPiRWTAPEAIAHRIFTTASDVWSFGIVMWeVLSFGDKPYGEMNNQEVMKSI 839
Cdd:cd14169   163 CGT-P-GYVAPELLEQKPYGKAVDVWAIGVISY-ILLCGYPPFYDENDSELFNQI 214
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
671-856 1.37e-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: 62.92  E-value: 1.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 671 LREATIMGQFNHPHILRL-EGVVTKRKpIMIVTEFMEN-----GALDAFLKEREDqlapgqLVAMLLGIASGMNYLSGHN 744
Cdd:cd14111    47 LQEYEILKSLHHERIMALhEAYITPRY-LVLIAEFCSGkellhSLIDRFRYSEDD------VVGYLVQILQGLEYLHGRR 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 745 YVHRDLAARNILVNQNLCCKVSDFG--------LTRLLDDFDGTYEtqggkipirWTAPEAIAHRIFTTASDVWSFGIVM 816
Cdd:cd14111   120 VLHLDIKPDNIMVTNLNAIKIVDFGsaqsfnplSLRQLGRRTGTLE---------YMAPEMVKGEPVGPPADIWSIGVLT 190
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2038291632 817 WEVLSfGDKPYGEMNNQEVMKSIEEG----YRLPPPVDCPAPLY 856
Cdd:cd14111   191 YIMLS-GRSPFEDQDPQETEAKILVAkfdaFKLYPNVSQSASLF 233
SAM_Arap1,2,3 cd09490
SAM domain of Arap1,2,3 (angiotensin receptor-associated protein); SAM (sterile alpha motif) ...
917-973 2.04e-10

SAM domain of Arap1,2,3 (angiotensin receptor-associated protein); SAM (sterile alpha motif) domain of Arap1,2,3 subfamily proteins (angiotensin receptor-associated) is a protein-protein interaction domain. Arap1,2,3 proteins are phosphatidylinositol-3,4,5-trisphosphate-dependent GTPase-activating proteins. They are involved in phosphatidylinositol-3 kinase (PI3K) signaling pathways. In addition to SAM domain, Arap1,2,3 proteins contain ArfGap, PH-like, RhoGAP and UBQ domains. SAM domain of Arap3 protein was shown to interact with SAM domain of Ship2 phosphatidylinositol-trisphosphate phosphatase proteins. Such interaction apparently plays a role in inhibition of PI3K regulated pathways since Ship2 converts PI(3,4,5)P3 into PI(3,4)P2. Proteins of this subfamily participate in regulation of signaling and trafficking associated with a number of different receptors (including EGFR, TRAIL-R1/DR4, TRAIL-R2/DR5) in normal and cancer cells; they are involved in regulation of actin cytoskeleton remodeling, cell spreading and formation of lamellipodia.


Pssm-ID: 188889  Cd Length: 63  Bit Score: 57.31  E-value: 2.04e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2038291632 917 SVSEWLESIRMKRYILHFRSAGLDTMECVLELTAEDLTQMGITLPGHQKRILCSIQG 973
Cdd:cd09490     5 DIAEWLASIHLEQYLDLFREHGYVTATDCQGINDSRLKQIGISPTGHRRRILKQLPI 61
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
621-839 3.31e-10

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: 61.98  E-value: 3.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 621 PTWLIVDTVIGEGEFGEVYrgaLRFPSQDCKTVAIKTLK---DTSPDGQWWNFLR-EATIMGQFNHPHILRLEGVV--TK 694
Cdd:cd06652     1 PTNWRLGKLLGQGAFGRVY---LCYDADTGRELAVKQVQfdpESPETSKEVNALEcEIQLLKNLLHERIVQYYGCLrdPQ 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 695 RKPIMIVTEFMENGALdaflkerEDQL-APGQLVAMLL-----GIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDF 768
Cdd:cd06652    78 ERTLSIFMEYMPGGSI-------KDQLkSYGALTENVTrkytrQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDF 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038291632 769 GLTRLLDD--FDGTYETQGGKIPIrWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMnnqEVMKSI 839
Cdd:cd06652   151 GASKRLQTicLSGTGMKSVTGTPY-WMSPEVISGEGYGRKADIWSVGCTVVEMLT-EKPPWAEF---EAMAAI 218
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
630-821 3.61e-10

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: 62.77  E-value: 3.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRgALRFPSQDCKTVAIKTLKDTspdGQWWNFLREATIMGQFNHPHILRLEGVVTKR--KPIMIVTEFMEN 707
Cdd:cd07868    25 VGRGTYGHVYK-AKRKDGKDDKDYALKQIEGT---GISMSACREIALLRELKHPNVISLQKVFLSHadRKVWLLFDYAEH 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GALDAFLKERED-------QLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILV----NQNLCCKVSDFGLTRL--- 773
Cdd:cd07868   101 DLWHIIKFHRASkankkpvQLPRGMVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLfns 180
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2038291632 774 ----LDDFDGTYETqggkipIRWTAPE-AIAHRIFTTASDVWSFGIVMWEVLS 821
Cdd:cd07868   181 plkpLADLDPVVVT------FWYRAPElLLGARHYTKAIDIWAIGCIFAELLT 227
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
628-870 4.01e-10

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: 62.69  E-value: 4.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 628 TVIGEGEFGEVYrgaLRFPSQDCKTVAIKTLK--DTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFM 705
Cdd:cd05573     7 KVIGRGAFGEVW---LVRDKDTGQVYAMKILRksDMLKREQIAHVRAERDILADADSPWIVRLHYAFQDEDHLYLVMEYM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 706 ENGALDAFLKER---EDQLAPGQLVAMLLGIasgmNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGL-TRLLDDFDGTY 781
Cdd:cd05573    84 PGGDLMNLLIKYdvfPEETARFYIAELVLAL----DSLHKLGFIHRDIKPDNILLDADGHIKLADFGLcTKMNKSGDRES 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 782 ETQGG---------KIPIRWT-----------------APEAIAHRIFTTASDVWSFGIVMWEVLsFGDKPYGEMNNQEV 835
Cdd:cd05573   160 YLNDSvntlfqdnvLARRRPHkqrrvraysavgtpdyiAPEVLRGTGYGPECDWWSLGVILYEML-YGFPPFYSDSLVET 238
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2038291632 836 MKSI---EEGYRLPPPVDCPAPLYELMKNCWAyDRARR 870
Cdd:cd05573   239 YSKImnwKESLVFPDDPDVSPEAIDLIRRLLC-DPEDR 275
SAM_AIDA1AB-like_repeat2 cd09500
SAM domain of AIDA1AB-like proteins, repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
911-971 4.36e-10

SAM domain of AIDA1AB-like proteins, repeat 2; SAM (sterile alpha motif) domain repeat 2 of AIDA1AB-like proteins is a protein-protein interaction domain. AIDA1AB-like proteins have two tandem SAM domains. They may form an intramolecular head-to-tail homodimer. One of two basic motifs of the nuclear localization signal (NLS) is located within helix 5 of the SAM2 (motif HKRK). This signal plays a role in decoupling of SAM2 from SAM1, thus facilitating translocation of this type proteins into the nucleus. SAM domains of the AIDA1AB-like subfamily can directly bind ubiquitin and participate in regulating the degradation of ubiquitinated EphA receptors, particularly EPH-A8 receptor. Additionally AIDA1AB-like proteins may participate in the regulation of nucleoplasmic coilin protein interactions.


Pssm-ID: 188899  Cd Length: 65  Bit Score: 56.54  E-value: 4.36e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2038291632 911 DGIPYRSVSEWLESIRMKRYILHFRSAGLDTMECVLELTAEDLTQ-MGITLPGHQKRILCSI 971
Cdd:cd09500     1 DGNSPASVSEWLDSIGLGDYIETFLKHGYTSMERVKRIWEVELTNvLEINKLGHRKRILASL 62
PHA02988 PHA02988
hypothetical protein; Provisional
628-871 5.99e-10

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 61.30  E-value: 5.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 628 TVIGEGEFGEVYRGALrfpsqDCKTVAIKTLKDTSPDGQWWNFLREATI--MGQFNHPHILRLEG----VVTKRKPIMIV 701
Cdd:PHA02988   26 VLIKENDQNSIYKGIF-----NNKEVIIRTFKKFHKGHKVLIDITENEIknLRRIDSNNILKIYGfiidIVDDLPRLSLI 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 702 TEFMENGALDAFLkEREDQLAPGQLVAMLLGIASGMNYLsgHNYV---HRDLAARNILVNQNLCCKVSDFGLTRLLDDfd 778
Cdd:PHA02988  101 LEYCTRGYLREVL-DKEKDLSFKTKLDMAIDCCKGLYNL--YKYTnkpYKNLTSVSFLVTENYKLKIICHGLEKILSS-- 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 779 gtyeTQGGKIPIRWTAPEAIAHRIF---TTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKS-IEEGYRLPPPVDCPAP 854
Cdd:PHA02988  176 ----PPFKNVNFMVYFSYKMLNDIFseyTIKDDIYSLGVVLWEIFT-GKIPFENLTTKEIYDLiINKNNSLKLPLDCPLE 250
                         250
                  ....*....|....*..
gi 2038291632 855 LYELMKNCWAYDRARRP 871
Cdd:PHA02988  251 IKCIVEACTSHDSIKRP 267
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
629-870 6.62e-10

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: 61.21  E-value: 6.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRfpsqdCKTVAIKTLKdtSPDGQWWNFLREATIMGQFNHPHILRLEGVvTKRKP-----IMIVTE 703
Cdd:cd14141     2 IKARGRFGCVWKAQLL-----NEYVAVKIFP--IQDKLSWQNEYEIYSLPGMKHENILQFIGA-EKRGTnldvdLWLITA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 704 FMENGALDAFLKEreDQLAPGQLVAMLLGIASGMNYL--------SGHN--YVHRDLAARNILVNQNLCCKVSDFGLTRL 773
Cdd:cd14141    74 FHEKGSLTDYLKA--NVVSWNELCHIAQTMARGLAYLhedipglkDGHKpaIAHRDIKSKNVLLKNNLTACIADFGLALK 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 774 LDDFDGTYETQGGKIPIRWTAPEAIAHRI-FTTAS----DVWSFGIVMWEVLS---FGDKPY-----------GEMNNQE 834
Cdd:cd14141   152 FEAGKSAGDTHGQVGTRRYMAPEVLEGAInFQRDAflriDMYAMGLVLWELASrctASDGPVdeymlpfeeevGQHPSLE 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 2038291632 835 VMKSIEEGYRLPPPV-DC------PAPLYELMKNCWAYDRARR 870
Cdd:cd14141   232 DMQEVVVHKKKRPVLrECwqkhagMAMLCETIEECWDHDAEAR 274
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
626-839 6.79e-10

Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PSKH1 is an autophosphorylating STK that is expressed ubiquitously and exhibits multiple intracellular localizations including the centrosome, Golgi apparatus, and splice factor compartments. It contains a catalytic kinase domain and an N-terminal SH4-like motif that is acylated to facilitate membrane attachment. PSKH1 plays a rile in the maintenance of the Golgi apparatus, an important organelle within the secretory pathway. It may also function as a novel splice factor and a regulator of prostate cancer cell growth. The PSKH1 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: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 61.01  E-value: 6.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 626 VDTVIGEGEFGEVYRGALRFPSQdckTVAIKTLKDTSPDGQWWNflREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFM 705
Cdd:cd14087     5 IKALIGRGSFSRVVRVEHRVTRQ---PYAIKMIETKCRGREVCE--SELNVLRRVRHTNIIQLIEVFETKERVYMVMELA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 706 ENGAL-DAFL-KEREDQLAPGQLVAMLLgiaSGMNYLSGHNYVHRDLAARNILV---NQNLCCKVSDFGLTRLLDDFDGT 780
Cdd:cd14087    80 TGGELfDRIIaKGSFTERDATRVLQMVL---DGVKYLHGLGITHRDLKPENLLYyhpGPDSKIMITDFGLASTRKKGPNC 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2038291632 781 YETQGGKIPiRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSI 839
Cdd:cd14087   157 LMKTTCGTP-EYIAPEILLRKPYTQSVDMWAVGVIAYILLS-GTMPFDDDNRTRLYRQI 213
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
624-839 7.01e-10

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: 61.86  E-value: 7.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 624 LIVDTVIGEGEFGEVYRGALRFPSQdckTVAIKTLKDT---SPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMI 700
Cdd:cd05619     7 FVLHKMLGKGSFGKVFLAELKGTNQ---FFAIKALKKDvvlMDDDVECTMVEKRVLSLAWEHPFLTHLFCTFQTKENLFF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 701 VTEFMENGALDAFLKE-REDQLAPGQLVAMllGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTR--LLDD- 776
Cdd:cd05619    84 VMEYLNGGDLMFHIQScHKFDLPRATFYAA--EIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKenMLGDa 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038291632 777 ----FDGTYEtqggkipirWTAPEAIAHRIFTTASDVWSFGIVMWEVLsFGDKPYGEMNNQEVMKSI 839
Cdd:cd05619   162 ktstFCGTPD---------YIAPEILLGQKYNTSVDWWSFGVLLYEML-IGQSPFHGQDEEELFQSI 218
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
671-846 8.11e-10

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: 61.56  E-value: 8.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 671 LREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGALDAFL-KER---EDQlapgqlvAMLLG--IASGMNYLSGHN 744
Cdd:cd05595    43 VTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGELFFHLsRERvftEDR-------ARFYGaeIVSALEYLHSRD 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 745 YVHRDLAARNILVNQNLCCKVSDFGLTR-------LLDDFDGTYEtqggkipirWTAPEAIAHRIFTTASDVWSFGIVMW 817
Cdd:cd05595   116 VVYRDIKLENLMLDKDGHIKITDFGLCKegitdgaTMKTFCGTPE---------YLAPEVLEDNDYGRAVDWWGLGVVMY 186
                         170       180       190
                  ....*....|....*....|....*....|
gi 2038291632 818 EVLSfGDKPYGEMNNQEVMKSI-EEGYRLP 846
Cdd:cd05595   187 EMMC-GRLPFYNQDHERLFELIlMEEIRFP 215
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
629-839 8.35e-10

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: 61.22  E-value: 8.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRFPSqdcKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENG 708
Cdd:cd14168    17 VLGTGAFSEVVLAEERATG---KLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGG 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 AL------DAFLKEREDQlapgqlvAMLLGIASGMNYLSGHNYVHRDLAARNIL-VNQNLCCKV--SDFGLTRLldDFDG 779
Cdd:cd14168    94 ELfdriveKGFYTEKDAS-------TLIRQVLDAVYYLHRMGIVHRDLKPENLLyFSQDEESKImiSDFGLSKM--EGKG 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 780 TYETQGGKIPiRWTAPEAIAHRIFTTASDVWSFGIVMWeVLSFGDKPYGEMNNQEVMKSI 839
Cdd:cd14168   165 DVMSTACGTP-GYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFEQI 222
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
733-829 8.85e-10

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: 60.42  E-value: 8.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 733 IASGMNYLSGHNYVHRDLAARNILVNQNLC--CKVSDFGLTRLLDDfdgTYETQGGKIPirWTAPE---AIAHRIFT--T 805
Cdd:cd13987   100 LASALDFMHSKNLVHRDIKPENVLLFDKDCrrVKLCDFGLTRRVGS---TVKRVSGTIP--YTAPEvceAKKNEGFVvdP 174
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2038291632 806 ASDVWSFGIVM---------WEVLSFGDKPYGE 829
Cdd:cd13987   175 SIDVWAFGVLLfccltgnfpWEKADSDDQFYEE 207
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
651-839 9.83e-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: 60.99  E-value: 9.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 651 KTVAIKTLKDTSpDGQWwnFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGAL------DAFLKEREDQLAPG 724
Cdd:cd14085    29 KPYAVKKLKKTV-DKKI--VRTEIGVLLRLSHPNIIKLKEIFETPTEISLVLELVTGGELfdriveKGYYSERDAADAVK 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 725 QlvamllgIASGMNYLSGHNYVHRDLAARNILV---NQNLCCKVSDFGLTRLLDDfDGTYETQGGKiPiRWTAPEAIAHR 801
Cdd:cd14085   106 Q-------ILEAVAYLHENGIVHRDLKPENLLYatpAPDAPLKIADFGLSKIVDQ-QVTMKTVCGT-P-GYCAPEILRGC 175
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2038291632 802 IFTTASDVWSFGIVMWeVLSFGDKP-YGEMNNQEVMKSI 839
Cdd:cd14085   176 AYGPEVDMWSVGVITY-ILLCGFEPfYDERGDQYMFKRI 213
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
681-848 1.25e-09

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: 59.99  E-value: 1.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 681 NHPHILRL----EGVVTKRKPIMIVTEFMENGALDAFLKEREDQLAPGQLVAMLL-GIASGMNYLSGHNYVHRDLAARNI 755
Cdd:cd14089    52 GCPHIVRIidvyENTYQGRKCLLVVMECMEGGELFSRIQERADSAFTEREAAEIMrQIGSAVAHLHSMNIAHRDLKPENL 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 756 LV---NQNLCCKVSDFGLTRllddfdgtyETQGGK-------IPIrWTAPEAIAHRIFTTASDVWSFGIVMWeVLSFGDK 825
Cdd:cd14089   132 LYsskGPNAILKLTDFGFAK---------ETTTKKslqtpcyTPY-YVAPEVLGPEKYDKSCDMWSLGVIMY-ILLCGYP 200
                         170       180
                  ....*....|....*....|....*...
gi 2038291632 826 PYGEMNNQEV---MKS-IEEG-YRLPPP 848
Cdd:cd14089   201 PFYSNHGLAIspgMKKrIRNGqYEFPNP 228
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
629-887 1.28e-09

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: 60.14  E-value: 1.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGE--VYRGALRFPSQDCKTVAIKTLKDTSPDgqwwNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFME 706
Cdd:cd08221     7 VLGRGAFGEavLYRKTEDNSLVVWKEVNLSRLSEKERR----DALNEIDILSLLNHDNIITYYNHFLDGESLFIEMEYCN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 707 NGALDAFLKEREDQLAPGQLVA-MLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYETQG 785
Cdd:cd08221    83 GGNLHDKIAQQKNQLFPEEVVLwYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKVLDSESSMAESIV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 786 GKipIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFgDKPYGEMNNQEVMKSIEEGYRLPPPVDCPAPLYELMKNCWAY 865
Cdd:cd08221   163 GT--PYYMSPELVQGVKYNFKSDIWAVGCVLYELLTL-KRTFDATNPLRLAVKIVQGEYEDIDEQYSEEIIQLVHDCLHQ 239
                         250       260
                  ....*....|....*....|..
gi 2038291632 866 DRARRPhflqlqaHLEQLLTDP 887
Cdd:cd08221   240 DPEDRP-------TAEELLERP 254
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
629-839 1.29e-09

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: 60.87  E-value: 1.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVyrgALRFPSQDCKTVAIKTLKDTS--PDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFME 706
Cdd:cd05593    22 LLGKGTFGKV---ILVREKASGKYYAMKILKKEViiAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVN 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 707 NGALdAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTR-------LLDDFDG 779
Cdd:cd05593    99 GGEL-FFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKegitdaaTMKTFCG 177
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 780 TYEtqggkipirWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSI 839
Cdd:cd05593   178 TPE---------YLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELI 227
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
453-535 1.42e-09

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 55.97  E-value: 1.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 453 LRLVKKEPRQLELAWagSRPRTPGGN-LSYELHVLNQDE-EWHQM----VLEPRVLLTKLQPDTTYIVRVRTMTPLGPGP 526
Cdd:cd00063     7 LRVTDVTSTSVTLSW--TPPEDDGGPiTGYVVEYREKGSgDWKEVevtpGSETSYTLTGLKPGTEYEFRVRAVNGGGESP 84

                  ....*....
gi 2038291632 527 FSPDHEFRT 535
Cdd:cd00063    85 PSESVTVTT 93
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
620-879 1.45e-09

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK1 is widely expressed and is most abundant in the testis. In hyperosmotic or hypotonic low-chloride stress conditions, WNK1 is activated and it phosphorylates its substrates including SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. Mutations in WNK1 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK1 negates WNK4-mediated inhibition of the sodium-chloride cotransporter NCC and activates the epithelial sodium channel ENaC by activating SGK1. WNK1 also decreases the surface expression of renal outer medullary potassium channel (ROMK) by stimulating their endocytosis. Hypertension and hyperkalemia in PHAII patients with WNK1 mutations may be due partly to increased activity of NCC and ENaC, and impaired renal potassium secretion by ROMK, respectively. In addition, WNK1 interacts with MEKK2/3 and acts as an activator of extracellular signal-regulated kinase (ERK) 5. It also negatively regulates TGFbeta signaling. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK1 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: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 60.45  E-value: 1.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 620 DPTWLIVDTVIGEGEFGEVYRGALRFPSQDCKTVAIKTLKDTSPDGQwwNFLREATIMGQFNHPHILRL----EGVVTKR 695
Cdd:cd14030    23 DGRFLKFDIEIGRGSFKTVYKGLDTETTVEVAWCELQDRKLSKSERQ--RFKEEAGMLKGLQHPNIVRFydswESTVKGK 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 696 KPIMIVTEFMENGALDAFLKeREDQLAPGQLVAMLLGIASGMNYLSGHN--YVHRDLAARNILVN-QNLCCKVSDFGLTR 772
Cdd:cd14030   101 KCIVLVTELMTSGTLKTYLK-RFKVMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLAT 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 773 L-----LDDFDGTYEtqggkipirWTAPEAIAHRiFTTASDVWSFGIVMWEvLSFGDKPYGEMNN-QEVMKSIEEGYRlP 846
Cdd:cd14030   180 LkrasfAKSVIGTPE---------FMAPEMYEEK-YDESVDVYAFGMCMLE-MATSEYPYSECQNaAQIYRRVTSGVK-P 247
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2038291632 847 PPVDCPA--PLYELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd14030   248 ASFDKVAipEVKEIIEGCIRQNKDERYAIKDLLNH 282
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
629-843 1.47e-09

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: 59.69  E-value: 1.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRFPSqdcKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENG 708
Cdd:cd14083    10 VLGTGAFSEVVLAEDKATG---KLVAIKCIDKKALKGKEDSLENEIAVLRKIKHPNIVQLLDIYESKSHLYLVMELVTGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 AL------DAFLKEREDQLAPGQlvamllgIASGMNYLSGHNYVHRDLAARNILV---NQNLCCKVSDFGLTRLLDDfdG 779
Cdd:cd14083    87 ELfdriveKGSYTEKDASHLIRQ-------VLEAVDYLHSLGIVHRDLKPENLLYyspDEDSKIMISDFGLSKMEDS--G 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038291632 780 TYETQGGKiPiRWTAPEAIAHRIFTTASDVWSFGIVMWeVLSFGDKPYGEMNNQEVMKSIEEGY 843
Cdd:cd14083   158 VMSTACGT-P-GYVAPEVLAQKPYGKAVDCWSIGVISY-ILLCGYPPFYDENDSKLFAQILKAE 218
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
628-887 1.50e-09

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are three PIM2 isoforms resulting from alternative translation initiation sites. PIM2 is highly expressed in leukemia and lymphomas and has been shown to promote the survival and proliferation of tumor cells. The PIM2 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: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 59.86  E-value: 1.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 628 TVIGEGEFGEVYRGAlRFpsQDCKTVAIKTLKDTSPDGqwWNFL-------REATIM----GQFNHPHILRLEGVVTKRK 696
Cdd:cd14101     6 NLLGKGGFGTVYAGH-RI--SDGLQVAIKQISRNRVQQ--WSKLpgvnpvpNEVALLqsvgGGPGHRGVIRLLDWFEIPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 697 PIMIVTE-----------FMENGALDAFLKERedqlapgqlvaMLLGIASGMNYLSGHNYVHRDLAARNILVN-QNLCCK 764
Cdd:cd14101    81 GFLLVLErpqhcqdlfdyITERGALDESLARR-----------FFKQVVEAVQHCHSKGVVHRDIKDENILVDlRTGDIK 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 765 VSDFGLTRLL-----DDFDGTYEtqggkipirWTAPEAIA-HRIFTTASDVWSFGIVMWEVLSfGDKPYGEmnNQEVMKS 838
Cdd:cd14101   150 LIDFGSGATLkdsmyTDFDGTRV---------YSPPEWILyHQYHALPATVWSLGILLYDMVC-GDIPFER--DTDILKA 217
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2038291632 839 iEEGYRLPPPVDCPAplyeLMKNCWAYDRARRPhflqlqaHLEQLLTDP 887
Cdd:cd14101   218 -KPSFNKRVSNDCRS----LIRSCLAYNPSDRP-------SLEQILLHP 254
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
623-832 1.61e-09

Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK2 is widely expressed and has been shown to be epigenetically silenced in gliomas. It inhibits cell growth by acting as a negative regulator of MEK1-ERK1/2 signaling. WNK2 modulates growth factor-induced cancer cell proliferation, suggesting that it may be a tumor suppressor gene. WNKs comprise a subfamily of STKs with an unusual placement of the 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. The WNK2-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: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 59.71  E-value: 1.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 623 WLIVDTVIGEGEFGEVYRGalrFPSQDCKTVAIKTLKD---TSPDGQwwNFLREATIMGQFNHPHILRL----EGVVTKR 695
Cdd:cd14032     2 FLKFDIELGRGSFKTVYKG---LDTETWVEVAWCELQDrklTKVERQ--RFKEEAEMLKGLQHPNIVRFydfwESCAKGK 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 696 KPIMIVTEFMENGALDAFLKeREDQLAPGQLVAMLLGIASGMNYLSGHN--YVHRDLAARNILVN-QNLCCKVSDFGLTR 772
Cdd:cd14032    77 RCIVLVTELMTSGTLKTYLK-RFKVMKPKVLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLAT 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 773 LLddfDGTYETQGGKIPiRWTAPEAIAHRiFTTASDVWSFGIVMWEvLSFGDKPYGEMNN 832
Cdd:cd14032   156 LK---RASFAKSVIGTP-EFMAPEMYEEH-YDESVDVYAFGMCMLE-MATSEYPYSECQN 209
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
630-839 1.62e-09

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: 59.53  E-value: 1.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFPSQD--CKTVAIKTLKDTSPdgqwwnfLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMEN 707
Cdd:cd14108    10 IGRGAFSYLRRVKEKSSDLSfaAKFIPVRAKKKTSA-------RRELALLAELDHKSIVRFHDAFEKRRVVIIVTELCHE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GALDAFLkeREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILV--NQNLCCKVSDFGLTRLLDDFDGTYETQG 785
Cdd:cd14108    83 ELLERIT--KRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMadQKTDQVRICDFGNAQELTPNEPQYCKYG 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2038291632 786 gkIPiRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSI 839
Cdd:cd14108   161 --TP-EFVAPEIVNQSPVSKVTDIWPVGVIAYLCLT-GISPFVGENDRTTLMNI 210
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
682-842 1.72e-09

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: 60.27  E-value: 1.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 682 HPHILRLEGVVTKRKPIMIVTEFMENGALDAFLKEREdQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILV---N 758
Cdd:cd14180    60 HPNIVALHEVLHDQYHTYLVMELLRGGELLDRIKKKA-RFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYadeS 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 759 QNLCCKVSDFGLTRLLDDfdGTYETQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLS----FGDKPYGEMNNQ- 833
Cdd:cd14180   139 DGAVLKVIDFGFARLRPQ--GSRPLQTPCFTLQYAAPELFSNQGYDESCDLWSLGVILYTMLSgqvpFQSKRGKMFHNHa 216
                         170
                  ....*....|
gi 2038291632 834 -EVMKSIEEG 842
Cdd:cd14180   217 aDIMHKIKEG 226
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
630-821 2.09e-09

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: 60.08  E-value: 2.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRgALRFPSQDCKTVAIKTLKDTspdGQWWNFLREATIMGQFNHPHILRLEGVVTKR--KPIMIVTEFMEN 707
Cdd:cd07867    10 VGRGTYGHVYK-AKRKDGKDEKEYALKQIEGT---GISMSACREIALLRELKHPNVIALQKVFLSHsdRKVWLLFDYAEH 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GA--LDAFLKEREDQLAPGQL-----VAMLLGIASGMNYLSGHNYVHRDLAARNILV----NQNLCCKVSDFGLTRL--- 773
Cdd:cd07867    86 DLwhIIKFHRASKANKKPMQLprsmvKSLLYQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLfns 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2038291632 774 ----LDDFDGTYETqggkipIRWTAPE-AIAHRIFTTASDVWSFGIVMWEVLS 821
Cdd:cd07867   166 plkpLADLDPVVVT------FWYRAPElLLGARHYTKAIDIWAIGCIFAELLT 212
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
671-842 2.18e-09

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: 59.45  E-value: 2.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 671 LREATIMGQFNHPHILRL-EGVVTKRKPIMIVTEFMENGALDAFLKEREDQLAPGQLVAMLL-GIASGMNYLSGHNYVHR 748
Cdd:cd14109    44 MREVDIHNSLDHPNIVQMhDAYDDEKLAVTVIDNLASTIELVRDNLLPGKDYYTERQVAVFVrQLLLALKHMHDLGIAHL 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 749 DLAARNILVNQNLCCkVSDFGLTRLLDDFDGTYETQGgkIPiRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYG 828
Cdd:cd14109   124 DLRPEDILLQDDKLK-LADFGQSRRLLRGKLTTLIYG--SP-EFVSPEIVNSYPVTLATDMWSVGVLTYVLLG-GISPFL 198
                         170
                  ....*....|....
gi 2038291632 829 EMNNQEVMKSIEEG 842
Cdd:cd14109   199 GDNDRETLTNVRSG 212
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
615-820 2.75e-09

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: 60.06  E-value: 2.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 615 FAQELDPT-WLIVD-----TVIGEGEFGEV---YRGALRfpsqdcKTVAIKTLkdTSPDGQWWN---FLREATIMGQFNH 682
Cdd:cd07878     2 YRQELNKTvWEVPEryqnlTPVGSGAYGSVcsaYDTRLR------QKVAVKKL--SRPFQSLIHarrTYRELRLLKHMKH 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 683 PHILRLEGVVTKRKPI------MIVTEFMenGA-LDAFLKERedQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNI 755
Cdd:cd07878    74 ENVIGLLDVFTPATSIenfnevYLVTNLM--GAdLNNIVKCQ--KLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNV 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038291632 756 LVNQNLCCKVSDFGLTRLLDDfdgtyeTQGGKIPIRW-TAPEAIAHRI-FTTASDVWSFGIVMWEVL 820
Cdd:cd07878   150 AVNEDCELRILDFGLARQADD------EMTGYVATRWyRAPEIMLNWMhYNQTVDIWSVGCIMAELL 210
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
629-842 2.90e-09

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: 59.27  E-value: 2.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRFPSQ--DCKTVAIKTLKDTSPDGQWWNflrEATIMGQFNHPHILRLEGVVTKRKPIMIVTEFME 706
Cdd:cd05630     7 VLGKGGFGEVCACQVRATGKmyACKKLEKKRIKKRKGEAMALN---EKQILEKVNSRFVVSLAYAYETKDALCLVLTLMN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 707 NGALDAFLKER-EDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDfdgtYETQG 785
Cdd:cd05630    84 GGDLKFHIYHMgQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVPE----GQTIK 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2038291632 786 GKI-PIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGE----MNNQEVMKSIEEG 842
Cdd:cd05630   160 GRVgTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIA-GQSPFQQrkkkIKREEVERLVKEV 220
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
630-876 3.38e-09

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: 59.06  E-value: 3.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVY--RGALrfpsqDCKTVAIK--TLKDTSPDgQWWNFLREATIMGQFNHPHILR-----LEGVVTKRKPIMI 700
Cdd:cd14049    14 LGKGGYGKVYkvRNKL-----DGQYYAIKkiLIKKVTKR-DCMKVLREVKVLAGLQHPNIVGyhtawMEHVQLMLYIQMQ 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 701 VTEFMENGALDA---FLKEREDQLAPGQLV------AMLLGIASGMNYLSGHNYVHRDLAARNILVN-QNLCCKVSDFGL 770
Cdd:cd14049    88 LCELSLWDWIVErnkRPCEEEFKSAPYTPVdvdvttKILQQLLEGVTYIHSMGIVHRDLKPRNIFLHgSDIHVRIGDFGL 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 771 --TRLLDD---------FDGTYETQGGKIPIrWTAPEAIAHRIFTTASDVWSFGIVMWEVLsfgdKPYG-EMNNQEVMKS 838
Cdd:cd14049   168 acPDILQDgndsttmsrLNGLTHTSGVGTCL-YAAPEQLEGSHYDFKSDMYSIGVILLELF----QPFGtEMERAEVLTQ 242
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2038291632 839 IEEGyRLPPPVDCPAPLY-ELMKNCWAYDRARRPHFLQL 876
Cdd:cd14049   243 LRNG-QIPKSLCKRWPVQaKYIKLLTSTEPSERPSASQL 280
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
671-826 4.00e-09

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: 59.31  E-value: 4.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 671 LREATIMGQFNHPHILRLEGVVT---KR--KPIMIVTEFMengalDAFLKE--REDQ-LAPGQLVAMLLGIASGMNYLSG 742
Cdd:cd07858    52 LREIKLLRHLDHENVIAIKDIMPpphREafNDVYIVYELM-----DTDLHQiiRSSQtLSDDHCQYFLYQLLRGLKYIHS 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 743 HNYVHRDLAARNILVNQNLCCKVSDFGLTRLLD---DFDGTYetqggkIPIRW-TAPEAIAH-RIFTTASDVWSFGIVMW 817
Cdd:cd07858   127 ANVLHRDLKPSNLLLNANCDLKICDFGLARTTSekgDFMTEY------VVTRWyRAPELLLNcSEYTTAIDVWSVGCIFA 200

                  ....*....
gi 2038291632 818 EVLsfGDKP 826
Cdd:cd07858   201 ELL--GRKP 207
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
698-876 4.20e-09

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 60.03  E-value: 4.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 698 IMIVTEFMENGALDAFLKEREDQLAPGQL--VAMLL-GIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLL 774
Cdd:PTZ00267  140 LLLIMEYGSGGDLNKQIKQRLKEHLPFQEyeVGLLFyQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQY 219
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 775 DD---------FDGTyetqggkiPIrWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFgDKPYGEMNNQEVMKSIEEGYRL 845
Cdd:PTZ00267  220 SDsvsldvassFCGT--------PY-YLAPELWERKRYSKKADMWSLGVILYELLTL-HRPFKGPSQREIMQQVLYGKYD 289
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2038291632 846 PPPVDCPAPLYELMKNCWAYDRARRPHFLQL 876
Cdd:PTZ00267  290 PFPCPVSSGMKALLDPLLSKNPALRPTTQQL 320
fn3 pfam00041
Fibronectin type III domain;
334-425 4.42e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 54.34  E-value: 4.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 334 SAPQNLSFSA-SGTQLSLCWEPPRDTGGrHDIRYSVDCLQCRgiaqDGGPCQPcgkgvRFTPGasglTESTVQVEGLEPY 412
Cdd:pfam00041   1 SAPSNLTVTDvTSTSLTVSWTPPPDGNG-PITGYEVEYRPKN----SGEPWNE-----ITVPG----TTTSVTLTGLKPG 66
                          90
                  ....*....|...
gi 2038291632 413 ANYTFTIKSQNRV 425
Cdd:pfam00041  67 TEYEVRVQAVNGG 79
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
673-827 4.60e-09

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: 58.45  E-value: 4.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 673 EATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGALDAFLKeREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAA 752
Cdd:cd14113    53 ELGVLQSLQHPQLVGLLDTFETPTSYILVLEMADQGRLLDYVV-RWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKP 131
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038291632 753 RNILVNQNLC---CKVSDFGLTRLLDDFDGTYETQGGKipiRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPY 827
Cdd:cd14113   132 ENILVDQSLSkptIKLADFGDAVQLNTTYYIHQLLGSP---EFAAPEIILGNPVSLTSDLWSIGVLTYVLLS-GVSPF 205
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
629-919 5.10e-09

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: 58.96  E-value: 5.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRFPSQDCKTVAIKTL---------KDTSpdgqwwNFLREATIMGQFNHPHILRLEGVVTKRKPIM 699
Cdd:cd05584     3 VLGKGGYGKVFQVRKTTGSDKGKIFAMKVLkkasivrnqKDTA------HTKAERNILEAVKHPFIVDLHYAFQTGGKLY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 700 IVTEFMENGALDAFLkEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDG 779
Cdd:cd05584    77 LILEYLSGGELFMHL-EREGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLCKESIHDGT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 780 TYETQGGKipIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSIEEGYRLPPP---VDCPAPLY 856
Cdd:cd05584   156 VTHTFCGT--IEYMAPEILTRSGHGKAVDWWSLGALMYDMLT-GAPPFTAENRKKTIDKILKGKLNLPPyltNEARDLLK 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 857 ELMK--------NCWAYDRARRPHFLQLQAHLEQLLT---DP------HSLRTIANFDPRVTLRLPSLSGSDGIPYRSVS 919
Cdd:cd05584   233 KLLKrnvssrlgSGPGDAEEIKAHPFFRHINWDDLLAkkvEPpfkpllQSEEDVSQFDSKFTKQTPVDSPDDSTLSESAN 312
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
629-879 5.37e-09

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 and three PIM2 isoforms as a result of alternative translation initiation sites, while there is only one PIM3 protein. Compound knockout mice deficient of all three PIM kinases that survive the perinatal period show a profound reduction in body size, indicating that PIMs are important for body growth. The PIM 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: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 58.02  E-value: 5.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGalrFPSQDCKTVAIKTLkDTSPDGQWWN------------FLREATIMGqfnHPHILRLEGVVTKRK 696
Cdd:cd14005     7 LLGKGGFGTVYSG---VRIRDGLPVAVKFV-PKSRVTEWAMingpvpvpleiaLLLKASKPG---VPGVIRLLDWYERPD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 697 PIMIVTEFMENGA-LDAFLKER---EDQLAP---GQLVAMLLGIASgmnylsgHNYVHRDLAARNILVNQN-LCCKVSDF 768
Cdd:cd14005    80 GFLLIMERPEPCQdLFDFITERgalSENLARiifRQVVEAVRHCHQ-------RGVLHRDIKDENLLINLRtGEVKLIDF 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 769 GLTRLL-----DDFDGTYEtqggkipirWTAPEAIAHRIF-TTASDVWSFGIVMWEVLsFGDKPYgeMNNQEVMKsieeG 842
Cdd:cd14005   153 GCGALLkdsvyTDFDGTRV---------YSPPEWIRHGRYhGRPATVWSLGILLYDML-CGDIPF--ENDEQILR----G 216
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2038291632 843 YRLPPPVDCPApLYELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd14005   217 NVLFRPRLSKE-CCDLISRCLQFDPSKRPSLEQILSH 252
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
668-842 5.46e-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: 58.85  E-value: 5.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 668 WNFLREATI--MGQfNHPHILRLEGVVTKRKPIMIVTEFMENGALDAFLKEREdQLAPGQLVAMLLGIASGMNYLSGHNY 745
Cdd:cd14092    43 LDTSREVQLlrLCQ-GHPNIVKLHEVFQDELHTYLVMELLRGGELLERIRKKK-RFTESEASRIMRQLVSAVSFMHSKGV 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 746 VHRDLAARNILV---NQNLCCKVSDFGLTRLLDdfdgtyETQGGKIP---IRWTAPEAIAHRIFTT----ASDVWSFGIV 815
Cdd:cd14092   121 VHRDLKPENLLFtdeDDDAEIKIVDFGFARLKP------ENQPLKTPcftLPYAAPEVLKQALSTQgydeSCDLWSLGVI 194
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2038291632 816 MWEVLSfGDKPY----GEMNNQEVMKSIEEG 842
Cdd:cd14092   195 LYTMLS-GQVPFqspsRNESAAEIMKRIKSG 224
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
628-820 7.38e-09

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: 58.39  E-value: 7.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 628 TVIGEGEFGEVyrgalRFpSQDCKT---VAIKTLK--DTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVT 702
Cdd:cd05599     7 KVIGRGAFGEV-----RL-VRKKDTghvYAMKKLRksEMLEKEQVAHVRAERDILAEADNPWVVKLYYSFQDEENLYLIM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 703 EFMENGALDAFLKeREDQLAPGQ---LVA-MLLGIASgmnyLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFD 778
Cdd:cd05599    81 EFLPGGDMMTLLM-KKDTLTEEEtrfYIAeTVLAIES----IHKLGYIHRDIKPDNLLLDARGHIKLSDFGLCTGLKKSH 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2038291632 779 GTYETQGgkIPiRWTAPEAIAHRIFTTASDVWSFGIVMWEVL 820
Cdd:cd05599   156 LAYSTVG--TP-DYIAPEVFLQKGYGKECDWWSLGVIMYEML 194
SAM_caskin1,2_repeat1 cd09497
SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 ...
918-971 7.96e-09

SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 proteins is a protein-protein interaction domain. Caskin has two tandem SAM domains. Caskin protein is known to interact with membrane-associated guanylate kinase CASK, and apparently may play a role in neural development, synaptic protein targeting, and regulation of gene expression.


Pssm-ID: 188896  Cd Length: 66  Bit Score: 52.65  E-value: 7.96e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2038291632 918 VSEWLESIRMKRYILHFRSAGLDtMECVLELTAEDLTQMGITLPGHQKRILCSI 971
Cdd:cd09497     7 IFDWLREFGLEEYTPNFIKAGYD-LPTISRMTPEDLTAIGITKPGHRKKLKSEI 59
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
672-827 8.14e-09

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: 58.38  E-value: 8.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 672 REATIMGQFNHPHILRLEGVVTKR------KPIMIVTEFMENGaldaFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNY 745
Cdd:cd07879    63 RELTLLKHMQHENVIGLLDVFTSAvsgdefQDFYLVMPYMQTD----LQKIMGHPLSEDKVQYLVYQMLCGLKYIHSAGI 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 746 VHRDLAARNILVNQNLCCKVSDFGLTRLLDdfdgtyETQGGKIPIRW-TAPEAIAHRI-FTTASDVWSFGIVMWEVLS-- 821
Cdd:cd07879   139 IHRDLKPGNLAVNEDCELKILDFGLARHAD------AEMTGYVVTRWyRAPEVILNWMhYNQTVDIWSVGCIMAEMLTgk 212

                  ....*...
gi 2038291632 822 --FGDKPY 827
Cdd:cd07879   213 tlFKGKDY 220
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
733-841 8.56e-09

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: 58.47  E-value: 8.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 733 IASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLlDDFDGTYETQGGKIPiRWTAPEAIAHRIFTTASDVWSF 812
Cdd:cd05616   110 IAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKE-NIWDGVTTKTFCGTP-DYIAPEIIAYQPYGKSVDWWAF 187
                          90       100
                  ....*....|....*....|....*....
gi 2038291632 813 GIVMWEVLSfGDKPYGEMNNQEVMKSIEE 841
Cdd:cd05616   188 GVLLYEMLA-GQAPFEGEDEDELFQSIME 215
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
629-880 1.00e-08

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: 58.06  E-value: 1.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRfpsQDCKTVAIKTLKDTS--PDGQWWNFLREATIM-GQFNHPHILRLEGVVTKRKPIMIVTEFM 705
Cdd:cd05603     2 VIGKGSFGKVLLAKRK---CDGKFYAVKVLQKKTilKKKEQNHIMAERNVLlKNLKHPFLVGLHYSFQTSEKLYFVLDYV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 706 ENGALDAFLkEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYETQG 785
Cdd:cd05603    79 NGGELFFHL-QRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKEGMEPEETTSTFC 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 786 GKiPiRWTAPEAIAHRIFTTASDVWSFGIVMWEVLsFGDKPYGEMNNQEVMKSI-EEGYRLPPPVDCPAplYELMKNCWA 864
Cdd:cd05603   158 GT-P-EYLAPEVLRKEPYDRTVDWWCLGAVLYEML-YGLPPFYSRDVSQMYDNIlHKPLHLPGGKTVAA--CDLLQGLLH 232
                         250       260
                  ....*....|....*....|
gi 2038291632 865 YDRARR----PHFLQLQAHL 880
Cdd:cd05603   233 KDQRRRlgakADFLEIKNHV 252
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
633-821 1.05e-08

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: 57.73  E-value: 1.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 633 GEFGEVYRGALRfpsQDCKTVAIKTLKDTspdgQWWNFLREATIMGQFNHPHILRLegVVTKRK------PIMIVTEFME 706
Cdd:cd14140     6 GRFGCVWKAQLM---NEYVAVKIFPIQDK----QSWQSEREIFSTPGMKHENLLQF--IAAEKRgsnlemELWLITAFHD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 707 NGALDAFLKEreDQLAPGQLVAMLLGIASGMNYL---------SGHN--YVHRDLAARNILVNQNLCCKVSDFGLTRLLD 775
Cdd:cd14140    77 KGSLTDYLKG--NIVSWNELCHIAETMARGLSYLhedvprckgEGHKpaIAHRDFKSKNVLLKNDLTAVLADFGLAVRFE 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2038291632 776 DFDGTYETQGGKIPIRWTAPEAIAHRI-FTTAS----DVWSFGIVMWEVLS 821
Cdd:cd14140   155 PGKPPGDTHGQVGTRRYMAPEVLEGAInFQRDSflriDMYAMGLVLWELVS 205
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
629-839 1.18e-08

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: 57.99  E-value: 1.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRfpsQDCKTVAIKTLKDTS--PDGQWWNFLREATIMG-QFNHPHILRLEGVVTKRKPIMIVTEFM 705
Cdd:cd05590     2 VLGKGSFGKVMLARLK---ESGRLYAVKVLKKDVilQDDDVECTMTEKRILSlARNHPFLTQLYCCFQTPDRLFFVMEFV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 706 ENGALDAFL-KEREDQLAPGQLVAMllGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRlLDDFDGTYETQ 784
Cdd:cd05590    79 NGGDLMFHIqKSRRFDEARARFYAA--EITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCK-EGIFNGKTTST 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2038291632 785 GGKIPiRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSI 839
Cdd:cd05590   156 FCGTP-DYIAPEILQEMLYGPSVDWWAMGVLLYEMLC-GHAPFEAENEDDLFEAI 208
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
683-879 1.42e-08

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 2 (MAPKAP2 or MK2) 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. MK2 is a bonafide substrate for the MAPK p38. It is closely related to MK3 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. The MK2 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: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 57.35  E-value: 1.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 683 PHILRL----EGVVTKRKPIMIVTEFMENGALDAFLKEREDQ-LAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILV 757
Cdd:cd14170    55 PHIVRIvdvyENLYAGRKCLLIVMECLDGGELFSRIQDRGDQaFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLY 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 758 NQ---NLCCKVSDFGLTRllddfdGTYETQGGKIPIR---WTAPEAIAHRIFTTASDVWSFGIVMWeVLSFGDKPY---- 827
Cdd:cd14170   135 TSkrpNAILKLTDFGFAK------ETTSHNSLTTPCYtpyYVAPEVLGPEKYDKSCDMWSLGVIMY-ILLCGYPPFysnh 207
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2038291632 828 GEMNNQEVMKSIEEG-YRLPPP--VDCPAPLYELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd14170   208 GLAISPGMKTRIRMGqYEFPNPewSEVSEEVKMLIRNLLKTEPTQRMTITEFMNH 262
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
626-879 1.63e-08

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 isoforms resulting from alternative translation initiation sites. PIM1 is the founding member of the PIM subfamily. It is involved in regulating cell growth, differentiation, and apoptosis. It promotes cancer development when overexpressed by inhibiting apoptosis, promoting cell proliferation, and promoting genomic instability. The PIM1 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: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 56.52  E-value: 1.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 626 VDTVIGEGEFGEVYRGaLRFpsQDCKTVAIKTL-KDTSPDgqwWNFLREAT---------------------IMGQFNHP 683
Cdd:cd14100     4 VGPLLGSGGFGSVYSG-IRV--ADGAPVAIKHVeKDRVSE---WGELPNGTrvpmeivllkkvgsgfrgvirLLDWFERP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 684 HILRLegVVTKRKPIMIVTEFM-ENGALdaflkerEDQLAPGQLVAMLLGIASGMNylSGhnYVHRDLAARNILVNQNLC 762
Cdd:cd14100    78 DSFVL--VLERPEPVQDLFDFItERGAL-------PEELARSFFRQVLEAVRHCHN--CG--VLHRDIKDENILIDLNTG 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 763 -CKVSDFGLTRLLDD-----FDGTYEtqggkipirWTAPEAIA-HRIFTTASDVWSFGIVMWEVLSfGDKPYGEmnNQEV 835
Cdd:cd14100   145 eLKLIDFGSGALLKDtvytdFDGTRV---------YSPPEWIRfHRYHGRSAAVWSLGILLYDMVC-GDIPFEH--DEEI 212
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2038291632 836 MKSiEEGYRLPPPVDCPaplyELMKNCWAYDRARRPHFLQLQAH 879
Cdd:cd14100   213 IRG-QVFFRQRVSSECQ----HLIKWCLALRPSDRPSFEDIQNH 251
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
672-820 1.70e-08

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK3 is expressed primarily in the brain, and to a lesser extent in the heart and testis. Mice deficient in JNK3 are protected against kainic acid-induced seizures, stroke, sciatic axotomy neural death, and neuronal death due to NGF deprivation, oxidative stress, or exposure to beta-amyloid peptide. This suggests that JNK3 may play roles in the pathogenesis of these diseases. 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 JNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 57.79  E-value: 1.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 672 REATIMGQFNHPHILRLEGVVTKRKP------IMIVTEFMENGALDAFLKEREDQLAPGQLVAMLLGIasgmNYLSGHNY 745
Cdd:cd07874    65 RELVLMKCVNHKNIISLLNVFTPQKSleefqdVYLVMELMDANLCQVIQMELDHERMSYLLYQMLCGI----KHLHSAGI 140
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2038291632 746 VHRDLAARNILVNQNLCCKVSDFGLTRLLddfdGTYETQGGKIPIR-WTAPEAIAHRIFTTASDVWSFGIVMWEVL 820
Cdd:cd07874   141 IHRDLKPSNIVVKSDCTLKILDFGLARTA----GTSFMMTPYVVTRyYRAPEVILGMGYKENVDIWSVGCIMGEMV 212
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
672-823 1.86e-08

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK1 is expressed in every cell and tissue type. It specifically binds with JAMP (JNK1-associated membrane protein), which regulates the duration of JNK1 activity in response to stimuli. Specific JNK1 substrates include Itch and SG10, which are implicated in Th2 responses and airway inflammation, and microtubule dynamics and axodendritic length, respectively. Mice deficient in JNK1 are protected against arthritis, obesity, type 2 diabetes, cardiac cell death, and non-alcoholic liver disease, suggesting that JNK1 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 that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 57.36  E-value: 1.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 672 REATIMGQFNHPHILRLEGVVTKRKP------IMIVTEFMENGALDAFLKEREDQLAPGQLVAMLLGIasgmNYLSGHNY 745
Cdd:cd07875    72 RELVLMKCVNHKNIIGLLNVFTPQKSleefqdVYIVMELMDANLCQVIQMELDHERMSYLLYQMLCGI----KHLHSAGI 147
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2038291632 746 VHRDLAARNILVNQNLCCKVSDFGLTRLLddfdGTYETQGGKIPIR-WTAPEAIAHRIFTTASDVWSFGIVMWEVLSFG 823
Cdd:cd07875   148 IHRDLKPSNIVVKSDCTLKILDFGLARTA----GTSFMMTPYVVTRyYRAPEVILGMGYKENVDIWSVGCIMGEMIKGG 222
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
629-841 2.26e-08

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: 56.93  E-value: 2.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRFPSQdckTVAIKTLKD--TSPDGQWWNFLREATIMGQFNHPHIL-RLEGVVTKRKPIMIVTEFM 705
Cdd:cd05615    17 VLGKGSFGKVMLAERKGSDE---LYAIKILKKdvVIQDDDVECTMVEKRVLALQDKPPFLtQLHSCFQTVDRLYFVMEYV 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 706 ENGALDAFLKEREDQLAPgQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLlDDFDGTYETQG 785
Cdd:cd05615    94 NGGDLMYHIQQVGKFKEP-QAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCKE-HMVEGVTTRTF 171
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2038291632 786 GKIPiRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSIEE 841
Cdd:cd05615   172 CGTP-DYIAPEIIAYQPYGRSVDWWAYGVLLYEMLA-GQPPFDGEDEDELFQSIME 225
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
672-827 2.44e-08

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: 56.21  E-value: 2.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 672 REATIMGQFNHPHILRLEGVV--TKRKPIMIVTEFMENGAL--DAFLKEREDQLAPGQLVAMLLGIasgmNYLSGHNYVH 747
Cdd:cd14118    63 REIAILKKLDHPNVVKLVEVLddPNEDNLYMVFELVDKGAVmeVPTDNPLSEETARSYFRDIVLGI----EYLHYQKIIH 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 748 RDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYETQGGKIPIRwtAPEAIA---HRIFTTASDVWSFGIVMWeVLSFGD 824
Cdd:cd14118   139 RDIKPSNLLLGDDGHVKIADFGVSNEFEGDDALLSSTAGTPAFM--APEALSesrKKFSGKALDIWAMGVTLY-CFVFGR 215

                  ...
gi 2038291632 825 KPY 827
Cdd:cd14118   216 CPF 218
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
650-849 2.59e-08

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 56.02  E-value: 2.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 650 CKTVAIKTlkdtspdgqwWNFLrE---ATIMGqfNHPHILRLEGVVTKRKPIMIVTEFMENGALDAFLKeREDQLAPGQL 726
Cdd:PHA03390   46 QKIIKAKN----------FNAI-EpmvHQLMK--DNPNFIKLYYSVTTLKGHVLIMDYIKDGDLFDLLK-KEGKLSEAEV 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 727 VAMLLGIASGMNYLSGHNYVHRDLAARNILVNQN-----LCckvsDFGLTRLLDD---FDGTYEtqggkipirWTAPEAI 798
Cdd:PHA03390  112 KKIIRQLVEALNDLHKHNIIHNDIKLENVLYDRAkdriyLC----DYGLCKIIGTpscYDGTLD---------YFSPEKI 178
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2038291632 799 AHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMNNQEV-MKSIEEGYRLPPPV 849
Cdd:PHA03390  179 KGHNYDVSFDWWAVGVLTYELLT-GKHPFKEDEDEELdLESLLKRQQKKLPF 229
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
595-834 2.91e-08

Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-beta is expressed ubiquitously in many tissues. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-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. This alignment model includes the dimerization domain.


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 57.33  E-value: 2.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 595 WLKPYVDL----QAYEDpaqgalDFAqeldptwliVDTVIGEGEFGEVyrGALRFPSQDcKTVAIKTLKDtspdgqwWNF 670
Cdd:cd05624    56 WAKPFTQLvkemQLHRD------DFE---------IIKVIGRGAFGEV--AVVKMKNTE-RIYAMKILNK-------WEM 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 671 LREA---------TIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGALDAFLKEREDQL----APGQLVAMLLGIASgm 737
Cdd:cd05624   111 LKRAetacfreerNVLVNGDCQWITTLHYAFQDENYLYLVMDYYVGGDLLTLLSKFEDKLpedmARFYIGEMVLAIHS-- 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 738 nyLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDfDGTYETQGGKIPIRWTAPEAI-----AHRIFTTASDVWSF 812
Cdd:cd05624   189 --IHQLHYVHRDIKPDNVLLDMNGHIRLADFGSCLKMND-DGTVQSSVAVGTPDYISPEILqamedGMGKYGPECDWWSL 265
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2038291632 813 GIVMWEVLsFGDKP---------YGEMNNQE 834
Cdd:cd05624   266 GVCMYEML-YGETPfyaeslvetYGKIMNHE 295
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
629-841 3.10e-08

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: 56.52  E-value: 3.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRFPSQ--DCKTVAIKTLKDTSPDGQWWNflrEATIMGQFNHPHILRLEGVVTKRKPIMIVTEFME 706
Cdd:cd05632     9 VLGKGGFGEVCACQVRATGKmyACKRLEKKRIKKRKGESMALN---EKQILEKVNSQFVVNLAYAYETKDALCLVLTIMN 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 707 NGALDAFLKEREDqlaPG----QLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDgtyE 782
Cdd:cd05632    86 GGDLKFHIYNMGN---PGfeeeRALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVKIPEGE---S 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038291632 783 TQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPY----GEMNNQEVMKSIEE 841
Cdd:cd05632   160 IRGRVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIE-GQSPFrgrkEKVKREEVDRRVLE 221
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
629-820 3.10e-08

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 57.35  E-value: 3.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRFPSQDcktVAIKTLKDtspDGQWWNflREATIMGQFNHPHILRL------EGVVTKRKPIM--I 700
Cdd:PTZ00036   73 IIGNGSFGVVYEAICIDTSEK---VAIKKVLQ---DPQYKN--RELLIMKNLNHINIIFLkdyyytECFKKNEKNIFlnV 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 701 VTEFMENgALDAFLK--EREDQLAPGQLVAML-LGIASGMNYLSGHNYVHRDLAARNILVNQNL-CCKVSDFGLTRLLdd 776
Cdd:PTZ00036  145 VMEFIPQ-TVHKYMKhyARNNHALPLFLVKLYsYQLCRALAYIHSKFICHRDLKPQNLLIDPNThTLKLCDFGSAKNL-- 221
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2038291632 777 fdgtyetQGGKIPIRWT------APE-AIAHRIFTTASDVWSFGIVMWEVL 820
Cdd:PTZ00036  222 -------LAGQRSVSYIcsrfyrAPElMLGATNYTTHIDLWSLGCIIAEMI 265
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
672-837 3.11e-08

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: 56.88  E-value: 3.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 672 REATIMGQFNHPHILRLEGVVT------KRKPIMIVTEFM--ENGALDAFLKEREDQLApgQLVAMLLgiaSGMNYLSGH 743
Cdd:cd07880    63 RELRLLKHMKHENVIGLLDVFTpdlsldRFHDFYLVMPFMgtDLGKLMKHEKLSEDRIQ--FLVYQML---KGLKYIHAA 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 744 NYVHRDLAARNILVNQNLCCKVSDFGLTRLLDdfdgtyETQGGKIPIRW-TAPEAIAHRI-FTTASDVWSFGIVMWEVLS 821
Cdd:cd07880   138 GIIHRDLKPGNLAVNEDCELKILDFGLARQTD------SEMTGYVVTRWyRAPEVILNWMhYTQTVDIWSVGCIMAEMLT 211
                         170       180
                  ....*....|....*....|.
gi 2038291632 822 fgDKPYGEMNNQ-----EVMK 837
Cdd:cd07880   212 --GKPLFKGHDHldqlmEIMK 230
SAM_Ship2 cd09491
SAM domain of Ship2 lipid phosphatase proteins; SAM (sterile alpha motif) domain of Ship2 ...
912-972 3.24e-08

SAM domain of Ship2 lipid phosphatase proteins; SAM (sterile alpha motif) domain of Ship2 subfamily is a protein-protein interaction domain. Ship2 proteins are lipid phosphatases (Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2) containing an N-terminal SH2 domain, a central phosphatase domain and a C-terminal SAM domain. Ship2 is involved in a number of PI3K signaling pathways. For example, it plays a role in regulation of the actin cytoskeleton remodeling, in insulin signaling pathways, and in EphA2 receptor endocytosis. SAM domain of Ship2 can interact with SAM domain of other proteins in these pathways, thus participating in signal transduction. In particular, SAM of Ship2 is known to form heterodimers with SAM domain of Eph-A2 receptor tyrosine kinase during receptor endocytosis as well as with SAM domain of PI3K effector protein Arap3 in the actin cytoskeleton signaling network. Since Ship2 plays a role in negatively regulating insulin signaling, it has been suggested that inhibition of its expression or function may contribute in treating type 2 diabetes and obesity-induced insulin resistance.


Pssm-ID: 188890  Cd Length: 63  Bit Score: 50.98  E-value: 3.24e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2038291632 912 GIPYRSVSEWLESIRMKRYILHFRSAGLDTMECVLELTAEDLTQMGITLPGHQKRILCSIQ 972
Cdd:cd09491     2 LSWPKTVSEWLMNLGLQQYEEGLMHNGWDSLEFLSDITEEDLEEAGVTNPAHKRRLLDSLQ 62
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
671-842 3.26e-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: 3.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 671 LREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGALDAFLKEReDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDL 750
Cdd:cd14110    47 LREYQVLRRLSHPRIAQLHSAYLSPRHLVLIEELCSGPELLYNLAER-NSYSEAEVTDYLWQILSAVDYLHSRRILHLDL 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 751 AARNILVNQNLCCKVSDFGLTRLLddfdgtyeTQGGKIP-------IRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfG 823
Cdd:cd14110   126 RSENMIITEKNLLKIVDLGNAQPF--------NQGKVLMtdkkgdyVETMAPELLEGQGAGPQTDIWAIGVTAFIMLS-A 196
                         170
                  ....*....|....*....
gi 2038291632 824 DKPYGEMNNQEVMKSIEEG 842
Cdd:cd14110   197 DYPVSSDLNWERDRNIRKG 215
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
629-821 3.32e-08

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: 56.24  E-value: 3.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRFPSQdckTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENG 708
Cdd:cd07844     7 KLGEGSYATVYKGRSKLTGQ---LVALKEIRLEHEEGAPFTAIREASLLKDLKHANIVTLHDIIHTKKTLTLVFEYLDTD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 aLDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYETQggkI 788
Cdd:cd07844    84 -LKQYMDDCGGGLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLARAKSVPSKTYSNE---V 159
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2038291632 789 PIRWTAPEAI--AHRIFTTASDVWSFGIVMWEVLS 821
Cdd:cd07844   160 VTLWYRPPDVllGSTEYSTSLDMWGVGCIFYEMAT 194
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
629-827 3.52e-08

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: 56.07  E-value: 3.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRFPSQ--DCKTVAIKTLKDTSPDGQwwnFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFME 706
Cdd:cd05607     9 VLGKGGFGEVCAVQVKNTGQmyACKKLDKKRLKKKSGEKM---ALLEKEILEKVNSPFIVSLAYAFETKTHLCLVMSLMN 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 707 NGALDAFLKE-REDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYETQG 785
Cdd:cd05607    86 GGDLKYHIYNvGERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVEVKEGKPITQRAG 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2038291632 786 GKipiRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPY 827
Cdd:cd05607   166 TN---GYMAPEILKEESYSYPVDWFAMGCSIYEMVA-GRTPF 203
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
630-827 3.68e-08

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 56.36  E-value: 3.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 630 IGEGEFGEVYRGALRFPSQdckTVAIKTLK--DTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMEN 707
Cdd:PTZ00263   26 LGTGSFGRVRIAKHKGTGE---YYAIKCLKkrEILKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFLLEFVVG 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 708 GALdaFLKEREDQLAPGQLVAMLLG-IASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDdfDGTYETQGg 786
Cdd:PTZ00263  103 GEL--FTHLRKAGRFPNDVAKFYHAeLVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVP--DRTFTLCG- 177
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2038291632 787 kIPiRWTAPEAIAHRIFTTASDVWSFGIVMWEVLS-----FGDKPY 827
Cdd:PTZ00263  178 -TP-EYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAgyppfFDDTPF 221
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
669-861 4.10e-08

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: 56.03  E-value: 4.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 669 NFLREATIMGQ-FNHPHILRLEGVVTKRKPIMIVTEFMENGALDAFLKEREDQLAPGQLVA-MLLGIASGMNYLSGHNYV 746
Cdd:cd08226    44 KALQNEVVLSHfFRHPNIMTHWTVFTEGSWLWVISPFMAYGSARGLLKTYFPEGMNEALIGnILYGAIKALNYLHQNGCI 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 747 HRDLAARNILVN----------QNLCCKVSDFGLTRLLDDFDgtyETQGGKIPirWTAPEAIAHRI--FTTASDVWSFGI 814
Cdd:cd08226   124 HRSVKASHILISgdglvslsglSHLYSMVTNGQRSKVVYDFP---QFSTSVLP--WLSPELLRQDLhgYNVKSDIYSVGI 198
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2038291632 815 VMWEvLSFGDKPYGEMN-NQEVMKSIEEGYRLPPPVDCPAPLYELMKN 861
Cdd:cd08226   199 TACE-LARGQVPFQDMRrTQMLLQKLKGPPYSPLDIFPFPELESRMKN 245
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
629-879 4.11e-08

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: 55.47  E-value: 4.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYrgaLRFPSQDCKTVAIKTLK---DTSPDGQWWNFLR-EATIMGQFNHPHILRLEGVVTKR--KPIMIVT 702
Cdd:cd06651    14 LLGQGAFGRVY---LCYDVDTGRELAAKQVQfdpESPETSKEVSALEcEIQLLKNLQHERIVQYYGCLRDRaeKTLTIFM 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 703 EFMENGALdaflkerEDQL-APGQLVAMLL-----GIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDD 776
Cdd:cd06651    91 EYMPGGSV-------KDQLkAYGALTESVTrkytrQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQT 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 777 --FDGTYETQGGKIPIrWTAPEAIAHRIFTTASDVWSFGIVMWEVLSfGDKPYGEMnnqEVMKSIEEGYRLPPPVDCPAP 854
Cdd:cd06651   164 icMSGTGIRSVTGTPY-WMSPEVISGEGYGRKADVWSLGCTVVEMLT-EKPPWAEY---EAMAAIFKIATQPTNPQLPSH 238
                         250       260
                  ....*....|....*....|....*...
gi 2038291632 855 LYELMKN---CWAYDRARRPHFLQLQAH 879
Cdd:cd06651   239 ISEHARDflgCIFVEARHRPSAEELLRH 266
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
333-424 4.41e-08

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 51.73  E-value: 4.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 333 PSAPQNLSFSA-SGTQLSLCWEPPRDTGGRHDiRYSVDCLQCrgiaqDGGPCQPCGKGVrftpgasgLTESTVQVEGLEP 411
Cdd:cd00063     1 PSPPTNLRVTDvTSTSVTLSWTPPEDDGGPIT-GYVVEYREK-----GSGDWKEVEVTP--------GSETSYTLTGLKP 66
                          90
                  ....*....|...
gi 2038291632 412 YANYTFTIKSQNR 424
Cdd:cd00063    67 GTEYEFRVRAVNG 79
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
333-425 4.95e-08

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 51.08  E-value: 4.95e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632  333 PSAPQNLSFSA-SGTQLSLCWEPPRDTGGRHDI-RYSVdclqcrgiaqdggpcQPCGKGVRFTPGASGLTESTVQVEGLE 410
Cdd:smart00060   1 PSPPSNLRVTDvTSTSVTLSWEPPPDDGITGYIvGYRV---------------EYREEGSEWKEVNVTPSSTSYTLTGLK 65
                           90
                   ....*....|....*
gi 2038291632  411 PYANYTFTIKSQNRV 425
Cdd:smart00060  66 PGTEYEFRVRAVNGA 80
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
672-836 5.71e-08

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein 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. They are also essential regulators of physiological and pathological processes and are involved in the pathogenesis of several diseases such as diabetes, atherosclerosis, stroke, Parkinson's and Alzheimer's. Vetebrates harbor three different JNK genes (Jnk1, Jnk2, and Jnk3) that are alternatively spliced to produce at least 10 isoforms. JNKs are specifically activated by the MAPK kinases MKK4 and MKK7, which are in turn activated by upstream MAPK kinase kinases as a result of different stimuli including stresses such as ultraviolet (UV) irradiation, hyperosmolarity, heat shock, or cytokines. JNKs activate a large number of different substrates based on specific stimulus, cell type, and cellular condition, and may be implicated in seemingly contradictory functions. The JNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 55.88  E-value: 5.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 672 REATIMGQFNHPHILRLEGVVTKRKP------IMIVTEFMengalDAFL---------KEREDQLapgqLVAMLLGIasg 736
Cdd:cd07850    48 RELVLMKLVNHKNIIGLLNVFTPQKSleefqdVYLVMELM-----DANLcqviqmdldHERMSYL----LYQMLCGI--- 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 737 mNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLlddfDGTYETQGGKIPIR-WTAPEAIAHRIFTTASDVWSFGIV 815
Cdd:cd07850   116 -KHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLART----AGTSFMMTPYVVTRyYRAPEVILGMGYKENVDIWSVGCI 190
                         170       180
                  ....*....|....*....|.
gi 2038291632 816 MwevlsfgdkpyGEMNNQEVM 836
Cdd:cd07850   191 M-----------GEMIRGTVL 200
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
673-818 8.85e-08

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 55.67  E-value: 8.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 673 EATIMGQFNHPHILRLEGV-VTKRKPIMIVTEFMENgaLDAFLKEREDQLAPGQLVAMLLGIASGMNYLSGHNYVHRDLA 751
Cdd:PHA03211  210 EARLLRRLSHPAVLALLDVrVVGGLTCLVLPKYRSD--LYTYLGARLRPLGLAQVTAVARQLLSAIDYIHGEGIIHRDIK 287
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2038291632 752 ARNILVN--QNLCckVSDFGLTRLLDDFDGTYETQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWE 818
Cdd:PHA03211  288 TENVLVNgpEDIC--LGDFGAACFARGSWSTPFHYGIAGTVDTNAPEVLAGDPYTPSVDIWSAGLVIFE 354
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
629-911 9.02e-08

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: 54.95  E-value: 9.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRFPSQdckTVAIKTLKDTS---PDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFM 705
Cdd:cd05620     2 VLGKGSFGKVLLAELKGKGE---YFAVKALKKDVvliDDDVECTMVEKRVLALAWENPFLTHLYCTFQTKEHLFFVMEFL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 706 ENGALDAFLKER-EDQLAPGQLVAMllGIASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYETQ 784
Cdd:cd05620    79 NGGDLMFHIQDKgRFDLYRATFYAA--EIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKENVFGDNRASTF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 785 GGKiPiRWTAPEAIAHRIFTTASDVWSFGIVMWEVLsFGDKPYGEMNNQEVMKSIEegyrlpppVDCPA-PLY------E 857
Cdd:cd05620   157 CGT-P-DYIAPEILQGLKYTFSVDWWSFGVLLYEML-IGQSPFHGDDEDELFESIR--------VDTPHyPRWitkeskD 225
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2038291632 858 LMKNCWAYDRARR----------PHFLQLQ-AHLEQLLTDP------HSLRTIANFDPRVTLRLPSLSGSD 911
Cdd:cd05620   226 ILEKLFERDPTRRlgvvgnirghPFFKTINwTALEKRELDPpfkpkvKSPSDYSNFDREFLSEKPRLSYSD 296
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
733-841 9.53e-08

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: 54.91  E-value: 9.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 733 IASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTR--LLDD-----FDGTYEtqggkipirWTAPEAIAHRIFTT 805
Cdd:cd05570   105 ICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMCKegIWGGnttstFCGTPD---------YIAPEILREQDYGF 175
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2038291632 806 ASDVWSFGIVMWEVLSfGDKPYGEMNNQEVMKSIEE 841
Cdd:cd05570   176 SVDWWALGVLLYEMLA-GQSPFEGDDEDELFEAILN 210
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
672-820 9.76e-08

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: 55.42  E-value: 9.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 672 REATIMGQFNHPHILRLEGVVTKRKP------IMIVTEFMENGALDAFLKEREDQlapgQLVAMLLGIASGMNYLSGHNY 745
Cdd:cd07876    69 RELVLLKCVNHKNIISLLNVFTPQKSleefqdVYLVMELMDANLCQVIHMELDHE----RMSYLLYQMLCGIKHLHSAGI 144
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2038291632 746 VHRDLAARNILVNQNLCCKVSDFGLTRllddfdgTYETQGGKIPIRWT----APEAIAHRIFTTASDVWSFGIVMWEVL 820
Cdd:cd07876   145 IHRDLKPSNIVVKSDCTLKILDFGLAR-------TACTNFMMTPYVVTryyrAPEVILGMGYKENVDIWSVGCIMGELV 216
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
629-846 1.05e-07

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: 54.72  E-value: 1.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRgALRFPSQDCKTVAIKTLKDTSPDGQWWNFLREATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENG 708
Cdd:cd14209     8 TLGTGSFGRVML-VRHKETGNYYAMKILDKQKVVKLKQVEHTLNEKRILQAINFPFLVKLEYSFKDNSNLYMVMEYVPGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 709 ALDAFLK------EREDQLAPGQLVAMLlgiasgmNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDD----FD 778
Cdd:cd14209    87 EMFSHLRrigrfsEPHARFYAAQIVLAF-------EYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKRVKGrtwtLC 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2038291632 779 GTYEtqggkipirWTAPEAIAHRIFTTASDVWSFGIVMWEvLSFGDKPYGEMNNQEVMKSIEEG-YRLP 846
Cdd:cd14209   160 GTPE---------YLAPEIILSKGYNKAVDWWALGVLIYE-MAAGYPPFFADQPIQIYEKIVSGkVRFP 218
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
673-839 1.15e-07

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: 54.55  E-value: 1.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 673 EATIMGQFNHPHILRLEGVVTKRKPIMIVTEFMENGALDAFLKEREDQLAPGQLV----AMLLgIAsgMNYLSGHNYVHR 748
Cdd:cd05574    51 EREILATLDHPFLPTLYASFQTSTHLCFVMDYCPGGELFRLLQKQPGKRLPEEVArfyaAEVL-LA--LEYLHLLGFVYR 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 749 DLAARNILVNQNLCCKVSDFGLTRLLDDF---------DGTYETQGGKIPIR------------------WTAPEAIAHR 801
Cdd:cd05574   128 DLKPENILLHESGHIMLTDFDLSKQSSVTpppvrkslrKGSRRSSVKSIEKEtfvaepsarsnsfvgteeYIAPEVIKGD 207
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2038291632 802 IFTTASDVWSFGIVMWEVLsFGDKPYGEMNNQEVMKSI 839
Cdd:cd05574   208 GHGSAVDWWTLGILLYEML-YGTTPFKGSNRDETFSNI 244
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
629-827 1.42e-07

Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-alpha is expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-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. This alignment model includes the dimerization domain.


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 55.02  E-value: 1.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVyrGALRFPSQDcKTVAIKTLKDtspdgqwWNFLREAT---------IMGQFNHPHILRLEGVVTKRKPIM 699
Cdd:cd05623    79 VIGRGAFGEV--AVVKLKNAD-KVFAMKILNK-------WEMLKRAEtacfreerdVLVNGDSQWITTLHYAFQDDNNLY 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 700 IVTEFMENGALDAFLKEREDQL----APGQLVAMLLGIASgmnyLSGHNYVHRDLAARNILVNQNLCCKVSDFG-LTRLL 774
Cdd:cd05623   149 LVMDYYVGGDLLTLLSKFEDRLpedmARFYLAEMVLAIDS----VHQLHYVHRDIKPDNILMDMNGHIRLADFGsCLKLM 224
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2038291632 775 DdfDGTYETQGGKIPIRWTAPEAI-----AHRIFTTASDVWSFGIVMWEVLsFGDKPY 827
Cdd:cd05623   225 E--DGTVQSSVAVGTPDYISPEILqamedGKGKYGPECDWWSLGVCMYEML-YGETPF 279
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
629-839 1.49e-07

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: 54.61  E-value: 1.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRGALRfpsQDCKTVAIKTLK--DTSPDGQWWNFLREATIMGQFN---HPHILRLEGVVTKRKPIMIVTE 703
Cdd:cd05589     6 VLGRGHFGKVLLAEYK---PTGELFAIKALKkgDIIARDEVESLMCEKRIFETVNsarHPFLVNLFACFQTPEHVCFVME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 704 FMENGAL------DAFLKEREDQLApgqlVAMLLGIasgmNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTR----- 772
Cdd:cd05589    83 YAAGGDLmmhiheDVFSEPRAVFYA----ACVVLGL----QFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKegmgf 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2038291632 773 --LLDDFDGTYEtqggkipirWTAPEAIAHRIFTTASDVWSFGIVMWEVLsFGDKPYGEMNNQEVMKSI 839
Cdd:cd05589   155 gdRTSTFCGTPE---------FLAPEVLTDTSYTRAVDWWGLGVLIYEML-VGESPFPGDDEEEVFDSI 213
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
626-821 1.62e-07

Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called U2AF homology motif (UHM) kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KIS (or UHMK1) contains an N-terminal kinase domain and a C-terminal domain with a UHM motif, a protein interaction motif initially found in the pre-mRNA splicing factor U2AF. It phosphorylates the splicing factor SF1, which enhances binding to the splice site to promote spliceosome assembly. KIS was first identified as a kinase that interacts with stathmin, a phosphoprotein that plays a role in axon development and microtubule dynamics. It localizes in RNA granules in neurons and is important in neurite outgrowth. The KIS/UHMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270922 [Multi-domain]  Cd Length: 285  Bit Score: 54.17  E-value: 1.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 626 VDTVIGEGEFGEVYRgALRFPSQDCKTVAIKTLK---DTSPDGQWWNFLREATIMGQFN-HPHILRLEGVVTKRKPIMIV 701
Cdd:cd14020     4 VQSRLGQGSSASVYR-VSSGRGADQPTSALKEFQldhQGSQESGDYGFAKERAALEQLQgHRNIVTLYGVFTNHYSANVP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 702 TEFMENGALDAFLKEREDQLAPgQLVAMLL------GIASGMNYLSGHNYVHRDLAARNILVN-QNLCCKVSDFGLTRLL 774
Cdd:cd14020    83 SRCLLLELLDVSVSELLLRSSN-QGCSMWMiqhcarDVLEALAFLHHEGYVHADLKPRNILWSaEDECFKLIDFGLSFKE 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2038291632 775 DDFDGTY-ETQGgkipirWTAPEAIAHRIF-----------TTASDVWSFGIVMWEVLS 821
Cdd:cd14020   162 GNQDVKYiQTDG------YRAPEAELQNCLaqaglqsetecTSAVDLWSLGIVLLEMFS 214
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
629-861 1.65e-07

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: 53.85  E-value: 1.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 629 VIGEGEFGEVYRgALRFPSQDC-KTVAIKTLKD------------TSPDGQWWNFLREAtimgqfnhPHILRLEGVVTKR 695
Cdd:cd05613     7 VLGTGAYGKVFL-VRKVSGHDAgKLYAMKVLKKativqkaktaehTRTERQVLEHIRQS--------PFLVTLHYAFQTD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 696 KPIMIVTEFMENGALDAFLKEREDqlAPGQLVAMLLG-IASGMNYLSGHNYVHRDLAARNILVNQNLCCKVSDFGLTR-- 772
Cdd:cd05613    78 TKLHLILDYINGGELFTHLSQRER--FTENEVQIYIGeIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKef 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291632 773 LLDDFDGTYETQGgkiPIRWTAPEAI-----AHrifTTASDVWSFGIVMWEVLSfGDKPY---GEMNNQ-EVMKSIeegY 843
Cdd:cd05613   156 LLDENERAYSFCG---TIEYMAPEIVrggdsGH---DKAVDWWSLGVLMYELLT-GASPFtvdGEKNSQaEISRRI---L 225
                         250
                  ....*....|....*...
gi 2038291632 844 RLPPPVdcPAPLYELMKN 861
Cdd:cd05613   226 KSEPPY--PQEMSALAKD 241
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
453-525 7.43e-07

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 47.99  E-value: 7.43e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2038291632  453 LRLVKKEPRQLELAWagSRPRTPGGN---LSYELHVLNQDEEWHQM---VLEPRVLLTKLQPDTTYIVRVRTMTPLGPG 525
Cdd:smart00060   7 LRVTDVTSTSVTLSW--EPPPDDGITgyiVGYRVEYREEGSEWKEVnvtPSSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
fn3 pfam00041
Fibronectin type III domain;
460-528 8.64e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 47.79  E-value: 8.64e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2038291632 460 PRQLELAWagSRPRTPGGNL-SYELHVLNQDEE--WHQMVL---EPRVLLTKLQPDTTYIVRVRTMTPLGPGPFS 528
Cdd:pfam00041  13 STSLTVSW--TPPPDGNGPItGYEVEYRPKNSGepWNEITVpgtTTSVTLTGLKPGTEYEVRVQAVNGGGEGPPS 85
 
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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