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Conserved domains on  [gi|13112048|ref|NP_075254|]
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fibroblast growth factor receptor 3 isoform 2 precursor [Homo sapiens]

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 ...
347-680 0e+00

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 cd05100:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 334  Bit Score: 697.15  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 347 LPADPKWELSRARLTLGKPLGEGCFGQVVMAEAIGIDKDRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIGKHKNI 426
Cdd:cd05100   1 LPADPKWELSRTRLTLGKPLGEGCFGQVVMAEAIGIDKDKPNKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIGKHKNI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 427 INLLGACTQGGPLYVLVEYAAKGNLREFLRARRPPGLDYSFDTCKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDL 506
Cdd:cd05100  81 INLLGACTQDGPLYVLVEYASKGNLREYLRARRPPGMDYSFDTCKLPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 507 AARNVLVTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGI 586
Cdd:cd05100 161 AARNVLVTEDNVMKIADFGLARDVHNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGI 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 587 PVEELFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVLTVTSTDEYLDLSAPFEQYSPGGQDTP 666
Cdd:cd05100 241 PVEELFKLLKEGHRMDKPANCTHELYMIMRECWHAVPSQRPTFKQLVEDLDRVLTVTSTDEYLDLSVPFEQYSPGCPDSP 320
                       330
                ....*....|....
gi 13112048 667 SSSSSGDDSVFAHD 680
Cdd:cd05100 321 SSCSSGDDSVFAHD 334
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
151-245 5.93e-64

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


:

Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 206.63  E-value: 5.93e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 151 PYWTRPERMDKKLLAVPAANTVRFRCPAAGNPTPSISWLKNGREFRGEHRIGGIKLRHQQWSLVMESVVPSDRGNYTCVV 230
Cdd:cd05857   1 PYWTNPEKMEKKLHAVPAANTVKFRCPAAGNPTPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCVV 80
                        90
                ....*....|....*
gi 13112048 231 ENKFGSIRQTYTLDV 245
Cdd:cd05857  81 ENEYGSINHTYHLDV 95
IgI_3_FGFR cd04974
Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of ...
253-355 4.71e-48

Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR). Fibroblast growth factors (FGFs) participate in morphogenesis, development, angiogenesis, and wound healing. These FGF-stimulated processes are mediated by four FGFR tyrosine kinases (FGRF1-4). FGFRs are comprised of an extracellular portion consisting of three Ig-like domains, a transmembrane helix, and a cytoplasmic portion having protein tyrosine kinase activity. The highly conserved Ig-like domains 2 and 3, and the linker region between D2 and D3 define a general binding site for FGFs. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


:

Pssm-ID: 409363  Cd Length: 102  Bit Score: 164.13  E-value: 4.71e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 253 PILQAGLPANQTAVLGSDVEFHCKVYSDAQPHIQWLKHVEVNGSKVGPDGTPYVTVLKVSLEsNASMSSNTPLVRIARL- 331
Cdd:cd04974   1 PILQAGLPANQTVVLGSDVEFHCKVYSDAQPHIQWLKHVEVNGSKYGPDGLPYVTVLKVAGV-NTTGEENTLTISNVTFd 79
                        90       100
                ....*....|....*....|....
gi 13112048 332 SSGEGPTLANVSeLELPADPKWEL 355
Cdd:cd04974  80 DAGEYICLAGNS-IGLSFHSAWLT 102
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
37-109 2.46e-07

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd04973:

Pssm-ID: 472250  Cd Length: 94  Bit Score: 49.12  E-value: 2.46e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13112048  37 EVPGPEPGQQEQLVFGSGDAVELSCPPPGGGPMGPtvWVKDGTGLVPSERVLVGPQRLQVLNASHEDSGAYSC 109
Cdd:cd04973   7 APPTYQISEVESYSAHPGDLLQLRCRLRDDVQSIN--WTKDGVQLGENNRTRITGEEVQIKDAVPRDSGLYAC 77
 
Name Accession Description Interval E-value
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
347-680 0e+00

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: 697.15  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 347 LPADPKWELSRARLTLGKPLGEGCFGQVVMAEAIGIDKDRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIGKHKNI 426
Cdd:cd05100   1 LPADPKWELSRTRLTLGKPLGEGCFGQVVMAEAIGIDKDKPNKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIGKHKNI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 427 INLLGACTQGGPLYVLVEYAAKGNLREFLRARRPPGLDYSFDTCKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDL 506
Cdd:cd05100  81 INLLGACTQDGPLYVLVEYASKGNLREYLRARRPPGMDYSFDTCKLPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 507 AARNVLVTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGI 586
Cdd:cd05100 161 AARNVLVTEDNVMKIADFGLARDVHNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGI 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 587 PVEELFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVLTVTSTDEYLDLSAPFEQYSPGGQDTP 666
Cdd:cd05100 241 PVEELFKLLKEGHRMDKPANCTHELYMIMRECWHAVPSQRPTFKQLVEDLDRVLTVTSTDEYLDLSVPFEQYSPGCPDSP 320
                       330
                ....*....|....
gi 13112048 667 SSSSSGDDSVFAHD 680
Cdd:cd05100 321 SSCSSGDDSVFAHD 334
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
360-636 2.97e-146

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: 426.14  E-value: 2.97e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048   360 LTLGKPLGEGCFGQVVMAEAIGIDKDraaKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPL 439
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKGEGEN---TKIKVAVKTLKEGADEEEREDFLEEASIMKKL-DHPNIVKLLGVCTQGEPL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048   440 YVLVEYAAKGNLREFLRARRPPgldysfdtckppeeqLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVM 519
Cdd:pfam07714  77 YIVTEYMPGGDLLDFLRKHKRK---------------LTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVV 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048   520 KIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGH 599
Cdd:pfam07714 142 KISDFGLSRDIYDDDYYRKRGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEFLEDGY 221
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 13112048   600 RMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDL 636
Cdd:pfam07714 222 RLPQPENCPDELYDLMKQCWAYDPEDRPTFSELVEDL 258
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
360-636 3.10e-142

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: 415.79  E-value: 3.10e-142
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048    360 LTLGKPLGEGCFGQVVMAEAIGIDKDraaKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPL 439
Cdd:smart00221   1 LTLGKKLGEGAFGEVYKGTLKGKGDG---KEVEVAVKTLKEDASEQQIEEFLREARIMRKL-DHPNIVKLLGVCTEEEPL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048    440 YVLVEYAAKGNLREFLRARRPPGLdysfdtckppeeqlTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVM 519
Cdd:smart00221  77 MIVMEYMPGGDLLDYLRKNRPKEL--------------SLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVV 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048    520 KIADFGLARDVHNLDYYKKTtNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGH 599
Cdd:smart00221 143 KISDFGLSRDLYDDDYYKVK-GGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEEPYPGMSNAEVLEYLKKGY 221
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 13112048    600 RMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDL 636
Cdd:smart00221 222 RLPKPPNCPPELYKLMLQCWAEDPEDRPTFSELVEIL 258
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
151-245 5.93e-64

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 206.63  E-value: 5.93e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 151 PYWTRPERMDKKLLAVPAANTVRFRCPAAGNPTPSISWLKNGREFRGEHRIGGIKLRHQQWSLVMESVVPSDRGNYTCVV 230
Cdd:cd05857   1 PYWTNPEKMEKKLHAVPAANTVKFRCPAAGNPTPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCVV 80
                        90
                ....*....|....*
gi 13112048 231 ENKFGSIRQTYTLDV 245
Cdd:cd05857  81 ENEYGSINHTYHLDV 95
IgI_3_FGFR cd04974
Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of ...
253-355 4.71e-48

Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR). Fibroblast growth factors (FGFs) participate in morphogenesis, development, angiogenesis, and wound healing. These FGF-stimulated processes are mediated by four FGFR tyrosine kinases (FGRF1-4). FGFRs are comprised of an extracellular portion consisting of three Ig-like domains, a transmembrane helix, and a cytoplasmic portion having protein tyrosine kinase activity. The highly conserved Ig-like domains 2 and 3, and the linker region between D2 and D3 define a general binding site for FGFs. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409363  Cd Length: 102  Bit Score: 164.13  E-value: 4.71e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 253 PILQAGLPANQTAVLGSDVEFHCKVYSDAQPHIQWLKHVEVNGSKVGPDGTPYVTVLKVSLEsNASMSSNTPLVRIARL- 331
Cdd:cd04974   1 PILQAGLPANQTVVLGSDVEFHCKVYSDAQPHIQWLKHVEVNGSKYGPDGLPYVTVLKVAGV-NTTGEENTLTISNVTFd 79
                        90       100
                ....*....|....*....|....
gi 13112048 332 SSGEGPTLANVSeLELPADPKWEL 355
Cdd:cd04974  80 DAGEYICLAGNS-IGLSFHSAWLT 102
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
359-694 2.19e-30

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 125.51  E-value: 2.19e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 359 RLTLGKPLGEGCFGQVVMAEAIGIDKdraakpvTVAVKMLKDDATD--KDLSDLVSEMEMMKMIgKHKNIINLLGACTQG 436
Cdd:COG0515   8 RYRILRLLGRGGMGVVYLARDLRLGR-------PVALKVLRPELAAdpEARERFRREARALARL-NHPNIVRVYDVGEED 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 437 GPLYVLVEYAAKGNLREFLRARRPpgldysfdtckppeeqLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTED 516
Cdd:COG0515  80 GRPYLVMEYVEGESLADLLRRRGP----------------LPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPD 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 517 NVMKIADFGLARDVHNLDyykKTTNGRLPVK--WMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEELFkl 594
Cdd:COG0515 144 GRVKLIDFGIARALGGAT---LTQTGTVVGTpgYMAPEQARGEPVDPRSDVYSLGVTLYELLT-GRPPFDGDSPAELL-- 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 595 lkEGHRMDKP-------ANCTHDLYMIMRECWHAAPSQRP-TFKQLVEDLDRVLTVTSTDEYLDLSAPFEQYSPGGQDTP 666
Cdd:COG0515 218 --RAHLREPPpppselrPDLPPALDAIVLRALAKDPEERYqSAAELAAALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAA 295
                       330       340
                ....*....|....*....|....*...
gi 13112048 667 SSSSSGDDSVFAHDLLPPAPPSSGGSRT 694
Cdd:COG0515 296 AAAAAAAAAAAAAAAAAAAAAAAAAAAP 323
PHA02988 PHA02988
hypothetical protein; Provisional
393-636 7.55e-18

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 84.41  E-value: 7.55e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048  393 VAVKMLKDDATD-KDLSDL-VSEMEMMKMIgKHKNIINLLG----ACTQGGPLYVLVEYAAKGNLREFLRArrppgldys 466
Cdd:PHA02988  46 VIIRTFKKFHKGhKVLIDItENEIKNLRRI-DSNNILKIYGfiidIVDDLPRLSLILEYCTRGYLREVLDK--------- 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048  467 fdtckppEEQLTFKDLVSCAYQVARGMEYL-ASQKCIHRDLAARNVLVTEDNVMKIADFGLARDVHNLDYykKTTNGrlp 545
Cdd:PHA02988 116 -------EKDLSFKTKLDMAIDCCKGLYNLyKYTNKPYKNLTSVSFLVTENYKLKIICHGLEKILSSPPF--KNVNF--- 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048  546 VKWMAPEALFD--RVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEELFKLL-KEGHRMDKPANCTHDLYMIMRECWHAA 622
Cdd:PHA02988 184 MVYFSYKMLNDifSEYTIKDDIYSLGVVLWEIFT-GKIPFENLTTKEIYDLIiNKNNSLKLPLDCPLEIKCIVEACTSHD 262
                        250
                 ....*....|....
gi 13112048  623 PSQRPTFKQLVEDL 636
Cdd:PHA02988 263 SIKRPNIKEILYNL 276
I-set pfam07679
Immunoglobulin I-set domain;
171-245 3.83e-15

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 71.13  E-value: 3.83e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13112048   171 TVRFRCPAAGNPTPSISWLKNGREFRGEHRIgGIKLRHQQWSLVMESVVPSDRGNYTCVVENKFGSIRQTYTLDV 245
Cdd:pfam07679  17 SARFTCTVTGTPDPEVSWFKDGQPLRSSDRF-KVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
171-245 3.84e-15

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 71.00  E-value: 3.84e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13112048    171 TVRFRCPAAGNPTPSISWLKNGREFRGEHRIGGIKLRHQQWSLVMESVVPSDRGNYTCVVENKFGSIRQTYTLDV 245
Cdd:smart00410  11 SVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
359-585 3.51e-12

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 69.44  E-value: 3.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048  359 RLTLGKPLGEGcfGqvvMAEA-IGIDK--DRaakpvTVAVKMLKDD-ATDKD--------------LSdlvsememmkmi 420
Cdd:NF033483   8 RYEIGERIGRG--G---MAEVyLAKDTrlDR-----DVAVKVLRPDlARDPEfvarfrreaqsaasLS------------ 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048  421 gkHKNIINLL--GactQGGPLYVLV-EYAAKGNLREFLRARRPpgldysfdtckppeeqLTFKDLVSCAYQVARGMEYLA 497
Cdd:NF033483  66 --HPNIVSVYdvG---EDGGIPYIVmEYVDGRTLKDYIREHGP----------------LSPEEAVEIMIQILSALEHAH 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048  498 SQKCIHRDLAARNVLVTEDNVMKIADFGLAR--DVHNLDYykktTNGRL-PVKWMAPE-ALFDRVyTHQSDVWSFGVLLW 573
Cdd:NF033483 125 RNGIVHRDIKPQNILITKDGRVKVTDFGIARalSSTTMTQ----TNSVLgTVHYLSPEqARGGTV-DARSDIYSLGIVLY 199
                        250
                 ....*....|..
gi 13112048  574 EIFTlGGSPYPG 585
Cdd:NF033483 200 EMLT-GRPPFDG 210
IgI_1_FGFR cd04973
First immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of ...
37-109 2.46e-07

First immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR). Fibroblast growth factors (FGFs) participate in morphogenesis, development, angiogenesis, and wound healing. These FGF-stimulated processes are mediated by four FGFR tyrosine kinases (FGRF1-4). FGFRs are comprised of an extracellular portion consisting of three Ig-like domains, a transmembrane helix, and a cytoplasmic portion having protein tyrosine kinase activity. The highly conserved Ig-like domains 2 and 3, and the linker region between D2 and D3 define a general binding site for all FGFs.


Pssm-ID: 409362  Cd Length: 94  Bit Score: 49.12  E-value: 2.46e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13112048  37 EVPGPEPGQQEQLVFGSGDAVELSCPPPGGGPMGPtvWVKDGTGLVPSERVLVGPQRLQVLNASHEDSGAYSC 109
Cdd:cd04973   7 APPTYQISEVESYSAHPGDLLQLRCRLRDDVQSIN--WTKDGVQLGENNRTRITGEEVQIKDAVPRDSGLYAC 77
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
48-110 1.04e-04

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 41.41  E-value: 1.04e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13112048    48 QLVFGSGDAVELSCPPPGGGPMGPTVWVKDGTGLVPSERVLVGPQR-----LQVLNASHEDSGAYSCR 110
Cdd:pfam00047   5 TVTVLEGDSATLTCSASTGSPGPDVTWSKEGGTLIESLKVKHDNGRttqssLLISNVTKEDAGTYTCV 72
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
260-289 1.24e-03

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 38.26  E-value: 1.24e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 13112048    260 PANQTAVLGSDVEFHCKVYSDAQPHIQWLK 289
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVTWYK 30
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
260-308 2.21e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 37.55  E-value: 2.21e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 13112048   260 PANQTAVLGSDVEFHCKVYSDAQPHIQWLKhvevNGSKVGPDGTPYVTV 308
Cdd:pfam13927   8 PSSVTVREGETVTLTCEATGSPPPTITWYK----NGEPISSGSTRSRSL 52
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
54-125 3.34e-03

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 37.10  E-value: 3.34e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13112048     54 GDAVELSCPPPGGGPMGPTvWVKDGTGLV-PSERVLV----GPQRLQVLNASHEDSGAYSCRQRLTQRVL-CHFSVRV 125
Cdd:smart00410   9 GESVTLSCEASGSPPPEVT-WYKQGGKLLaESGRFSVsrsgSTSTLTISNVTPEDSGTYTCAATNSSGSAsSGTTLTV 85
 
Name Accession Description Interval E-value
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
347-680 0e+00

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: 697.15  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 347 LPADPKWELSRARLTLGKPLGEGCFGQVVMAEAIGIDKDRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIGKHKNI 426
Cdd:cd05100   1 LPADPKWELSRTRLTLGKPLGEGCFGQVVMAEAIGIDKDKPNKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIGKHKNI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 427 INLLGACTQGGPLYVLVEYAAKGNLREFLRARRPPGLDYSFDTCKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDL 506
Cdd:cd05100  81 INLLGACTQDGPLYVLVEYASKGNLREYLRARRPPGMDYSFDTCKLPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 507 AARNVLVTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGI 586
Cdd:cd05100 161 AARNVLVTEDNVMKIADFGLARDVHNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGI 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 587 PVEELFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVLTVTSTDEYLDLSAPFEQYSPGGQDTP 666
Cdd:cd05100 241 PVEELFKLLKEGHRMDKPANCTHELYMIMRECWHAVPSQRPTFKQLVEDLDRVLTVTSTDEYLDLSVPFEQYSPGCPDSP 320
                       330
                ....*....|....
gi 13112048 667 SSSSSGDDSVFAHD 680
Cdd:cd05100 321 SSCSSGDDSVFAHD 334
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
347-660 0e+00

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: 654.73  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 347 LPADPKWELSRARLTLGKPLGEGCFGQVVMAEAIGIDKDRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIGKHKNI 426
Cdd:cd05099   1 LPLDPKWEFPRDRLVLGKPLGEGCFGQVVRAEAYGIDKSRPDQTVTVAVKMLKDNATDKDLADLISEMELMKLIGKHKNI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 427 INLLGACTQGGPLYVLVEYAAKGNLREFLRARRPPGLDYSFDTCKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDL 506
Cdd:cd05099  81 INLLGVCTQEGPLYVIVEYAAKGNLREFLRARRPPGPDYTFDITKVPEEQLSFKDLVSCAYQVARGMEYLESRRCIHRDL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 507 AARNVLVTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGI 586
Cdd:cd05099 161 AARNVLVTEDNVMKIADFGLARGVHDIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILMWEIFTLGGSPYPGI 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13112048 587 PVEELFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVLTVTStDEYLDLSAPFEQYSP 660
Cdd:cd05099 241 PVEELFKLLREGHRMDKPSNCTHELYMLMRECWHAVPTQRPTFKQLVEALDKVLAAVS-EEYLDLSMPFEQYSP 313
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
347-641 0e+00

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: 653.33  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 347 LPADPKWELSRARLTLGKPLGEGCFGQVVMAEAIGIDKdRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIGKHKNI 426
Cdd:cd05053   1 LPLDPEWELPRDRLTLGKPLGEGAFGQVVKAEAVGLDN-KPNEVVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 427 INLLGACTQGGPLYVLVEYAAKGNLREFLRARRPPGLDYSFDTCKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDL 506
Cdd:cd05053  80 INLLGACTQDGPLYVVVEYASKGNLREFLRARRPPGEEASPDDPRVPEEQLTQKDLVSFAYQVARGMEYLASKKCIHRDL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 507 AARNVLVTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGI 586
Cdd:cd05053 160 AARNVLVTEDNVMKIADFGLARDIHHIDYYRKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGI 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 13112048 587 PVEELFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVLT 641
Cdd:cd05053 240 PVEELFKLLKEGHRMEKPQNCTQELYMLMRDCWHEVPSQRPTFKQLVEDLDRILT 294
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
335-647 0e+00

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: 628.97  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 335 EGPTLANVSELELPADPKWELSRARLTLGKPLGEGCFGQVVMAEAIGIDKDRAAKPVTVAVKMLKDDATDKDLSDLVSEM 414
Cdd:cd05101   1 DAPMLAGVSEYELPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPKEAVTVAVKMLKDDATEKDLSDLVSEM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 415 EMMKMIGKHKNIINLLGACTQGGPLYVLVEYAAKGNLREFLRARRPPGLDYSFDTCKPPEEQLTFKDLVSCAYQVARGME 494
Cdd:cd05101  81 EMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGME 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 495 YLASQKCIHRDLAARNVLVTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWE 574
Cdd:cd05101 161 YLASQKCIHRDLAARNVLVTENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWE 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13112048 575 IFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVLTVTSTDE 647
Cdd:cd05101 241 IFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRILTLTTNEE 313
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
346-647 0e+00

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: 597.76  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 346 ELPADPKWELSRARLTLGKPLGEGCFGQVVMAEAIGIDKDRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIGKHKN 425
Cdd:cd05098   1 ELPEDPRWELPRDRLVLGKPLGEGCFGQVVLAEAIGLDKDKPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIGKHKN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 426 IINLLGACTQGGPLYVLVEYAAKGNLREFLRARRPPGLDYSFDTCKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRD 505
Cdd:cd05098  81 IINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPGMEYCYNPSHNPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 506 LAARNVLVTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPG 585
Cdd:cd05098 161 LAARNVLVTEDNVMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSPYPG 240
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13112048 586 IPVEELFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVLTVTSTDE 647
Cdd:cd05098 241 VPVEELFKLLKEGHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIVALTSNQE 302
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
364-637 4.32e-149

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: 433.50  E-value: 4.32e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVMAEAIGIDKdraaKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIGkHKNIINLLGACTQGGPLYVLV 443
Cdd:cd00192   1 KKLGEGAFGEVYKGKLKGGDG----KTVDVAVKTLKEDASESERKDFLKEARVMKKLG-HPNVVRLLGVCTEEEPLYLVM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 444 EYAAKGNLREFLRARRPPGLDYSFDTckppeeqLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIAD 523
Cdd:cd00192  76 EYMEGGDLLDFLRKSRPVFPSPEPST-------LSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISD 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 524 FGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGHRMDK 603
Cdd:cd00192 149 FGLSRDIYDDDYYRKKTGGKLPIRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTLGATPYPGLSNEEVLEYLRKGYRLPK 228
                       250       260       270
                ....*....|....*....|....*....|....
gi 13112048 604 PANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLD 637
Cdd:cd00192 229 PENCPDELYELMLSCWQLDPEDRPTFSELVERLE 262
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
360-636 2.97e-146

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: 426.14  E-value: 2.97e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048   360 LTLGKPLGEGCFGQVVMAEAIGIDKDraaKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPL 439
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKGEGEN---TKIKVAVKTLKEGADEEEREDFLEEASIMKKL-DHPNIVKLLGVCTQGEPL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048   440 YVLVEYAAKGNLREFLRARRPPgldysfdtckppeeqLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVM 519
Cdd:pfam07714  77 YIVTEYMPGGDLLDFLRKHKRK---------------LTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVV 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048   520 KIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGH 599
Cdd:pfam07714 142 KISDFGLSRDIYDDDYYRKRGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEFLEDGY 221
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 13112048   600 RMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDL 636
Cdd:pfam07714 222 RLPQPENCPDELYDLMKQCWAYDPEDRPTFSELVEDL 258
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
360-636 3.10e-142

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: 415.79  E-value: 3.10e-142
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048    360 LTLGKPLGEGCFGQVVMAEAIGIDKDraaKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPL 439
Cdd:smart00221   1 LTLGKKLGEGAFGEVYKGTLKGKGDG---KEVEVAVKTLKEDASEQQIEEFLREARIMRKL-DHPNIVKLLGVCTEEEPL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048    440 YVLVEYAAKGNLREFLRARRPPGLdysfdtckppeeqlTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVM 519
Cdd:smart00221  77 MIVMEYMPGGDLLDYLRKNRPKEL--------------SLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVV 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048    520 KIADFGLARDVHNLDYYKKTtNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGH 599
Cdd:smart00221 143 KISDFGLSRDLYDDDYYKVK-GGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEEPYPGMSNAEVLEYLKKGY 221
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 13112048    600 RMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDL 636
Cdd:smart00221 222 RLPKPPNCPPELYKLMLQCWAEDPEDRPTFSELVEIL 258
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
360-636 4.43e-142

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 415.39  E-value: 4.43e-142
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048    360 LTLGKPLGEGCFGQVVMAEAIGIDKDraaKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPL 439
Cdd:smart00219   1 LTLGKKLGEGAFGEVYKGKLKGKGGK---KKVEVAVKTLKEDASEQQIEEFLREARIMRKL-DHPNVVKLLGVCTEEEPL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048    440 YVLVEYAAKGNLREFLRARRPpgldysfdtckppeeQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVM 519
Cdd:smart00219  77 YIVMEYMEGGDLLSYLRKNRP---------------KLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVV 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048    520 KIADFGLARDVHNLDYYKKTtNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGH 599
Cdd:smart00219 142 KISDFGLSRDLYDDDYYRKR-GGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEYLKNGY 220
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 13112048    600 RMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDL 636
Cdd:smart00219 221 RLPQPPNCPPELYDLMLQCWAEDPEDRPTFSELVEIL 257
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
352-636 3.95e-129

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: 383.76  E-value: 3.95e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 352 KWELSRARLTLGKPLGEGCFGQVVMAEAIGIDKDRAAKpvTVAVKMLKDDATDKDLSDLVSEMEMMKMIGKHKNIINLLG 431
Cdd:cd05054   1 KWEFPRDRLKLGKPLGRGAFGKVIQASAFGIDKSATCR--TVAVKMLKEGATASEHKALMTELKILIHIGHHLNVVNLLG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 432 ACT-QGGPLYVLVEYAAKGNLREFLRARRP---PGLDYSFDTCKPPE-------EQLTFKDLVSCAYQVARGMEYLASQK 500
Cdd:cd05054  79 ACTkPGGPLMVIVEFCKFGNLSNYLRSKREefvPYRDKGARDVEEEEdddelykEPLTLEDLICYSFQVARGMEFLASRK 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 501 CIHRDLAARNVLVTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGG 580
Cdd:cd05054 159 CIHRDLAARNILLSENNVVKICDFGLARDIYKDPDYVRKGDARLPLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFSLGA 238
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 13112048 581 SPYPGIPVEELF-KLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDL 636
Cdd:cd05054 239 SPYPGVQMDEEFcRRLKEGTRMRAPEYTTPEIYQIMLDCWHGEPKERPTFSELVEKL 295
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
326-633 4.83e-122

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: 365.65  E-value: 4.83e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 326 VRIARLSSGEGPTLANVSELELPADPKWELSRARLTLGKPLGEGCFGQVVMAEAIGIDKDRAAkpVTVAVKMLKDDATDK 405
Cdd:cd05055   3 VRWKVIESINGNEYVYIDPTQLPYDLKWEFPRNNLSFGKTLGAGAFGKVVEATAYGLSKSDAV--MKVAVKMLKPTAHSS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 406 DLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYVLVEYAAKGNLREFLRARRppgldysfdtckppEEQLTFKDLVSC 485
Cdd:cd05055  81 EREALMSELKIMSHLGNHENIVNLLGACTIGGPILVITEYCCYGDLLNFLRRKR--------------ESFLTLEDLLSF 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 486 AYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDV 565
Cdd:cd05055 147 SYQVAKGMAFLASKNCIHRDLAARNVLLTHGKIVKICDFGLARDIMNDSNYVVKGNARLPVKWMAPESIFNCVYTFESDV 226
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13112048 566 WSFGVLLWEIFTLGGSPYPGIPVEELF-KLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLV 633
Cdd:cd05055 227 WSYGILLWEIFSLGSNPYPGMPVDSKFyKLIKEGYRMAQPEHAPAEIYDIMKTCWDADPLKRPTFKQIV 295
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
352-640 1.61e-118

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: 358.52  E-value: 1.61e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 352 KWELSRARLTLGKPLGEGCFGQVVMAEAIGIDKDRAAKpvTVAVKMLKDDATDKDLSDLVSEMEMMKMIGKHKNIINLLG 431
Cdd:cd05103   1 KWEFPRDRLKLGKPLGRGAFGQVIEADAFGIDKTATCR--TVAVKMLKEGATHSEHRALMSELKILIHIGHHLNVVNLLG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 432 ACTQ-GGPLYVLVEYAAKGNLREFLRARRPPGLDY--------------------------------------------- 465
Cdd:cd05103  79 ACTKpGGPLMVIVEFCKFGNLSAYLRSKRSEFVPYktkgarfrqgkdyvgdisvdlkrrldsitssqssassgfveeksl 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 466 ---------SFDTCKPPeeqLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARDVHNLDYY 536
Cdd:cd05103 159 sdveeeeagQEDLYKDF---LTLEDLICYSFQVAKGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKDPDY 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 537 KKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELF-KLLKEGHRMDKPANCTHDLYMIM 615
Cdd:cd05103 236 VRKGDARLPLKWMAPETIFDRVYTIQSDVWSFGVLLWEIFSLGASPYPGVKIDEEFcRRLKEGTRMRAPDYTTPEMYQTM 315
                       330       340
                ....*....|....*....|....*
gi 13112048 616 RECWHAAPSQRPTFKQLVEDLDRVL 640
Cdd:cd05103 316 LDCWHGEPSQRPTFSELVEHLGNLL 340
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
359-640 7.05e-115

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: 346.95  E-value: 7.05e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 359 RLTLGKPLGEGCFGQVVMAEAIGIdKDRAAKpVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGP 438
Cdd:cd05045   1 NLVLGKTLGEGEFGKVVKATAFRL-KGRAGY-TTVAVKMLKENASSSELRDLLSEFNLLKQV-NHPHVIKLYGACSQDGP 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 439 LYVLVEYAAKGNLREFLRARRPPGLDY--------SFDTCKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARN 510
Cdd:cd05045  78 LLLIVEYAKYGSLRSFLRESRKVGPSYlgsdgnrnSSYLDNPDERALTMGDLISFAWQISRGMQYLAEMKLVHRDLAARN 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 511 VLVTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEE 590
Cdd:cd05045 158 VLVAEGRKMKISDFGLSRDVYEEDSYVKRSKGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIAPER 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 13112048 591 LFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVL 640
Cdd:cd05045 238 LFNLLKTGYRMERPENCSEEMYNLMLTCWKQEPDKRPTFADISKELEKMM 287
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
352-636 1.56e-112

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: 342.75  E-value: 1.56e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 352 KWELSRARLTLGKPLGEGCFGQVVMAEAIGIDKDRAAKpvTVAVKMLKDDATDKDLSDLVSEMEMMKMIGKHKNIINLLG 431
Cdd:cd14207   1 KWEFARERLKLGKSLGRGAFGKVVQASAFGIKKSPTCR--VVAVKMLKEGATASEYKALMTELKILIHIGHHLNVVNLLG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 432 ACT-QGGPLYVLVEYAAKGNLREFLRARR--------------------PPGL------------------------DYS 466
Cdd:cd14207  79 ACTkSGGPLMVIVEYCKYGNLSNYLKSKRdffvtnkdtslqeelikekkEAEPtggkkkrlesvtssesfassgfqeDKS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 467 FDTCKPPEEQ--------LTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARDVH-NLDYYK 537
Cdd:cd14207 159 LSDVEEEEEDsgdfykrpLTMEDLISYSFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLARDIYkNPDYVR 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 538 KTtNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPV-EELFKLLKEGHRMDKPANCTHDLYMIMR 616
Cdd:cd14207 239 KG-DARLPLKWMAPESIFDKIYSTKSDVWSYGVLLWEIFSLGASPYPGVQIdEDFCSKLKEGIRMRAPEFATSEIYQIML 317
                       330       340
                ....*....|....*....|
gi 13112048 617 ECWHAAPSQRPTFKQLVEDL 636
Cdd:cd14207 318 DCWQGDPNERPRFSELVERL 337
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
352-640 1.71e-111

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: 340.03  E-value: 1.71e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 352 KWELSRARLTLGKPLGEGCFGQVVMAEAIGIDKDRAAKpvTVAVKMLKDDATDKDLSDLVSEMEMMKMIGKHKNIINLLG 431
Cdd:cd05102   1 QWEFPRDRLRLGKVLGHGAFGKVVEASAFGIDKSSSCE--TVAVKMLKEGATASEHKALMSELKILIHIGNHLNVVNLLG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 432 ACTQ-GGPLYVLVEYAAKGNLREFLRA------------------------------RRPPGLDYSFD------TCKPPE 474
Cdd:cd05102  79 ACTKpNGPLMVIVEFCKYGNLSNFLRAkregfspyrersprtrsqvrsmveavradrRSRQGSDRVASftestsSTNQPR 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 475 EQ--------LTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPV 546
Cdd:cd05102 159 QEvddlwqspLTMEDLICYSFQVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKDPDYVRKGSARLPL 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 547 KWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELF-KLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQ 625
Cdd:cd05102 239 KWMAPESIFDKVYTTQSDVWSFGVLLWEIFSLGASPYPGVQINEEFcQRLKDGTRMRAPEYATPEIYRIMLSCWHGDPKE 318
                       330
                ....*....|....*
gi 13112048 626 RPTFKQLVEDLDRVL 640
Cdd:cd05102 319 RPTFSDLVEILGDLL 333
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
346-640 1.05e-105

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: 326.48  E-value: 1.05e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 346 ELPADPKWELSRARLTLGKPLGEGCFGQVVMAEAIGIDKDRAAkpVTVAVKMLKDDATDKDLSDLVSEMEMMKMIGKHKN 425
Cdd:cd05104  23 QLPYDHKWEFPRDRLRFGKTLGAGAFGKVVEATAYGLAKADSA--MTVAVKMLKPSAHSTEREALMSELKVLSYLGNHIN 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 426 IINLLGACTQGGPLYVLVEYAAKGNLREFLRARR-------------------------------------PPGLDYSFD 468
Cdd:cd05104 101 IVNLLGACTVGGPTLVITEYCCYGDLLNFLRRKRdsficpkfedlaeaalyrnllhqremacdslneymdmKPSVSYVVP 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 469 TCK--------------------PPEEQLTF--KDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGL 526
Cdd:cd05104 181 TKAdkrrgvrsgsyvdqdvtseiLEEDELALdtEDLLSFSYQVAKGMEFLASKNCIHRDLAARNILLTHGRITKICDFGL 260
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 527 ARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELF-KLLKEGHRMDKPA 605
Cdd:cd05104 261 ARDIRNDSNYVVKGNARLPVKWMAPESIFECVYTFESDVWSYGILLWEIFSLGSSPYPGMPVDSKFyKMIKEGYRMDSPE 340
                       330       340       350
                ....*....|....*....|....*....|....*
gi 13112048 606 NCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVL 640
Cdd:cd05104 341 FAPSEMYDIMRSCWDADPLKRPTFKQIVQLIEQQL 375
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
326-640 7.41e-105

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: 324.11  E-value: 7.41e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 326 VRIARLSSGEGPTLANVSELELPADPKWELSRARLTLGKPLGEGCFGQVVMAEAIGIDKDRAAkpVTVAVKMLKDDATDK 405
Cdd:cd05106   6 IRWKIIEAAEGNNYTFIDPTQLPYNEKWEFPRDNLQFGKTLGAGAFGKVVEATAFGLGKEDNV--LRVAVKMLKASAHTD 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 406 DLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYVLVEYAAKGNLREFLRAR--------------------------- 458
Cdd:cd05106  84 EREALMSELKILSHLGQHKNIVNLLGACTHGGPVLVITEYCCYGDLLNFLRKKaetflnfvmalpeisetssdyknitle 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 459 ---------------------RP------PGLDYSFDTCKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNV 511
Cdd:cd05106 164 kkyirsdsgfssqgsdtyvemRPvsssssQSSDSKDEEDTEDSWPLDLDDLLRFSSQVAQGMDFLASKNCIHRDVAARNV 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 512 LVTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEEL 591
Cdd:cd05106 244 LLTDGRVAKICDFGLARDIMNDSNYVVKGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGKSPYPGILVNSK 323
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 13112048 592 F-KLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVL 640
Cdd:cd05106 324 FyKMVKRGYQMSRPDFAPPEIYSIMKMCWNLEPTERPTFSQISQLIQRQL 373
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
333-641 5.44e-98

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: 307.32  E-value: 5.44e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 333 SGEGPTLANVSELELPADPKWELSRARLTLGKPLGEGCFGQVVMAEAIGIDKDRAAkpVTVAVKMLKDDATDKDLSDLVS 412
Cdd:cd05107  12 SSDGHEYIYVDPMQLPYDSAWEMPRDNLVLGRTLGSGAFGRVVEATAHGLSHSQST--MKVAVKMLKSTARSSEKQALMS 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 413 EMEMMKMIGKHKNIINLLGACTQGGPLYVLVEYAAKGNLREFLR------------ARRPPGLDYS-------------- 466
Cdd:cd05107  90 ELKIMSHLGPHLNIVNLLGACTKGGPIYIITEYCRYGDLVDYLHrnkhtflqyyldKNRDDGSLISggstplsqrkshvs 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 467 -------------------------------------------FDTCKPPEEQ-------------LTFKDLVSCAYQVA 490
Cdd:cd05107 170 lgsesdggymdmskdesadyvpmqdmkgtvkyadiessnyespYDQYLPSAPErtrrdtlinespaLSYMDLVGFSYQVA 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 491 RGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARDV-HNLDYYKKTTNgRLPVKWMAPEALFDRVYTHQSDVWSFG 569
Cdd:cd05107 250 NGMEFLASKNCVHRDLAARNVLICEGKLVKICDFGLARDImRDSNYISKGST-FLPLKWMAPESIFNNLYTTLSDVWSFG 328
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13112048 570 VLLWEIFTLGGSPYPGIPVEELF-KLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVLT 641
Cdd:cd05107 329 ILLWEIFTLGGTPYPELPMNEQFyNAIKRGYRMAKPAHASDEIYEIMQKCWEEKFEIRPDFSQLVHLVGDLLT 401
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
353-638 8.70e-97

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: 299.64  E-value: 8.70e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 353 WELSRARLTLGKPLGEGCFGQVVMAEAIGIDKDRAAKPVtvAVKMLKDDATDKDLSDLVSEMEMMKMIGKHkNIINLLGA 432
Cdd:cd05032   1 WELPREKITLIRELGQGSFGMVYEGLAKGVVKGEPETRV--AIKTVNENASMRERIEFLNEASVMKEFNCH-HVVRLLGV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 433 CTQGGPLYVLVEYAAKGNLREFLRARRPPgldysfDTCKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVL 512
Cdd:cd05032  78 VSTGQPTLVVMELMAKGDLKSYLRSRRPE------AENNPGLGPPTLQKFIQMAAEIADGMAYLAAKKFVHRDLAARNCM 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 513 VTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELF 592
Cdd:cd05032 152 VAEDLTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMAPESLKDGVFTTKSDVWSFGVVLWEMATLAEQPYQGLSNEEVL 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 13112048 593 KLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDR 638
Cdd:cd05032 232 KFVIDGGHLDLPENCPDKLLELMRMCWQYNPKMRPTFLEIVSSLKD 277
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
327-640 1.57e-93

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: 295.78  E-value: 1.57e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 327 RIARLSSGEGPTLANVSELELPADPKWELSRARLTLGKPLGEGCFGQVVMAEAIGIDKdraAKPVT-VAVKMLKDDATDK 405
Cdd:cd05105   6 RVIESISPDGHEYIYVDPMQLPYDSRWEFPRDGLVLGRILGSGAFGKVVEGTAYGLSR---SQPVMkVAVKMLKPTARSS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 406 DLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYVLVEYAAKGNL-------REFLRARRPP---------GLD----- 464
Cdd:cd05105  83 EKQALMSELKIMTHLGPHLNIVNLLGACTKSGPIYIITEYCFYGDLvnylhknRDNFLSRHPEkpkkdldifGINpades 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 465 ------YSFDTC-----------------------------------KPPE------------------EQLTFKDLVSC 485
Cdd:cd05105 163 trsyviLSFENKgdymdmkqadttqyvpmleikeaskysdiqrsnydRPASykgsndsevknllsddgsEGLTTLDLLSF 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 486 AYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARDV-HNLDYYKKTTNgRLPVKWMAPEALFDRVYTHQSD 564
Cdd:cd05105 243 TYQVARGMEFLASKNCVHRDLAARNVLLAQGKIVKICDFGLARDImHDSNYVSKGST-FLPVKWMAPESIFDNLYTTLSD 321
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13112048 565 VWSFGVLLWEIFTLGGSPYPGIPVEELF-KLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVL 640
Cdd:cd05105 322 VWSYGILLWEIFSLGGTPYPGMIVDSTFyNKIKSGYRMAKPDHATQEVYDIMVKCWNSEPEKRPSFLHLSDIVESLL 398
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
353-639 7.02e-92

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: 286.17  E-value: 7.02e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 353 WELSRARLTLGKPLGEGCFGQVVMAEAIGidkdraakpVTVAVKMLKDDATDKDlsDLVSEMEMMKMIgKHKNIINLLGA 432
Cdd:cd05039   1 WAINKKDLKLGELIGKGEFGDVMLGDYRG---------QKVAVKCLKDDSTAAQ--AFLAEASVMTTL-RHPNLVQLLGV 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 433 CTQGGPLYVLVEYAAKGNLREFLRARRppgldysfdtckppEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVL 512
Cdd:cd05039  69 VLEGNGLYIVTEYMAKGSLVDYLRSRG--------------RAVITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVL 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 513 VTEDNVMKIADFGLARDVHnldyyKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELF 592
Cdd:cd05039 135 VSEDNVAKVSDFGLAKEAS-----SNQDGGKLPIKWTAPEALREKKFSTKSDVWSFGILLWEIYSFGRVPYPRIPLKDVV 209
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 13112048 593 KLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRV 639
Cdd:cd05039 210 PHVEKGYRMEAPEGCPPEVYKVMKNCWELDPAKRPTFKQLREKLEHI 256
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
354-637 1.38e-90

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: 283.51  E-value: 1.38e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 354 ELSRARLTLGKPLGEGCFGQVVMAEAIGIDKDraAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGAC 433
Cdd:cd05036   2 EVPRKNLTLIRALGQGAFGEVYEGTVSGMPGD--PSPLQVAVKTLPELCSEQDEMDFLMEALIMSKF-NHPNIVRCIGVC 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 434 TQGGPLYVLVEYAAKGNLREFLRARRPpgldysfDTCKPPeeQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLV 513
Cdd:cd05036  79 FQRLPRFILLELMAGGDLKSFLRENRP-------RPEQPS--SLTMLDLLQLAQDVAKGCRYLEENHFIHRDIAARNCLL 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 514 T---EDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEE 590
Cdd:cd05036 150 TckgPGRVAKIGDFGMARDIYRADYYRKGGKAMLPVKWMPPEAFLDGIFTSKTDVWSFGVLLWEIFSLGYMPYPGKSNQE 229
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 13112048 591 LFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLD 637
Cdd:cd05036 230 VMEFVTSGGRMDPPKNCPGPVYRIMTQCWQHIPEDRPNFSTILERLN 276
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
366-636 2.11e-90

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: 282.77  E-value: 2.11e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKDrAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd05044   3 LGSGAFGEVFEGTAKDILGD-GSGETKVAVKTLRKGATDQEKAEFLKEAHLMSNF-KHPNILKLLGVCLDNDPQYIILEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLREFLRARRPPgldysfdtcKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTE----DNVMKI 521
Cdd:cd05044  81 MEGGDLLSYLRAARPT---------AFTPPLLTLKDLLSICVDVAKGCVYLEDMHFVHRDLAARNCLVSSkdyrERVVKI 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 522 ADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGHRM 601
Cdd:cd05044 152 GDFGLARDIYKNDYYRKEGEGLLPVRWMAPESLVDGVFTTQSDVWAFGVLMWEILTLGQQPYPARNNLEVLHFVRAGGRL 231
                       250       260       270
                ....*....|....*....|....*....|....*
gi 13112048 602 DKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDL 636
Cdd:cd05044 232 DQPDNCPDDLYELMLRCWSTDPEERPSFARILEQL 266
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
366-640 5.58e-87

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: 273.84  E-value: 5.58e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEaigIDKDraAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd05047   3 IGEGNFGQVLKAR---IKKD--GLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLREFLRARRPPGLDYSFDTCKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFG 525
Cdd:cd05047  78 APHGNLLDFLRKSRVLETDPAFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 526 LARdvhNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPA 605
Cdd:cd05047 158 LSR---GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPL 234
                       250       260       270
                ....*....|....*....|....*....|....*
gi 13112048 606 NCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVL 640
Cdd:cd05047 235 NCDDEVYDLMRQCWREKPYERPSFAQILVSLNRML 269
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
364-637 1.02e-85

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: 269.92  E-value: 1.02e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVMAEAIGIdkdraakpVTVAVKMLKDDATDKDlsDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLV 443
Cdd:cd05034   1 KKLGAGQFGEVWMGVWNGT--------TKVAVKTLKPGTMSPE--AFLQEAQIMKKL-RHDKLVQLYAVCSDEEPIYIVT 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 444 EYAAKGNLREFLRarrppgldysfdtcKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIAD 523
Cdd:cd05034  70 ELMSKGSLLDYLR--------------TGEGRALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNVCKVAD 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 524 FGLARDVHNlDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGHRMDK 603
Cdd:cd05034 136 FGLARLIED-DEYTAREGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLYEIVTYGRVPYPGMTNREVLEQVERGYRMPK 214
                       250       260       270
                ....*....|....*....|....*....|....
gi 13112048 604 PANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLD 637
Cdd:cd05034 215 PPGCPDELYDIMLQCWKKEPEERPTFEYLQSFLE 248
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
353-637 1.79e-85

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: 269.69  E-value: 1.79e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 353 WELSRARLTLGKPLGEGCFGQVVMaeaiGIDKDRaakpVTVAVKMLKDDATDKdLSDLVSEMEMMKMIgKHKNIINLLGA 432
Cdd:cd05148   1 WERPREEFTLERKLGSGYFGEVWE----GLWKNR----VRVAIKILKSDDLLK-QQDFQKEVQALKRL-RHKHLISLFAV 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 433 CTQGGPLYVLVEYAAKGNLREFLRArrppgldysfdtckpPEEQ-LTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNV 511
Cdd:cd05148  71 CSVGEPVYIITELMEKGSLLAFLRS---------------PEGQvLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNI 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 512 LVTEDNVMKIADFGLARDVHNlDYYKkTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEEL 591
Cdd:cd05148 136 LVGEDLVCKVADFGLARLIKE-DVYL-SSDKKIPYKWTAPEAASHGTFSTKSDVWSFGILLYEMFTYGQVPYPGMNNHEV 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 13112048 592 FKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLD 637
Cdd:cd05148 214 YDQITAGYRMPCPAKCPQEIYKIMLECWAAEPEDRPSFKALREELD 259
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
366-664 5.46e-85

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: 269.56  E-value: 5.46e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEaigIDKDraAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd05089  10 IGEGNFGQVIKAM---IKKD--GLKMNAAIKMLKEFASENDHRDFAGELEVLCKLGHHPNIINLLGACENRGYLYIAIEY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLREFLRARRPPGLDYSFDTCKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFG 525
Cdd:cd05089  85 APYGNLLDFLRKSRVLETDPAFAKEHGTASTLTSQQLLQFASDVAKGMQYLSEKQFIHRDLAARNVLVGENLVSKIADFG 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 526 LARdvhNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPA 605
Cdd:cd05089 165 LSR---GEEVYVKKTMGRLPVRWMAIESLNYSVYTTKSDVWSFGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRMEKPR 241
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 13112048 606 NCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVLTVTSTdeYLDLSApFEQYSPGGQD 664
Cdd:cd05089 242 NCDDEVYELMRQCWRDRPYERPPFSQISVQLSRMLEARKA--YVNMAL-FENFTYAGID 297
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
354-632 1.14e-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: 265.78  E-value: 1.14e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 354 ELSRARLTLGKPLGEGCFGQVVMAEAIGidKDRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGAC 433
Cdd:cd05048   1 EIPLSAVRFLEELGEGAFGKVYKGELLG--PSSEESAISVAIKTLKENASPKTQQDFRREAELMSDL-QHPNIVCLLGVC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 434 TQGGPLYVLVEYAAKGNLREFLRARRP---PGLDYSFDTCKPPEEQLtfkDLVSCAYQVARGMEYLASQKCIHRDLAARN 510
Cdd:cd05048  78 TKEQPQCMLFEYMAHGDLHEFLVRHSPhsdVGVSSDDDGTASSLDQS---DFLHIAIQIAAGMEYLSSHHYVHRDLAARN 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 511 VLVTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEE 590
Cdd:cd05048 155 CLVGDGLTVKISDFGLSRDIYSSDYYRVQSKSLLPVRWMPPEAILYGKFTTESDVWSFGVVLWEIFSYGLQPYYGYSNQE 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 13112048 591 LFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQL 632
Cdd:cd05048 235 VIEMIRSRQLLPCPEDCPARVYSLMVECWHEIPSRRPRFKEI 276
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
354-638 1.06e-81

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: 260.92  E-value: 1.06e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 354 ELSRARLTLGKPLGEGCFGQVVMAEAIGIDKDRaakPVT-VAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGA 432
Cdd:cd05050   1 EYPRNNIEYVRDIGQGAFGRVFQARAPGLLPYE---PFTmVAVKMLKEEASADMQADFQREAALMAEF-DHPNIVKLLGV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 433 CTQGGPLYVLVEYAAKGNLREFLRARRPPGL------DYSFDTCKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDL 506
Cdd:cd05050  77 CAVGKPMCLLFEYMAYGDLNEFLRHRSPRAQcslshsTSSARKCGLNPLPLSCTEQLCIAKQVAAGMAYLSERKFVHRDL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 507 AARNVLVTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGI 586
Cdd:cd05050 157 ATRNCLVGENMVVKIADFGLSRNIYSADYYKASENDAIPIRWMPPESIFYNRYTTESDVWAYGVVLWEIFSYGMQPYYGM 236
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 13112048 587 PVEELFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDR 638
Cdd:cd05050 237 AHEEVIYYVRDGNVLSCPDNCPLELYNLMRLCWSKLPSDRPSFASINRILQR 288
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
352-632 6.82e-79

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: 252.71  E-value: 6.82e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 352 KWELSRARLTLGKPLGEGCFGQVVmaeaigidKDRAAKPVTVAVKMLKDDATDKDlsDLVSEMEMMKMIgKHKNIINLLG 431
Cdd:cd05068   2 QWEIDRKSLKLLRKLGSGQFGEVW--------EGLWNNTTPVAVKTLKPGTMDPE--DFLREAQIMKKL-RHPKLIQLYA 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 432 ACTQGGPLYVLVEYAAKGNLREFLRARRppgldysfdtckppeEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNV 511
Cdd:cd05068  71 VCTLEEPIYIITELMKHGSLLEYLQGKG---------------RSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNV 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 512 LVTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEEL 591
Cdd:cd05068 136 LVGENNICKVADFGLARVIKVEDEYEAREGAKFPIKWTAPEAANYNRFSIKSDVWSFGILLTEIVTYGRIPYPGMTNAEV 215
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 13112048 592 FKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQL 632
Cdd:cd05068 216 LQQVERGYRMPCPPNCPPQLYDIMLECWKADPMERPTFETL 256
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
353-636 8.35e-79

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: 253.35  E-value: 8.35e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 353 WELSRARLTLGKPLGEGCFGQVVmaEAIGIDKDRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIGKHkNIINLLGA 432
Cdd:cd05061   1 WEVSREKITLLRELGQGSFGMVY--EGNARDIIKGEAETRVAVKTVNESASLRERIEFLNEASVMKGFTCH-HVVRLLGV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 433 CTQGGPLYVLVEYAAKGNLREFLRARRPpglDYSFDTCKPPEeqlTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVL 512
Cdd:cd05061  78 VSKGQPTLVVMELMAHGDLKSYLRSLRP---EAENNPGRPPP---TLQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCM 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 513 VTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELF 592
Cdd:cd05061 152 VAHDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMAPESLKDGVFTTSSDMWSFGVVLWEITSLAEQPYQGLSNEQVL 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 13112048 593 KLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDL 636
Cdd:cd05061 232 KFVMDGGYLDQPDNCPERVTDLMRMCWQFNPKMRPTFLEIVNLL 275
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
354-636 1.28e-78

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: 252.39  E-value: 1.28e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 354 ELSRARLTLGKPLGEGCFGQVVMAEAIGIDKDRAAkpVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGAC 433
Cdd:cd05049   1 HIKRDTIVLKRELGEGAFGKVFLGECYNLEPEQDK--MLVAVKTLKDASSPDARKDFEREAELLTNL-QHENIVKFYGVC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 434 TQGGPLYVLVEYAAKGNLREFLRARRPpglDYSFDTCKP-PEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVL 512
Cdd:cd05049  78 TEGDPLLMVFEYMEHGDLNKFLRSHGP---DAAFLASEDsAPGELTLSQLLHIAVQIASGMVYLASQHFVHRDLATRNCL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 513 VTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELF 592
Cdd:cd05049 155 VGTNLVVKIGDFGMSRDIYSTDYYRVGGHTMLPIRWMPPESILYRKFTTESDVWSFGVVLWEIFTYGKQPWFQLSNTEVI 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 13112048 593 KLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDL 636
Cdd:cd05049 235 ECITQGRLLQRPRTCPSEVYAVMLGCWKREPQQRLNIKDIHKRL 278
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
366-664 2.88e-78

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: 252.23  E-value: 2.88e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEaigIDKDraAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd05088  15 IGEGNFGQVLKAR---IKKD--GLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEY 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLREFLRARRPPGLDYSFDTCKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFG 525
Cdd:cd05088  90 APHGNLLDFLRKSRVLETDPAFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFG 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 526 LARdvhNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPA 605
Cdd:cd05088 170 LSR---GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPL 246
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 13112048 606 NCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVLTVTSTdeYLDLSApFEQYSPGGQD 664
Cdd:cd05088 247 NCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLEERKT--YVNTTL-YEKFTYAGID 302
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
354-632 2.39e-76

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: 246.87  E-value: 2.39e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 354 ELSRARLTLGKPLGEGCFGQVVMAEAIGID---------KDRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHK 424
Cdd:cd05051   1 EFPREKLEFVEKLGEGQFGEVHLCEANGLSdltsddfigNDNKDEPVLVAVKMLRPDASKNAREDFLKEVKIMSQL-KDP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 425 NIINLLGACTQGGPLYVLVEYAAKGNLREFLRARRPPGLDYSfdtcKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHR 504
Cdd:cd05051  80 NIVRLLGVCTRDEPLCMIVEYMENGDLNQFLQKHEAETQGAS----ATNSKTLSYGTLLYMATQIASGMKYLESLNFVHR 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 505 DLAARNVLVTEDNVMKIADFGLARDVHNLDYYKktTNGR--LPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGG-S 581
Cdd:cd05051 156 DLATRNCLVGPNYTIKIADFGMSRNLYSGDYYR--IEGRavLPIRWMAWESILLGKFTTKSDVWAFGVTLWEILTLCKeQ 233
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 13112048 582 PYPGIPVE-------ELFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQL 632
Cdd:cd05051 234 PYEHLTDEqvienagEFFRDDGMEVYLSRPPNCPKEIYELMLECWRRDEEDRPTFREI 291
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
364-638 2.86e-76

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: 245.34  E-value: 2.86e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVMaeaiGIDKDRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACtQGGPLYVLV 443
Cdd:cd05060   1 KELGHGNFGSVRK----GVYLMKSGKEVEVAVKTLKQEHEKAGKKEFLREASVMAQL-DHPCIVRLIGVC-KGEPLMLVM 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 444 EYAAKGNLREFLRARRppgldysfdtckppeeQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIAD 523
Cdd:cd05060  75 ELAPLGPLLKYLKKRR----------------EIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISD 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 524 FGLARDVH-NLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGHRMD 602
Cdd:cd05060 139 FGMSRALGaGSDYYRATTAGRWPLKWYAPECINYGKFSSKSDVWSYGVTLWEAFSYGAKPYGEMKGPEVIAMLESGERLP 218
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 13112048 603 KPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDR 638
Cdd:cd05060 219 RPEECPQEIYSIMLSCWKYRPEDRPTFSELESTFRR 254
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
353-638 4.98e-76

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: 244.78  E-value: 4.98e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 353 WELSRARLTLGKPLGEGCFGQVVMAEAIGidkdraakpVTVAVKMLKDDATDKDLSDLVSEMEMMKmigkHKNIINLLGA 432
Cdd:cd05083   1 WLLNLQKLTLGEIIGEGEFGAVLQGEYMG---------QKVAVKNIKCDVTAQAFLEETAVMTKLQ----HKNLVRLLGV 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 433 CTQGGpLYVLVEYAAKGNLREFLRARRPPGLdysfdtckPPEEQLTFkdlvscAYQVARGMEYLASQKCIHRDLAARNVL 512
Cdd:cd05083  68 ILHNG-LYIVMELMSKGNLVNFLRSRGRALV--------PVIQLLQF------SLDVAEGMEYLESKKLVHRDLAARNIL 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 513 VTEDNVMKIADFGLAR-DVHNLDyykkttNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEEL 591
Cdd:cd05083 133 VSEDGVAKISDFGLAKvGSMGVD------NSRLPVKWTAPEALKNKKFSSKSDVWSYGVLLWEVFSYGRAPYPKMSVKEV 206
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 13112048 592 FKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDR 638
Cdd:cd05083 207 KEAVEKGYRMEPPEGCPPDVYSIMTSCWEAEPGKRPSFKKLREKLEK 253
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
353-640 5.27e-76

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: 245.02  E-value: 5.27e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 353 WELSRARLTLGKPLGEGCFGQVVMaeaiGIDKDRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGA 432
Cdd:cd05056   1 YEIQREDITLGRCIGEGQFGDVYQ----GVYMSPENEKIAVAVKTCKNCTSPSVREKFLQEAYIMRQF-DHPHIVKLIGV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 433 CTQGgPLYVLVEYAAKGNLREFLRARRppgldysfdtckppeEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVL 512
Cdd:cd05056  76 ITEN-PVWIVMELAPLGELRSYLQVNK---------------YSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVL 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 513 VTEDNVMKIADFGLARDVHNLDYYKKTTnGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELF 592
Cdd:cd05056 140 VSSPDCVKLGDFGLSRYMEDESYYKASK-GKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMLGVKPFQGVKNNDVI 218
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 13112048 593 KLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVL 640
Cdd:cd05056 219 GRIENGERLPMPPNCPPTLYSLMTKCWAYDPSKRPRFTELKAQLSDIL 266
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
360-640 8.53e-76

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: 244.75  E-value: 8.53e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 360 LTLGKPLGEGCFGQVVMAEAigidKDRAAKPVTVAVKMLK-DDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGP 438
Cdd:cd05035   1 LKLGKILGEGEFGSVMEAQL----KQDDGSQLKVAVKTMKvDIHTYSEIEEFLSEAACMKDF-DHPNVMRLIGVCFTASD 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 439 L------YVLVEYAAKGNLREFLRARRPPGLdysfdtckppEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVL 512
Cdd:cd05035  76 LnkppspMVILPFMKHGDLHSYLLYSRLGGL----------PEKLPLQTLLKFMVDIAKGMEYLSNRNFIHRDLAARNCM 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 513 VTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELF 592
Cdd:cd05035 146 LDENMTVCVADFGLSRKIYSGDYYRQGRISKMPVKWIALESLADNVYTSKSDVWSFGVTMWEIATRGQTPYPGVENHEIY 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 13112048 593 KLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVL 640
Cdd:cd05035 226 DYLRNGNRLKQPEDCLDEVYFLMYFCWTVDPKDRPTFTKLREVLENIL 273
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
353-637 1.37e-75

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: 243.87  E-value: 1.37e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 353 WELSRARLTLGKPLGEGCFGQVVmaEAIGIDKDRaakpvTVAVKMLKDDATDkdLSDLVSEMEMMKMIgKHKNIINLLGA 432
Cdd:cd05052   1 WEIERTDITMKHKLGGGQYGEVY--EGVWKKYNL-----TVAVKTLKEDTME--VEEFLKEAAVMKEI-KHPNLVQLLGV 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 433 CTQGGPLYVLVEYAAKGNLREFLRarrppgldysfdtcKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVL 512
Cdd:cd05052  71 CTREPPFYIITEFMPYGNLLDYLR--------------ECNREELNAVVLLYMATQIASAMEYLEKKNFIHRDLAARNCL 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 513 VTEDNVMKIADFGLARDVHNlDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELF 592
Cdd:cd05052 137 VGENHLVKVADFGLSRLMTG-DTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVY 215
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 13112048 593 KLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLD 637
Cdd:cd05052 216 ELLEKGYRMERPEGCPPKVYELMRACWQWNPSDRPSFAEIHQALE 260
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
360-640 1.15e-74

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: 242.29  E-value: 1.15e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 360 LTLGKPLGEGCFGQVVMAEaigIDKDRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACT-QGGP 438
Cdd:cd05038   6 LKFIKQLGEGHFGSVELCR---YDPLGDNTGEQVAVKSLQPSGEEQHMSDFKREIEILRTL-DHEYIVKYKGVCEsPGRR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 439 -LYVLVEYAAKGNLREFLRARRPpgldysfdtckppeeQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDN 517
Cdd:cd05038  82 sLRLIMEYLPSGSLRDYLQRHRD---------------QIDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILVESED 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 518 VMKIADFGLARDV-HNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIP--------- 587
Cdd:cd05038 147 LVKISDFGLAKVLpEDKEYYYVKEPGESPIFWYAPECLRESRFSSASDVWSFGVTLYELFTYGDPSQSPPAlflrmigia 226
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 13112048 588 -----VEELFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVL 640
Cdd:cd05038 227 qgqmiVTRLLELLKSGERLPRPPSCPDEVYDLMKECWEYEPQDRPSFSDLILIIDRLR 284
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
353-639 1.14e-72

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: 236.03  E-value: 1.14e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 353 WELSRARLTLGKPLGEGCFGQVVMAEAIGidkdraakpVTVAVKMLKDDATDKDLsdlVSEMEMMKMIgKHKNIINLLGA 432
Cdd:cd05082   1 WALNMKELKLLQTIGKGEFGDVMLGDYRG---------NKVAVKCIKNDATAQAF---LAEASVMTQL-RHSNLVQLLGV 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 433 CTQ-GGPLYVLVEYAAKGNLREFLRARRPPGLD------YSFDTCKppeeqltfkdlvscayqvarGMEYLASQKCIHRD 505
Cdd:cd05082  68 IVEeKGGLYIVTEYMAKGSLVDYLRSRGRSVLGgdcllkFSLDVCE--------------------AMEYLEGNNFVHRD 127
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 506 LAARNVLVTEDNVMKIADFGLARDVHNLDyykktTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPG 585
Cdd:cd05082 128 LAARNVLVSEDNVAKVSDFGLTKEASSTQ-----DTGKLPVKWTAPEALREKKFSTKSDVWSFGILLWEIYSFGRVPYPR 202
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 13112048 586 IPVEELFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRV 639
Cdd:cd05082 203 IPLKDVVPRVEKGYKMDAPDGCPPAVYDVMKNCWHLDAAMRPSFLQLREQLEHI 256
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
366-637 1.63e-72

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: 235.42  E-value: 1.63e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAigidkdrAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd05041   3 IGRGNFGDVYRGVL-------KPDNTEVAVKTCRETLPPDLKRKFLQEARILKQY-DHPNIVKLIGVCVQKQPIMIVMEL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLREFLRArrppgldysfdtckpPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFG 525
Cdd:cd05041  75 VPGGSLLTFLRK---------------KGARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFG 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 526 LARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPA 605
Cdd:cd05041 140 MSREEEDGEYTVSDGLKQIPIKWTAPEALNYGRYTSESDVWSFGILLWEIFSLGATPYPGMSNQQTREQIESGYRMPAPE 219
                       250       260       270
                ....*....|....*....|....*....|..
gi 13112048 606 NCTHDLYMIMRECWHAAPSQRPTFKQLVEDLD 637
Cdd:cd05041 220 LCPEAVYRLMLQCWAYDPENRPSFSEIYNELQ 251
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
355-636 2.49e-72

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: 235.82  E-value: 2.49e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 355 LSRARLTLGKPLGEGCFGQVVMAEAIGIDKDRAAKPVtvAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACT 434
Cdd:cd05046   2 FPRSNLQEITTLGRGEFGEVFLAKAKGIEEEGGETLV--LVKALQKTKDENLQSEFRRELDMFRKL-SHKNVVRLLGLCR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 435 QGGPLYVLVEYAAKGNLREFLRARRPpgldySFDTCKPPEeqLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVT 514
Cdd:cd05046  79 EAEPHYMILEYTDLGDLKQFLRATKS-----KDEKLKPPP--LSTKQKVALCTQIALGMDHLSNARFVHRDLAARNCLVS 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 515 EDNVMKIADFGLARDVHNLDYYKkTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKL 594
Cdd:cd05046 152 SQREVKVSLLSLSKDVYNSEYYK-LRNALIPLRWLAPEAVQEDDFSTKSDVWSFGVLMWEVFTQGELPFYGLSDEEVLNR 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 13112048 595 LKEGH-RMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDL 636
Cdd:cd05046 231 LQAGKlELPVPEGCPSRLYKLMTRCWAVNPKDRPSFSELVSAL 273
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
366-640 4.00e-72

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: 234.68  E-value: 4.00e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIgidkDRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGAC--TQGGPLYVLv 443
Cdd:cd05058   3 IGKGHFGCVYHGTLI----DSDGQKIHCAVKSLNRITDIEEVEQFLKEGIIMKDF-SHPNVLSLLGIClpSEGSPLVVL- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 444 EYAAKGNLREFLRArrppgldysfdtckpPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIAD 523
Cdd:cd05058  77 PYMKHGDLRNFIRS---------------ETHNPTVKDLIGFGLQVAKGMEYLASKKFVHRDLAARNCMLDESFTVKVAD 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 524 FGLARDVHNLDYYK--KTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGHRM 601
Cdd:cd05058 142 FGLARDIYDKEYYSvhNHTGAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELMTRGAPPYPDVDSFDITVYLLQGRRL 221
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 13112048 602 DKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVL 640
Cdd:cd05058 222 LQPEYCPDPLYEVMLSCWHPKPEMRPTFSELVSRISQIF 260
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
360-636 5.51e-72

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: 233.88  E-value: 5.51e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 360 LTLGKPLGEGCFGQVVMAEAIGIDKdraakpvtVAVKMLKDDATDKDlsDLVSEMEMMKMIgKHKNIINLLGACTQGGPL 439
Cdd:cd05059   6 LTFLKELGSGQFGVVHLGKWRGKID--------VAIKMIKEGSMSED--DFIEEAKVMMKL-SHPKLVQLYGVCTKQRPI 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 440 YVLVEYAAKGNLREFLRARRppgldysfdtckppeEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVM 519
Cdd:cd05059  75 FIVTEYMANGCLLNYLRERR---------------GKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVV 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 520 KIADFGLARDVHNlDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGH 599
Cdd:cd05059 140 KVSDFGLARYVLD-DEYTSSVGTKFPVKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSEGKMPYERFSNSEVVEHISQGY 218
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 13112048 600 RMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDL 636
Cdd:cd05059 219 RLYRPHLAPTEVYTIMYSCWHEKPEERPTFKILLSQL 255
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
354-640 7.93e-72

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: 234.62  E-value: 7.93e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 354 ELSRARLTLGKPLGEGCFGQVvmAEAIGIDKDRAAKpVTVAVKMLKDDATDKDLSDLVSEMEMMKMIGkHKNIINLLGAC 433
Cdd:cd05057   3 IVKETELEKGKVLGSGAFGTV--YKGVWIPEGEKVK-IPVAIKVLREETGPKANEEILDEAYVMASVD-HPHLVRLLGIC 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 434 TqGGPLYVLVEYAAKGNLREFLRARRppgldysfdtckppeEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLV 513
Cdd:cd05057  79 L-SSQVQLITQLMPLGCLLDYVRNHR---------------DNIGSQLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLV 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 514 TEDNVMKIADFGLAR--DVHNLDYykKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEEL 591
Cdd:cd05057 143 KTPNHVKITDFGLAKllDVDEKEY--HAEGGKVPIKWMALESIQYRIYTHKSDVWSYGVTVWELMTFGAKPYEGIPAVEI 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 13112048 592 FKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVL 640
Cdd:cd05057 221 PDLLEKGERLPQPPICTIDVYMVLVKCWMIDAESRPTFKELANEFSKMA 269
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
366-636 1.06e-71

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: 232.81  E-value: 1.06e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDkdraakpvtVAVKMLK-DDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVE 444
Cdd:cd13999   1 IGSGSFGEVYKGKWRGTD---------VAIKKLKvEDDNDELLKEFRREVSILSKL-RHPNIVQFIGACLSPPPLCIVTE 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 445 YAAKGNLREFLRARRPPgldysfdtckppeeqLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADF 524
Cdd:cd13999  71 YMPGGSLYDLLHKKKIP---------------LSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADF 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 525 GLARDVHNLDYYKKTTNGRlpVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGI-PVEELFKLLKEGHRMDK 603
Cdd:cd13999 136 GLSRIKNSTTEKMTGVVGT--PRWMAPEVLRGEPYTEKADVYSFGIVLWELLT-GEVPFKELsPIQIAAAVVQKGLRPPI 212
                       250       260       270
                ....*....|....*....|....*....|...
gi 13112048 604 PANCTHDLYMIMRECWHAAPSQRPTFKQLVEDL 636
Cdd:cd13999 213 PPDCPPELSKLIKRCWNEDPEKRPSFSEIVKRL 245
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
355-632 5.41e-70

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: 229.85  E-value: 5.41e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 355 LSRARLTLGKPLGEGCFGQVVMAEAIGIDKDRaaKPVTVAVKMLKDdATDKDLSDLVSEMEMMKMIgKHKNIINLLGACT 434
Cdd:cd05092   2 IKRRDIVLKWELGEGAFGKVFLAECHNLLPEQ--DKMLVAVKALKE-ATESARQDFQREAELLTVL-QHQHIVRFYGVCT 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 435 QGGPLYVLVEYAAKGNLREFLRARRPPG--LDYSFDTckpPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVL 512
Cdd:cd05092  78 EGEPLIMVFEYMRHGDLNRFLRSHGPDAkiLDGGEGQ---APGQLTLGQMLQIASQIASGMVYLASLHFVHRDLATRNCL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 513 VTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELF 592
Cdd:cd05092 155 VGQGLVVKIGDFGMSRDIYSTDYYRVGGRTMLPIRWMPPESILYRKFTTESDIWSFGVVLWEIFTYGKQPWYQLSNTEAI 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 13112048 593 KLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQL 632
Cdd:cd05092 235 ECITQGRELERPRTCPPEVYAIMQGCWQREPQQRHSIKDI 274
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
360-640 6.54e-70

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: 228.80  E-value: 6.54e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 360 LTLGKPLGEGCFGQVVMaeaiGIDKDRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPL 439
Cdd:cd05033   6 VTIEKVIGGGEFGEVCS----GSLKLPGKKEIDVAIKTLKSGYSDKQRLDFLTEASIMGQF-DHPNVIRLEGVVTKSRPV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 440 YVLVEYAAKGNLREFLRARrppgldysfdtckppEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVM 519
Cdd:cd05033  81 MIVTEYMENGSLDKFLREN---------------DGKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLVC 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 520 KIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGH 599
Cdd:cd05033 146 KVSDFGLSRRLEDSEATYTTKGGKIPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSYGERPYWDMSNQDVIKAVEDGY 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 13112048 600 RMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVL 640
Cdd:cd05033 226 RLPPPMDCPSALYQLMLDCWQKDRNERPTFSQIVSTLDKMI 266
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
353-636 8.91e-70

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: 229.15  E-value: 8.91e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 353 WELSRARLTLGKPLGEGCFGQVVMAEAIGIDKDraaKPVT-VAVKMLKDDATDKDLSDLVSEMEMMKMIGKHkNIINLLG 431
Cdd:cd05062   1 WEVAREKITMSRELGQGSFGMVYEGIAKGVVKD---EPETrVAIKTVNEAASMRERIEFLNEASVMKEFNCH-HVVRLLG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 432 ACTQGGPLYVLVEYAAKGNLREFLRARRPPgldysfDTCKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNV 511
Cdd:cd05062  77 VVSQGQPTLVIMELMTRGDLKSYLRSLRPE------MENNPVQAPPSLKKMIQMAGEIADGMAYLNANKFVHRDLAARNC 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 512 LVTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEEL 591
Cdd:cd05062 151 MVAEDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTYSDVWSFGVVLWEIATLAEQPYQGMSNEQV 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 13112048 592 FKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDL 636
Cdd:cd05062 231 LRFVMEGGLLDKPDNCPDMLFELMRMCWQYNPKMRPSFLEIISSI 275
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
356-636 1.59e-69

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: 228.49  E-value: 1.59e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 356 SRARLTLGKPLGEGCFGQVVMaeaiGIDKDRAAKPVTVAVKMLKDDATDKDLSDLVSEMemMKMIG-KHKNIINLLGACT 434
Cdd:cd05043   4 SRERVTLSDLLQEGTFGRIFH----GILRDEKGKEEEVLVKTVKDHASEIQVTMLLQES--SLLYGlSHQNLLPILHVCI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 435 Q-GGPLYVLVEYAAKGNLREFLRarrppgldysfdTCKPPEEQ----LTFKDLVSCAYQVARGMEYLASQKCIHRDLAAR 509
Cdd:cd05043  78 EdGEKPMVLYPYMNWGNLKLFLQ------------QCRLSEANnpqaLSTQQLVHMALQIACGMSYLHRRGVIHKDIAAR 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 510 NVLVTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVE 589
Cdd:cd05043 146 NCVIDDELQVKITDNALSRDLFPMDYHCLGDNENRPIKWMSLESLVNKEYSSASDVWSFGVLLWELMTLGQTPYVEIDPF 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 13112048 590 ELFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDL 636
Cdd:cd05043 226 EMAAYLKDGYRLAQPINCPDELFAVMACCWALDPEERPSFQQLVQCL 272
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
355-640 4.08e-69

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: 227.51  E-value: 4.08e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 355 LSRARLTLGKPLGEGCFGQVVMAEAigidKDRAAKPVTVAVKMLK-DDATDKDLSDLVSEMEMMKMIgKHKNIINLLGAC 433
Cdd:cd14204   4 IDRNLLSLGKVLGEGEFGSVMEGEL----QQPDGTNHKVAVKTMKlDNFSQREIEEFLSEAACMKDF-NHPNVIRLLGVC 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 434 TQGGPLY-----VLVEYAAKGNLREFL-RARRPPGLDYsfdtckppeeqLTFKDLVSCAYQVARGMEYLASQKCIHRDLA 507
Cdd:cd14204  79 LEVGSQRipkpmVILPFMKYGDLHSFLlRSRLGSGPQH-----------VPLQTLLKFMIDIALGMEYLSSRNFLHRDLA 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 508 ARNVLVTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIP 587
Cdd:cd14204 148 ARNCMLRDDMTVCVADFGLSKKIYSGDYYRQGRIAKMPVKWIAVESLADRVYTVKSDVWAFGVTMWEIATRGMTPYPGVQ 227
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 13112048 588 VEELFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVL 640
Cdd:cd14204 228 NHEIYDYLLHGHRLKQPEDCLDELYDIMYSCWRSDPTDRPTFTQLRENLEKLL 280
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
359-640 7.73e-68

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: 223.73  E-value: 7.73e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 359 RLTLGKPLGEGCFGQVVMAEaigIDKDRAAkpVTVAVKMLKDD-ATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQG- 436
Cdd:cd05075   1 KLALGKTLGEGEFGSVMEGQ---LNQDDSV--LKVAVKTMKIAiCTRSEMEDFLSEAVCMKEF-DHPNVMRLIGVCLQNt 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 437 ------GPLyVLVEYAAKGNLREFLRarrppgldYSFDTCKPPeeQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARN 510
Cdd:cd05075  75 esegypSPV-VILPFMKHGDLHSFLL--------YSRLGDCPV--YLPTQMLVKFMTDIASGMEYLSSKNFIHRDLAARN 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 511 VLVTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEE 590
Cdd:cd05075 144 CMLNENMNVCVADFGLSKKIYNGDYYRQGRISKMPVKWIAIESLADRVYTTKSDVWSFGVTMWEIATRGQTPYPGVENSE 223
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 13112048 591 LFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVL 640
Cdd:cd05075 224 IYDYLRQGNRLKQPPDCLDGLYELMSSCWLLNPKDRPSFETLRCELEKIL 273
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
363-636 1.43e-66

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: 219.49  E-value: 1.43e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 363 GKPLGEGCFGQVVMaeaiGIDKDRAAkpvtVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVL 442
Cdd:cd05085   1 GELLGKGNFGEVYK----GTLKDKTP----VAVKTCKEDLPQELKIKFLSEARILKQY-DHPNIVKLIGVCTQRQPIYIV 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 443 VEYAAKGNLREFLRARRppgldysfdtckppeEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIA 522
Cdd:cd05085  72 MELVPGGDFLSFLRKKK---------------DELKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNALKIS 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 523 DFGLARDvHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGHRMD 602
Cdd:cd05085 137 DFGMSRQ-EDDGVYSSSGLKQIPIKWTAPEALNYGRYSSESDVWSFGILLWETFSLGVCPYPGMTNQQAREQVEKGYRMS 215
                       250       260       270
                ....*....|....*....|....*....|....
gi 13112048 603 KPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDL 636
Cdd:cd05085 216 APQRCPEDIYKIMQRCWDYNPENRPKFSELQKEL 249
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
359-640 4.14e-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: 216.71  E-value: 4.14e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 359 RLTLGKPLGEGCFGQVVMAEaIGIDKDRAAKpvtVAVKMLKDDA-TDKDLSDLVSEMEMMKMIgKHKNIINLLGAC---- 433
Cdd:cd05074  10 QFTLGRMLGKGEFGSVREAQ-LKSEDGSFQK---VAVKMLKADIfSSSDIEEFLREAACMKEF-DHPNVIKLIGVSlrsr 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 434 TQGG---PLyVLVEYAAKGNLREFLRARRPPglDYSFDtckppeeqLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARN 510
Cdd:cd05074  85 AKGRlpiPM-VILPFMKHGDLHTFLLMSRIG--EEPFT--------LPLQTLVRFMIDIASGMEYLSSKNFIHRDLAARN 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 511 VLVTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEE 590
Cdd:cd05074 154 CMLNENMTVCVADFGLSKKIYSGDYYRQGCASKLPVKWLALESLADNVYTTHSDVWAFGVTMWEIMTRGQTPYAGVENSE 233
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 13112048 591 LFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVL 640
Cdd:cd05074 234 IYNYLIKGNRLKQPPDCLEDVYELMCQCWSPEPKCRPSFQHLRDQLELIW 283
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
364-636 7.97e-65

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: 215.28  E-value: 7.97e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVMAEAigidKDRAAKPVTVAVKMLKDDATDKD--LSDLVSEMEMMKMIgKHKNIINLLGACTQGgPLYV 441
Cdd:cd05040   1 EKLGDGSFGVVRRGEW----TTPSGKVIQVAVKCLKSDVLSQPnaMDDFLKEVNAMHSL-DHPNLIRLYGVVLSS-PLMM 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 442 LVEYAAKGNLREFLRARRPPgldysfdtckppeeqLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKI 521
Cdd:cd05040  75 VTELAPLGSLLDRLRKDQGH---------------FLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLASKDKVKI 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 522 ADFGLARDV-HNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEE-LFKLLKEGH 599
Cdd:cd05040 140 GDFGLMRALpQNEDHYVMQEHRKVPFAWCAPESLKTRKFSHASDVWMFGVTLWEMFTYGEEPWLGLNGSQiLEKIDKEGE 219
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 13112048 600 RMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDL 636
Cdd:cd05040 220 RLERPDDCPQDIYNVMLQCWAHKPADRPTFVALRDFL 256
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
363-636 1.80e-64

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: 214.02  E-value: 1.80e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 363 GKPLGEGCFGQVVMAEAigidkdrAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVL 442
Cdd:cd05084   1 GERIGRGNFGEVFSGRL-------RADNTPVAVKSCRETLPPDLKAKFLQEARILKQY-SHPNIVRLIGVCTQKQPIYIV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 443 VEYAAKGNLREFLRARRPpgldysfdtckppeeQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIA 522
Cdd:cd05084  73 MELVQGGDFLTFLRTEGP---------------RLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKIS 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 523 DFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGHRMD 602
Cdd:cd05084 138 DFGMSREEEDGVYAATGGMKQIPVKWTAPEALNYGRYSSESDVWSFGILLWETFSLGAVPYANLSNQQTREAVEQGVRLP 217
                       250       260       270
                ....*....|....*....|....*....|....
gi 13112048 603 KPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDL 636
Cdd:cd05084 218 CPENCPDEVYRLMEQCWEYDPRKRPSFSTVHQDL 251
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
151-245 5.93e-64

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 206.63  E-value: 5.93e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 151 PYWTRPERMDKKLLAVPAANTVRFRCPAAGNPTPSISWLKNGREFRGEHRIGGIKLRHQQWSLVMESVVPSDRGNYTCVV 230
Cdd:cd05857   1 PYWTNPEKMEKKLHAVPAANTVKFRCPAAGNPTPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCVV 80
                        90
                ....*....|....*
gi 13112048 231 ENKFGSIRQTYTLDV 245
Cdd:cd05857  81 ENEYGSINHTYHLDV 95
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
361-635 4.00e-63

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 210.46  E-value: 4.00e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048    361 TLGKPLGEGCFGQVVMAEAIGIDKdraakpvTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLY 440
Cdd:smart00220   2 EILEKLGEGSFGKVYLARDKKTGK-------LVAIKVIKKKKIKKDRERILREIKILKKL-KHPNIVRLYDVFEDEDKLY 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048    441 VLVEYAAKGNLREFLRARRPpgldysfdtckppeeqLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMK 520
Cdd:smart00220  74 LVMEYCEGGDLFDLLKKRGR----------------LSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVK 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048    521 IADFGLARDVHNLDYYKK---TTNgrlpvkWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGI-PVEELFKLLK 596
Cdd:smart00220 138 LADFGLARQLDPGEKLTTfvgTPE------YMAPEVLLGKGYGKAVDIWSLGVILYELLT-GKPPFPGDdQLLELFKKIG 210
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 13112048    597 EGHR--MDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVED 635
Cdd:smart00220 211 KPKPpfPPPEWDISPEAKDLIRKLLVKDPEKRLTAEEALQH 251
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
353-645 9.67e-63

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: 210.28  E-value: 9.67e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 353 WELSRARLTLGKPLGEGCFGQVVMAEAIGIDKdraakpvtVAVKMLKDDATDkdLSDLVSEMEMMKMIgKHKNIINLLGA 432
Cdd:cd05072   2 WEIPRESIKLVKKLGAGQFGEVWMGYYNNSTK--------VAVKTLKPGTMS--VQAFLEEANLMKTL-QHDKLVRLYAV 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 433 CTQGGPLYVLVEYAAKGNLREFLRARRppgldysfdtckppEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVL 512
Cdd:cd05072  71 VTKEEPIYIITEYMAKGSLLDFLKSDE--------------GGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVL 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 513 VTEDNVMKIADFGLARDVHNlDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELF 592
Cdd:cd05072 137 VSESLMCKIADFGLARVIED-NEYTAREGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLYEIVTYGKIPYPGMSNSDVM 215
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 13112048 593 KLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVLTVTST 645
Cdd:cd05072 216 SALQRGYRMPRMENCPDELYDIMKTCWKEKAEERPTFDYLQSVLDDFYTATEG 268
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
354-632 9.63e-62

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: 208.31  E-value: 9.63e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 354 ELSRARLTLGKPLGEGCFGQVVMAEAIGI----DKD-----RAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHK 424
Cdd:cd05095   1 EFPRKLLTFKEKLGEGQFGEVHLCEAEGMekfmDKDfalevSENQPVLVAVKMLRADANKNARNDFLKEIKIMSRL-KDP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 425 NIINLLGACTQGGPLYVLVEYAAKGNLREFLRARRPPGLDYSFDTCKPpeeqLTFKDLVSCAYQVARGMEYLASQKCIHR 504
Cdd:cd05095  80 NIIRLLAVCITDDPLCMITEYMENGDLNQFLSRQQPEGQLALPSNALT----VSYSDLRFMAAQIASGMKYLSSLNFVHR 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 505 DLAARNVLVTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTL-GGSPY 583
Cdd:cd05095 156 DLATRNCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETLTFcREQPY 235
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 13112048 584 PGIPVE-------ELFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQL 632
Cdd:cd05095 236 SQLSDEqvientgEFFRDQGRQTYLPQPALCPDSVYKLMLSCWRRDTKDRPSFQEI 291
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
355-632 1.23e-61

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: 207.59  E-value: 1.23e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 355 LSRARLTLGKPLGEGCFGQVVMAEAIGIDKDRaaKPVTVAVKMLKDdATDKDLSDLVSEMEMMKMIgKHKNIINLLGACT 434
Cdd:cd05093   2 IKRHNIVLKRELGEGAFGKVFLAECYNLCPEQ--DKILVAVKTLKD-ASDNARKDFHREAELLTNL-QHEHIVKFYGVCV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 435 QGGPLYVLVEYAAKGNLREFLRARRPPGLDYSfdTCKPPEEqLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVT 514
Cdd:cd05093  78 EGDPLIMVFEYMKHGDLNKFLRAHGPDAVLMA--EGNRPAE-LTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 515 EDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKL 594
Cdd:cd05093 155 ENLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIEC 234
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 13112048 595 LKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQL 632
Cdd:cd05093 235 ITQGRVLQRPRTCPKEVYDLMLGCWQREPHMRLNIKEI 272
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
352-641 2.01e-60

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: 203.58  E-value: 2.01e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 352 KWELSRARLTLGKPLGEGCFGQVVMAEAIGIDKdraakpvtVAVKMLKDDATDKDLsdLVSEMEMMKMIgKHKNIINLLG 431
Cdd:cd05067   1 EWEVPRETLKLVERLGAGQFGEVWMGYYNGHTK--------VAIKSLKQGSMSPDA--FLAEANLMKQL-QHQRLVRLYA 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 432 ACTQGgPLYVLVEYAAKGNLREFLRArrPPGLDysfdtckppeeqLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNV 511
Cdd:cd05067  70 VVTQE-PIYIITEYMENGSLVDFLKT--PSGIK------------LTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANI 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 512 LVTEDNVMKIADFGLARDVHNLDYYKKTtNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEEL 591
Cdd:cd05067 135 LVSDTLSCKIADFGLARLIEDNEYTARE-GAKFPIKWTAPEAINYGTFTIKSDVWSFGILLTEIVTHGRIPYPGMTNPEV 213
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 13112048 592 FKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVLT 641
Cdd:cd05067 214 IQNLERGYRMPRPDNCPEELYQLMRLCWKERPEDRPTFEYLRSVLEDFFT 263
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
354-632 4.27e-60

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: 203.32  E-value: 4.27e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 354 ELSRARLTLGKPLGEGCFGQVVMAEAIGIDKDRAAkpvTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGAC 433
Cdd:cd05090   1 ELPLSAVRFMEELGECAFGKIYKGHLYLPGMDHAQ---LVAIKTLKDYNNPQQWNEFQQEASLMTEL-HHPNIVCLLGVV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 434 TQGGPLYVLVEYAAKGNLREFLRARRP-PGLDYSFDTCKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVL 512
Cdd:cd05090  77 TQEQPVCMLFEFMNQGDLHEFLIMRSPhSDVGCSSDEDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNIL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 513 VTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELF 592
Cdd:cd05090 157 VGEQLHVKISDLGLSREIYSSDYYRVQNKSLLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVI 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 13112048 593 KLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQL 632
Cdd:cd05090 237 EMVRKRQLLPCSEDCPPRMYSLMTECWQEIPSRRPRFKDI 276
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
354-632 6.68e-60

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: 202.94  E-value: 6.68e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 354 ELSRARLTLGKPLGEGCFGQVVMAEAIGIDKDRAAKpvTVAVKMLKDDAtDKDLSDLVSEMEMMKMIGKHKNIINLLGAC 433
Cdd:cd05091   2 EINLSAVRFMEELGEDRFGKVYKGHLFGTAPGEQTQ--AVAIKTLKDKA-EGPLREEFRHEAMLRSRLQHPNIVCLLGVV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 434 TQGGPLYVLVEYAAKGNLREFLRARRPPGLDYSFDTCKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLV 513
Cdd:cd05091  79 TKEQPMSMIFSYCSHGDLHEFLVMRSPHSDVGSTDDDKTVKSTLEPADFLHIVTQIAAGMEYLSSHHVVHKDLATRNVLV 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 514 TEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFK 593
Cdd:cd05091 159 FDKLNVKISDLGLFREVYAADYYKLMGNSLLPIRWMSPEAIMYGKFSIDSDIWSYGVVLWEVFSYGLQPYCGYSNQDVIE 238
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 13112048 594 LLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQL 632
Cdd:cd05091 239 MIRNRQVLPCPDDCPAWVYTLMLECWNEFPSRRPRFKDI 277
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
355-639 1.04e-59

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: 202.18  E-value: 1.04e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 355 LSRARLTLGKPLGEGCFGQVVmaEAIGIDKDRAAKpVTVAVKMLKDDATDKDLSDLVSEMEMMKMIGKhKNIINLLGACT 434
Cdd:cd05109   4 LKETELKKVKVLGSGAFGTVY--KGIWIPDGENVK-IPVAIKVLRENTSPKANKEILDEAYVMAGVGS-PYVCRLLGICL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 435 QGgPLYVLVEYAAKGNLREFLRARRppgldysfdtckppeEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVT 514
Cdd:cd05109  80 TS-TVQLVTQLMPYGCLLDYVRENK---------------DRIGSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVK 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 515 EDNVMKIADFGLAR--DVHNLDYYkkTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELF 592
Cdd:cd05109 144 SPNHVKITDFGLARllDIDETEYH--ADGGKVPIKWMALESILHRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIP 221
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 13112048 593 KLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRV 639
Cdd:cd05109 222 DLLEKGERLPQPPICTIDVYMIMVKCWMIDSECRPRFRELVDEFSRM 268
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
354-632 2.39e-59

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: 2.39e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 354 ELSRARLTLGKPLGEGCFGQVVMAEAIGIDK-------DRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNI 426
Cdd:cd05097   1 EFPRQQLRLKEKLGEGQFGEVHLCEAEGLAEflgegapEFDGQPVLVAVKMLRADVTKTARNDFLKEIKIMSRL-KNPNI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 427 INLLGACTQGGPLYVLVEYAAKGNLREFLRARRPpgldYSFDTCKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDL 506
Cdd:cd05097  80 IRLLGVCVSDDPLCMITEYMENGDLNQFLSQREI----ESTFTHANNIPSVSIANLLYMAVQIASGMKYLASLNFVHRDL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 507 AARNVLVTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTL-GGSPYPG 585
Cdd:cd05097 156 ATRNCLVGNHYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMAWESILLGKFTTASDVWAFGVTLWEMFTLcKEQPYSL 235
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 13112048 586 IPVEELFKLLKEGHR-------MDKPANCTHDLYMIMRECWHAAPSQRPTFKQL 632
Cdd:cd05097 236 LSDEQVIENTGEFFRnqgrqiyLSQTPLCPSPVFKLMMRCWSRDIKDRPTFNKI 289
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
355-633 7.79e-59

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: 198.95  E-value: 7.79e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 355 LSRARLTLGKPLGEGCFGQVVMAEAIGidkdraakPVTVAVKMLKDDATDKDlsDLVSEME-MMKMigKHKNIINLLGAC 433
Cdd:cd05113   1 IDPKDLTFLKELGTGQFGVVKYGKWRG--------QYDVAIKMIKEGSMSED--EFIEEAKvMMNL--SHEKLVQLYGVC 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 434 TQGGPLYVLVEYAAKGNLREFLRARRppgldysfdtckppeEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLV 513
Cdd:cd05113  69 TKQRPIFIITEYMANGCLLNYLREMR---------------KRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLV 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 514 TEDNVMKIADFGLARDVHNlDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFK 593
Cdd:cd05113 134 NDQGVVKVSDFGLSRYVLD-DEYTSSVGSKFPVRWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSLGKMPYERFTNSETVE 212
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 13112048 594 LLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLV 633
Cdd:cd05113 213 HVSQGLRLYRPHLASEKVYTIMYSCWHEKADERPTFKILL 252
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
355-632 1.05e-58

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: 199.85  E-value: 1.05e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 355 LSRARLTLGKPLGEGCFGQVVMAEAIGID--KDRaakpVTVAVKMLKDdATDKDLSDLVSEMEMMKMIgKHKNIINLLGA 432
Cdd:cd05094   2 IKRRDIVLKRELGEGAFGKVFLAECYNLSptKDK----MLVAVKTLKD-PTLAARKDFQREAELLTNL-QHDHIVKFYGV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 433 CTQGGPLYVLVEYAAKGNLREFLRARRPPGLDYSFDTCKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVL 512
Cdd:cd05094  76 CGDGDPLIMVFEYMKHGDLNKFLRAHGPDAMILVDGQPRQAKGELGLSQMLHIATQIASGMVYLASQHFVHRDLATRNCL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 513 VTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELF 592
Cdd:cd05094 156 VGANLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTYGKQPWFQLSNTEVI 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 13112048 593 KLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQL 632
Cdd:cd05094 236 ECITQGRVLERPRVCPKEVYDIMLGCWQREPQQRLNIKEI 275
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
358-640 1.76e-58

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: 198.55  E-value: 1.76e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 358 ARLTLGKPLGEGCFGQVVMaeaiGIDKDRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGG 437
Cdd:cd05066   4 SCIKIEKVIGAGEFGEVCS----GRLKLPGKREIPVAIKTLKAGYTEKQRRDFLSEASIMGQF-DHPNIIHLEGVVTRSK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 438 PLYVLVEYAAKGNLREFLRARrppgldysfdtckppEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDN 517
Cdd:cd05066  79 PVMIVTEYMENGSLDAFLRKH---------------DGQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNL 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 518 VMKIADFGLARDVHN-LDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLK 596
Cdd:cd05066 144 VCKVSDFGLSRVLEDdPEAAYTTRGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWEMSNQDVIKAIE 223
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 13112048 597 EGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVL 640
Cdd:cd05066 224 EGYRLPAPMDCPAALHQLMLDCWQKDRNERPKFEQIVSILDKLI 267
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
354-632 1.41e-57

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: 197.46  E-value: 1.41e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 354 ELSRARLTLGKPLGEGCFGQVVMAEAIGIDK---------DRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHK 424
Cdd:cd05096   1 KFPRGHLLFKEKLGEGQFGEVHLCEVVNPQDlptlqfpfnVRKGRPLLVAVKILRPDANKNARNDFLKEVKILSRL-KDP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 425 NIINLLGACTQGGPLYVLVEYAAKGNLREFLRARRPPGLDYSFDTCKPPEEQL---TFKDLVSCAYQVARGMEYLASQKC 501
Cdd:cd05096  80 NIIRLLGVCVDEDPLCMITEYMENGDLNQFLSSHHLDDKEENGNDAVPPAHCLpaiSYSSLLHVALQIASGMKYLSSLNF 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 502 IHRDLAARNVLVTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTL-GG 580
Cdd:cd05096 160 VHRDLATRNCLVGENLTIKIADFGMSRNLYAGDYYRIQGRAVLPIRWMAWECILMGKFTTASDVWAFGVTLWEILMLcKE 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 13112048 581 SPYPGIPVE-------ELFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQL 632
Cdd:cd05096 240 QPYGELTDEqvienagEFFRDQGRQVYLFRPPPCPQGLYELMLQCWSRDCRERPSFSDI 298
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
366-636 3.57e-57

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: 193.26  E-value: 3.57e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKDraakpvtVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd00180   1 LGKGSFGKVYKARDKETGKK-------VAVKVIPKEKLKKLLEELLREIEILKKL-NHPNIVKLYDVFETENFLYLVMEY 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLREFLRARRPPgldysfdtckppeeqLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFG 525
Cdd:cd00180  73 CEGGSLKDLLKENKGP---------------LSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFG 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 526 LARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFtlggspypgipveelfkllkeghrmdkpa 605
Cdd:cd00180 138 LAKDLDSDDSLLKTTGGTTPPYYAPPELLGGRYYGPKVDIWSLGVILYELE----------------------------- 188
                       250       260       270
                ....*....|....*....|....*....|.
gi 13112048 606 ncthDLYMIMRECWHAAPSQRPTFKQLVEDL 636
Cdd:cd00180 189 ----ELKDLIRRMLQYDPKKRPSAKELLEHL 215
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
354-640 4.11e-57

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: 194.81  E-value: 4.11e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 354 ELSRARLTLGKPLGEGCFGQVVMaeaiGIDKDRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIGkHKNIINLLGAC 433
Cdd:cd05063   1 EIHPSHITKQKVIGAGEFGEVFR----GILKMPGRKEVAVAIKTLKPGYTEKQRQDFLSEASIMGQFS-HHNIIRLEGVV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 434 TQGGPLYVLVEYAAKGNLREFLRARrppglDYSFDTCKppeeqltfkdLVSCAYQVARGMEYLASQKCIHRDLAARNVLV 513
Cdd:cd05063  76 TKFKPAMIITEYMENGALDKYLRDH-----DGEFSSYQ----------LVGMLRGIAAGMKYLSDMNYVHRDLAARNILV 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 514 TEDNVMKIADFGLARDVHNL-DYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELF 592
Cdd:cd05063 141 NSNLECKVSDFGLSRVLEDDpEGTYTTSGGKIPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSFGERPYWDMSNHEVM 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 13112048 593 KLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVL 640
Cdd:cd05063 221 KAINDGFRLPAPMDCPSAVYQLMLQCWQQDRARRPRFVDIVNLLDKLL 268
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
360-636 1.48e-56

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: 192.86  E-value: 1.48e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 360 LTLGKPLGEGCFGQVVMAEAIGIDKdraakpvtVAVKMLKDDATDKDlsDLVSEME-MMKMigKHKNIINLLGACTQGGP 438
Cdd:cd05112   6 LTFVQEIGSGQFGLVHLGYWLNKDK--------VAIKTIREGAMSEE--DFIEEAEvMMKL--SHPKLVQLYGVCLEQAP 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 439 LYVLVEYAAKGNLREFLRARRppGLdysfdtckppeeqLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNV 518
Cdd:cd05112  74 ICLVFEFMEHGCLSDYLRTQR--GL-------------FSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQV 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 519 MKIADFGLARDVHNlDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEG 598
Cdd:cd05112 139 VKVSDFGMTRFVLD-DQYTSSTGTKFPVKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSEGKIPYENRSNSEVVEDINAG 217
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 13112048 599 HRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDL 636
Cdd:cd05112 218 FRLYKPRLASTHVYEIMNHCWKERPEDRPSFSLLLRQL 255
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
364-639 6.10e-56

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: 193.32  E-value: 6.10e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVmaEAIGIDKDRAAKpVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGpLYVLV 443
Cdd:cd05108  13 KVLGSGAFGTVY--KGLWIPEGEKVK-IPVAIKELREATSPKANKEILDEAYVMASV-DNPHVCRLLGICLTST-VQLIT 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 444 EYAAKGNLREFLRARRppgldysfdtckppeEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIAD 523
Cdd:cd05108  88 QLMPFGCLLDYVREHK---------------DNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITD 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 524 FGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGHRMDK 603
Cdd:cd05108 153 FGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQ 232
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 13112048 604 PANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRV 639
Cdd:cd05108 233 PPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKM 268
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
353-632 1.98e-55

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: 190.24  E-value: 1.98e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 353 WELSRARLTLGKPLGEGCFGQVVMAEAigidkdraAKPVTVAVKMLKDDATDkdLSDLVSEMEMMKMIgKHKNIINLLGA 432
Cdd:cd05073   6 WEIPRESLKLEKKLGAGQFGEVWMATY--------NKHTKVAVKTMKPGSMS--VEAFLAEANVMKTL-QHDKLVKLHAV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 433 CTQGgPLYVLVEYAAKGNLREFLRARRPpgldysfdtckppeEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVL 512
Cdd:cd05073  75 VTKE-PIYIITEFMAKGSLLDFLKSDEG--------------SKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANIL 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 513 VTEDNVMKIADFGLARDVHNLDYYKKTtNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELF 592
Cdd:cd05073 140 VSASLVCKIADFGLARVIEDNEYTARE-GAKFPIKWTAPEAINFGSFTIKSDVWSFGILLMEIVTYGRIPYPGMSNPEVI 218
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 13112048 593 KLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQL 632
Cdd:cd05073 219 RALERGYRMPRPENCPEELYNIMMRCWKNRPEERPTFEYI 258
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
358-640 8.53e-55

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: 188.53  E-value: 8.53e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 358 ARLTLGKPLGEGCFGQVVMAeaigidKDRAAkpVTVAVKMLKDDATDKDlsDLVSEME-MMKMigKHKNIINLLGACTQG 436
Cdd:cd05114   4 SELTFMKELGSGLFGVVRLG------KWRAQ--YKVAIKAIREGAMSEE--DFIEEAKvMMKL--THPKLVQLYGVCTQQ 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 437 GPLYVLVEYAAKGNLREFLRARRppgldysfdtckppeEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTED 516
Cdd:cd05114  72 KPIYIVTEFMENGCLLNYLRQRR---------------GKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDT 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 517 NVMKIADFGLARDVHNlDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLK 596
Cdd:cd05114 137 GVVKVSDFGMTRYVLD-DQYTSSSGAKFPVKWSPPEVFNYSKFSSKSDVWSFGVLMWEVFTEGKMPFESKSNYEVVEMVS 215
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 13112048 597 EGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVL 640
Cdd:cd05114 216 RGHRLYRPKLASKSVYEVMYSCWHEKPEGRPTFADLLRTITEIA 259
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
355-639 1.13e-54

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: 188.63  E-value: 1.13e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 355 LSRARLTLGKPLGEGCFGQVvmAEAIGIDKDRAAKpVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACT 434
Cdd:cd05111   4 FKETELRKLKVLGSGVFGTV--HKGIWIPEGDSIK-IPVAIKVIQDRSGRQSFQAVTDHMLAIGSL-DHAYIVRLLGICP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 435 qGGPLYVLVEYAAKGNLREFLRARRppgldysfDTCKPpeeQLtfkdLVSCAYQVARGMEYLASQKCIHRDLAARNVLVT 514
Cdd:cd05111  80 -GASLQLVTQLLPLGSLLDHVRQHR--------GSLGP---QL----LLNWCVQIAKGMYYLEEHRMVHRNLAARNVLLK 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 515 EDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKL 594
Cdd:cd05111 144 SPSQVQVADFGVADLLYPDDKKYFYSEAKTPIKWMALESIHFGKYTHQSDVWSYGVTVWEMMTFGAEPYAGMRLAEVPDL 223
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 13112048 595 LKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRV 639
Cdd:cd05111 224 LEKGERLAQPQICTIDVYMVMVKCWMIDENIRPTFKELANEFTRM 268
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
366-639 5.51e-54

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: 187.03  E-value: 5.51e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEaigIDKDRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGP--LYVLV 443
Cdd:cd05080  12 LGEGHFGKVSLYC---YDPTNDGTGEMVAVKALKADCGPQHRSGWKQEIDILKTL-YHENIVKYKGCCSEQGGksLQLIM 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 444 EYAAKGNLREFLrarrppgldysfdtckpPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIAD 523
Cdd:cd05080  88 EYVPLGSLRDYL-----------------PKHSIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGD 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 524 FGLARDV-HNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFT--------------LGGSPYPGIPV 588
Cdd:cd05080 151 FGLAKAVpEGHEYYRVREDGDSPVFWYAPECLKEYKFYYASDVWSFGVTLYELLThcdssqspptkfleMIGIAQGQMTV 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 13112048 589 EELFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRV 639
Cdd:cd05080 231 VRLIELLERGERLPCPDKCPQEVYHLMKNCWETEASFRPTFENLIPILKTV 281
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
364-632 8.08e-54

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: 185.12  E-value: 8.08e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVMAEAIGIDKdraakpvtVAVKMLKDDATDKDlsDLVSEMEMMKMIgKHKNIINLLGACTQGgPLYVLV 443
Cdd:cd14203   1 VKLGQGCFGEVWMGTWNGTTK--------VAIKTLKPGTMSPE--AFLEEAQIMKKL-RHDKLVQLYAVVSEE-PIYIVT 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 444 EYAAKGNLREFLRarrppgldysfdtcKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIAD 523
Cdd:cd14203  69 EFMSKGSLLDFLK--------------DGEGKYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIAD 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 524 FGLARDVHNlDYYKKTTNGRLPVKWMAPEA-LFDRvYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGHRMD 602
Cdd:cd14203 135 FGLARLIED-NEYTARQGAKFPIKWTAPEAaLYGR-FTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMP 212
                       250       260       270
                ....*....|....*....|....*....|
gi 13112048 603 KPANCTHDLYMIMRECWHAAPSQRPTFKQL 632
Cdd:cd14203 213 CPPGCPESLHELMCQCWRKDPEERPTFEYL 242
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
364-629 1.25e-53

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: 185.17  E-value: 1.25e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVMaeaiGIDKDRAAKPvTVAVKMLKDDATDKDLSD-LVSEMEMMKMIgKHKNIINLLGACtQGGPLYVL 442
Cdd:cd05116   1 GELGSGNFGTVKK----GYYQMKKVVK-TVAVKILKNEANDPALKDeLLREANVMQQL-DNPYIVRMIGIC-EAESWMLV 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 443 VEYAAKGNLREFLRARRppgldysfdtckppeeQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIA 522
Cdd:cd05116  74 MEMAELGPLNKFLQKNR----------------HVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKIS 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 523 DFGLARDV-HNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGHRM 601
Cdd:cd05116 138 DFGLSKALrADENYYKAQTHGKWPVKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSYGQKPYKGMKGNEVTQMIEKGERM 217
                       250       260
                ....*....|....*....|....*...
gi 13112048 602 DKPANCTHDLYMIMRECWHAAPSQRPTF 629
Cdd:cd05116 218 ECPAGCPPEMYDLMKLCWTYDVDERPGF 245
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
349-661 5.11e-53

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: 184.12  E-value: 5.11e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 349 ADPKWELSRARLTLGKPLGEGCFGQVVMAEAIGIDKdraakpvtVAVKMLKDDATDKDLsdLVSEMEMMKMIgKHKNIIN 428
Cdd:cd05069   3 AKDAWEIPRESLRLDVKLGQGCFGEVWMGTWNGTTK--------VAIKTLKPGTMMPEA--FLQEAQIMKKL-RHDKLVP 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 429 LLGACTQGgPLYVLVEYAAKGNLREFLRarrppgldysfdtcKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAA 508
Cdd:cd05069  72 LYAVVSEE-PIYIVTEFMGKGSLLDFLK--------------EGDGKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRA 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 509 RNVLVTEDNVMKIADFGLARDVHNLDYYKKTtNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPV 588
Cdd:cd05069 137 ANILVGDNLVCKIADFGLARLIEDNEYTARQ-GAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMVN 215
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13112048 589 EELFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVLTVTSTdeyldlsapfeQYSPG 661
Cdd:cd05069 216 REVLEQVERGYRMPCPQGCPESLHELMKLCWKKDPDERPTFEYIQSFLEDYFTATEP-----------QYQPG 277
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
366-639 7.91e-53

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: 184.06  E-value: 7.91e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKDRAAkpvTVAVKMLKDdATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGG--PLYVLV 443
Cdd:cd14205  12 LGKGNFGSVEMCRYDPLQDNTGE---VVAVKKLQH-STEEHLRDFEREIEILKSL-QHDNIVKYKGVCYSAGrrNLRLIM 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 444 EYAAKGNLREFLRARRppgldysfdtckppeEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIAD 523
Cdd:cd14205  87 EYLPYGSLRDYLQKHK---------------ERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGD 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 524 FGLARDV-HNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFT---------------LGGSPYPGIP 587
Cdd:cd14205 152 FGLTKVLpQDKEYYKVKEPGESPIFWYAPESLTESKFSVASDVWSFGVVLYELFTyieksksppaefmrmIGNDKQGQMI 231
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 13112048 588 VEELFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRV 639
Cdd:cd14205 232 VFHLIELLKNNGRLPRPDGCPDEIYMIMTECWNNNVNQRPSFRDLALRVDQI 283
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
364-640 5.31e-52

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: 181.67  E-value: 5.31e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVvmaEAIGIDKDRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGG--PLYV 441
Cdd:cd05079  10 RDLGEGHFGKV---ELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNL-YHENIVKYKGICTEDGgnGIKL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 442 LVEYAAKGNLREFLRARRppgldysfdtckppeEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKI 521
Cdd:cd05079  86 IMEFLPSGSLKEYLPRNK---------------NKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKI 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 522 ADFGLARDVH-NLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFT--------------LGGSPYPGI 586
Cdd:cd05079 151 GDFGLTKAIEtDKEYYTVKDDLDSPVFWYAPECLIQSKFYIASDVWSFGVTLYELLTycdsesspmtlflkMIGPTHGQM 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 13112048 587 PVEELFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVL 640
Cdd:cd05079 231 TVTRLVRVLEEGKRLPRPPNCPEEVYQLMRKCWEFQPSKRTTFQNLIEGFEAIL 284
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
366-640 7.06e-52

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: 180.84  E-value: 7.06e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMaeaiGIDKDRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd05065  12 IGAGEFGEVCR----GRLKLPGKREIFVAIKTLKSGYTEKQRRDFLSEASIMGQF-DHPNIIHLEGVVTKSRPVMIITEF 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLREFLRARrppgldysfdtckppEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFG 525
Cdd:cd05065  87 MENGALDSFLRQN---------------DGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFG 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 526 LAR---DVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGHRMD 602
Cdd:cd05065 152 LSRfleDDTSDPTYTSSLGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVINAIEQDYRLP 231
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 13112048 603 KPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVL 640
Cdd:cd05065 232 PPMDCPTALHQLMLDCWQKDRNLRPKFGQIVNTLDKMI 269
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
355-654 7.82e-52

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: 181.80  E-value: 7.82e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 355 LSRARLTLGKPLGEGCFGQVVmaEAIGIDKDRAAKpVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACT 434
Cdd:cd05110   4 LKETELKRVKVLGSGAFGTVY--KGIWVPEGETVK-IPVAIKILNETTGPKANVEFMDEALIMASM-DHPHLVRLLGVCL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 435 QGgPLYVLVEYAAKGNLREFLRARRppgldysfdtckppeEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVT 514
Cdd:cd05110  80 SP-TIQLVTQLMPHGCLLDYVHEHK---------------DNIGSQLLLNWCVQIAKGMMYLEERRLVHRDLAARNVLVK 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 515 EDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKL 594
Cdd:cd05110 144 SPNHVKITDFGLARLLEGDEKEYNADGGKMPIKWMALECIHYRKFTHQSDVWSYGVTIWELMTFGGKPYDGIPTREIPDL 223
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13112048 595 LKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRV------LTVTSTDEYLDLSAP 654
Cdd:cd05110 224 LEKGERLPQPPICTIDVYMVMVKCWMIDADSRPKFKELAAEFSRMardpqrYLVIQGDDRMKLPSP 289
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
366-629 8.29e-52

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: 180.53  E-value: 8.29e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMaeaiGIDKDRAaKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACtQGGPLYVLVEY 445
Cdd:cd05115  12 LGSGNFGCVKK----GVYKMRK-KQIDVAIKVLKQGNEKAVRDEMMREAQIMHQL-DNPYIVRMIGVC-EAEALMLVMEM 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLREFLRARRppgldysfdtckppeEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFG 525
Cdd:cd05115  85 ASGGPLNKFLSGKK---------------DEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFG 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 526 LARDVHNLD-YYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKP 604
Cdd:cd05115 150 LSKALGADDsYYKARSAGKWPLKWYAPECINFRKFSSRSDVWSYGVTMWEAFSYGQKPYKKMKGPEVMSFIEQGKRMDCP 229
                       250       260
                ....*....|....*....|....*
gi 13112048 605 ANCTHDLYMIMRECWHAAPSQRPTF 629
Cdd:cd05115 230 AECPPEMYALMSDCWIYKWEDRPNF 254
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
366-637 1.57e-51

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: 180.47  E-value: 1.57e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKDRAAkpvTVAVKMLKDDATDKdLSDLVSEMEMMKMIgKHKNIINLLGACTQGG--PLYVLV 443
Cdd:cd05081  12 LGKGNFGSVELCRYDPLGDNTGA---LVAVKQLQHSGPDQ-QRDFQREIQILKAL-HSDFIVKYRGVSYGPGrrSLRLVM 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 444 EYAAKGNLREFLRARRppgldysfdtckppeEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIAD 523
Cdd:cd05081  87 EYLPSGCLRDFLQRHR---------------ARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIAD 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 524 FGLARDV-HNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFT--------------LGGSPYPGIPV 588
Cdd:cd05081 152 FGLAKLLpLDKDYYVVREPGQSPIFWYAPESLSDNIFSRQSDVWSFGVVLYELFTycdkscspsaeflrMMGCERDVPAL 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 13112048 589 EELFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLD 637
Cdd:cd05081 232 CRLLELLEEGQRLPAPPACPAEVHELMKLCWAPSPQDRPSFSALGPQLD 280
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
353-661 4.22e-51

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: 178.72  E-value: 4.22e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 353 WELSRARLTLGKPLGEGCFGQVVMAEAIGIDKdraakpvtVAVKMLKDDATDKDlsDLVSEMEMMKMIgKHKNIINLLGA 432
Cdd:cd05070   4 WEIPRESLQLIKRLGNGQFGEVWMGTWNGNTK--------VAIKTLKPGTMSPE--SFLEEAQIMKKL-KHDKLVQLYAV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 433 CTQGgPLYVLVEYAAKGNLREFLRarrppgldysfdtcKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVL 512
Cdd:cd05070  73 VSEE-PIYIVTEYMSKGSLLDFLK--------------DGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANIL 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 513 VTEDNVMKIADFGLARDVHNLDYYKKTtNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELF 592
Cdd:cd05070 138 VGNGLICKIADFGLARLIEDNEYTARQ-GAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVL 216
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13112048 593 KLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVLTVTSTdeyldlsapfeQYSPG 661
Cdd:cd05070 217 EQVERGYRMPCPQDCPISLHELMIHCWKKDPEERPTFEYLQGFLEDYFTATEP-----------QYQPG 274
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
353-661 1.52e-50

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: 177.57  E-value: 1.52e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 353 WELSRARLTLGKPLGEGCFGQVVMAEAIGIDKdraakpvtVAVKMLKDDATDKDLsdLVSEMEMMKMIgKHKNIINLLGA 432
Cdd:cd05071   4 WEIPRESLRLEVKLGQGCFGEVWMGTWNGTTR--------VAIKTLKPGTMSPEA--FLQEAQVMKKL-RHEKLVQLYAV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 433 CTQGgPLYVLVEYAAKGNLREFLRARRppgldysfdtckppEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVL 512
Cdd:cd05071  73 VSEE-PIYIVTEYMSKGSLLDFLKGEM--------------GKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANIL 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 513 VTEDNVMKIADFGLARDVHNLDYYKKTtNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELF 592
Cdd:cd05071 138 VGENLVCKVADFGLARLIEDNEYTARQ-GAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVL 216
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13112048 593 KLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVLTVTSTdeyldlsapfeQYSPG 661
Cdd:cd05071 217 DQVERGYRMPCPPECPESLHDLMCQCWRKEPEERPTFEYLQAFLEDYFTSTEP-----------QYQPG 274
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
354-640 6.49e-49

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: 172.42  E-value: 6.49e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 354 ELSRARLTLGKPLGEGCFGQVVMaeaiGIDKDRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGAC 433
Cdd:cd05064   1 ELDNKSIKIERILGTGRFGELCR----GCLKLPSKRELPVAIHTLRAGCSDKQRRGFLAEALTLGQF-DHSNIVRLEGVI 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 434 TQGGPLYVLVEYAAKGNLREFLRARrppgldysfdtckppEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLV 513
Cdd:cd05064  76 TRGNTMMIVTEYMSNGALDSFLRKH---------------EGQLVAGQLMGMLPGLASGMKYLSEMGYVHKGLAAHKVLV 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 514 TEDNVMKIADFG-LARDVHNLDYykKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELF 592
Cdd:cd05064 141 NSDLVCKISGFRrLQEDKSEAIY--TTMSGKSPVLWAAPEAIQYHHFSSASDVWSFGIVMWEVMSYGERPYWDMSGQDVI 218
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 13112048 593 KLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVL 640
Cdd:cd05064 219 KAVEDGFRLPAPRNCPNLLHQLMLDCWQKERGERPRFSQIHSILSKMV 266
IgI_3_FGFR cd04974
Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of ...
253-355 4.71e-48

Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR). Fibroblast growth factors (FGFs) participate in morphogenesis, development, angiogenesis, and wound healing. These FGF-stimulated processes are mediated by four FGFR tyrosine kinases (FGRF1-4). FGFRs are comprised of an extracellular portion consisting of three Ig-like domains, a transmembrane helix, and a cytoplasmic portion having protein tyrosine kinase activity. The highly conserved Ig-like domains 2 and 3, and the linker region between D2 and D3 define a general binding site for FGFs. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409363  Cd Length: 102  Bit Score: 164.13  E-value: 4.71e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 253 PILQAGLPANQTAVLGSDVEFHCKVYSDAQPHIQWLKHVEVNGSKVGPDGTPYVTVLKVSLEsNASMSSNTPLVRIARL- 331
Cdd:cd04974   1 PILQAGLPANQTVVLGSDVEFHCKVYSDAQPHIQWLKHVEVNGSKYGPDGLPYVTVLKVAGV-NTTGEENTLTISNVTFd 79
                        90       100
                ....*....|....*....|....
gi 13112048 332 SSGEGPTLANVSeLELPADPKWEL 355
Cdd:cd04974  80 DAGEYICLAGNS-IGLSFHSAWLT 102
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
366-639 8.96e-45

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: 161.02  E-value: 8.96e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGidkdraakpVTVAVKMLKDDAtDKDLS----DLVSEMEMMKMIgKHKNIINLLGACTQGGPLYV 441
Cdd:cd14061   2 IGVGGFGKVYRGIWRG---------EEVAVKAARQDP-DEDISvtleNVRQEARLFWML-RHPNIIALRGVCLQPPNLCL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 442 LVEYAAKGNLREFLRARR-PPGLdysfdtckppeeqltfkdLVSCAYQVARGMEYLASQK---CIHRDLAARNVLVTE-- 515
Cdd:cd14061  71 VMEYARGGALNRVLAGRKiPPHV------------------LVDWAIQIARGMNYLHNEApvpIIHRDLKSSNILILEai 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 516 ------DNVMKIADFGLARDVHnldyykKTTngRLPV----KWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPG 585
Cdd:cd14061 133 enedleNKTLKITDFGLAREWH------KTT--RMSAagtyAWMAPEVIKSSTFSKASDVWSYGVLLWELLT-GEVPYKG 203
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 13112048 586 IPveelFKLLKEGHRMDK-----PANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRV 639
Cdd:cd14061 204 ID----GLAVAYGVAVNKltlpiPSTCPEPFAQLMKDCWQPDPHDRPSFADILKQLENI 258
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
392-637 1.01e-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: 157.27  E-value: 1.01e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 392 TVAVKMLKDDaTDKDLSDLvsememMKMigKHKNIINLLGACTQGgPLY-VLVEYAAKGNLREFLRARRPpgldysfdtc 470
Cdd:cd14059  18 EVAVKKVRDE-KETDIKHL------RKL--NHPNIIKFKGVCTQA-PCYcILMEYCPYGQLYEVLRAGRE---------- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 471 kppeeqLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARDVhNLDYYKKTTNGrlPVKWMA 550
Cdd:cd14059  78 ------ITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKEL-SEKSTKMSFAG--TVAWMA 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 551 PEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEE-LFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTF 629
Cdd:cd14059 149 PEVIRNEPCSEKVDIWSFGVVLWELLT-GEIPYKDVDSSAiIWGVGSNSLQLPVPSTCPDGFKLLMKQCWNSKPRNRPSF 227

                ....*...
gi 13112048 630 KQLVEDLD 637
Cdd:cd14059 228 RQILMHLD 235
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
151-245 2.67e-43

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 150.83  E-value: 2.67e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 151 PYWTRPERMDKKLLAVPAANTVRFRCPAAGNPTPSISWLKNGREFRGEHRIGGIKLRHQQWSLVMESVVPSDRGNYTCVV 230
Cdd:cd05729   1 PRFTDTEKMEEREHALPAANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKVEEKGWSLIIERAIPRDKGKYTCIV 80
                        90
                ....*....|....*
gi 13112048 231 ENKFGSIRQTYTLDV 245
Cdd:cd05729  81 ENEYGSINHTYDVDV 95
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
366-632 1.91e-42

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: 155.11  E-value: 1.91e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGidkdrAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd14206   5 IGNGWFGKVILGEIFS-----DYTPAQVVVKELRVSAGPLEQRKFISEAQPYRSL-QHPNILQCLGLCTETIPFLLIMEF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLREFLRARRPP-GLDYSFdtckPPEEQLTFKDLvscAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADF 524
Cdd:cd14206  79 CQLGDLKRYLRAQRKAdGMTPDL----PTRDLRTLQRM---AYEITLGLLHLHKNNYIHSDLALRNCLLTSDLTVRIGDY 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 525 GLARDVHNLDYYKKTTNGRLPVKWMAPEaLFDRVY--------THQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFK-LL 595
Cdd:cd14206 152 GLSHNNYKEDYYLTPDRLWIPLRWVAPE-LLDELHgnlivvdqSKESNVWSLGVTIWELFEFGAQPYRHLSDEEVLTfVV 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 13112048 596 KEGH-RMDKPA-NCTHD--LYMIMRECWhAAPSQRPTFKQL 632
Cdd:cd14206 231 REQQmKLAKPRlKLPYAdyWYEIMQSCW-LPPSQRPSVEEL 270
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
359-635 2.87e-42

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: 153.83  E-value: 2.87e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 359 RLTLGKPLGEGCFGQVVMAeaigIDKDraaKPVTVAVKMLK-DDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGG 437
Cdd:cd06606   1 RWKKGELLGKGSFGSVYLA----LNLD---TGELMAVKEVElSGDSEEELEALEREIRILSSL-KHPNIVRYLGTERTEN 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 438 PLYVLVEYAAKGNLREFLRarrppgldysfdTCKPPEEQLtfkdLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDN 517
Cdd:cd06606  73 TLNIFLEYVPGGSLASLLK------------KFGKLPEPV----VRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDG 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 518 VMKIADFGLARDVHNLDY--YKKTTNGRLPvkWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGI--PVEELFK 593
Cdd:cd06606 137 VVKLADFGCAKRLAEIATgeGTKSLRGTPY--WMAPEVIRGEGYGRAADIWSLGCTVIEMAT-GKPPWSELgnPVAALFK 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 13112048 594 LLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVED 635
Cdd:cd06606 214 IGSSGEPPPIPEHLSEEAKDFLRKCLQRDPKKRPTADELLQH 255
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
367-637 5.74e-42

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: 152.42  E-value: 5.74e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 367 GEGCFGQVVMAEAIGIDKDRAAKpvtvavKMLKDDATDKDLSDLvsememmkmigKHKNIINLLGACTQGGPLYVLVEYA 446
Cdd:cd14060   2 GGGSFGSVYRAIWVSQDKEVAVK------KLLKIEKEAEILSVL-----------SHRNIIQFYGAILEAPNYGIVTEYA 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 447 AKGNLREFLRARRppgldysfdtckppEEQLTFKDLVSCAYQVARGMEYL---ASQKCIHRDLAARNVLVTEDNVMKIAD 523
Cdd:cd14060  65 SYGSLFDYLNSNE--------------SEEMDMDQIMTWATDIAKGMHYLhmeAPVKVIHRDLKSRNVVIAADGVLKICD 130
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 524 FGLARdvhnldYYKKTTN----GRLPvkWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLgGSPYPGIPVEELFKLLKEGH 599
Cdd:cd14060 131 FGASR------FHSHTTHmslvGTFP--WMAPEVIQSLPVSETCDTYSYGVVLWEMLTR-EVPFKGLEGLQVAWLVVEKN 201
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 13112048 600 -RMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLD 637
Cdd:cd14060 202 eRPTIPSSCPRSFAELMRRCWEADVKERPSFKQIIGILE 240
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
366-633 6.59e-41

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: 149.89  E-value: 6.59e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDkdraakpvtVAVKMLKDDATDKDLSDLVSEMEMMKmigkHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd14058   1 VGRGSFGVVCKARWRNQI---------VAVKIIESESEKKAFEVEVRQLSRVD----HPNIIKLYGACSNQKPVCLVMEY 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLREFLRARRPpgldysfdtcKPpeeQLTFKDLVSCAYQVARGMEYLASQK---CIHRDLAARNVLVTED-NVMKI 521
Cdd:cd14058  68 AEGGSLYNVLHGKEP----------KP---IYTAAHAMSWALQCAKGVAYLHSMKpkaLIHRDLKPPNLLLTNGgTVLKI 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 522 ADFGLARDVHNldyykKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLgGSPYPGI--PVEELFKLLKEGH 599
Cdd:cd14058 135 CDFGTACDIST-----HMTNNKGSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITR-RKPFDHIggPAFRIMWAVHNGE 208
                       250       260       270
                ....*....|....*....|....*....|....
gi 13112048 600 RMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLV 633
Cdd:cd14058 209 RPPLIKNCPKPIESLMTRCWSKDPEKRPSMKEIV 242
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
354-636 4.82e-39

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: 145.18  E-value: 4.82e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 354 ELSRARLTLGKPLGEGCFGQVVMAEAIGIDkdraakpvtVAVKMLKDDAtDKDLSDLV----SEMEMMKMIgKHKNIINL 429
Cdd:cd14145   2 EIDFSELVLEEIIGIGGFGKVYRAIWIGDE---------VAVKAARHDP-DEDISQTIenvrQEAKLFAML-KHPNIIAL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 430 LGACTQGGPLYVLVEYAAKGNLREFLRARR-PPGLdysfdtckppeeqltfkdLVSCAYQVARGMEYLASQK---CIHRD 505
Cdd:cd14145  71 RGVCLKEPNLCLVMEFARGGPLNRVLSGKRiPPDI------------------LVNWAVQIARGMNYLHCEAivpVIHRD 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 506 LAARNVLVTE--------DNVMKIADFGLARDVHNLDyyKKTTNGrlPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFT 577
Cdd:cd14145 133 LKSSNILILEkvengdlsNKILKITDFGLAREWHRTT--KMSAAG--TYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLT 208
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13112048 578 lGGSPYPGIpvEELfkLLKEGHRMDK-----PANCTHDLYMIMRECWHAAPSQRPTFKQLVEDL 636
Cdd:cd14145 209 -GEVPFRGI--DGL--AVAYGVAMNKlslpiPSTCPEPFARLMEDCWNPDPHSRPPFTNILDQL 267
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
364-641 1.38e-38

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: 143.88  E-value: 1.38e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVMAEaigIDKDRAakPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLV 443
Cdd:cd05042   1 QEIGNGWFGKVLLGE---IYSGTS--VAQVVVKELKASANPKEQDTFLKEGQPYRIL-QHPNILQCLGQCVEAIPYLLVM 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 444 EYAAKGNLREFLRARRPPGLdysfdtckPPEEQLTFKDLvscAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIAD 523
Cdd:cd05042  75 EFCDLGDLKAYLRSEREHER--------GDSDTRTLQRM---ACEVAAGLAHLHKLNFVHSDLALRNCLLTSDLTVKIGD 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 524 FGLARDVHNLDYYKKTTNGRLPVKWMAPEaLFDRVY--------THQSDVWSFGVLLWEIFTLGGSPYPGIPVEE-LFKL 594
Cdd:cd05042 144 YGLAHSRYKEDYIETDDKLWFPLRWTAPE-LVTEFHdrllvvdqTKYSNIWSLGVTLWELFENGAQPYSNLSDLDvLAQV 222
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 13112048 595 LKEGH-RMDKPA---NCTHDLYMIMRECWhAAPSQRPTfkqlVEDLDRVLT 641
Cdd:cd05042 223 VREQDtKLPKPQlelPYSDRWYEVLQFCW-LSPEQRPA----AEDVHLLLT 268
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
361-632 4.87e-38

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


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 141.96  E-value: 4.87e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 361 TLGKPLGEGCFGQVVMAeaigidKDRAAKpVTVAVKMLKDDaTDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLY 440
Cdd:cd05122   3 EILEKIGKGGFGVVYKA------RHKKTG-QIVAIKKINLE-SKEKKESILNEIAILKKC-KHPNIVKYYGSYLKKDELW 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 441 VLVEYAAKGNLREFLRArrppgldysfdTCKP-PEEQltfkdlvsCAY---QVARGMEYLASQKCIHRDLAARNVLVTED 516
Cdd:cd05122  74 IVMEFCSGGSLKDLLKN-----------TNKTlTEQQ--------IAYvckEVLKGLEYLHSHGIIHRDIKAANILLTSD 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 517 NVMKIADFGLARDVhNLDYYKKTTNGRLPvkWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGI-PVEELFKLL 595
Cdd:cd05122 135 GEVKLIDFGLSAQL-SDGKTRNTFVGTPY--WMAPEVIQGKPYGFKADIWSLGITAIEMAE-GKPPYSELpPMKALFLIA 210
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 13112048 596 KEGH-RMDKPANCTHDLYMIMRECWHAAPSQRPTFKQL 632
Cdd:cd05122 211 TNGPpGLRNPKKWSKEFKDFLKKCLQKDPEKRPTAEQL 248
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
366-639 2.98e-37

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: 139.74  E-value: 2.98e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMaeaiGIDKDRAakpvtVAVKMLKDDAtDKDLS----DLVSEMEMMKMIgKHKNIINLLGACTQGGPLYV 441
Cdd:cd14148   2 IGVGGFGKVYK----GLWRGEE-----VAVKAARQDP-DEDIAvtaeNVRQEARLFWML-QHPNIIALRGVCLNPPHLCL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 442 LVEYAAKGNLREFLRARR-PPGLdysfdtckppeeqltfkdLVSCAYQVARGMEYLASQK---CIHRDLAARNVLVTE-- 515
Cdd:cd14148  71 VMEYARGGALNRALAGKKvPPHV------------------LVNWAVQIARGMNYLHNEAivpIIHRDLKSSNILILEpi 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 516 ------DNVMKIADFGLARDVHnldyykKTT--NGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYpgip 587
Cdd:cd14148 133 enddlsGKTLKITDFGLAREWH------KTTkmSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLT-GEVPY---- 201
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 13112048 588 vEELFKL-LKEGHRMDK-----PANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRV 639
Cdd:cd14148 202 -REIDALaVAYGVAMNKltlpiPSTCPEPFARLLEECWDPDPHGRPDFGSILKRLEDI 258
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
366-636 4.76e-37

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: 139.79  E-value: 4.76e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDkdraakpvtVAVKMLKDDAtDKDLS----DLVSEMEMMKMIgKHKNIINLLGACTQGGPLYV 441
Cdd:cd14146   2 IGVGGFGKVYRATWKGQE---------VAVKAARQDP-DEDIKataeSVRQEAKLFSML-RHPNIIKLEGVCLEEPNLCL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 442 LVEYAAKGNLREFLRARrPPGLDYSFDTCKPPEEqltfkdLVSCAYQVARGMEYLASQK---CIHRDLAARNVLVTE--- 515
Cdd:cd14146  71 VMEFARGGTLNRALAAA-NAAPGPRRARRIPPHI------LVNWAVQIARGMLYLHEEAvvpILHRDLKSSNILLLEkie 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 516 -----DNVMKIADFGLARDVHNLDyyKKTTNGRLpvKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIP-VE 589
Cdd:cd14146 144 hddicNKTLKITDFGLAREWHRTT--KMSAAGTY--AWMAPEVIKSSLFSKGSDIWSYGVLLWELLT-GEVPYRGIDgLA 218
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 13112048 590 ELFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDL 636
Cdd:cd14146 219 VAYGVAVNKLTLPIPSTCPEPFAKLMKECWEQDPHIRPSFALILEQL 265
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
360-637 6.44e-37

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: 139.39  E-value: 6.44e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 360 LTLGKPLGEGCFGQVVMAEAIGidkdraakpVTVAVKMLKDDAtDKDLS----DLVSEMEMMKMIGkHKNIINLLGACTQ 435
Cdd:cd14147   5 LRLEEVIGIGGFGKVYRGSWRG---------ELVAVKAARQDP-DEDISvtaeSVRQEARLFAMLA-HPNIIALKAVCLE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 436 GGPLYVLVEYAAKGNLREFLRARR-PPGLdysfdtckppeeqltfkdLVSCAYQVARGMEYLASQK---CIHRDLAARNV 511
Cdd:cd14147  74 EPNLCLVMEYAAGGPLSRALAGRRvPPHV------------------LVNWAVQIARGMHYLHCEAlvpVIHRDLKSNNI 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 512 LVT--------EDNVMKIADFGLARDVHNLDyyKKTTNGRLpvKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPY 583
Cdd:cd14147 136 LLLqpienddmEHKTLKITDFGLAREWHKTT--QMSAAGTY--AWMAPEVIKASTFSKGSDVWSFGVLLWELLT-GEVPY 210
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 13112048 584 PGIP-VEELFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLD 637
Cdd:cd14147 211 RGIDcLAVAYGVAVNKLTLPIPSTCPEPFAQLMADCWAQDPHRRPDFASILQQLE 265
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
366-638 5.81e-36

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: 136.43  E-value: 5.81e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEaigidkdRAAKPVTVAVKMLK-DDATDKDLSDLVSEMEMMKMiGKHKNIINLLGACTQGGPLYVLVE 444
Cdd:cd13978   1 LGSGGFGTVSKAR-------HVSWFGMVAIKCLHsSPNCIEERKALLKEAEKMER-ARHSYVLPLLGVCVERRSLGLVME 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 445 YAAKGNLREFLRARRPPgldysfdtCKPPeeqLTFKDLvscaYQVARGMEYL--ASQKCIHRDLAARNVLVTEDNVMKIA 522
Cdd:cd13978  73 YMENGSLKSLLEREIQD--------VPWS---LRFRII----HEIALGMNFLhnMDPPLLHHDLKPENILLDNHFHVKIS 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 523 DFGLARDVH----NLDYYKKTTNGRLPVkWMAPEAL--FDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGI--PVEELFKL 594
Cdd:cd13978 138 DFGLSKLGMksisANRRRGTENLGGTPI-YMAPEAFddFNKKPTSKSDVYSFAIVIWAVLT-RKEPFENAinPLLIMQIV 215
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 13112048 595 LKeGHRMDKPA--------NCTHdLYMIMRECWHAAPSQRPTFkqlVEDLDR 638
Cdd:cd13978 216 SK-GDRPSLDDigrlkqieNVQE-LISLMIRCWDGNPDARPTF---LECLDR 262
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
364-632 8.80e-36

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: 136.27  E-value: 8.80e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVMAEAigidkDRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLV 443
Cdd:cd05087   3 KEIGHGWFGKVFLGEV-----NSGLSSTQVVVKELKASASVQDQMQFLEEAQPYRAL-QHTNLLQCLAQCAEVTPYLLVM 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 444 EYAAKGNLREFLRARRppgldySFDTCKPpeEQLTFKDLvscAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIAD 523
Cdd:cd05087  77 EFCPLGDLKGYLRSCR------AAESMAP--DPLTLQRM---ACEVACGLLHLHRNNFVHSDLALRNCLLTADLTVKIGD 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 524 FGLARDVHNLDYYKKTTNGRLPVKWMAPEaLFDRVY--------THQSDVWSFGVLLWEIFTLGGSPYPGIPVEEL--FK 593
Cdd:cd05087 146 YGLSHCKYKEDYFVTADQLWVPLRWIAPE-LVDEVHgnllvvdqTKQSNVWSLGVTIWELFELGNQPYRHYSDRQVltYT 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 13112048 594 LLKEGHRMDKPA---NCTHDLYMIMRECWhAAPSQRPTFKQL 632
Cdd:cd05087 225 VREQQLKLPKPQlklSLAERWYEVMQFCW-LQPEQRPTAEEV 265
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
366-636 3.07e-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: 134.16  E-value: 3.07e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEaigidkDRAAKPVTVaVKMLKDDATDKDLsdlVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd14065   1 LGKGFFGEVYKVT------HRETGKVMV-MKELKRFDEQRSF---LKEVKLMRRL-SHPNILRFIGVCVKDNKLNFITEY 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLREFLrarrppgldysfdtcKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMK---IA 522
Cdd:cd14065  70 VNGGTLEELL---------------KSMDEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVREANRGRnavVA 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 523 DFGLARDVHNLDYYKKTTNGRLPV----KWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEG 598
Cdd:cd14065 135 DFGLAREMPDEKTKKPDRKKRLTVvgspYWMAPEMLRGESYDEKVDVFSFGIVLCEIIGRVPADPDYLPRTMDFGLDVRA 214
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 13112048 599 HRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDL 636
Cdd:cd14065 215 FRTLYVPDCPPSFLPLAIRCCQLDPEKRPSFVELEHHL 252
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
359-632 9.46e-35

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: 132.73  E-value: 9.46e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 359 RLTLGKPLGEGCFGQVVMaeaiGIDKDRAAkpvTVAVKMLK-DDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGG 437
Cdd:cd06627   1 NYQLGDLIGRGAFGSVYK----GLNLNTGE---FVAIKQISlEKIPKSDLKSVMGEIDLLKKL-NHPNIVKYIGSVKTKD 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 438 PLYVLVEYAAKGNLREFLRArrppgldysFDTCkpPEEqltfkdLVSC-AYQVARGMEYLASQKCIHRDLAARNVLVTED 516
Cdd:cd06627  73 SLYIILEYVENGSLASIIKK---------FGKF--PES------LVAVyIYQVLEGLAYLHEQGVIHRDIKGANILTTKD 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 517 NVMKIADFGLARdvhNLDYYKKTTNGrlPV---KWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGI-PVEELF 592
Cdd:cd06627 136 GLVKLADFGVAT---KLNEVEKDENS--VVgtpYWMAPEVIEMSGVTTASDIWSVGCTVIELLT-GNPPYYDLqPMAALF 209
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 13112048 593 KLLKEGHrMDKPANCTHDLYMIMRECWHAAPSQRPTFKQL 632
Cdd:cd06627 210 RIVQDDH-PPLPENISPELRDFLLQCFQKDPTLRPSAKEL 248
IgI_3_FGFR2 cd05858
Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); member ...
253-312 9.60e-35

Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain of human fibroblast growth factor receptor 2 (FGFR2). Fibroblast growth factors (FGFs) participate in morphogenesis, development, angiogenesis, and wound healing. These FGF-stimulated processes are mediated by four FGFR tyrosine kinases (FGRF1-4). FGFRs are comprised of an extracellular portion consisting of three Ig-like domains, a transmembrane helix, and a cytoplasmic portion having protein tyrosine kinase activity. The highly conserved Ig-like domains 2 and 3, and the linker region between D2 and D3 define a general binding site for FGFs. FGFR2 is required for male sex determination. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409444  Cd Length: 105  Bit Score: 127.38  E-value: 9.60e-35
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 253 PILQAGLPANQTAVLGSDVEFHCKVYSDAQPHIQWLKHVEVNGSKVGPDGTPYVTVLKVS 312
Cdd:cd05858   1 PILQAGLPANTSVVVGTDAEFVCKVYSDAQPHIQWLKHVEKNGSKYGPDGLPYVEVLKTA 60
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
366-525 1.17e-34

Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 128.33  E-value: 1.17e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGidkdraaKPVTVAVKMLKDDATDkDLSDLVSEMEMMKMIGKH-KNIINLLGACTQGGPLYVLVE 444
Cdd:cd13968   1 MGEGASAKVFWAEGEC-------TTIGVAVKIGDDVNNE-EGEDLESEMDILRRLKGLeLNIPKVLVTEDVDGPNILLME 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 445 YAAKGNLREFLRarrppgldysfdtckppEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADF 524
Cdd:cd13968  73 LVKGGTLIAYTQ-----------------EEELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDF 135

                .
gi 13112048 525 G 525
Cdd:cd13968 136 G 136
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
366-638 3.38e-34

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: 131.63  E-value: 3.38e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVmaeaigidKDRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd14066   1 IGSGGFGTVY--------KGVLENGTVVAVKRLNEMNCAASKKEFLTELEMLGRL-RHPNLVRLLGYCLESDEKLLVYEY 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLREFLRarrppgldysfdtCKPPEEQLTFKDLVSCAYQVARGMEYL---ASQKCIHRDLAARNVLVTEDNVMKIA 522
Cdd:cd14066  72 MPNGSLEDRLH-------------CHKGSPPLPWPQRLKIAKGIARGLEYLheeCPPPIIHGDIKSSNILLDEDFEPKLT 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 523 DFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEELFKLLKEGHRMD 602
Cdd:cd14066 139 DFGLARLIPPSESVSKTSAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLT-GKPAVDENRENASRKDLVEWVESK 217
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 13112048 603 KPANC------------THDLYMIMR------ECWHAAPSQRPTFKQLVEDLDR 638
Cdd:cd14066 218 GKEELedildkrlvdddGVEEEEVEAllrlalLCTRSDPSLRPSMKEVVQMLEK 271
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
361-638 3.12e-33

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: 128.47  E-value: 3.12e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 361 TLGKPLGEGCFGQVVMAEAIGIDKDraakpvtVAVKMLKDDATDKD--LSDLVSEMEMMKMIgKHKNIINLLGACTQGGP 438
Cdd:cd14014   3 RLVRLLGRGGMGEVYRARDTLLGRP-------VAIKVLRPELAEDEefRERFLREARALARL-SHPNIVRVYDVGEDDGR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 439 LYVLVEYAAKGNLREFLRARRPpgldysfdtckppeeqLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNV 518
Cdd:cd14014  75 PYIVMEYVEGGSLADLLRERGP----------------LPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGR 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 519 MKIADFGLARDVHNLdyyKKTTNGRLP--VKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGI-PVEELFKLL 595
Cdd:cd14014 139 VKLTDFGIARALGDS---GLTQTGSVLgtPAYMAPEQARGGPVDPRSDIYSLGVVLYELLT-GRPPFDGDsPAAVLAKHL 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 13112048 596 KEGHRMDKPAN--CTHDLYMIMRECWHAAPSQRP-TFKQLVEDLDR 638
Cdd:cd14014 215 QEAPPPPSPLNpdVPPALDAIILRALAKDPEERPqSAAELLAALRA 260
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
364-635 2.16e-32

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: 125.79  E-value: 2.16e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVMAeaigidKDRAAKpVTVAVKMLKddATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLV 443
Cdd:cd06614   6 EKIGEGASGEVYKA------TDRATG-KEVAIKKMR--LRKQNKELIINEILIMKEC-KHPNIVDYYDSYLVGDELWVVM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 444 EYAAKGNLREFLrarrppglDYSFDTCKppEEQLtfkdlvscAY---QVARGMEYLASQKCIHRDLAARNVLVTEDNVMK 520
Cdd:cd06614  76 EYMDGGSLTDII--------TQNPVRMN--ESQI--------AYvcrEVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVK 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 521 IADFGLARDVHNLDYYKKTTNGRlPVkWMAPEALFDRVYTHQSDVWSFGVLLWEIfTLGGSPY---PgiPVEELFKLLKE 597
Cdd:cd06614 138 LADFGFAAQLTKEKSKRNSVVGT-PY-WMAPEVIKRKDYGPKVDIWSLGIMCIEM-AEGEPPYleeP--PLRALFLITTK 212
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 13112048 598 G-HRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVED 635
Cdd:cd06614 213 GiPPLKNPEKWSPEFKDFLNKCLVKDPEKRPSAEELLQH 251
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
361-635 2.57e-32

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: 125.71  E-value: 2.57e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 361 TLGKPLGEGCFGQVVMAeaigIDKDRAAKpvtVAVKML-KDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPL 439
Cdd:cd14003   3 ELGKTLGEGSFGKVKLA----RHKLTGEK---VAIKIIdKSKLKEEIEEKIKREIEIMKLL-NHPNIIKLYEVIETENKI 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 440 YVLVEYAAKGNLREFLRARRPpgLDysfdtckPPEEQLTFKDLVScayqvarGMEYLASQKCIHRDLAARNVLVTEDNVM 519
Cdd:cd14003  75 YLVMEYASGGELFDYIVNNGR--LS-------EDEARRFFQQLIS-------AVDYCHSNGIVHRDLKLENILLDKNGNL 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 520 KIADFGLARdVHNLDYYKKTTNGRLPvkWMAPEALFDRVY-THQSDVWSFGVLLWEIFTlGGSPYPGIPVEELFKLLKEG 598
Cdd:cd14003 139 KIIDFGLSN-EFRGGSLLKTFCGTPA--YAAPEVLLGRKYdGPKADVWSLGVILYAMLT-GYLPFDDDNDSKLFRKILKG 214
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 13112048 599 HrMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVED 635
Cdd:cd14003 215 K-YPIPSHLSPDARDLIRRMLVVDPSKRITIEEILNH 250
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
359-634 5.23e-31

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


Pssm-ID: 270802 [Multi-domain]  Cd Length: 259  Bit Score: 122.13  E-value: 5.23e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 359 RLTLGKPLGEGCFGQVVmaeaIGIDKDRAAkpvTVAVKMLKDDATDKDLSDLVSEMEM-MKMIGK--HKNIINLLGACTQ 435
Cdd:cd06632   1 RWQKGQLLGSGSFGSVY----EGFNGDTGD---FFAVKEVSLVDDDKKSRESVKQLEQeIALLSKlrHPNIVQYYGTERE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 436 GGPLYVLVEYAAKGNLREFLRarrppglDYSfdtckppeeqlTFKDLVSCAY--QVARGMEYLASQKCIHRDLAARNVLV 513
Cdd:cd06632  74 EDNLYIFLEYVPGGSIHKLLQ-------RYG-----------AFEEPVIRLYtrQILSGLAYLHSRNTVHRDIKGANILV 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 514 TEDNVMKIADFGLARDVHNLDYYKKttngrlpVK----WMAPEAL--FDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGI- 586
Cdd:cd06632 136 DTNGVVKLADFGMAKHVEAFSFAKS-------FKgspyWMAPEVImqKNSGYGLAVDIWSLGCTVLEMAT-GKPPWSQYe 207
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 13112048 587 PVEELFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVE 634
Cdd:cd06632 208 GVAAIFKIGNSGELPPIPDHLSPDAKDFIRLCLQRDPEDRPTASQLLE 255
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
366-639 6.74e-31

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: 122.23  E-value: 6.74e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAeaigidKDRAAKPVTVAVKMLK-DDATDKDLsdlVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVE 444
Cdd:cd14154   1 LGKGFFGQAIKV------THRETGEVMVMKELIRfDEEAQRNF---LKEVKVMRSL-DHPNVLKFIGVLYKDKKLNLITE 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 445 YAAKGNLREFLrarrppgldysfdtcKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADF 524
Cdd:cd14154  71 YIPGGTLKDVL---------------KDMARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADF 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 525 GLARDVHN----LDYYKKTTNGRLPVK--------------WMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGI 586
Cdd:cd14154 136 GLARLIVEerlpSGNMSPSETLRHLKSpdrkkrytvvgnpyWMAPEMLNGRSYDEKVDIFSFGIVLCEIIGRVEADPDYL 215
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 13112048 587 PVEELFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRV 639
Cdd:cd14154 216 PRTKDFGLNVDSFREKFCAGCPPPFFKLAFLCCDLDPEKRPPFETLEEWLEAL 268
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
359-632 6.87e-31

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: 121.73  E-value: 6.87e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 359 RLTLGKPLGEGCFGQVVMAEAIGIDKDRAAKPVTVAvkmlkdDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGP 438
Cdd:cd08530   1 DFKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNLG------SLSQKEREDSVNEIRLLASV-NHPNIIRYKEAFLDGNR 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 439 LYVLVEYAAKGNLREFLRARRPPGldysfdtcKPPEEQLTFKDLVscayQVARGMEYLASQKCIHRDLAARNVLVTEDNV 518
Cdd:cd08530  74 LCIVMEYAPFGDLSKLISKRKKKR--------RLFPEDDIWRIFI----QMLRGLKALHDQKILHRDLKSANILLSAGDL 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 519 MKIADFGLARDVH-NLDYYKKTTngrlPVkWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLgGSPYPGIPVEELFKLLKE 597
Cdd:cd08530 142 VKIGDLGISKVLKkNLAKTQIGT----PL-YAAPEVWKGRPYDYKSDIWSLGCLLYEMATF-RPPFEARTMQELRYKVCR 215
                       250       260       270
                ....*....|....*....|....*....|....*
gi 13112048 598 GHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQL 632
Cdd:cd08530 216 GKFPPIPPVYSQDLQQIIRSLLQVNPKKRPSCDKL 250
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
359-694 2.19e-30

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 125.51  E-value: 2.19e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 359 RLTLGKPLGEGCFGQVVMAEAIGIDKdraakpvTVAVKMLKDDATD--KDLSDLVSEMEMMKMIgKHKNIINLLGACTQG 436
Cdd:COG0515   8 RYRILRLLGRGGMGVVYLARDLRLGR-------PVALKVLRPELAAdpEARERFRREARALARL-NHPNIVRVYDVGEED 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 437 GPLYVLVEYAAKGNLREFLRARRPpgldysfdtckppeeqLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTED 516
Cdd:COG0515  80 GRPYLVMEYVEGESLADLLRRRGP----------------LPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPD 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 517 NVMKIADFGLARDVHNLDyykKTTNGRLPVK--WMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEELFkl 594
Cdd:COG0515 144 GRVKLIDFGIARALGGAT---LTQTGTVVGTpgYMAPEQARGEPVDPRSDVYSLGVTLYELLT-GRPPFDGDSPAELL-- 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 595 lkEGHRMDKP-------ANCTHDLYMIMRECWHAAPSQRP-TFKQLVEDLDRVLTVTSTDEYLDLSAPFEQYSPGGQDTP 666
Cdd:COG0515 218 --RAHLREPPpppselrPDLPPALDAIVLRALAKDPEERYqSAAELAAALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAA 295
                       330       340
                ....*....|....*....|....*...
gi 13112048 667 SSSSSGDDSVFAHDLLPPAPPSSGGSRT 694
Cdd:COG0515 296 AAAAAAAAAAAAAAAAAAAAAAAAAAAP 323
Pkinase pfam00069
Protein kinase domain;
360-635 4.15e-30

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 118.12  E-value: 4.15e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048   360 LTLGKPLGEGCFGQVVMAeaigIDKDRAakpVTVAVKML-KDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGP 438
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKA----KHRDTG---KIVAIKKIkKEKIKKKKDKNILREIKILKKL-NHPNIVRLYDAFEDKDN 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048   439 LYVLVEYAAKGNLREFLRARRPpgldysfdtckppeeqLTFKDLVSCAYQVARGMEylasqkcihRDLAARNVLVTEDnv 518
Cdd:pfam00069  73 LYLVLEYVEGGSLFDLLSEKGA----------------FSEREAKFIMKQILEGLE---------SGSSLTTFVGTPW-- 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048   519 mkiadfglardvhnldyykkttngrlpvkWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEELFKLLKEG 598
Cdd:pfam00069 126 -----------------------------YMAPEVLGGNPYGPKVDVWSLGCILYELLT-GKPPFPGINGNEIYELIIDQ 175
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 13112048   599 HRM--DKPANCTHDLYMIMRECWHAAPSQRPTFKQLVED 635
Cdd:pfam00069 176 PYAfpELPSNLSEEAKDLLKKLLKKDPSKRLTATQALQH 214
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
362-585 5.63e-30

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: 119.12  E-value: 5.63e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 362 LGKPLGEGCFGQVVMAeaigidKDRAAKPVtVAVKML-KDDATDKDLSDLV-SEMEMMKMIgKHKNIINLLGACTQGGPL 439
Cdd:cd14007   4 IGKPLGKGKFGNVYLA------REKKSGFI-VALKVIsKSQLQKSGLEHQLrREIEIQSHL-RHPNILRLYGYFEDKKRI 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 440 YVLVEYAAKGNLREFLRARRPpgldysFDtckppeEQLTFKDLvscaYQVARGMEYLASQKCIHRDLAARNVLVTEDNVM 519
Cdd:cd14007  76 YLILEYAPNGELYKELKKQKR------FD------EKEAAKYI----YQLALALDYLHSKNIIHRDIKPENILLGSNGEL 139
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13112048 520 KIADFGLArdVHNLDYYKKTTNGRLpvKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPG 585
Cdd:cd14007 140 KLADFGWS--VHAPSNRRKTFCGTL--DYLPPEMVEGKEYDYKVDIWSLGVLCYELLV-GKPPFES 200
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
363-635 2.78e-29

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: 117.27  E-value: 2.78e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 363 GKPLGEGCFGQVVMAEAIGIDKDRAAKpvTVAVKMLKDdatDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVL 442
Cdd:cd14099   6 GKFLGKGGFAKCYEVTDMSTGKVYAGK--VVPKSSLTK---PKQREKLKSEIKIHRSL-KHPNIVKFHDCFEDEENVYIL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 443 VEYAAKGNLREFLRARRPpgldysfdtckppeeqLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIA 522
Cdd:cd14099  80 LELCSNGSLMELLKRRKA----------------LTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIG 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 523 DFGLARDVHNLDYYKKTTNGRlPvKWMAPEALFDRV-YTHQSDVWSFGVLLweiFTL--GGSPYPGIPVEELFKLLKEGH 599
Cdd:cd14099 144 DFGLAARLEYDGERKKTLCGT-P-NYIAPEVLEKKKgHSFEVDIWSLGVIL---YTLlvGKPPFETSDVKETYKRIKKNE 218
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 13112048 600 -RMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVED 635
Cdd:cd14099 219 ySFPSHLSISDEAKDLIRSMLQPDPTKRPSLDEILSH 255
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
367-582 3.52e-29

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: 116.58  E-value: 3.52e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 367 GEGCFGQVVMAEaigidkdRAAKPVTVAVKML-KDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd14002  10 GEGSFGKVYKGR-------RKYTGQVVALKFIpKRGKSEKELRNLRQEIEILRKL-NHPNIIEMLDSFETKKEFVVVTEY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAkGNLREFLRarrppgldysfDTCKPPEEQLTfkdlvSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFG 525
Cdd:cd14002  82 AQ-GELFQILE-----------DDGTLPEEEVR-----SIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFG 144
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13112048 526 LAR----DVHNLDYYKKTtngrlPVkWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlgGSP 582
Cdd:cd14002 145 FARamscNTLVLTSIKGT-----PL-YMAPELVQEQPYDHTADLWSLGCILYELFV--GQP 197
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
361-629 4.57e-29

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: 117.42  E-value: 4.57e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 361 TLGKpLGEGCFGQVVMAeaigidKDRAAKPVtVAVKMLKDDATDKDLSDL-VSEMEMMKMIgKHKNIINLLGACTQGGPL 439
Cdd:cd07833   5 VLGV-VGEGAYGVVLKC------RNKATGEI-VAIKKFKESEDDEDVKKTaLREVKVLRQL-RHENIVNLKEAFRRKGRL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 440 YVLVEYAAKgNLREFLRARrPPGLDYsfDTCKppeeqltfkdlvSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVM 519
Cdd:cd07833  76 YLVFEYVER-TLLELLEAS-PGGLPP--DAVR------------SYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVL 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 520 KIADFGLARDVH-----NLDYYKKTtngrlpvKWM-APEALF-DRVYTHQSDVWSFGVLLWEIFTlgGSPypgipveeLF 592
Cdd:cd07833 140 KLCDFGFARALTarpasPLTDYVAT-------RWYrAPELLVgDTNYGKPVDVWAIGCIMAELLD--GEP--------LF 202
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 13112048 593 kllkeghrmdkPANCTHD-LYMIMRECWHAAPSQRPTF 629
Cdd:cd07833 203 -----------PGDSDIDqLYLIQKCLGPLPPSHQELF 229
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
366-636 1.27e-28

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: 115.79  E-value: 1.27e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGID-----------KDRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACT 434
Cdd:cd14000   2 LGDGGFGSVYRASYKGEPvavkifnkhtsSNFANVPADTMLRHLRATDAMKNFRLLRQELTVLSHL-HHPSIVYLLGIGI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 435 QggPLYVLVEYAAKGNLREFLRARRPPGLdysfdtckpPEEQLTFKDLvscAYQVARGMEYLASQKCIHRDLAARNVLVT 514
Cdd:cd14000  81 H--PLMLVLELAPLGSLDHLLQQDSRSFA---------SLGRTLQQRI---ALQVADGLRYLHSAMIIYRDLKSHNVLVW 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 515 EDNV-----MKIADFGLARDVHNLDyyKKTTNGrlPVKWMAPE-ALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPV 588
Cdd:cd14000 147 TLYPnsaiiIKIADYGISRQCCRMG--AKGSEG--TPGFRAPEiARGNVIYNEKVDVFSFGMLLYEILSGGAPMVGHLKF 222
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 13112048 589 EELFKLLKE-----GHRMDKPANCTHDLymiMRECWHAAPSQRPTFKQLVEDL 636
Cdd:cd14000 223 PNEFDIHGGlrpplKQYECAPWPEVEVL---MKKCWKENPQQRPTAVTVVSIL 272
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
410-634 5.02e-28

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: 113.75  E-value: 5.02e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 410 LVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEYAAKGNLREFLRARRPPgldysfdtckppeeqLTFKDLVscAYQV 489
Cdd:cd14027  38 LLEEGKMMNRL-RHSRVVKLLGVILEEGKYSLVMEYMEKGNLMHVLKKVSVP---------------LSVKGRI--ILEI 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 490 ARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLA---------RDVHNL--DYYKKTTNGRLPVKWMAPEALFD-- 556
Cdd:cd14027 100 IEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwskltKEEHNEqrEVDGTAKKNAGTLYYMAPEHLNDvn 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 557 RVYTHQSDVWSFGVLLWEIFTlGGSPYP-GIPVEELFKLLKEGHRMDK---PANCTHDLYMIMRECWHAAPSQRPTFKQL 632
Cdd:cd14027 180 AKPTEKSDVYSFAIVLWAIFA-NKEPYEnAINEDQIIMCIKSGNRPDVddiTEYCPREIIDLMKLCWEANPEARPTFPGI 258

                ..
gi 13112048 633 VE 634
Cdd:cd14027 259 EE 260
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
366-578 5.75e-28

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: 113.33  E-value: 5.75e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKDRAAKPVTVAvKMlkddaTDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd08215   8 IGKGSFGSAYLVRRKSDGKLYVLKEIDLS-NM-----SEKEREEALNEVKLLSKL-KHPNIVKYYESFEENGKLCIVMEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLREFLRARRPPGLdysfdtcKPPEEQLTFKdLVscayQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFG 525
Cdd:cd08215  81 ADGGDLAQKIKKQKKKGQ-------PFPEEQILDW-FV----QICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFG 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 13112048 526 LARDVHNLDYYKKTTNGRlPVkWMAPEALFDRVYTHQSDVWSFGVLLWEIFTL 578
Cdd:cd08215 149 ISKVLESTTDLAKTVVGT-PY-YLSPELCENKPYNYKSDIWALGCVLYELCTL 199
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
395-640 8.14e-28

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: 112.95  E-value: 8.14e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 395 VKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEYAAKGNLREFLRARRPpgldysfdtckppe 474
Cdd:cd14155  20 VMALKMNTLSSNRANMLREVQLMNRL-SHPNILRFMGVCVHQGQLHALTEYINGGNLEQLLDSNEP-------------- 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 475 eqLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDN---VMKIADFGLARDVHNLDYYKKttngRLPV----K 547
Cdd:cd14155  85 --LSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIKRDEngyTAVVGDFGLAEKIPDYSDGKE----KLAVvgspY 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 548 WMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLlkeghrmDKPA------NCTHDLYMIMRECWHA 621
Cdd:cd14155 159 WMAPEVLRGEPYNEKADVFSYGIILCEIIARIQADPDYLPRTEDFGL-------DYDAfqhmvgDCPPDFLQLAFNCCNM 231
                       250
                ....*....|....*....
gi 13112048 622 APSQRPTFKQLVEDLDRVL 640
Cdd:cd14155 232 DPKSRPSFHDIVKTLEEIL 250
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
353-640 8.82e-28

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: 113.23  E-value: 8.82e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 353 WELSRARLTLGKPLGEGCFGQVVMAEAIGidkdraakpvTVAVKMLKDDA-TDKDLSDLVSEMEMMKMIgKHKNIINLLG 431
Cdd:cd14151   3 WEIPDGQITVGQRIGSGSFGTVYKGKWHG----------DVAVKMLNVTApTPQQLQAFKNEVGVLRKT-RHVNILLFMG 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 432 ACTQGgPLYVLVEYAAKGNLREFLRArrppgldysfdtckpPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNV 511
Cdd:cd14151  72 YSTKP-QLAIVTQWCEGSSLYHHLHI---------------IETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNI 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 512 LVTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALF---DRVYTHQSDVWSFGVLLWEIFTlGGSPYPGI-P 587
Cdd:cd14151 136 FLHEDLTVKIGDFGLATVKSRWSGSHQFEQLSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMT-GQLPYSNInN 214
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 588 VEELFKLLKEGH---RMDK-PANCTHDLYMIMRECWHAAPSQRPTFKQL---VEDLDRVL 640
Cdd:cd14151 215 RDQIIFMVGRGYlspDLSKvRSNCPKAMKRLMAECLKKKRDERPLFPQIlasIELLARSL 274
PTKc_Aatyk2 cd05086
Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs ...
366-641 2.37e-27

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: 111.88  E-value: 2.37e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIgidkdRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd05086   5 IGNGWFGKVLLGEIY-----TGTSVARVVVKELKASANPKEQDDFLQQGEPYYIL-QHPNILQCVGQCVEAIPYLLVFEF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLREFLRARRppgldysfDTCKPPEEQLTFKDLvscAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFG 525
Cdd:cd05086  79 CDLGDLKTYLANQQ--------EKLRGDSQIMLLQRM---ACEIAAGLAHMHKHNFLHSDLALRNCYLTSDLTVKVGDYG 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 526 LARDVHNLDYYKKTTNGRLPVKWMAPE---ALFDRVY----THQSDVWSFGVLLWEIFTLGGSPYPGIP-VEELFKLLKE 597
Cdd:cd05086 148 IGFSRYKEDYIETDDKKYAPLRWTAPElvtSFQDGLLaaeqTKYSNIWSLGVTLWELFENAAQPYSDLSdREVLNHVIKE 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 13112048 598 GH-RMDKP---ANCTHDLYMIMRECWhAAPSQRPTfkqlVEDLDRVLT 641
Cdd:cd05086 228 RQvKLFKPhleQPYSDRWYEVLQFCW-LSPEKRPT----AEEVHRLLT 270
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
366-635 2.49e-27

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: 112.14  E-value: 2.49e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKDRAAKPVTVavkmlKDDAtdkDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd06611  13 LGDGAFGKVYKAQHKETGLFAAAKIIQI-----ESEE---ELEDFMVEIDILSEC-KHPNIVGLYEAYFYENKLWILIEF 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLREFLRArrppgLDYSFDtckppEEQLTFkdlvsCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFG 525
Cdd:cd06611  84 CDGGALDSIMLE-----LERGLT-----EPQIRY-----VCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFG 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 526 L-ARDVHNLDyyKKTTNGRLPVkWMAPEALF-----DRVYTHQSDVWSFGVLLWEIfTLGGSPYPGI-PVEELFKLLK-E 597
Cdd:cd06611 149 VsAKNKSTLQ--KRDTFIGTPY-WMAPEVVAcetfkDNPYDYKADIWSLGITLIEL-AQMEPPHHELnPMRVLLKILKsE 224
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 13112048 598 GHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVED 635
Cdd:cd06611 225 PPTLDQPSKWSSSFNDFLKSCLVKDPDDRPTAAELLKH 262
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
366-640 5.94e-27

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: 110.82  E-value: 5.94e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAeaigidKDRAAKPVTVAVKMLK-DDATDKDLsdlVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVE 444
Cdd:cd14221   1 LGKGCFGQAIKV------THRETGEVMVMKELIRfDEETQRTF---LKEVKVMRCL-EHPNVLKFIGVLYKDKRLNFITE 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 445 YAAKGNLREFLRarrppgldySFDTCKPPEEQLTFkdlvscAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADF 524
Cdd:cd14221  71 YIKGGTLRGIIK---------SMDSHYPWSQRVSF------AKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADF 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 525 GLAR--------DVHNLDYYKKTTNGRLPV----KWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELF 592
Cdd:cd14221 136 GLARlmvdektqPEGLRSLKKPDRKKRYTVvgnpYWMAPEMINGRSYDEKVDVFSFGIVLCEIIGRVNADPDYLPRTMDF 215
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 13112048 593 KLLKEGHrMDK--PANCTHDLYMIMRECWHAAPSQRPTFKQL---VEDLDRVL 640
Cdd:cd14221 216 GLNVRGF-LDRycPPNCPPSFFPIAVLCCDLDPEKRPSFSKLehwLETLRMHL 267
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
369-638 8.07e-27

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: 110.17  E-value: 8.07e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 369 GCFGQVVMAEAIGIDKDRaakpvTVAVKML--KDDATDKDLSDLVSEMEMmkmigKHKNIINLLGACTQGGPLYVLVEYA 446
Cdd:cd13992   9 SHTGEPKYVKKVGVYGGR-----TVAIKHItfSRTEKRTILQELNQLKEL-----VHDNLNKFIGICINPPNIAVVTEYC 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 447 AKGNLREFLrARRPPGLDYSFdtckppeeQLTFkdlvscAYQVARGMEYLASQKCI-HRDLAARNVLVTEDNVMKIADFG 525
Cdd:cd13992  79 TRGSLQDVL-LNREIKMDWMF--------KSSF------IKDIVKGMNYLHSSSIGyHGRLKSSNCLVDSRWVVKLTDFG 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 526 LARDVHN-LDYYKKTTNGRLPVKWMAPEALFDRVYTH----QSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGHR 600
Cdd:cd13992 144 LRNLLEEqTNHQLDEDAQHKKLLWTAPELLRGSLLEVrgtqKGDVYSFAIILYEILFRSDPFALEREVAIVEKVISGGNK 223
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 13112048 601 MDKP------ANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDR 638
Cdd:cd13992 224 PFRPelavllDEFPPRLVLLVKQCWAENPEKRPSFKQIKKTLTE 267
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
366-635 1.62e-26

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


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 108.89  E-value: 1.62e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAeaigIDKDRAAkpvTVAVKMLKddaTDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd06612  11 LGEGSYGSVYKA----IHKETGQ---VVAIKVVP---VEEDLQEIIKEISILKQC-DSPYIVKYYGSYFKNTDLWIVMEY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLREFLRArrppgldysfdTCKP-PEEQLTFkdlvsCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADF 524
Cdd:cd06612  80 CGAGSVSDIMKI-----------TNKTlTEEEIAA-----ILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADF 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 525 GLARDVHNLDYYKKTTNGRlPVkWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGI-PVEELFKL-------LK 596
Cdd:cd06612 144 GVSGQLTDTMAKRNTVIGT-PF-WMAPEVIQEIGYNNKADIWSLGITAIEMAE-GKPPYSDIhPMRAIFMIpnkppptLS 220
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 13112048 597 EGHRMDKPANcthDLymiMRECWHAAPSQRPTFKQLVED 635
Cdd:cd06612 221 DPEKWSPEFN---DF---VKKCLVKDPEERPSAIQLLQH 253
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
366-637 2.03e-26

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: 108.63  E-value: 2.03e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGidkdraakpvTVAVKMLK-DDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGpLYVLVE 444
Cdd:cd14062   1 IGSGSFGTVYKGRWHG----------DVAVKKLNvTDPTPSQLQAFKNEVAVLRKT-RHVNILLFMGYMTKPQ-LAIVTQ 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 445 YAAKGNLREFLRArrppgLDYSFDTCKppeeqltfkdLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADF 524
Cdd:cd14062  69 WCEGSSLYKHLHV-----LETKFEMLQ----------LIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDF 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 525 GLArDVHNldyyKKTTNGRLP-----VKWMAPEALF---DRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEE--LFKL 594
Cdd:cd14062 134 GLA-TVKT----RWSGSQQFEqptgsILWMAPEVIRmqdENPYSFQSDVYAFGIVLYELLT-GQLPYSHINNRDqiLFMV 207
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 13112048 595 lkeGHRMDKP------ANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLD 637
Cdd:cd14062 208 ---GRGYLRPdlskvrSDTPKALRRLMEDCIKFQRDERPLFPQILASLE 253
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
363-636 2.43e-26

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: 109.51  E-value: 2.43e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 363 GKPLGEGCFGQVVMaeaiGIDKDRaakpvTVAVKMLKD--DATDKDLSDLV-SEMEMMKMIgKHKNIINLLGaCTQGGPL 439
Cdd:cd14158  20 GNKLGEGGFGVVFK----GYINDK-----NVAVKKLAAmvDISTEDLTKQFeQEIQVMAKC-QHENLVELLG-YSCDGPQ 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 440 YVLV-EYAAKGNLREFLrarrppgldysfdTCKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNV 518
Cdd:cd14158  89 LCLVyTYMPNGSLLDRL-------------ACLNDTPPLSWHMRCKIAQGTANGINYLHENNHIHRDIKSANILLDETFV 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 519 MKIADFGLARDVHNldyYKKTTNGRLPV---KWMAPEALFDRVyTHQSDVWSFGVLLWEIFTlgGSPypgiPVEE----- 590
Cdd:cd14158 156 PKISDFGLARASEK---FSQTIMTERIVgttAYMAPEALRGEI-TPKSDIFSFGVVLLEIIT--GLP----PVDEnrdpq 225
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 591 LFKLLKEGH-------------RM-DKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDL 636
Cdd:cd14158 226 LLLDIKEEIedeektiedyvdkKMgDWDSTSIEAMYSVASQCLNDKKNRRPDIAKVQQLL 285
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
366-632 3.41e-26

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


Pssm-ID: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 108.49  E-value: 3.41e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMaeaiGIDKDraaKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd06609   9 IGKGSFGEVYK----GIDKR---TNQVVAIKVIDLEEAEDEIEDIQQEIQFLSQC-DSPYITKYYGSFLKGSKLWIIMEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLREFLRArrppgldysfdtCKPPEEQLTFkdlvsCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFG 525
Cdd:cd06609  81 CGGGSVLDLLKP------------GPLDETYIAF-----ILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFG 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 526 LARDVHNLDYYKKTTNGRlPVkWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGI-PVEELFKLLKEghrmdKP 604
Cdd:cd06609 144 VSGQLTSTMSKRNTFVGT-PF-WMAPEVIKQSGYDEKADIWSLGITAIELAK-GEPPLSDLhPMRVLFLIPKN-----NP 215
                       250       260       270
                ....*....|....*....|....*....|...
gi 13112048 605 ANCTHDLYM-----IMRECWHAAPSQRPTFKQL 632
Cdd:cd06609 216 PSLEGNKFSkpfkdFVELCLNKDPKERPSAKEL 248
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
359-634 3.57e-26

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: 108.12  E-value: 3.57e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 359 RLTLGKPLGEGCFGQVVMAEAIGIDKDRAAKPVTVAVKMLKDDATDKDLSDLVSEMemmkmigKHKNIINLLGACTQGGP 438
Cdd:cd08225   1 RYEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPVKEKEASKKEVILLAKM-------KHPNIVTFFASFQENGR 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 439 LYVLVEYAAKGNLREflRARRPPGLDYSfdtckppEEQLtfkdlVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDN- 517
Cdd:cd08225  74 LFIVMEYCDGGDLMK--RINRQRGVLFS-------EDQI-----LSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGm 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 518 VMKIADFGLARDVHNLDYYKKTTNGRlPVkWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLgGSPYPGIPVEELFKLLKE 597
Cdd:cd08225 140 VAKLGDFGIARQLNDSMELAYTCVGT-PY-YLSPEICQNRPYNNKTDIWSLGCVLYELCTL-KHPFEGNNLHQLVLKICQ 216
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 13112048 598 GHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVE 634
Cdd:cd08225 217 GYFAPISPNFSRDLRSLISQLFKVSPRDRPSITSILK 253
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
365-634 4.46e-26

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: 108.21  E-value: 4.46e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 365 PLGEGCFGQVVMAEAIgidkdraAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVE 444
Cdd:cd06610   8 VIGSGATAVVYAAYCL-------PKKEKVAIKRIDLEKCQTSMDELRKEIQAMSQC-NHPNVVSYYTSFVVGDELWLVMP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 445 YAAKGNLREFLRARRPPG-LDYSFdtckppeeqltfkdLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIAD 523
Cdd:cd06610  80 LLSGGSLLDIMKSSYPRGgLDEAI--------------IATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIAD 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 524 FG----LARDVHNLDYYKKTTNGRlPVkWMAPEALF-DRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEELFKLLKEG 598
Cdd:cd06610 146 FGvsasLATGGDRTRKVRKTFVGT-PC-WMAPEVMEqVRGYDFKADIWSFGITAIELAT-GAAPYSKYPPMKVLMLTLQN 222
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 13112048 599 HRMDKPANCTHDLY------MImRECWHAAPSQRPTFKQLVE 634
Cdd:cd06610 223 DPPSLETGADYKKYsksfrkMI-SLCLQKDPSKRPTAEELLK 263
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
363-633 9.49e-26

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: 107.23  E-value: 9.49e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 363 GKPLGEGCFGQVVMAEAIGIDKDRAAKPVTVAVKMLKDDATDKDLSD-LVSEMEMMKMIgKHKNIINLLGACTQGGPLYV 441
Cdd:cd06628   5 GALIGSGSFGSVYLGMNASSGELMAVKQVELPSVSAENKDRKKSMLDaLQREIALLREL-QHENIVQYLGSSSDANHLNI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 442 LVEYAAKGNLREFLRarrppglDY-SFdtckppEEQLTfKDLVScayQVARGMEYLASQKCIHRDLAARNVLVTEDNVMK 520
Cdd:cd06628  84 FLEYVPGGSVATLLN-------NYgAF------EESLV-RNFVR---QILKGLNYLHNRGIIHRDIKGANILVDNKGGIK 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 521 IADFGLARDVHnLDYYKKTTNGRLP-----VKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIP-VEELFKL 594
Cdd:cd06628 147 ISDFGISKKLE-ANSLSTKNNGARPslqgsVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLT-GTHPFPDCTqMQAIFKI 224
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 13112048 595 LKEGhRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLV 633
Cdd:cd06628 225 GENA-SPTIPSNISSEARDFLEKTFEIDHNKRPTADELL 262
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
361-598 9.63e-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: 106.79  E-value: 9.63e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 361 TLGKPLGEGCFGQVVMAEAIGIDKDRAAKpvtvavKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLY 440
Cdd:cd05117   3 ELGKVLGRGSFGVVRLAVHKKTGEEYAVK------IIDKKKLKSEDEEMLRREIEILKRL-DHPNIVKLYEVFEDDKNLY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 441 VLVEYAAKGNLreflrarrppgLDYSFDTCKPPEEQLTFkdlvsCAYQVARGMEYLASQKCIHRDLAARNVLVT---EDN 517
Cdd:cd05117  76 LVMELCTGGEL-----------FDRIVKKGSFSEREAAK-----IMKQILSAVAYLHSQGIVHRDLKPENILLAskdPDS 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 518 VMKIADFGLARDVHNlDYYKKTTNGRLpvKWMAPEALFDRVYTHQSDVWSFGVLLweiFTL--GGSPYPGIPVEELFKLL 595
Cdd:cd05117 140 PIKIIDFGLAKIFEE-GEKLKTVCGTP--YYVAPEVLKGKGYGKKCDIWSLGVIL---YILlcGYPPFYGETEQELFEKI 213

                ...
gi 13112048 596 KEG 598
Cdd:cd05117 214 LKG 216
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
364-596 1.05e-25

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: 106.55  E-value: 1.05e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVMAeaigidKDRAAKPVtVAVKMLK--DDATDKDLSDLVSeMEMMKMIGKHKNIINLLGACT--QGGPL 439
Cdd:cd05118   5 RKIGEGAFGTVWLA------RDKVTGEK-VAIKKIKndFRHPKAALREIKL-LKHLNDVEGHPNIVKLLDVFEhrGGNHL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 440 YVLVEYAaKGNLREFLRARRPPgldysfdtckppeeqLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDN-V 518
Cdd:cd05118  77 CLVFELM-GMNLYELIKDYPRG---------------LPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLELgQ 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 519 MKIADFGLARDVHNLDYYKKTTngrlPVKWMAPEALF-DRVYTHQSDVWSFGVLLWEIFTlgGSP-YPGI-PVEELFKLL 595
Cdd:cd05118 141 LKLADFGLARSFTSPPYTPYVA----TRWYRAPEVLLgAKPYGSSIDIWSLGCILAELLT--GRPlFPGDsEVDQLAKIV 214

                .
gi 13112048 596 K 596
Cdd:cd05118 215 R 215
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
366-593 1.54e-25

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: 106.80  E-value: 1.54e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAeaigidKDRAAKpVTVAVKMLKDDATDKDL-SDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVE 444
Cdd:cd07829   7 LGEGTYGVVYKA------KDKKTG-EIVALKKIRLDNEEEGIpSTALREISLLKEL-KHPNIVKLLDVIHTENKLYLVFE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 445 YAAKgNLREFLRaRRPPGLdysfdtckPPEEQLTFkdlvscAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADF 524
Cdd:cd07829  79 YCDQ-DLKKYLD-KRPGPL--------PPNLIKSI------MYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADF 142
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13112048 525 GLARDV-HNLDYYkkTTNgrlpVK--WM-APEALF-DRVYTHQSDVWSFGVLLWEIFTlgGSP-YPG-IPVEELFK 593
Cdd:cd07829 143 GLARAFgIPLRTY--THE----VVtlWYrAPEILLgSKHYSTAVDIWSVGCIFAELIT--GKPlFPGdSEIDQLFK 210
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
360-636 3.27e-25

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: 105.26  E-value: 3.27e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 360 LTLGKPLGEGCFGQVVMaeaiGIDK---DRAAKPVTVAVKMLKDDATDKDLSDLVSeMEMMKMIgKHKNIINLLGACTQG 436
Cdd:cd05037   1 ITFHEHLGQGTFTNIYD----GILRevgDGRVQEVEVLLKVLDSDHRDISESFFET-ASLMSQI-SHKHLVKLYGVCVAD 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 437 GPLYVLvEYAAKGNLREFLRARR-PPGLDYSFDTckppeeqltfkdlvscAYQVARGMEYLASQKCIHRDLAARNVLVTE 515
Cdd:cd05037  75 ENIMVQ-EYVRYGPLDKYLRRMGnNVPLSWKLQV----------------AKQLASALHYLEDKKLIHGNVRGRNILLAR 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 516 DNV------MKIADFGLARDVHNLDYYKkttngrLPVKWMAPEALFD--RVYTHQSDVWSFGVLLWEIFTLGGSPYPGIP 587
Cdd:cd05037 138 EGLdgyppfIKLSDPGVPITVLSREERV------DRIPWIAPECLRNlqANLTIAADKWSFGTTLWEICSGGEEPLSALS 211
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 13112048 588 VEELFKLLKEGHRMDKPaNCThDLYMIMRECWHAAPSQRPTFKQLVEDL 636
Cdd:cd05037 212 SQEKLQFYEDQHQLPAP-DCA-ELAELIMQCWTYEPTKRPSFRAILRDL 258
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
359-641 4.02e-25

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: 105.16  E-value: 4.02e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 359 RLTLGKPLGEGCFGQVVMAEAIGidkdraakpVTVAVKMLKDDATDKDLSD-LVSEMEMMKMigKHKNIINLLGA---CT 434
Cdd:cd13979   4 PLRLQEPLGSGGFGSVYKATYKG---------ETVAVKIVRRRRKNRASRQsFWAELNAARL--RHENIVRVLAAetgTD 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 435 QGGPLYVLVEYAAKGNLREFLRARRPPgldysfdtckppeeqLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVT 514
Cdd:cd13979  73 FASLGLIIMEYCGNGTLQQLIYEGSEP---------------LPLAHRILISLDIARALRFCHSHGIVHLDVKPANILIS 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 515 EDNVMKIADFGLA------RDVHNLDYYKKTTNGrlpvkWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPV 588
Cdd:cd13979 138 EQGVCKLCDFGCSvklgegNEVGTPRSHIGGTYT-----YRAPELLKGERVTPKADIYSFGITLWQMLT-RELPYAGLRQ 211
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 13112048 589 EELFKLLKEGHRMDKPANCTHD----LYMIMRECWHAAPSQRPTfkqLVEDLDRVLT 641
Cdd:cd13979 212 HVLYAVVAKDLRPDLSGLEDSEfgqrLRSLISRCWSAQPAERPN---ADESLLKSLE 265
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
366-632 4.83e-25

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: 104.94  E-value: 4.83e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKdraakpvTVAVKMLK------------DDATDKD-LSDLVSEMEMMKmigK--HKNIINLL 430
Cdd:cd14008   1 LGRGSFGKVKLALDTETGQ-------LYAIKIFNksrlrkrregknDRGKIKNaLDDVRREIAIMK---KldHPNIVRLY 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 431 GACT--QGGPLYVLVEYAAKGNLREFLRARRPPGLdysfdtckpPEEQL--TFKDLVscayqvaRGMEYLASQKCIHRDL 506
Cdd:cd14008  71 EVIDdpESDKLYLVLEYCEGGPVMELDSGDRVPPL---------PEETArkYFRDLV-------LGLEYLHENGIVHRDI 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 507 AARNVLVTEDNVMKIADFGLARDVHNLDYYKKTTNGRlPVkWMAPEaLFDRVYTHQS----DVWSFGVLLWeIFTLGGSP 582
Cdd:cd14008 135 KPENLLLTADGTVKISDFGVSEMFEDGNDTLQKTAGT-PA-FLAPE-LCDGDSKTYSgkaaDIWALGVTLY-CLVFGRLP 210
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 13112048 583 YPGIPVEELFKLLKEGHRM-DKPANCTHDLYMIMRECWHAAPSQRPTFKQL 632
Cdd:cd14008 211 FNGDNILELYEAIQNQNDEfPIPPELSPELKDLLRRMLEKDPEKRITLKEI 261
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
362-632 5.38e-25

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: 104.80  E-value: 5.38e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 362 LGKPLGEGCFGQVVMAEaigidkdRAAKPVTVAVKMLK-DDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLY 440
Cdd:cd08529   4 ILNKLGKGSFGVVYKVV-------RKVDGRVYALKQIDiSRMSRKMREEAIDEARVLSKL-NSPYVIKYYDSFVDKGKLN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 441 VLVEYAAKGNLREFLRARRPpgldysfdtcKPPEEQLTFKDLVscayQVARGMEYLASQKCIHRDLAARNVLVTEDNVMK 520
Cdd:cd08529  76 IVMEYAENGDLHSLIKSQRG----------RPLPEDQIWKFFI----QTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVK 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 521 IADFGLARDVHNLDYYKKTTNGRlPVkWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEELFKLLKEGHR 600
Cdd:cd08529 142 IGDLGVAKILSDTTNFAQTIVGT-PY-YLSPELCEDKPYNEKSDVWALGCVLYELCT-GKHPFEAQNQGALILKIVRGKY 218
                       250       260       270
                ....*....|....*....|....*....|..
gi 13112048 601 MDKPANCTHDLYMIMRECWHAAPSQRPTFKQL 632
Cdd:cd08529 219 PPISASYSQDLSQLIDSCLTKDYRQRPDTTEL 250
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
366-634 9.74e-25

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: 104.73  E-value: 9.74e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEaigiDKDRAAkpvtVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd06644  20 LGDGAFGKVYKAK----NKETGA----LAAAKVIETKSEEELEDYMVEIEILATC-NHPYIVKLLGAFYWDGKLWIMIEF 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLREFLRArrppgLDYSFdtcKPPEEQLTFKdlvscayQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFG 525
Cdd:cd06644  91 CPGGAVDAIMLE-----LDRGL---TEPQIQVICR-------QMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 526 L-ARDVHNLDyyKKTTNGRLPVkWMAPEALF-----DRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLK-EG 598
Cdd:cd06644 156 VsAKNVKTLQ--RRDSFIGTPY-WMAPEVVMcetmkDTPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKsEP 232
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 13112048 599 HRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVE 634
Cdd:cd06644 233 PTLSQPSKWSMEFRDFLKTALDKHPETRPSAAQLLE 268
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
364-635 1.83e-24

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: 103.15  E-value: 1.83e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVMAeaigidKDRAAKPVtVAVKMLKDDATDkDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLV 443
Cdd:cd06613   6 QRIGSGTYGDVYKA------RNIATGEL-AAVKVIKLEPGD-DFEIIQQEISMLKEC-RHPNIVAYFGSYLRRDKLWIVM 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 444 EYAAKGNLREFLRARRPPgldysfdtckpPEEQLTFkdlVScaYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIAD 523
Cdd:cd06613  77 EYCGGGSLQDIYQVTGPL-----------SELQIAY---VC--RETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLAD 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 524 FGLARDVHNLDYYKKTTNGRLpvKWMAPEALFDR---VYTHQSDVWSFGVLLWEIFTLgGSPYPGI-PVEELFKLLKEGh 599
Cdd:cd06613 141 FGVSAQLTATIAKRKSFIGTP--YWMAPEVAAVErkgGYDGKCDIWALGITAIELAEL-QPPMFDLhPMRALFLIPKSN- 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 13112048 600 rMDKPA-----NCTHDLYMIMRECWHAAPSQRPTFKQLVED 635
Cdd:cd06613 217 -FDPPKlkdkeKWSPDFHDFIKKCLTKNPKKRPTATKLLQH 256
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
363-635 2.13e-24

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: 103.23  E-value: 2.13e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 363 GKPLGEGCFGQVVMAEAIGIDKDRAAKPVTV-AVKMLKDDATDKDLSD-LVSEMEMMKMIgKHKNIINLLGACTQGGPLY 440
Cdd:cd06629   6 GELIGKGTYGRVYLAMNATTGEMLAVKQVELpKTSSDRADSRQKTVVDaLKSEIDTLKDL-DHPNIVQYLGFEETEDYFS 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 441 VLVEYAAKGNLREFLRARRPpgldysFdtckppEEQLTfkdlVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMK 520
Cdd:cd06629  85 IFLEYVPGGSIGSCLRKYGK------F------EEDLV----RFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICK 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 521 IADFGLARDVHNLDYYKKTTNGRLPVKWMAPEAL--FDRVYTHQSDVWSFGVLLWEIFTlGGSPYPgiPVEELFKLLKEG 598
Cdd:cd06629 149 ISDFGISKKSDDIYGNNGATSMQGSVFWMAPEVIhsQGQGYSAKVDIWSLGCVVLEMLA-GRRPWS--DDEAIAAMFKLG 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 13112048 599 HRMDKP-----ANCTHDLYMIMRECWHAAPSQRPTFKQLVED 635
Cdd:cd06629 226 NKRSAPpvpedVNLSPEALDFLNACFAIDPRDRPTAAELLSH 267
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
366-642 3.08e-24

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: 103.10  E-value: 3.08e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAeaigidKDRAAKPVTVAVKMLK-DDATDKDLsdlVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVE 444
Cdd:cd14222   1 LGKGFFGQAIKV------THKATGKVMVMKELIRcDEETQKTF---LTEVKVMRSL-DHPNVLKFIGVLYKDKRLNLLTE 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 445 YAAKGNLREFLRARRPpgldysfdtckppeeqLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADF 524
Cdd:cd14222  71 FIEGGTLKDFLRADDP----------------FPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADF 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 525 GLARDV--------HNLDYYKKTTNGRLPVK----------WMAPEALFDRVYTHQSDVWSFGVLLWEIFtlgGSPYPGi 586
Cdd:cd14222 135 GLSRLIveekkkppPDKPTTKKRTLRKNDRKkrytvvgnpyWMAPEMLNGKSYDEKVDIFSFGIVLCEII---GQVYAD- 210
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13112048 587 PvEELFKLLKEGHRM----DK--PANCTHDLYMIMRECWHAAPSQRPTFKQLvEDLDRVLTV 642
Cdd:cd14222 211 P-DCLPRTLDFGLNVrlfwEKfvPKDCPPAFFPLAAICCRLEPDSRPAFSKL-EDSFEALSL 270
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
360-634 3.11e-24

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: 102.67  E-value: 3.11e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 360 LTLGKPLGEGCFGQVVMAeaigIDKDRAAkpvTVAVKMLKDDATDKDLSDLVSEMEMMKmIGKHKNIINLLGACTQGGPL 439
Cdd:cd06623   3 LERVKVLGQGSSGVVYKV----RHKPTGK---IYALKKIHVDGDEEFRKQLLRELKTLR-SCESPYVVKCYGAFYKEGEI 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 440 YVLVEYAAKGNLREFLRARRppgldysfdtcKPPEEQLTFkdlvsCAYQVARGMEYLASQ-KCIHRDLAARNVLVTEDNV 518
Cdd:cd06623  75 SIVLEYMDGGSLADLLKKVG-----------KIPEPVLAY-----IARQILKGLDYLHTKrHIIHRDIKPSNLLINSKGE 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 519 MKIADFGLARDVHNLDYYKKTTNGrlPVKWMAPEALFDRVYTHQSDVWSFGVLLWEiFTLGGSPYPGIPVEELFKLLKeg 598
Cdd:cd06623 139 VKIADFGISKVLENTLDQCNTFVG--TVTYMSPERIQGESYSYAADIWSLGLTLLE-CALGKFPFLPPGQPSFFELMQ-- 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 13112048 599 HRMDKPA------NCTHDLYMIMRECWHAAPSQRPTFKQLVE 634
Cdd:cd06623 214 AICDGPPpslpaeEFSPEFRDFISACLQKDPKKRPSAAELLQ 255
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
361-572 4.18e-24

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: 102.26  E-value: 4.18e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 361 TLGKPLGEGCFGQVVMAEAIgidkdRAAKPVTVAVKML-KDDATDKDLSD-LVSEMEMMKMIgKHKNIINLLGACTQGGP 438
Cdd:cd14080   3 RLGKTIGEGSYSKVKLAEYT-----KSGLKEKVACKIIdKKKAPKDFLEKfLPRELEILRKL-RHPNIIQVYSIFERGSK 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 439 LYVLVEYAAKGNLREFLRARRPPgldysfdtckpPEEQ--LTFkdlvscaYQVARGMEYLASQKCIHRDLAARNVLVTED 516
Cdd:cd14080  77 VFIFMEYAEHGDLLEYIQKRGAL-----------SESQarIWF-------RQLALAVQYLHSLDIAHRDLKCENILLDSN 138
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 13112048 517 NVMKIADFGLARDVH--NLDYYKKTTNGRLpvKWMAPEALFDRVYT-HQSDVWSFGVLL 572
Cdd:cd14080 139 NNVKLSDFGFARLCPddDGDVLSKTFCGSA--AYAAPEILQGIPYDpKKYDIWSLGVIL 195
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
361-632 7.65e-24

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: 101.84  E-value: 7.65e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 361 TLGKPLGEGCFGQVVMAeaigidKDRAAKPVtVAVKMLKddATDKDLSDLVS--EMEMMKMIGKHKNIINLLGACTQGGP 438
Cdd:cd07830   2 KVIKQLGDGTFGSVYLA------RNKETGEL-VAIKKMK--KKFYSWEECMNlrEVKSLRKLNEHPNIVKLKEVFRENDE 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 439 LYVLVEYAaKGNLREFLRARRPPGLdysfdtckpPEEQLtfKDLVscaYQVARGMEYLASQKCIHRDLAARNVLVTEDNV 518
Cdd:cd07830  73 LYFVFEYM-EGNLYQLMKDRKGKPF---------SESVI--RSII---YQILQGLAHIHKHGFFHRDLKPENLLVSGPEV 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 519 MKIADFGLARDVHNLDYYKKTTNGRlpvkWM-APEALF-DRVYTHQSDVWSFGVLLWEIFTLggSP-YPGI-PVEELFKL 594
Cdd:cd07830 138 VKIADFGLAREIRSRPPYTDYVSTR----WYrAPEILLrSTSYSSPVDIWALGCIMAELYTL--RPlFPGSsEIDQLYKI 211
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13112048 595 LK-----------EGHRMDK------PA-----------NCTHDLYMIMRECWHAAPSQRPTFKQL 632
Cdd:cd07830 212 CSvlgtptkqdwpEGYKLASklgfrfPQfaptslhqlipNASPEAIDLIKDMLRWDPKKRPTASQA 277
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
366-634 8.44e-24

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: 8.44e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEaigiDKDRAakpVTVAVKMLkDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd06643  13 LGDGAFGKVYKAQ----NKETG---ILAAAKVI-DTKSEEELEDYMVEIDILASC-DHPNIVKLLDAFYYENNLWILIEF 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLRE-FLRARRPpgldysfdtckppeeqLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADF 524
Cdd:cd06643  84 CAGGAVDAvMLELERP----------------LTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADF 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 525 GLA----RDVHNLDYYKKTTngrlpvKWMAPEALF-----DRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLL 595
Cdd:cd06643 148 GVSakntRTLQRRDSFIGTP------YWMAPEVVMcetskDRPYDYKADVWSLGVTLIEMAQIEPPHHELNPMRVLLKIA 221
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 13112048 596 K-EGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVE 634
Cdd:cd06643 222 KsEPPTLAQPSRWSPEFKDFLRKCLEKNVDARWTTSQLLQ 261
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
361-635 8.63e-24

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


Pssm-ID: 270971 [Multi-domain]  Cd Length: 261  Bit Score: 101.25  E-value: 8.63e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 361 TLGKPLGEGCFGQVVMAEaigidKDRAAKpvTVAVKML-KDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPL 439
Cdd:cd14069   4 DLVQTLGEGAFGEVFLAV-----NRNTEE--AVAVKFVdMKRAPGDCPENIKKEVCIQKML-SHKNVVRFYGHRREGEFQ 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 440 YVLVEYAAKGNLreFLRARRPPGLDysfdtckPPEEQLTFKDLVScayqvarGMEYLASQKCIHRDLAARNVLVTEDNVM 519
Cdd:cd14069  76 YLFLEYASGGEL--FDKIEPDVGMP-------EDVAQFYFQQLMA-------GLKYLHSCGITHRDIKPENLLLDENDNL 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 520 KIADFGLArdvhNLDYYKKTTN------GRLPvkWMAPEALFDRVYTHQ-SDVWSFGVLLWEIFTlGGSPY--PgIPVEE 590
Cdd:cd14069 140 KISDFGLA----TVFRYKGKERllnkmcGTLP--YVAPELLAKKKYRAEpVDVWSCGIVLFAMLA-GELPWdqP-SDSCQ 211
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 13112048 591 LFKLLKEGH--------RMDKPAncthdlYMIMRECWHAAPSQRPTFKQLVED 635
Cdd:cd14069 212 EYSDWKENKktyltpwkKIDTAA------LSLLRKILTENPNKRITIEDIKKH 258
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
366-605 1.61e-23

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: 100.37  E-value: 1.61e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAeaigidkdRAAKPVT-VAVK-MLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLV 443
Cdd:cd14009   1 IGRGSFATVWKG--------RHKQTGEvVAIKeISRKKLNKKLQENLESEIAILKSI-KHPNIVRLYDVQKTEDFIYLVL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 444 EYAAKGNLREFLRARRppgldysfdtcKPPEEqlTFKDLVScayQVARGMEYLASQKCIHRDLAARNVLVT---EDNVMK 520
Cdd:cd14009  72 EYCAGGDLSQYIRKRG-----------RLPEA--VARHFMQ---QLASGLKFLRSKNIIHRDLKPQNLLLStsgDDPVLK 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 521 IADFGLARDVHNLDYyKKTTNGRlPVkWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEELFKLLKEGHR 600
Cdd:cd14009 136 IADFGFARSLQPASM-AETLCGS-PL-YMAPEILQFQKYDAKADLWSVGAILFEMLV-GKPPFRGSNHVQLLRNIERSDA 211

                ....*
gi 13112048 601 MDKPA 605
Cdd:cd14009 212 VIPFP 216
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
366-635 3.86e-23

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: 99.54  E-value: 3.86e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAeaigidKDRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLG------ACTqggpL 439
Cdd:cd08217   8 IGKGSFGTVRKV------RRKSDGKILVWKEIDYGKMSEKEKQQLVSEVNILREL-KHPNIVRYYDrivdraNTT----L 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 440 YVLVEYAAKGNLREFL-RARRppgldysfDTCKPPEEQL--TFKDLVSCAYQVARGMEylASQKCIHRDLAARNVLVTED 516
Cdd:cd08217  77 YIVMEYCEGGDLAQLIkKCKK--------ENQYIPEEFIwkIFTQLLLALYECHNRSV--GGGKILHRDLKPANIFLDSD 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 517 NVMKIADFGLARDVHNLDYYKKTTNGRlPVkWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLgGSPYPGIPVEELFKLLK 596
Cdd:cd08217 147 NNVKLGDFGLARVLSHDSSFAKTYVGT-PY-YMSPELLNEQSYDEKSDIWSLGCLIYELCAL-HPPFQAANQLELAKKIK 223
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 13112048 597 EGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVED 635
Cdd:cd08217 224 EGKFPRIPSRYSSELNEVIKSMLNVDPDKRPSVEELLQL 262
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
364-592 7.79e-23

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: 99.98  E-value: 7.79e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVMAEAIGIDKdraakpvTVAVKMLKDDA--TDKDLSDLVSEMEMMKMIGKHKNIINLLgACTQGGP-LY 440
Cdd:cd05570   1 KVLGKGSFGKVMLAERKKTDE-------LYAIKVLKKEViiEDDDVECTMTEKRVLALANRHPFLTGLH-ACFQTEDrLY 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 441 VLVEYAAKGNLR-EFLRARRppgldysFDtckppEEQLTFKdlvscAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVM 519
Cdd:cd05570  73 FVMEYVNGGDLMfHIQRARR-------FT-----EERARFY-----AAEICLALQFLHERGIIYRDLKLDNVLLDAEGHI 135
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13112048 520 KIADFGLARDvhNLdYYKKTTN---GRLpvKWMAPEALFDRVYTHQSDVWSFGVLLWEiFTLGGSPYPGIPVEELF 592
Cdd:cd05570 136 KIADFGMCKE--GI-WGGNTTStfcGTP--DYIAPEILREQDYGFSVDWWALGVLLYE-MLAGQSPFEGDDEDELF 205
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
359-634 1.10e-22

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: 98.53  E-value: 1.10e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 359 RLTLGKPLGEGCFGQVVMAeaigidKDRAAKPVtVAVKMLKDDATDKDlsDLVSEMEMMKMIGKHKNIINLLGACTQGGP 438
Cdd:cd06608   7 IFELVEVIGEGTYGKVYKA------RHKKTGQL-AAIKIMDIIEDEEE--EIKLEINILRKFSNHPNIATFYGAFIKKDP 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 439 ------LYVLVEYAAKGNLREFLRARRPPGldysfdtcKP-PEEQLtfkdlvscAY---QVARGMEYLASQKCIHRDLAA 508
Cdd:cd06608  78 pggddqLWLVMEYCGGGSVTDLVKGLRKKG--------KRlKEEWI--------AYilrETLRGLAYLHENKVIHRDIKG 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 509 RNVLVTEDNVMKIADFGLARDVhnldyykKTTNGR------LPVkWMAPEAL-----FDRVYTHQSDVWSFGVLLWEIFT 577
Cdd:cd06608 142 QNILLTEEAEVKLVDFGVSAQL-------DSTLGRrntfigTPY-WMAPEVIacdqqPDASYDARCDVWSLGITAIELAD 213
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 13112048 578 lGGSPYPGI-PVEELFKLLKE-GHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVE 634
Cdd:cd06608 214 -GKPPLCDMhPMRALFKIPRNpPPTLKSPEKWSKEFNDFISECLIKNYEQRPFTEELLE 271
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
395-637 1.43e-22

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: 97.59  E-value: 1.43e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 395 VKMLKDDAtdkDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEYAAKGNLREFLRARRPPgldysfdtckppe 474
Cdd:cd14156  23 VKIYKNDV---DQHKIVREISLLQKL-SHPNIVRYLGICVKDEKLHPILEYVSGGCLEELLAREELP------------- 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 475 eqLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLV-TEDNVMK--IADFGLARDVhnldyykkttnGRLPVK---- 547
Cdd:cd14156  86 --LSWREKVELACDISRGMVYLHSKNIYHRDLNSKNCLIrVTPRGREavVTDFGLAREV-----------GEMPANdper 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 548 ---------WMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGHRmDKPANCTHDLYMIMREC 618
Cdd:cd14156 153 klslvgsafWMAPEMLRGEPYDRKVDVFSFGIVLCEILARIPADPEVLPRTGDFGLDVQAFK-EMVPGCPEPFLDLAASC 231
                       250
                ....*....|....*....
gi 13112048 619 WHAAPSQRPTFKQLVEDLD 637
Cdd:cd14156 232 CRMDAFKRPSFAELLDELE 250
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
364-639 1.52e-22

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: 97.78  E-value: 1.52e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVMAEAIGidkdraakpvTVAVKMLK-DDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGpLYVL 442
Cdd:cd14150   6 KRIGTGSFGTVFRGKWHG----------DVAVKILKvTEPTPEQLQAFKNEMQVLRKT-RHVNILLFMGFMTRPN-FAII 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 443 VEYAAKGNLREFLRArrppgLDYSFDTCKppeeqltfkdLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIA 522
Cdd:cd14150  74 TQWCEGSSLYRHLHV-----TETRFDTMQ----------LIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIG 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 523 DFGLARdvhnldyYKKTTNGRLPVK-------WMAPEALF---DRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPV-EEL 591
Cdd:cd14150 139 DFGLAT-------VKTRWSGSQQVEqpsgsilWMAPEVIRmqdTNPYSFQSDVYAYGVVLYELMS-GTLPYSNINNrDQI 210
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 13112048 592 FKLLKEGH---RMDK-PANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRV 639
Cdd:cd14150 211 IFMVGRGYlspDLSKlSSNCPKAMKRLLIDCLKFKREERPLFPQILVSIELL 262
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
362-604 1.91e-22

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: 98.84  E-value: 1.91e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 362 LGKPLGEGCFGQVVMAEAIGIDKdraakpvTVAVKMLKDDAT--DKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPL 439
Cdd:cd05619   9 LHKMLGKGSFGKVFLAELKGTNQ-------FFAIKALKKDVVlmDDDVECTMVEKRVLSLAWEHPFLTHLFCTFQTKENL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 440 YVLVEYAAKGNLReflrarrppgldYSFDTC-KPPEEQLTFKdlvscAYQVARGMEYLASQKCIHRDLAARNVLVTEDNV 518
Cdd:cd05619  82 FFVMEYLNGGDLM------------FHIQSChKFDLPRATFY-----AAEIICGLQFLHSKGIVYRDLKLDNILLDKDGH 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 519 MKIADFGLARDvhNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFtLGGSPYPGIPVEELFKLLkeg 598
Cdd:cd05619 145 IKIADFGMCKE--NMLGDAKTSTFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEML-IGQSPFHGQDEEELFQSI--- 218

                ....*.
gi 13112048 599 hRMDKP 604
Cdd:cd05619 219 -RMDNP 223
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
393-632 2.28e-22

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: 97.67  E-value: 2.28e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 393 VAVKMLKDDATDKDLSDLVsEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEYAAKGNLREFLRarrppgldysfdtckp 472
Cdd:cd14042  33 VAIKKVNKKRIDLTREVLK-ELKHMRDL-QHDNLTRFIGACVDPPNICILTEYCPKGSLQDILE---------------- 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 473 pEEQLTFKDL--VSCAYQVARGMEYL-ASQKCIHRDLAARNVLVTEDNVMKIADFGLA---------RDVHNldYYKKtt 540
Cdd:cd14042  95 -NEDIKLDWMfrYSLIHDIVKGMHYLhDSEIKSHGNLKSSNCVVDSRFVLKITDFGLHsfrsgqeppDDSHA--YYAK-- 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 541 ngRLpvkWMAPEALFDRVY----THQSDVWSFGVLLWEIFTLGGsPYpGIPVEELFK--LLKEGHRMD---------KPA 605
Cdd:cd14042 170 --LL---WTAPELLRDPNPpppgTQKGDVYSFGIILQEIATRQG-PF-YEEGPDLSPkeIIKKKVRNGekppfrpslDEL 242
                       250       260
                ....*....|....*....|....*..
gi 13112048 606 NCTHDLYMIMRECWHAAPSQRPTFKQL 632
Cdd:cd14042 243 ECPDEVLSLMQRCWAEDPEERPDFSTL 269
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
366-635 2.86e-22

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: 97.09  E-value: 2.86e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGqVVMAeaiGIDKDRAakpVTVAVKmlkdDATDKDLSD---LVSEMEMMKMIgKHKNIINLLGACTQGGPLYVL 442
Cdd:cd06624  16 LGKGTFG-VVYA---ARDLSTQ---VRIAIK----EIPERDSREvqpLHEEIALHSRL-SHKNIVQYLGSVSEDGFFKIF 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 443 VEYAAKGNLREFLRARRPPgldysfdtCKPPEEQLTFkdlvscaY--QVARGMEYLASQKCIHRDLAARNVLV-TEDNVM 519
Cdd:cd06624  84 MEQVPGGSLSALLRSKWGP--------LKDNENTIGY-------YtkQILEGLKYLHDNKIVHRDIKGDNVLVnTYSGVV 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 520 KIADFGLARDVHNLDYYKKTTNGRLpvKWMAPEALfD---RVYTHQSDVWSFGVLLWEIFTlGGSPY--PGIPVEELFKL 594
Cdd:cd06624 149 KISDFGTSKRLAGINPCTETFTGTL--QYMAPEVI-DkgqRGYGPPADIWSLGCTIIEMAT-GKPPFieLGEPQAAMFKV 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 13112048 595 LKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVED 635
Cdd:cd06624 225 GMFKIHPEIPESLSEEAKSFILRCFEPDPDKRATASDLLQD 265
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
360-638 3.28e-22

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: 97.03  E-value: 3.28e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 360 LTLGKPLGEGCFGQVVMAEAIGidkdraakpvTVAVKMLK-DDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGgP 438
Cdd:cd14063   2 LEIKEVIGKGRFGRVHRGRWHG----------DVAIKLLNiDYLNEEQLEAFKEEVAAYKNT-RHDNLVLFMGACMDP-P 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 439 LYVLVEYAAKGN-LREFLRARRppgldysfdtckppeEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVtEDN 517
Cdd:cd14063  70 HLAIVTSLCKGRtLYSLIHERK---------------EKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFL-ENG 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 518 VMKIADFGLArDVHNLDYYKKTTNG-RLPVKW---MAPEAL----FDRV------YTHQSDVWSFGVLLWEIFTlGGSPY 583
Cdd:cd14063 134 RVVITDFGLF-SLSGLLQPGRREDTlVIPNGWlcyLAPEIIralsPDLDfeeslpFTKASDVYAFGTVWYELLA-GRWPF 211
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 13112048 584 PGIPVEELFKLLKEGHRMdKPANCT--HDLYMIMRECWHAAPSQRPTFKQLVEDLDR 638
Cdd:cd14063 212 KEQPAESIIWQVGCGKKQ-SLSQLDigREVKDILMQCWAYDPEKRPTFSDLLRMLER 267
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
364-634 3.64e-22

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: 96.42  E-value: 3.64e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVMAEaigiDKDRAAKPVTVAVKMLKDDATDKDLSDlvSEMEMMKMIgKHKNIINLLGACTQGGPLYVLV 443
Cdd:cd08218   6 KKIGEGSFGKALLVK----SKEDGKQYVIKEINISKMSPKEREESR--KEVAVLSKM-KHPNIVQYQESFEENGNLYIVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 444 EYAAKGNLREFLRARRppGLDYsfdtckpPEEQLtfkdlVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIAD 523
Cdd:cd08218  79 DYCDGGDLYKRINAQR--GVLF-------PEDQI-----LDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGD 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 524 FGLARDVHNLDYYKKTTNGRlPVkWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKeGHRMDK 603
Cdd:cd08218 145 FGIARVLNSTVELARTCIGT-PY-YLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFEAGNMKNLVLKIIR-GSYPPV 221
                       250       260       270
                ....*....|....*....|....*....|.
gi 13112048 604 PANCTHDLYMIMRECWHAAPSQRPTFKQLVE 634
Cdd:cd08218 222 PSRYSYDLRSLVSQLFKRNPRDRPSINSILE 252
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
423-637 5.79e-22

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: 95.67  E-value: 5.79e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 423 HKNIINLLGACTQGGPLYVLV-EYAAKGNLREFLRARRPPgLDysfdtckpPEEQLTFkdlvscAYQVARGMEYL--ASQ 499
Cdd:cd14064  50 HPCVIQFVGACLDDPSQFAIVtQYVSGGSLFSLLHEQKRV-ID--------LQSKLII------AVDVAKGMEYLhnLTQ 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 500 KCIHRDLAARNVLVTEDNVMKIADFGLARDVHNLDYYKKTTN-GRLpvKWMAPEaLFDRV--YTHQSDVWSFGVLLWEIF 576
Cdd:cd14064 115 PIIHRDLNSHNILLYEDGHAVVADFGESRFLQSLDEDNMTKQpGNL--RWMAPE-VFTQCtrYSIKADVFSYALCLWELL 191
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13112048 577 TlGGSPY----PGIPVEELfkllkEGHRMDKPANCT---HDLYMIMReCWHAAPSQRPTFKQLVEDLD 637
Cdd:cd14064 192 T-GEIPFahlkPAAAAADM-----AYHHIRPPIGYSipkPISSLLMR-GWNAEPESRPSFVEIVALLE 252
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
362-632 8.84e-22

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: 95.50  E-value: 8.84e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 362 LGKPLGEGCFGQVVMAeaigIDKDRAAKpvtVAVKMLKDDATDKDLSDLVS----EMEMMKMIgKHKNIINLLGACTQGG 437
Cdd:cd06625   4 QGKLLGQGAFGQVYLC----YDADTGRE---LAVKQVEIDPINTEASKEVKalecEIQLLKNL-QHERIVQYYGCLQDEK 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 438 PLYVLVEYAAKGNLREFLRARRPpgldysfdtckppeeqLTfkDLVSCAY--QVARGMEYLASQKCIHRDLAARNVLVTE 515
Cdd:cd06625  76 SLSIFMEYMPGGSVKDEIKAYGA----------------LT--ENVTRKYtrQILEGLAYLHSNMIVHRDIKGANILRDS 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 516 DNVMKIADFGLARDVHNLdyykKTTNGRLPVK----WMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEEL 591
Cdd:cd06625 138 NGNVKLGDFGASKRLQTI----CSSTGMKSVTgtpyWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPWAEFEPMAAI 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 13112048 592 FKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQL 632
Cdd:cd06625 214 FKIATQPTNPQLPPHVSEDARDFLSLIFVRNKKQRPSAEEL 254
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
361-600 2.10e-21

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: 94.29  E-value: 2.10e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 361 TLGKPLGEGCFGQVVMAeaigidKDRAAKpVTVAVKML-KDDATDKDLSD-LVSEMEMMKMIgKHKNIINLLGACTQGGP 438
Cdd:cd14162   3 IVGKTLGHGSYAVVKKA------YSTKHK-CKVAIKIVsKKKAPEDYLQKfLPREIEVIKGL-KHPNLICFYEAIETTSR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 439 LYVLVEYAAKGNLREFLRARRppgldysfdtcKPPEEQ--LTFKDLVScayqvarGMEYLASQKCIHRDLAARNVLVTED 516
Cdd:cd14162  75 VYIIMELAENGDLLDYIRKNG-----------ALPEPQarRWFRQLVA-------GVEYCHSKGVVHRDLKCENLLLDKN 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 517 NVMKIADFGLARDVHnldyykKTTNGRLPVK--------WMAPEALFDRVYTHQ-SDVWSFGVLLweiFTL--GGSPYPG 585
Cdd:cd14162 137 NNLKITDFGFARGVM------KTKDGKPKLSetycgsyaYASPEILRGIPYDPFlSDIWSMGVVL---YTMvyGRLPFDD 207
                       250
                ....*....|....*
gi 13112048 586 ipvEELFKLLKEGHR 600
Cdd:cd14162 208 ---SNLKVLLKQVQR 219
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
353-637 3.25e-21

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: 94.33  E-value: 3.25e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 353 WELSRARLTLGKPLGEGCFGQVVMAEAIGidkdraakpvTVAVKMLK-DDATDKDLSDLVSEMEMMKMIgKHKNIINLLG 431
Cdd:cd14149   7 WEIEASEVMLSTRIGSGSFGTVYKGKWHG----------DVAVKILKvVDPTPEQFQAFRNEVAVLRKT-RHVNILLFMG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 432 ACTQGGpLYVLVEYAAKGNLREFLRARrppgldysfdtckppEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNV 511
Cdd:cd14149  76 YMTKDN-LAIVTQWCEGSSLYKHLHVQ---------------ETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNI 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 512 LVTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALF---DRVYTHQSDVWSFGVLLWEIFTlGGSPYP---- 584
Cdd:cd14149 140 FLHEGLTVKIGDFGLATVKSRWSGSQQVEQPTGSILWMAPEVIRmqdNNPFSFQSDVYSYGIVLYELMT-GELPYShinn 218
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13112048 585 ----------GIPVEELFKLLKeghrmdkpaNCTHDLYMIMRECWHAAPSQRPTFKQLVEDLD 637
Cdd:cd14149 219 rdqiifmvgrGYASPDLSKLYK---------NCPKAMKRLVADCIKKVKEERPLFPQILSSIE 272
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
361-628 3.54e-21

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: 93.87  E-value: 3.54e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 361 TLGKPLGEGCFGQVVMAEAIGIDKdraakpvTVAVKMLK-DDATD-KDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGP 438
Cdd:cd08224   3 EIEKKIGKGQFSVVYRARCLLDGR-------LVALKKVQiFEMMDaKARQDCLKEIDLLQQL-NHPNIIKYLASFIENNE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 439 LYVLVEYAAKGNLREFLRARRPPGldysfdtcKPPEEQLTFKDLVscayQVARGMEYLASQKCIHRDLAARNVLVTEDNV 518
Cdd:cd08224  75 LNIVLELADAGDLSRLIKHFKKQK--------RLIPERTIWKYFV----QLCSALEHMHSKRIMHRDIKPANVFITANGV 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 519 MKIADFGLARdvhnldYYK-KTTNGRLPVK---WMAPEALFDRVYTHQSDVWSFGVLLWEIFTLgGSPY--PGIPVEELF 592
Cdd:cd08224 143 VKLGDLGLGR------FFSsKTTAAHSLVGtpyYMSPERIREQGYDFKSDIWSLGCLLYEMAAL-QSPFygEKMNLYSLC 215
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 13112048 593 KLLKEGHRMDKPANC-THDLYMIMRECWHAAPSQRPT 628
Cdd:cd08224 216 KKIEKCEYPPLPADLySQELRDLVAACIQPDPEKRPD 252
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
366-634 3.56e-21

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: 93.96  E-value: 3.56e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMaeaiGIDKDRAAkpvTVAVKMLKDDATDKDLSDLVSEMEMMKMIGKhKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd06640  12 IGKGSFGEVFK----GIDNRTQQ---VVAIKIIDLEEAEDEIEDIQQEITVLSQCDS-PYVTKYYGSYLKGTKLWIIMEY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLREFLRArrppgldysfdtckPPEEQLTFKDLVScayQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFG 525
Cdd:cd06640  84 LGGGSALDLLRA--------------GPFDEFQIATMLK---EILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFG 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 526 LARDVHNLDYYKKTTNGRlPVkWMAPEALFDRVYTHQSDVWSFGVLLWEIfTLGGSPYPGI-PVEELFKLLKeghrmDKP 604
Cdd:cd06640 147 VAGQLTDTQIKRNTFVGT-PF-WMAPEVIQQSAYDSKADIWSLGITAIEL-AKGEPPNSDMhPMRVLFLIPK-----NNP 218
                       250       260       270
                ....*....|....*....|....*....|....
gi 13112048 605 ANCTHDLYMIMRE----CWHAAPSQRPTFKQLVE 634
Cdd:cd06640 219 PTLVGDFSKPFKEfidaCLNKDPSFRPTAKELLK 252
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
366-639 4.98e-21

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: 93.33  E-value: 4.98e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVmaeaigidKDRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd14664   1 IGRGGAGTVY--------KGVMPNGTLVAVKRLKGEGTQGGDHGFQAEIQTLGMI-RHRNIVRLRGYCSNPTTNLLVYEY 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLREFLRARRPPGldysfdtckppeEQLTFKDLVSCAYQVARGMEYL---ASQKCIHRDLAARNVLVTEDNVMKIA 522
Cdd:cd14664  72 MPNGSLGELLHSRPESQ------------PPLDWETRQRIALGSARGLAYLhhdCSPLIIHRDVKSNNILLDEEFEAHVA 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 523 DFGLARdVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEELFKLLKEGHRMD 602
Cdd:cd14664 140 DFGLAK-LMDDKDSHVMSSVAGSYGYIAPEYAYTGKVSEKSDVYSYGVVLLELIT-GKRPFDEAFLDDGVDIVDWVRGLL 217
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 13112048 603 KPANCTH----DL--YMIMRE----------CWHAAPSQRPTFKQLVEDLDRV 639
Cdd:cd14664 218 EEKKVEAlvdpDLqgVYKLEEveqvfqvallCTQSSPMERPTMREVVRMLEGD 270
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
362-635 4.98e-21

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


Pssm-ID: 270974 [Multi-domain]  Cd Length: 253  Bit Score: 92.97  E-value: 4.98e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 362 LGKPLGEGCFGQVVMAEAIGIDKDraakpvtVAVKML-KDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLY 440
Cdd:cd14072   4 LLKTIGKGNFAKVKLARHVLTGRE-------VAIKIIdKTQLNPSSLQKLFREVRIMKIL-NHPNIVKLFEVIETEKTLY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 441 VLVEYAAKGNLREFLRARrppgldysfDTCKPPEEQLTFKDLVScayqvarGMEYLASQKCIHRDLAARNVLVTEDNVMK 520
Cdd:cd14072  76 LVMEYASGGEVFDYLVAH---------GRMKEKEARAKFRQIVS-------AVQYCHQKRIVHRDLKAENLLLDADMNIK 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 521 IADFGLARDV---HNLDyykkTTNGRLPvkWMAPEALFDRVYTH-QSDVWSFGVLLWEIFTlGGSPYPGIPVEELF-KLL 595
Cdd:cd14072 140 IADFGFSNEFtpgNKLD----TFCGSPP--YAAPELFQGKKYDGpEVDVWSLGVILYTLVS-GSLPFDGQNLKELReRVL 212
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 13112048 596 KEGHRMdkPANCTHDLYMIMRECWHAAPSQRPTFKQLVED 635
Cdd:cd14072 213 RGKYRI--PFYMSTDCENLLKKFLVLNPSKRGTLEQIMKD 250
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
392-632 6.09e-21

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: 93.31  E-value: 6.09e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 392 TVAVKMLKDDATDKDLSDLVSEMEMMK--MIGKHKNIINLLGACTQGGPLYVLVEYAAKGNLREFLRArrppgldysfdt 469
Cdd:cd06917  28 VVALKVLNLDTDDDDVSDIQKEVALLSqlKLGQPKNIIKYYGSYLKGPSLWIIMDYCEGGSIRTLMRA------------ 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 470 cKPPEEQltFKDLVSCAYQVArgMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARDVhNLDYYKKTTNGRLPVkWM 549
Cdd:cd06917  96 -GPIAER--YIAVIMREVLVA--LKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASL-NQNSSKRSTFVGTPY-WM 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 550 APEALFD-RVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEELFKLLKEghrmDKPANCTHDLY-MIMRE----CWHAAP 623
Cdd:cd06917 169 APEVITEgKYYDTKADIWSLGITTYEMAT-GNPPYSDVDALRAVMLIPK----SKPPRLEGNGYsPLLKEfvaaCLDEEP 243

                ....*....
gi 13112048 624 SQRPTFKQL 632
Cdd:cd06917 244 KDRLSADEL 252
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
366-636 7.97e-21

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


Pssm-ID: 270898 [Multi-domain]  Cd Length: 273  Bit Score: 92.74  E-value: 7.97e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIgIDKdraakpVTVAVKMLKddATDKDLSdlvSEMEMM--KMIGK--HKNIINLLGACTQGGPLYV 441
Cdd:cd13996  14 LGSGGFGSVYKVRNK-VDG------VTYAIKKIR--LTEKSSA---SEKVLRevKALAKlnHPNIVRYYTAWVEEPPLYI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 442 LVEYAAKGNLREFLRARRppGLDYSFDTCkppeeqltfkdLVSCAYQVARGMEYLASQKCIHRDLAARNVLVT-EDNVMK 520
Cdd:cd13996  82 QMELCEGGTLRDWIDRRN--SSSKNDRKL-----------ALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDnDDLQVK 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 521 IADFGLARDVHNLDYYKKTTNGRLP------------VKWMAPEALFDRVYTHQSDVWSFGVLLWEIFtlggspYPGIPV 588
Cdd:cd13996 149 IGDFGLATSIGNQKRELNNLNNNNNgntsnnsvgigtPLYASPEQLDGENYNEKADIYSLGIILFEML------HPFKTA 222
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 13112048 589 EELFKLLKEGHRMDKPANCTHDLY---MIMRECWHAAPSQRPTFKQLVEDL 636
Cdd:cd13996 223 MERSTILTDLRNGILPESFKAKHPkeaDLIQSLLSKNPEERPSAEQLLRSL 273
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
151-245 1.01e-20

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409442  Cd Length: 92  Bit Score: 87.22  E-value: 1.01e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 151 PYWTRPERMDKKLLAVPAANTVRFRCPAAGNPTPSISWLKNGREFRgEHRIGgiKLRHQQWSLVMESVVPSDRGNYTCVV 230
Cdd:cd05856   1 PRFTQPAKMRRRVIARPVGSSVRLKCVASGNPRPDITWLKDNKPLT-PPEIG--ENKKKKWTLSLKNLKPEDSGKYTCHV 77
                        90
                ....*....|....*
gi 13112048 231 ENKFGSIRQTYTLDV 245
Cdd:cd05856  78 SNRAGEINATYKVDV 92
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
366-632 1.20e-20

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: 91.93  E-value: 1.20e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVvmAEAIGIDKDRaakpvTVAVKMLKDDATDK---DLSDLVSEMEMMKMIgKHKNIINLLGACT--QGGPLY 440
Cdd:cd14119   1 LGEGSYGKV--KEVLDTETLC-----RRAVKILKKRKLRRipnGEANVKREIQILRRL-NHRNVIKLVDVLYneEKQKLY 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 441 VLVEYAAkGNLREFLRA----RRPPGldysfdtckppEEQLTFKDLVscayqvaRGMEYLASQKCIHRDLAARNVLVTED 516
Cdd:cd14119  73 MVMEYCV-GGLQEMLDSapdkRLPIW-----------QAHGYFVQLI-------DGLEYLHSQGIIHKDIKPGNLLLTTD 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 517 NVMKIADFGLARDVHNL--DYYKKTTNGRlPvKWMAPE-ALFDRVYT-HQSDVWSFGVLLWEIFTlGGSPYPGIPVEELF 592
Cdd:cd14119 134 GTLKISDFGVAEALDLFaeDDTCTTSQGS-P-AFQPPEiANGQDSFSgFKVDIWSAGVTLYNMTT-GKYPFEGDNIYKLF 210
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 13112048 593 KLLKEGhRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQL 632
Cdd:cd14119 211 ENIGKG-EYTIPDDVDPDLQDLLRGMLEKDPEKRFTIEQI 249
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
362-634 1.30e-20

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: 91.94  E-value: 1.30e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 362 LGKPLGEGCFGQVVMAeaigidKDRAAKPVtVAVKMLKDDATDKDLSD--LVSEMEMMKMIgKHKNIINLLGACTQGGPL 439
Cdd:cd14116   9 IGRPLGKGKFGNVYLA------REKQSKFI-LALKVLFKAQLEKAGVEhqLRREVEIQSHL-RHPNILRLYGYFHDATRV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 440 YVLVEYAAKGNL-REFLRARRppgldysfdtckppeeqltFKDLVSCAY--QVARGMEYLASQKCIHRDLAARNVLVTED 516
Cdd:cd14116  81 YLILEYAPLGTVyRELQKLSK-------------------FDEQRTATYitELANALSYCHSKRVIHRDIKPENLLLGSA 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 517 NVMKIADFGLArdVHNLDYYKKTTNGRLpvKWMAPEALFDRVYTHQSDVWSFGVLLWEiFTLGGSPYPGIPVEELFKLLK 596
Cdd:cd14116 142 GELKIADFGWS--VHAPSSRRTTLCGTL--DYLPPEMIEGRMHDEKVDLWSLGVLCYE-FLVGKPPFEANTYQETYKRIS 216
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 13112048 597 EgHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVE 634
Cdd:cd14116 217 R-VEFTFPDFVTEGARDLISRLLKHNPSQRPMLREVLE 253
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
366-634 1.90e-20

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: 92.06  E-value: 1.90e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMaeaiGIDKdRAAKpvTVAVKMLKDDATDKDLSDLVSEMEMMKMIGKhKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd06641  12 IGKGSFGEVFK----GIDN-RTQK--VVAIKIIDLEEAEDEIEDIQQEITVLSQCDS-PYVTKYYGSYLKDTKLWIIMEY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLREFLRarrpPGldysfdtckPPEEqltfKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFG 525
Cdd:cd06641  84 LGGGSALDLLE----PG---------PLDE----TQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFG 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 526 LARDVHNLDYYKKTTNGRlPVkWMAPEALFDRVYTHQSDVWSFGVLLWEIfTLGGSPYPGI-PVEELFKLLKEGHRMDKp 604
Cdd:cd06641 147 VAGQLTDTQIKRN*FVGT-PF-WMAPEVIKQSAYDSKADIWSLGITAIEL-ARGEPPHSELhPMKVLFLIPKNNPPTLE- 222
                       250       260       270
                ....*....|....*....|....*....|
gi 13112048 605 ANCTHDLYMIMRECWHAAPSQRPTFKQLVE 634
Cdd:cd06641 223 GNYSKPLKEFVEACLNKEPSFRPTAKELLK 252
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
360-582 3.73e-20

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: 91.49  E-value: 3.73e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 360 LTLGKPLGEGCFGQVVMAEAIGIDKdraakpvTVAVKMLK--DDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGG 437
Cdd:cd05580   3 FEFLKTLGTGSFGRVRLVKHKDSGK-------YYALKILKkaKIIKLKQVEHVLNEKRILSEV-RHPFIVNLLGSFQDDR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 438 PLYVLVEYAAKGNLREFLRARRppgldysfdtcKPPEEQLTFKdlvscAYQVARGMEYLASQKCIHRDLAARNVLVTEDN 517
Cdd:cd05580  75 NLYMVMEYVPGGELFSLLRRSG-----------RFPNDVAKFY-----AAEVVLALEYLHSLDIVYRDLKPENLLLDSDG 138
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13112048 518 VMKIADFGLARDVHNLDYykkTTNGRlPvKWMAPEALFDRVYTHQSDVWSFGVLLWEIftLGGSP 582
Cdd:cd05580 139 HIKITDFGFAKRVKDRTY---TLCGT-P-EYLAPEIILSKGHGKAVDWWALGILIYEM--LAGYP 196
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
358-627 3.78e-20

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: 90.86  E-value: 3.78e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 358 ARLTLGKPLGEGCFGQVVMAEAIGIDKDRAAKPVTVAVKMlkdDAtdKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGG 437
Cdd:cd08228   2 ANFQIEKKIGRGQFSEVYRATCLLDRKPVALKKVQIFEMM---DA--KARQDCVKEIDLLKQL-NHPNVIKYLDSFIEDN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 438 PLYVLVEYAAKGNLREFLRarrppgldYSFDTCKPPEEQLTFKDLVscayQVARGMEYLASQKCIHRDLAARNVLVTEDN 517
Cdd:cd08228  76 ELNIVLELADAGDLSQMIK--------YFKKQKRLIPERTVWKYFV----QLCSAVEHMHSRRVMHRDIKPANVFITATG 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 518 VMKIADFGLARdvhnlDYYKKTTNGRLPVK---WMAPEALFDRVYTHQSDVWSFGVLLWEIFTLgGSPYPGIPVeELFKL 594
Cdd:cd08228 144 VVKLGDLGLGR-----FFSSKTTAAHSLVGtpyYMSPERIHENGYNFKSDIWSLGCLLYEMAAL-QSPFYGDKM-NLFSL 216
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 13112048 595 LKEGHRMDKPANCTHDLYMIMRE----CWHAAPSQRP 627
Cdd:cd08228 217 CQKIEQCDYPPLPTEHYSEKLRElvsmCIYPDPDQRP 253
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
393-591 3.90e-20

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: 90.43  E-value: 3.90e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 393 VAVK-MLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEYAAKGNLREFLRARRppgldysfdtcK 471
Cdd:cd14121  24 VAVKcVSKSSLNKASTENLLTEIELLKKL-KHPHIVELKDFQWDEEHIYLIMEYCSGGDLSRFIRSRR-----------T 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 472 PPEEQLTfkdlvSCAYQVARGMEYLASQKCIHRDLAARNVLVT--EDNVMKIADFGLARDVHNLDYyKKTTNGRlPVkWM 549
Cdd:cd14121  92 LPESTVR-----RFLQQLASALQFLREHNISHMDLKPQNLLLSsrYNPVLKLADFGFAQHLKPNDE-AHSLRGS-PL-YM 163
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 13112048 550 APEALFDRVYTHQSDVWSFGVLLWEIFtLGGSPYPGIPVEEL 591
Cdd:cd14121 164 APEMILKKKYDARVDLWSVGVILYECL-FGRAPFASRSFEEL 204
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
366-626 4.38e-20

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: 91.98  E-value: 4.38e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKdraakpvTVAVKMLKDDAT--DKDLSDLVSEMEMMKMIGKhKNIINLLGACTQG-GPLYVL 442
Cdd:cd05616   8 LGKGSFGKVMLAERKGTDE-------LYAVKILKKDVViqDDDVECTMVEKRVLALSGK-PPFLTQLHSCFQTmDRLYFV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 443 VEYAAKGNL----REFLRARRPPGLDYsfdtckppeeqltfkdlvscAYQVARGMEYLASQKCIHRDLAARNVLVTEDNV 518
Cdd:cd05616  80 MEYVNGGDLmyhiQQVGRFKEPHAVFY--------------------AAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGH 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 519 MKIADFGLARDvHNLDYYKKTTNGRLPvKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEELFKLLKEg 598
Cdd:cd05616 140 IKIADFGMCKE-NIWDGVTTKTFCGTP-DYIAPEIIAYQPYGKSVDWWAFGVLLYEMLA-GQAPFEGEDEDELFQSIME- 215
                       250       260
                ....*....|....*....|....*...
gi 13112048 599 HRMDKPANCTHDLYMIMRECWHAAPSQR 626
Cdd:cd05616 216 HNVAYPKSMSKEAVAICKGLMTKHPGKR 243
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
363-582 5.49e-20

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: 90.74  E-value: 5.49e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 363 GKPLGEGCFGQVVMAEAIGIDKdraakpvTVAVKMLkddatDKDL------SDLVS-EMEMMKMIgKHKNIINLLGACTQ 435
Cdd:cd05581   6 GKPLGEGSYSTVVLAKEKETGK-------EYAIKVL-----DKRHiikekkVKYVTiEKEVLSRL-AHPGIVKLYYTFQD 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 436 GGPLYVLVEYAAKGNLREFLRARrppgldYSFDtckppeeqltFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTE 515
Cdd:cd05581  73 ESKLYFVLEYAPNGDLLEYIRKY------GSLD----------EKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDE 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 516 DNVMKIADFGLARDVHNLD---------------YYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlgG 580
Cdd:cd05581 137 DMHIKITDFGTAKVLGPDSspestkgdadsqiayNQARAASFVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLT--G 214

                ..
gi 13112048 581 SP 582
Cdd:cd05581 215 KP 216
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
366-634 5.85e-20

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: 90.50  E-value: 5.85e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMaeaiGIDKDraAKPVtVAVKMLKDDATDKDLSDLVSEMEMMKMIGKhKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd06642  12 IGKGSFGEVYK----GIDNR--TKEV-VAIKIIDLEEAEDEIEDIQQEITVLSQCDS-PYITRYYGSYLKGTKLWIIMEY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLREFLRarrpPGldysfdtckPPEEQLtfkdLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFG 525
Cdd:cd06642  84 LGGGSALDLLK----PG---------PLEETY----IATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFG 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 526 LARDVHNLDYYKKTTNGRlPVkWMAPEALFDRVYTHQSDVWSFGVLLWEIfTLGGSPYPGI-PVEELFkLLKEGHRMDKP 604
Cdd:cd06642 147 VAGQLTDTQIKRNTFVGT-PF-WMAPEVIKQSAYDFKADIWSLGITAIEL-AKGEPPNSDLhPMRVLF-LIPKNSPPTLE 222
                       250       260       270
                ....*....|....*....|....*....|
gi 13112048 605 ANCTHDLYMIMRECWHAAPSQRPTFKQLVE 634
Cdd:cd06642 223 GQHSKPFKEFVEACLNKDPRFRPTAKELLK 252
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
359-634 5.85e-20

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: 90.07  E-value: 5.85e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 359 RLTLGKPLGEGCFGQVVMAEAIGIDKDRAAK--PVTVAVKMLKDDATDKdlsdlvsEMEMMKMIgKHKNIINLLGACTQG 436
Cdd:cd14188   2 RYCRGKVLGKGGFAKCYEMTDLTTNKVYAAKiiPHSRVSKPHQREKIDK-------EIELHRIL-HHKHVVQFYHYFEDK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 437 GPLYVLVEYAAKGNLREFLRARRppgldysfdTCKPPEEQLTFKDLVScayqvarGMEYLASQKCIHRDLAARNVLVTED 516
Cdd:cd14188  74 ENIYILLEYCSRRSMAHILKARK---------VLTEPEVRYYLRQIVS-------GLKYLHEQEILHRDLKLGNFFINEN 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 517 NVMKIADFGLARDVHNLDYYKKTTNGrlPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFtLGGSPYPGIPVEELFKLLK 596
Cdd:cd14188 138 MELKVGDFGLAARLEPLEHRRRTICG--TPNYLSPEVLNKQGHGCESDIWALGCVMYTML-LGRPPFETTNLKETYRCIR 214
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 13112048 597 EGhRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVE 634
Cdd:cd14188 215 EA-RYSLPSSLLAPAKHLIASMLSKNPEDRPSLDEIIR 251
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
366-585 5.96e-20

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: 90.70  E-value: 5.96e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKdraakpvTVAVKMLKDDaTDKDLSDLVS--EMEMMKMIgKHKNIINLLGACT------QGG 437
Cdd:cd07840   7 IGEGTYGQVYKARNKKTGE-------LVALKKIRME-NEKEGFPITAirEIKLLQKL-DHPNVVRLKEIVTskgsakYKG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 438 PLYVLVEYAA---KGNLREflrarrppgldysfdtckpPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVT 514
Cdd:cd07840  78 SIYMVFEYMDhdlTGLLDN-------------------PEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILIN 138
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13112048 515 EDNVMKIADFGLAR---DVHNLDYykktTNGRLPVKWMAPEALF-DRVYTHQSDVWSFGVLLWEIFTlGGSPYPG 585
Cdd:cd07840 139 NDGVLKLADFGLARpytKENNADY----TNRVITLWYRPPELLLgATRYGPEVDMWSVGCILAELFT-GKPIFQG 208
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
352-604 5.97e-20

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: 90.46  E-value: 5.97e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 352 KWELSRARLtlgkpLGEGCFGQVVMAeaigidKDRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLG 431
Cdd:cd14202   1 KFEFSRKDL-----IGHGAFAVVFKG------RHKEKHDLEVAVKCINKKNLAKSQTLLGKEIKILKEL-KHENIVALYD 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 432 ACTQGGPLYVLVEYAAKGNLREFLRARRPPGLDysfdtckppeeqlTFKDLVScayQVARGMEYLASQKCIHRDLAARNV 511
Cdd:cd14202  69 FQEIANSVYLVMEYCNGGDLADYLHTMRTLSED-------------TIRLFLQ---QIAGAMKMLHSKGIIHRDLKPQNI 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 512 LVT--------EDNV-MKIADFGLARDVHNlDYYKKTTNGRlPVkWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSP 582
Cdd:cd14202 133 LLSysggrksnPNNIrIKIADFGFARYLQN-NMMAATLCGS-PM-YMAPEVIMSQHYDAKADLWSIGTIIYQCLT-GKAP 208
                       250       260
                ....*....|....*....|..
gi 13112048 583 YPGIPVEELfKLLKEGHRMDKP 604
Cdd:cd14202 209 FQASSPQDL-RLFYEKNKSLSP 229
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
366-635 6.15e-20

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: 90.06  E-value: 6.15e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEaigiDKDRAAKpVTVAVKMLK---DDATDKDLSD-LVSEMEMMKMIgKHKNIINLLGACTQGGPLYV 441
Cdd:cd13994   1 IGKGATSVVRIVT----KKNPRSG-VLYAVKEYRrrdDESKRKDYVKrLTSEYIISSKL-HHPNIVKVLDLCQDLHGKWC 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 442 LV-EYAAKGNLREFLRARRPPGLDysfdtckppEEQLTFKdlvscayQVARGMEYLASQKCIHRDLAARNVLVTEDNVMK 520
Cdd:cd13994  75 LVmEYCPGGDLFTLIEKADSLSLE---------EKDCFFK-------QILRGVAYLHSHGIAHRDLKPENILLDEDGVLK 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 521 IADFGLARDVHNL-DYYKKTTN---GRLPvkWMAPEALFDRVYTHQS-DVWSFGVLLWEIFT------------LGGSPY 583
Cdd:cd13994 139 LTDFGTAEVFGMPaEKESPMSAglcGSEP--YMAPEVFTSGSYDGRAvDVWSCGIVLFALFTgrfpwrsakksdSAYKAY 216
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 13112048 584 PGIPVEelFKLLKEGHRMDKPANCTHDLYMIMrecwHAAPSQRPTFKQLVED 635
Cdd:cd13994 217 EKSGDF--TNGPYEPIENLLPSECRRLIYRML----HPDPEKRITIDEALND 262
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
364-628 9.03e-20

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: 89.26  E-value: 9.03e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVMAEAIGIDKDRAAKPVTVAvKMLKDDATDKDLSDLVSEMemmkmigKHKNIINLLGACTQGGPLYVLV 443
Cdd:cd08219   6 RVVGEGSFGRALLVQHVNSDQKYAMKEIRLP-KSSSAVEDSRKEAVLLAKM-------KHPNIVAFKESFEADGHLYIVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 444 EYAAKGNLREFLRARRppgldysfdtckppeEQLTFKDLVSCAY-QVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIA 522
Cdd:cd08219  78 EYCDGGDLMQKIKLQR---------------GKLFPEDTILQWFvQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLG 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 523 DFGLARDVHNLDYYKKTTNGRlPVkWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLgGSPYPGIPVEELFKLLKEGHRMD 602
Cdd:cd08219 143 DFGSARLLTSPGAYACTYVGT-PY-YVPPEIWENMPYNNKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQGSYKP 219
                       250       260
                ....*....|....*....|....*.
gi 13112048 603 KPANCTHDLYMIMRECWHAAPSQRPT 628
Cdd:cd08219 220 LPSHYSYELRSLIKQMFKRNPRSRPS 245
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
359-633 9.66e-20

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: 89.72  E-value: 9.66e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 359 RLTLGKPLGEGCFGQVVMAEAIgidkdraAKPVTVAVKMLKDDATD-KDLSDLVS-----EMEMMKMIGKHKNIINLLGA 432
Cdd:cd13993   1 RYQLISPIGEGAYGVVYLAVDL-------RTGRKYAIKCLYKSGPNsKDGNDFQKlpqlrEIDLHRRVSRHPNIITLHDV 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 433 CTQGGPLYVLVEYAAKGNLREFLRARRppgldysfdtckppEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVL 512
Cdd:cd13993  74 FETEVAIYIVLEYCPNGDLFEAITENR--------------IYVGKTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENIL 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 513 VTED-NVMKIADFGLA-RDVHNLDYykkttnGRLPVKWMAPEaLFDRV-------YTHQSDVWSFGVLLWEIfTLGGSPY 583
Cdd:cd13993 140 LSQDeGTVKLCDFGLAtTEKISMDF------GVGSEFYMAPE-CFDEVgrslkgyPCAAGDIWSLGIILLNL-TFGRNPW 211
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 13112048 584 PgIPVEE----LFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLV 633
Cdd:cd13993 212 K-IASESdpifYDYYLNSPNLFDVILPMSDDFYNLLRQIFTVNPNNRILLPELQ 264
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
359-640 1.59e-19

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: 89.40  E-value: 1.59e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 359 RLTLGKPLGEGCFGQVVMAEaigidkDRAAKPVTVAVKMLKDDATD-KDLSDLVSEMEMMKMIGK--HKNIINLLGACTQ 435
Cdd:cd14052   1 RFANVELIGSGEFSQVYKVS------ERVPTGKVYAVKKLKPNYAGaKDRLRRLEEVSILRELTLdgHDNIVQLIDSWEY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 436 GGPLYVLVEYAAKGNLREFLRAR-RPPGLDysfdtckppeEQLTFKDLVscayQVARGMEYLASQKCIHRDLAARNVLVT 514
Cdd:cd14052  75 HGHLYIQTELCENGSLDVFLSELgLLGRLD----------EFRVWKILV----ELSLGLRFIHDHHFVHLDLKPANVLIT 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 515 EDNVMKIADFGLARdvhnldyykkttngRLPV----------KWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYP 584
Cdd:cd14052 141 FEGTLKIGDFGMAT--------------VWPLirgieregdrEYIAPEILSEHMYDKPADIFSLGLILLEAAANVVLPDN 206
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 13112048 585 GIPveelFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQrPTFKQLVEDLDRVL 640
Cdd:cd14052 207 GDA----WQKLRSGDLSDAPRLSSTDLHSASSPSSNPPPDP-PNMPILSGSLDRVV 257
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
359-631 1.61e-19

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: 89.55  E-value: 1.61e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 359 RLTLGKPLGEGCFGQVVMAEaigiDKDRAAKpvtVAVKMLK--DDATDKDLSDLVS--EMEMMKMIgKHKNIINLLGACT 434
Cdd:cd07841   1 RYEKGKKLGEGTYAVVYKAR----DKETGRI---VAIKKIKlgERKEAKDGINFTAlrEIKLLQEL-KHPNIIGLLDVFG 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 435 QGGPLYVLVEYAAkGNLREFLRARRPPgldysfdtckppeeqLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVT 514
Cdd:cd07841  73 HKSNINLVFEFME-TDLEKVIKDKSIV---------------LTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIA 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 515 EDNVMKIADFGLARDVHNLDyYKKTTNgrLPVKWM-APEALFD-RVYTHQSDVWSFGVLLWE------------------ 574
Cdd:cd07841 137 SDGVLKLADFGLARSFGSPN-RKMTHQ--VVTRWYrAPELLFGaRHYGVGVDMWSVGCIFAElllrvpflpgdsdidqlg 213
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13112048 575 -IFTLGGSP-------------------YPGIPVEELFKllkeghrmdkpaNCTHDLYMIMRECWHAAPSQRPTFKQ 631
Cdd:cd07841 214 kIFEALGTPteenwpgvtslpdyvefkpFPPTPLKQIFP------------AASDDALDLLQRLLTLNPNKRITARQ 278
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
366-634 2.78e-19

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: 88.21  E-value: 2.78e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIgidkdraAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd14078  11 IGSGGFAKVKLATHI-------LTGEKVAIKIMDKKALGDDLPRVKTEIEALKNL-SHQHICRLYHVIETDNKIFMVLEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLREFLRARrppgldysfDTCKPPEEQLTFKDLVSCayqVArgmeYLASQKCIHRDLAARNVLVTEDNVMKIADFG 525
Cdd:cd14078  83 CPGGELFDYIVAK---------DRLSEDEARVFFRQIVSA---VA----YVHSQGYAHRDLKPENLLLDEDQNLKLIDFG 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 526 L-ARDVHNLDYYKKTTNGRLpvKWMAPEALFDRVYT-HQSDVWSFGVLLWEIFTlGGSPYPGIPVEELFKLLKEGhRMDK 603
Cdd:cd14078 147 LcAKPKGGMDHHLETCCGSP--AYAAPELIQGKPYIgSEADVWSMGVLLYALLC-GFLPFDDDNVMALYRKIQSG-KYEE 222
                       250       260       270
                ....*....|....*....|....*....|.
gi 13112048 604 PANCTHDLYMIMRECWHAAPSQRPTFKQLVE 634
Cdd:cd14078 223 PEWLSPSSKLLLDQMLQVDPKKRITVKELLN 253
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
366-598 3.37e-19

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: 87.57  E-value: 3.37e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKdraakpvTVAVKML-KDDATDKDLSDLV-SEMEMMKMIgKHKNIINLLGACTQGGPLYVLV 443
Cdd:cd05123   1 LGKGSFGKVLLVRKKDTGK-------LYAMKVLrKKEIIKRKEVEHTlNERNILERV-NHPFIVKLHYAFQTEEKLYLVL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 444 EYAAKGNLREFLRARRppgldySFdtckpPEEQLTFkdlvsCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIAD 523
Cdd:cd05123  73 DYVPGGELFSHLSKEG------RF-----PEERARF-----YAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTD 136
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13112048 524 FGLARDVHNLDYYKKTTNGRLPvkWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEELFKLLKEG 598
Cdd:cd05123 137 FGLAKELSSDGDRTYTFCGTPE--YLAPEVLLGKGYGKAVDWWSLGVLLYEMLT-GKPPFYAENRKEIYEKILKS 208
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
357-634 3.66e-19

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: 88.22  E-value: 3.66e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 357 RARLTLGKPLGEGCFGQVVMAeaigIDKDRAAKpvtVAVKMLKDD-------ATDKDLSDLVSEMEMMKMIgKHKNIINL 429
Cdd:cd14084   5 RKKYIMSRTLGSGACGEVKLA----YDKSTCKK---VAIKIINKRkftigsrREINKPRNIETEIEILKKL-SHPCIIKI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 430 LGACTQGGPLYVLVEYAAKGNLreFLRARRPPGLdySFDTCKppeeqLTFkdlvscaYQVARGMEYLASQKCIHRDLAAR 509
Cdd:cd14084  77 EDFFDAEDDYYIVLELMEGGEL--FDRVVSNKRL--KEAICK-----LYF-------YQMLLAVKYLHSNGIIHRDLKPE 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 510 NVLVT---EDNVMKIADFGLARDVHNlDYYKKTTNGrlPVKWMAPEAL--FDRV-YTHQSDVWSFGVLLWeiFTLGGSP- 582
Cdd:cd14084 141 NVLLSsqeEECLIKITDFGLSKILGE-TSLMKTLCG--TPTYLAPEVLrsFGTEgYTRAVDCWSLGVILF--ICLSGYPp 215
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 13112048 583 ----YPGIPVEElfKLLKEGHRMDKPA--NCTHDLYMIMRECWHAAPSQRPTFKQLVE 634
Cdd:cd14084 216 fseeYTQMSLKE--QILSGKYTFIPKAwkNVSEEAKDLVKKMLVVDPSRRPSIEEALE 271
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
366-637 4.42e-19

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: 87.31  E-value: 4.42e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDkdraakpvtVAVKMLKDDATDKDLSdlvSEMEMMKMIgKHKNIINLLGACTQggPLYVLVEY 445
Cdd:cd14068   2 LGDGGFGSVYRAVYRGED---------VAVKIFNKHTSFRLLR---QELVVLSHL-HHPSLVALLAAGTA--PRMLVMEL 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLREFLRARRPpgldysfdtckppeeQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLV-----TEDNVMK 520
Cdd:cd14068  67 APKGSLDALLQQDNA---------------SLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLftlypNCAIIAK 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 521 IADFGLARdvHNLDYYKKTTNGRLPVKwmAPE-ALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGH 599
Cdd:cd14068 132 IADYGIAQ--YCCRMGIKTSEGTPGFR--APEvARGNVIYNQQADVYSFGLLLYDILTCGERIVEGLKFPNEFDELAIQG 207
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 13112048 600 RMDKPA---NCT--HDLYMIMRECWHAAPSQRPTFKQLVEDLD 637
Cdd:cd14068 208 KLPDPVkeyGCApwPGVEALIKDCLKENPQCRPTSAQVFDILN 250
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
392-639 5.59e-19

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: 87.61  E-value: 5.59e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 392 TVAVKMLKDDA--TDKDLSDLVSEMEMMKmigkHKNIINLLGACTQGGPLYVLVEYAAKGNLREFLRARRPPgLDYSFDt 469
Cdd:cd14045  32 TVAIKKIAKKSftLSKRIRKEVKQVRELD----HPNLCKFIGGCIEVPNVAIITEYCPKGSLNDVLLNEDIP-LNWGFR- 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 470 ckppeeqltfkdlVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLA-----RDVHNLDYYKKttngRL 544
Cdd:cd14045 106 -------------FSFATDIARGMAYLHQHKIYHGRLKSSNCVIDDRWVCKIADYGLTtyrkeDGSENASGYQQ----RL 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 545 PVKWMAPEA--LFDRVYTHQSDVWSFGVLLWEIFTLgGSPYPG----------IPVEELfkllkEGHRMDKPANCTHDLY 612
Cdd:cd14045 169 MQVYLPPENhsNTDTEPTQATDVYSYAIILLEIATR-NDPVPEddysldeawcPPLPEL-----ISGKTENSCPCPADYV 242
                       250       260
                ....*....|....*....|....*..
gi 13112048 613 MIMRECWHAAPSQRPTFKQLVEDLDRV 639
Cdd:cd14045 243 ELIRRCRKNNPAQRPTFEQIKKTLHKI 269
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
359-577 5.99e-19

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: 88.35  E-value: 5.99e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 359 RLTLGKPLGEGCFGQVVMAeaigIDKDRAAKpvtVAVKMLKDdaTDKDLSD---LVSEMEMMKMIgKHKNIINLLGACTQ 435
Cdd:cd07834   1 RYELLKPIGSGAYGVVCSA----YDKRTGRK---VAIKKISN--VFDDLIDakrILREIKILRHL-KHENIIGLLDILRP 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 436 GGP-----LYVLVEYAAKgNLREFLRARRPpgldysfdtckppeeqLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARN 510
Cdd:cd07834  71 PSPeefndVYIVTELMET-DLHKVIKSPQP----------------LTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSN 133
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13112048 511 VLVTEDNVMKIADFGLAR------DVHNLDYYKKTtngrlpvKWM-APEAL--FDRvYTHQSDVWSFGVLLWEIFT 577
Cdd:cd07834 134 ILVNSNCDLKICDFGLARgvdpdeDKGFLTEYVVT-------RWYrAPELLlsSKK-YTKAIDIWSVGCIFAELLT 201
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
357-632 7.42e-19

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


Pssm-ID: 271063 [Multi-domain]  Cd Length: 255  Bit Score: 86.93  E-value: 7.42e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 357 RARLTLGKPLGEGCFGQVVMAeaigidKDRAAKpvTVAVKMLKDDAT--DKDLSDLVSEMEMMKMIgKHKNIINLLGACT 434
Cdd:cd14161   2 KHRYEFLETLGKGTYGRVKKA------RDSSGR--LVAIKSIRKDRIkdEQDLLHIRREIEIMSSL-NHPHIISVYEVFE 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 435 QGGPLYVLVEYAAKGNLREFLRARRPpgldysfdtCKPPEEQLTFKDLVSCAYqvargmeYLASQKCIHRDLAARNVLVT 514
Cdd:cd14161  73 NSSKIVIVMEYASRGDLYDYISERQR---------LSELEARHFFRQIVSAVH-------YCHANGIVHRDLKLENILLD 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 515 EDNVMKIADFGLArDVHNLDYYKKTTNGRlPVkWMAPEALFDRVYTH-QSDVWSFGVLLWeIFTLGGSPYPGIPVEELFK 593
Cdd:cd14161 137 ANGNIKIADFGLS-NLYNQDKFLQTYCGS-PL-YASPEIVNGRPYIGpEVDSWSLGVLLY-ILVHGTMPFDGHDYKILVK 212
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 13112048 594 LLKEG--HRMDKPAN-CTHDLYMIMrecwhAAPSQRPTFKQL 632
Cdd:cd14161 213 QISSGayREPTKPSDaCGLIRWLLM-----VNPERRATLEDV 249
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
362-641 7.72e-19

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


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 86.78  E-value: 7.72e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 362 LGKPLGEGCFGQVVMAEAIGIDKDRAAKPVTvavkmlkdDATDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGplyv 441
Cdd:cd13975   4 LGRELGRGQYGVVYACDSWGGHFPCALKSVV--------PPDDKHWNDLALEFHYTRSLPKHERIVSLHGSVIDYS---- 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 442 lveYAAKGNLREFLRARRppgldYSFDTCKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKI 521
Cdd:cd13975  72 ---YGGGSSIAVLLIMER-----LHRDLYTGIKAGLSLEERLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKI 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 522 ADFGLARDvhnldyyKKTTNGRL---PVKwMAPEaLFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGI-----PVEELFK 593
Cdd:cd13975 144 TDLGFCKP-------EAMMSGSIvgtPIH-MAPE-LFSGKYDNSVDVYAFGILFWYLCA-GHVKLPEAfeqcaSKDHLWN 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 13112048 594 LLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVLT 641
Cdd:cd13975 214 NVRKGVRPERLPVFDEECWNLMEACWSGDPSQRPLLGIVQPKLQGIMD 261
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
364-592 8.01e-19

Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. There are four nPKC isoforms, delta, epsilon, eta, and theta. The nPKC-theta-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270744 [Multi-domain]  Cd Length: 320  Bit Score: 87.83  E-value: 8.01e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVMAEAIGidkdraaKPVTVAVKMLKDDAT--DKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYV 441
Cdd:cd05592   1 KVLGKGSFGKVMLAELKG-------TNQYFAIKALKKDVVleDDDVECTMIERRVLALASQHPFLTHLFCTFQTESHLFF 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 442 LVEYAAKGNL----REFLRarrppgldysFDtckppEEQLTFKdlvscAYQVARGMEYLASQKCIHRDLAARNVLVTEDN 517
Cdd:cd05592  74 VMEYLNGGDLmfhiQQSGR----------FD-----EDRARFY-----GAEIICGLQFLHSRGIIYRDLKLDNVLLDREG 133
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13112048 518 VMKIADFGLARDvhNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFtLGGSPYPGIPVEELF 592
Cdd:cd05592 134 HIKIADFGMCKE--NIYGENKASTFCGTPDYIAPEILKGQKYNQSVDWWSFGVLLYEML-IGQSPFHGEDEDELF 205
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
366-640 9.04e-19

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: 87.28  E-value: 9.04e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEaigidkdRAAKPVTVAVKMLKDDA--TDKDLSDLVSEMEMMKMiGKHKNIINLLGACTQGGPLYVLV 443
Cdd:cd14026   5 LSRGAFGTVSRAR-------HADWRVTVAIKCLKLDSpvGDSERNCLLKEAEILHK-ARFSYILPILGICNEPEFLGIVT 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 444 EYAAKGNLREFLRARrppglDYSFDTCKPpeeqLTFKDLvscaYQVARGMEYL--ASQKCIHRDLAARNVLVTEDNVMKI 521
Cdd:cd14026  77 EYMTNGSLNELLHEK-----DIYPDVAWP----LRLRIL----YEIALGVNYLhnMSPPLLHHDLKTQNILLDGEFHVKI 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 522 ADFGLARdVHNLDYYKKTTNGRLP----VKWMAPEALFDRVYTHQS---DVWSFGVLLWEIFTLgGSPYPGI--PVEELF 592
Cdd:cd14026 144 ADFGLSK-WRQLSISQSRSSKSAPeggtIIYMPPEEYEPSQKRRASvkhDIYSYAIIMWEVLSR-KIPFEEVtnPLQIMY 221
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 13112048 593 KLLKeGHRMDK-----PANCTHDLYMI--MRECWHAAPSQRPTFKQLVEDLDRVL 640
Cdd:cd14026 222 SVSQ-GHRPDTgedslPVDIPHRATLInlIESGWAQNPDERPSFLKCLIELEPVL 275
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
359-628 1.10e-18

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


Pssm-ID: 270975 [Multi-domain]  Cd Length: 254  Bit Score: 86.29  E-value: 1.10e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 359 RLTLGKPLGEGCFGQVVMAEAIGIDKdraakpvTVAVKMLKDDA--TDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQG 436
Cdd:cd14073   2 RYELLETLGKGTYGKVKLAIERATGR-------EVAIKSIKKDKieDEQDMVRIRREIEIMSSL-NHPHIIRIYEVFENK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 437 GPLYVLVEYAAKGNLREFLRARRppgldysfdtckppeeQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTED 516
Cdd:cd14073  74 DKIVIVMEYASGGELYDYISERR----------------RLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQN 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 517 NVMKIADFGLArDVHNLDYYKKTTNGRlPVkWMAPEALFDRVYTH-QSDVWSFGVLLWeIFTLGGSPYPGIPVEELFKLL 595
Cdd:cd14073 138 GNAKIADFGLS-NLYSKDKLLQTFCGS-PL-YASPEIVNGTPYQGpEVDCWSLGVLLY-TLVYGTMPFDGSDFKRLVKQI 213
                       250       260       270
                ....*....|....*....|....*....|....*
gi 13112048 596 KEG--HRMDKPAncthDLYMIMRECWHAAPSQRPT 628
Cdd:cd14073 214 SSGdyREPTQPS----DASGLIRWMLTVNPKRRAT 244
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
362-585 1.18e-18

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: 87.00  E-value: 1.18e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 362 LGKpLGEGCFGQVVMAeaigidKDRAaKPVTVAVK-MLKDDATDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLY 440
Cdd:cd07832   5 LGR-IGEGAHGIVFKA------KDRE-TGETVALKkVALRKLEGGIPNQALREIKALQACQGHPYVVKLRDVFPHGTGFV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 441 VLVEYAAKGnLREFLRARRPPgldysfdtckppeeqLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMK 520
Cdd:cd07832  77 LVFEYMLSS-LSEVLRDEERP---------------LTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLK 140
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13112048 521 IADFGLARdVHNLDYYKKTTNgRLPVKW-MAPEALF-DRVYTHQSDVWSFGVLLWEIftLGGSP-YPG 585
Cdd:cd07832 141 IADFGLAR-LFSEEDPRLYSH-QVATRWyRAPELLYgSRKYDEGVDLWAVGCIFAEL--LNGSPlFPG 204
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
364-628 1.30e-18

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: 86.56  E-value: 1.30e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVMAEAIGiDKdraakpvtVAVKMLkddaTDKDLSDLVSEMEM--MKMIgKHKNIINLLGA-------CT 434
Cdd:cd14056   1 KTIGKGRYGEVWLGKYRG-EK--------VAVKIF----SSRDEDSWFRETEIyqTVML-RHENILGFIAAdikstgsWT 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 435 QggpLYVLVEYAAKGNLREFLRarrppgldysfdtckppEEQLTFKDLVSCAYQVARGMEYLASQ--------KCIHRDL 506
Cdd:cd14056  67 Q---LWLITEYHEHGSLYDYLQ-----------------RNTLDTEEALRLAYSAASGLAHLHTEivgtqgkpAIAHRDL 126
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 507 AARNVLVTEDNVMKIADFGLArdvhnLDYYKKTTNGRLP-------VKWMAPEALFDRVYTH------QSDVWSFGVLLW 573
Cdd:cd14056 127 KSKNILVKRDGTCCIADLGLA-----VRYDSDTNTIDIPpnprvgtKRYMAPEVLDDSINPKsfesfkMADIYSFGLVLW 201
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13112048 574 EIFTLGGS---------PYPGI----P-VEELFKLLKEGHRMDKPAN------CTHDLYMIMRECWHAAPSQRPT 628
Cdd:cd14056 202 EIARRCEIggiaeeyqlPYFGMvpsdPsFEEMRKVVCVEKLRPPIPNrwksdpVLRSMVKLMQECWSENPHARLT 276
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
367-628 1.30e-18

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: 86.72  E-value: 1.30e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 367 GEGCFGQVVMAEaigIDKDraakpvTVAVKMLkddaTDKDLSDLVSEMEMMKMIG-KHKNIINLLGA---CTQGGPLYVL 442
Cdd:cd13998   4 GKGRFGEVWKAS---LKNE------PVAVKIF----SSRDKQSWFREKEIYRTPMlKHENILQFIAAderDTALRTELWL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 443 V-EYAAKGNLREFLRArrppgldysfdtckppeEQLTFKDLVSCAYQVARGMEYLASQKCI---------HRDLAARNVL 512
Cdd:cd13998  71 VtAFHPNGSL*DYLSL-----------------HTIDWVSLCRLALSVARGLAHLHSEIPGctqgkpaiaHRDLKSKNIL 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 513 VTEDNVMKIADFGLA-RDVHNLDYYKKTTNGRLPVK-WMAPEALFDRVYTH------QSDVWSFGVLLWEIFT----LGG 580
Cdd:cd13998 134 VKNDGTCCIADFGLAvRLSPSTGEEDNANNGQVGTKrYMAPEVLEGAINLRdfesfkRVDIYAMGLVLWEMASrctdLFG 213
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13112048 581 S------PY----PGIP-VEELFKL-LKEGHRMDKPANCTHD-----LYMIMRECWHAAPSQRPT 628
Cdd:cd13998 214 IveeykpPFysevPNHPsFEDMQEVvVRDKQRPNIPNRWLSHpglqsLAETIEECWDHDAEARLT 278
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
366-644 1.57e-18

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: 86.01  E-value: 1.57e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKDRAAKpvtVAVKMLKDDatdKDLSDLVSEMEMMKMIgKHKNIINLLGACTQggPLYVLVEY 445
Cdd:cd14025   4 VGSGGFGQVYKVRHKHWKTWLAIK---CPPSLHVDD---SERMELLEEAKKMEMA-KFRHILPVYGICSE--PVGLVMEY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLREFLRArrppgldysfdtckppeEQLTFKDLVSCAYQVARGMEYLASQK--CIHRDLAARNVLVTEDNVMKIAD 523
Cdd:cd14025  75 METGSLEKLLAS-----------------EPLPWELRFRIIHETAVGMNFLHCMKppLLHLDLKPANILLDAHYHVKISD 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 524 FGLAR---DVHNLDYYKKTTNGRLpvKWMAPEALF--DRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPvEELFKLLK-- 596
Cdd:cd14025 138 FGLAKwngLSHSHDLSRDGLRGTI--AYLPPERFKekNRCPDTKHDVYSFAIVIWGILT-QKKPFAGEN-NILHIMVKvv 213
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 13112048 597 EGHRMD-------KPANCTHDLYMiMRECWHAAPSQRPTFKQLVEDLDRVLTVTS 644
Cdd:cd14025 214 KGHRPSlspiprqRPSECQQMICL-MKRCWDQDPRKRPTFQDITSETENLLSLLE 267
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
363-634 1.61e-18

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: 85.75  E-value: 1.61e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 363 GKPLGEGCFGQVVMAEAIGIDKDRAAKpVTVAVKMLKDDATDKdlsdLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVL 442
Cdd:cd14189   6 GRLLGKGGFARCYEMTDLATNKTYAVK-VIPHSRVAKPHQREK----IVNEIELHRDL-HHKHVVKFSHHFEDAENIYIF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 443 VEYAAKGNLREFLRARRppgldysfdTCKPPEEQLTFKDLVScayqvarGMEYLASQKCIHRDLAARNVLVTEDNVMKIA 522
Cdd:cd14189  80 LELCSRKSLAHIWKARH---------TLLEPEVRYYLKQIIS-------GLKYLHLKGILHRDLKLGNFFINENMELKVG 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 523 DFGLARDVHNLDYYKKTTNGRlPvKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEELFKLLKEGHRMd 602
Cdd:cd14189 144 DFGLAARLEPPEQRKKTICGT-P-NYLAPEVLLRQGHGPESDVWSLGCVMYTLLC-GNPPFETLDLKETYRCIKQVKYT- 219
                       250       260       270
                ....*....|....*....|....*....|..
gi 13112048 603 KPANCTHDLYMIMRECWHAAPSQRPTFKQLVE 634
Cdd:cd14189 220 LPASLSLPARHLLAGILKRNPGDRLTLDQILE 251
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
364-604 1.64e-18

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: 86.92  E-value: 1.64e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVMAEAIGidkdraaKPVTVAVKMLKDDAT--DKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYV 441
Cdd:cd05620   1 KVLGKGSFGKVLLAELKG-------KGEYFAVKALKKDVVliDDDVECTMVEKRVLALAWENPFLTHLYCTFQTKEHLFF 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 442 LVEYAAKGNLREFLRARRppgldySFDTCKPpeeqlTFKdlvscAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKI 521
Cdd:cd05620  74 VMEFLNGGDLMFHIQDKG------RFDLYRA-----TFY-----AAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKI 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 522 ADFGLARDvHNLDYYKKTTNGRLPvKWMAPEALFDRVYTHQSDVWSFGVLLWEIFtLGGSPYPGIPVEELFkllkEGHRM 601
Cdd:cd05620 138 ADFGMCKE-NVFGDNRASTFCGTP-DYIAPEILQGLKYTFSVDWWSFGVLLYEML-IGQSPFHGDDEDELF----ESIRV 210

                ...
gi 13112048 602 DKP 604
Cdd:cd05620 211 DTP 213
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
348-634 1.92e-18

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: 85.57  E-value: 1.92e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 348 PADPkwelsRARLTLGKPLGEGCFGQVVMAEAIGIDKdraakpvTVAVKMLkdDATDKDLSDLV-SEMEMMKMIgKHKNI 426
Cdd:cd06648   2 PGDP-----RSDLDNFVKIGEGSTGIVCIATDKSTGR-------QVAVKKM--DLRKQQRRELLfNEVVIMRDY-QHPNI 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 427 INLLGACTQGGPLYVLVEYAAKGNLREFLRARRppgLDysfdtckppEEQLTfkdlvSCAYQVARGMEYLASQKCIHRDL 506
Cdd:cd06648  67 VEMYSSYLVGDELWVVMEFLEGGALTDIVTHTR---MN---------EEQIA-----TVCRAVLKALSFLHSQGVIHRDI 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 507 AARNVLVTEDNVMKIADFGLARDVHNLDYYKKTTNGRlPVkWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGI 586
Cdd:cd06648 130 KSDSILLTSDGRVKLSDFGFCAQVSKEVPRRKSLVGT-PY-WMAPEVISRLPYGTEVDIWSLGIMVIEMVD-GEPPYFNE 206
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 13112048 587 PVEELFKLLK--EGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVE 634
Cdd:cd06648 207 PPLQAMKRIRdnEPPKLKNLHKVSPRLRSFLDRMLVRDPAQRATAAELLN 256
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
366-633 2.15e-18

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: 85.13  E-value: 2.15e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEaigidkdraaKPV---TVAVKMLKDD-ATDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYV 441
Cdd:cd13997   8 IGSGSFSEVFKVR----------SKVdgcLYAVKKSKKPfRGPKERARALREVEAHAALGQHPNIVRYYSSWEEGGHLYI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 442 LVEYAAKGNLREFLRARRPPGldysfdtcKPPEEQLtfKDLvscAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKI 521
Cdd:cd13997  78 QMELCENGSLQDALEELSPIS--------KLSEAEV--WDL---LLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKI 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 522 ADFGLArdvhnldyykKTTNGRLPV-----KWMAPEALFD-RVYTHQSDVWSFGVLLWEIFTlgGSPYP--GipveELFK 593
Cdd:cd13997 145 GDFGLA----------TRLETSGDVeegdsRYLAPELLNEnYTHLPKADIFSLGVTVYEAAT--GEPLPrnG----QQWQ 208
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 13112048 594 LLKEGHRMDKP-ANCTHDLYMIMRECWHAAPSQRPTFKQLV 633
Cdd:cd13997 209 QLRQGKLPLPPgLVLSQELTRLLKVMLDPDPTRRPTADQLL 249
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
366-634 2.94e-18

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: 85.93  E-value: 2.94e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKdraakpvTVAVKMLkdDATDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGP------L 439
Cdd:cd06637  14 VGNGTYGQVYKGRHVKTGQ-------LAAIKVM--DVTGDEEEEIKQEINMLKKYSHHRNIATYYGAFIKKNPpgmddqL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 440 YVLVEYAAKGNLREFLRARRPPGLDysfdtckppEEQLTFkdlvsCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVM 519
Cdd:cd06637  85 WLVMEFCGAGSVTDLIKNTKGNTLK---------EEWIAY-----ICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 520 KIADFGLARDVHNLDYYKKTTNGRlPVkWMAPEALF-----DRVYTHQSDVWSFGVLLWEIfTLGGSPYPGI-PVEELFK 593
Cdd:cd06637 151 KLVDFGVSAQLDRTVGRRNTFIGT-PY-WMAPEVIAcdenpDATYDFKSDLWSLGITAIEM-AEGAPPLCDMhPMRALFL 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 13112048 594 LLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVE 634
Cdd:cd06637 228 IPRNPAPRLKSKKWSKKFQSFIESCLVKNHSQRPSTEQLMK 268
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
361-632 4.91e-18

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: 84.53  E-value: 4.91e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 361 TLGKPLGEGCFGQVVMAEAigidkdrAAKPVTVAVKMLKDDATDKDLSD--LVSEMEMMKMIgKHKNIINLLgACTQ--G 436
Cdd:cd14164   3 TLGTTIGEGSFSKVKLATS-------QKYCCKVAIKIVDRRRASPDFVQkfLPRELSILRRV-NHPNIVQMF-ECIEvaN 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 437 GPLYVLVEYAAKGNLREFLRARRPPGLDYsfdtckppeeqltfKDLVScayQVARGMEYLASQKCIHRDLAARNVLVT-E 515
Cdd:cd14164  74 GRLYIVMEAAATDLLQKIQEVHHIPKDLA--------------RDMFA---QMVGAVNYLHDMNIVHRDLKCENILLSaD 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 516 DNVMKIADFGLARDVHnlDYYKKTTNGRLPVKWMAPEALFDRVYTHQS-DVWSFGVLLWEIFTlGGSPYPGIPVeELFKL 594
Cdd:cd14164 137 DRKIKIADFGFARFVE--DYPELSTTFCGSRAYTPPEVILGTPYDPKKyDVWSLGVVLYVMVT-GTMPFDETNV-RRLRL 212
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 13112048 595 LKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQL 632
Cdd:cd14164 213 QQRGVLYPSGVALEEPCRALIRTLLQFNPSTRPSIQQV 250
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
375-634 5.12e-18

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: 85.08  E-value: 5.12e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 375 VMAEAIGIDK----DRAAKPVT---VAVKMLkddatDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYVLVEYAA 447
Cdd:cd14175   4 VVKETIGVGSysvcKRCVHKATnmeYAVKVI-----DKSKRDPSEEIEILLRYGQHPNIITLKDVYDDGKHVYLVTELMR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 448 KGNLRE-FLRarrppgldysfdtckppEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDN----VMKIA 522
Cdd:cd14175  79 GGELLDkILR-----------------QKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYVDESgnpeSLRIC 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 523 DFGLARDVhnldyykKTTNGRL-----PVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPY---PGIPVEELF-- 592
Cdd:cd14175 142 DFGFAKQL-------RAENGLLmtpcyTANFVAPEVLKRQGYDEGCDIWSLGILLYTMLA-GYTPFangPSDTPEEILtr 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 13112048 593 ----KLLKEGHRMDKPANCTHDLYMIMrecWHAAPSQRPTFKQLVE 634
Cdd:cd14175 214 igsgKFTLSGGNWNTVSDAAKDLVSKM---LHVDPHQRLTAKQVLQ 256
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
349-660 5.27e-18

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: 85.16  E-value: 5.27e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 349 ADPKWELSRArltlgKPLGEGCFGQVVMAEAIGIDKDRAAKPVTVAVKmlkddaTDKDLsdLVSEMEMMKMIgKHKNIIN 428
Cdd:cd06655  15 GDPKKKYTRY-----EKIGQGASGTVFTAIDVATGQEVAIKQINLQKQ------PKKEL--IINEILVMKEL-KNPNIVN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 429 LLGACTQGGPLYVLVEYAAKGNLReflrarrppglDYSFDTCKPPEEqltfkdLVSCAYQVARGMEYLASQKCIHRDLAA 508
Cdd:cd06655  81 FLDSFLVGDELFVVMEYLAGGSLT-----------DVVTETCMDEAQ------IAAVCRECLQALEFLHANQVIHRDIKS 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 509 RNVLVTEDNVMKIADFGLARDVhNLDYYKKTTNGRLPVkWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGI-P 587
Cdd:cd06655 144 DNVLLGMDGSVKLTDFGFCAQI-TPEQSKRSTMVGTPY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPYLNEnP 220
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13112048 588 VEELFKLLKEGH-RMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEdldrvltvtstDEYLDLSAPFEQYSP 660
Cdd:cd06655 221 LRALYLIATNGTpELQNPEKLSPIFRDFLNRCLEMDVEKRGSAKELLQ-----------HPFLKLAKPLSSLTP 283
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
362-634 7.23e-18

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: 84.06  E-value: 7.23e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 362 LGKPLGEGCFGQVVMAEAIGIDKDraakpvtVAVKMLKDDATDKDLSD--LVSEMEMMKMIgKHKNIINLLGAC-TQGGP 438
Cdd:cd14165   5 LGINLGEGSYAKVKSAYSERLKCN-------VAIKIIDKKKAPDDFVEkfLPRELEILARL-NHKSIIKTYEIFeTSDGK 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 439 LYVLVEYAAKGNLREFLRARrppgldysfdtCKPPEeqltfkDLVSCAY-QVARGMEYLASQKCIHRDLAARNVLVTEDN 517
Cdd:cd14165  77 VYIVMELGVQGDLLEFIKLR-----------GALPE------DVARKMFhQLSSAIKYCHELDIVHRDLKCENLLLDKDF 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 518 VMKIADFGLARDVhnldyyKKTTNGRLPVK--------WMAPEALFDRVYTHQ-SDVWSFGVLLWeIFTLGGSPYPGIPV 588
Cdd:cd14165 140 NIKLTDFGFSKRC------LRDENGRIVLSktfcgsaaYAAPEVLQGIPYDPRiYDIWSLGVILY-IMVCGSMPYDDSNV 212
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 13112048 589 EELFKLLKEgHRMDKPANC--THDLYMIMRECWHAAPSQRPTFKQLVE 634
Cdd:cd14165 213 KKMLKIQKE-HRVRFPRSKnlTSECKDLIYRLLQPDVSQRLCIDEVLS 259
PHA02988 PHA02988
hypothetical protein; Provisional
393-636 7.55e-18

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 84.41  E-value: 7.55e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048  393 VAVKMLKDDATD-KDLSDL-VSEMEMMKMIgKHKNIINLLG----ACTQGGPLYVLVEYAAKGNLREFLRArrppgldys 466
Cdd:PHA02988  46 VIIRTFKKFHKGhKVLIDItENEIKNLRRI-DSNNILKIYGfiidIVDDLPRLSLILEYCTRGYLREVLDK--------- 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048  467 fdtckppEEQLTFKDLVSCAYQVARGMEYL-ASQKCIHRDLAARNVLVTEDNVMKIADFGLARDVHNLDYykKTTNGrlp 545
Cdd:PHA02988 116 -------EKDLSFKTKLDMAIDCCKGLYNLyKYTNKPYKNLTSVSFLVTENYKLKIICHGLEKILSSPPF--KNVNF--- 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048  546 VKWMAPEALFD--RVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEELFKLL-KEGHRMDKPANCTHDLYMIMRECWHAA 622
Cdd:PHA02988 184 MVYFSYKMLNDifSEYTIKDDIYSLGVVLWEIFT-GKIPFENLTTKEIYDLIiNKNNSLKLPLDCPLEIKCIVEACTSHD 262
                        250
                 ....*....|....
gi 13112048  623 PSQRPTFKQLVEDL 636
Cdd:PHA02988 263 SIKRPNIKEILYNL 276
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
422-632 8.20e-18

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


Pssm-ID: 270945 [Multi-domain]  Cd Length: 267  Bit Score: 84.00  E-value: 8.20e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 422 KHKNIINLLGACTQGGPLYVLVEYAAKGNLREFLRARrppglDYSFDtckppeeqLTFK-----DLVscayqvaRGMEYL 496
Cdd:cd14043  54 RHENVNLFLGLFVDCGILAIVSEHCSRGSLEDLLRND-----DMKLD--------WMFKsslllDLI-------KGMRYL 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 497 ASQKCIHRDLAARNVLVTEDNVMKIADFGLAR--DVHNLDYYKKTTNGRLpvkWMAPEALFDRVY----THQSDVWSFGV 570
Cdd:cd14043 114 HHRGIVHGRLKSRNCVVDGRFVLKITDYGYNEilEAQNLPLPEPAPEELL---WTAPELLRDPRLerrgTFPGDVFSFAI 190
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13112048 571 LLWEIFTLGGsPYP--GIPVEELFK-------LLKEGHRMDK-PANCTHdlymIMRECWHAAPSQRPTFKQL 632
Cdd:cd14043 191 IMQEVIVRGA-PYCmlGLSPEEIIEkvrspppLCRPSVSMDQaPLECIQ----LMKQCWSEAPERRPTFDQI 257
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
366-592 8.31e-18

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: 85.04  E-value: 8.31e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEaigidkDRAAKPVtVAVKMLK--DDATDKDLSDLVSEMEMMKMIG--KHKNIINLLgACTQGgPLYV 441
Cdd:cd05589   7 LGRGHFGKVLLAE------YKPTGEL-FAIKALKkgDIIARDEVESLMCEKRIFETVNsaRHPFLVNLF-ACFQT-PEHV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 442 --LVEYAAKGNLREFLRARrppgldySFdtckpPEEQLTFkdLVSCayqVARGMEYLASQKCIHRDLAARNVLVTEDNVM 519
Cdd:cd05589  78 cfVMEYAAGGDLMMHIHED-------VF-----SEPRAVF--YAAC---VVLGLQFLHEHKIVYRDLKLDNLLLDTEGYV 140
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13112048 520 KIADFGLARDvhNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFtLGGSPYPGIPVEELF 592
Cdd:cd05589 141 KIADFGLCKE--GMGFGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEML-VGESPFPGDDEEEVF 210
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
366-634 1.04e-17

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: 83.25  E-value: 1.04e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKDRAAKPVTVAvkmlkdDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd08221   8 LGRGAFGEAVLYRKTEDNSLVVWKEVNLS------RLSEKERRDALNEIDILSLL-NHDNIITYYNHFLDGESLFIEMEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLREFLRARRPPGLdysfdtckpPEEQLTFKdlvscAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFG 525
Cdd:cd08221  81 CNGGNLHDKIAQQKNQLF---------PEEVVLWY-----LYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFG 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 526 LARdVHNLDYYKKTTNGRLPVkWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKeGHRMDKPA 605
Cdd:cd08221 147 ISK-VLDSESSMAESIVGTPY-YMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRTFDATNPLRLAVKIVQ-GEYEDIDE 223
                       250       260
                ....*....|....*....|....*....
gi 13112048 606 NCTHDLYMIMRECWHAAPSQRPTFKQLVE 634
Cdd:cd08221 224 QYSEEIIQLVHDCLHQDPEDRPTAEELLE 252
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
366-577 1.11e-17

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


Pssm-ID: 270889 [Multi-domain]  Cd Length: 259  Bit Score: 83.53  E-value: 1.11e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEaigiDKDRAAKpvtVAVKMLKDDATDkdLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYVLV-E 444
Cdd:cd13987   1 LGEGTYGKVLLAV----HKGSGTK---MALKFVPKPSTK--LKDFLREYNISLELSVHPHIIKTYDVAFETEDYYVFAqE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 445 YAAKGNLREFLRARRppGLDYsfDTCKppeeqltfkdlvSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDN--VMKIA 522
Cdd:cd13987  72 YAPYGDLFSIIPPQV--GLPE--ERVK------------RCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDcrRVKLC 135
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13112048 523 DFGLARDVHNLDYYKKTTNgrlpvKWMAPEAL-------FdrVYTHQSDVWSFGVLLWEIFT 577
Cdd:cd13987 136 DFGLTRRVGSTVKRVSGTI-----PYTAPEVCeakknegF--VVDPSIDVWAFGVLLFCCLT 190
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
361-635 1.25e-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: 83.26  E-value: 1.25e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 361 TLGKPLGEGCFGQVVMAeaigidKDRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGAC-TQGGPL 439
Cdd:cd08223   3 QFLRVIGKGSYGEVWLV------RHKRDRKQYVIKKLNLKNASKRERKAAEQEAKLLSKL-KHPNIVSYKESFeGEDGFL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 440 YVLVEYAAKGNLREFLRARRPPGLdysfdtckpPEEQLtfkdlVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVM 519
Cdd:cd08223  76 YIVMGFCEGGDLYTRLKEQKGVLL---------EERQV-----VEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNII 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 520 KIADFGLARDVHNLDYYKKTTNGRlPVkWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSpYPGIPVEELFKLLKEGH 599
Cdd:cd08223 142 KVGDLGIARVLESSSDMATTLIGT-PY-YMSPELFSNKPYNHKSDVWALGCCVYEMATLKHA-FNAKDMNSLVYKILEGK 218
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 13112048 600 RMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVED 635
Cdd:cd08223 219 LPPMPKQYSPELGELIKAMLHQDPEKRPSVKRILRQ 254
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
361-598 1.36e-17

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: 83.09  E-value: 1.36e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 361 TLGKPLGEGCFGQVVMAEaigidkdRAAKPVTVAVKMLkddatDKDLsdlvseMEMMKMIGK------------HKNIIN 428
Cdd:cd14079   5 ILGKTLGVGSFGKVKLAE-------HELTGHKVAVKIL-----NRQK------IKSLDMEEKirreiqilklfrHPHIIR 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 429 LLGACTQGGPLYVLVEYAAKGNLreflrarrppgLDYSFDTCKPPEEQLT--FKDLVScayqvarGMEYLASQKCIHRDL 506
Cdd:cd14079  67 LYEVIETPTDIFMVMEYVSGGEL-----------FDYIVQKGRLSEDEARrfFQQIIS-------GVEYCHRHMVVHRDL 128
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 507 AARNVLVTEDNVMKIADFGLA---RDVHNLdyykKTTNGRlPvKWMAPEALFDRVYT-HQSDVWSFGVLLWEIftLGGS- 581
Cdd:cd14079 129 KPENLLLDSNMNVKIADFGLSnimRDGEFL----KTSCGS-P-NYAAPEVISGKLYAgPEVDVWSCGVILYAL--LCGSl 200
                       250
                ....*....|....*..
gi 13112048 582 PYPGIPVEELFKLLKEG 598
Cdd:cd14079 201 PFDDEHIPNLFKKIKSG 217
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
366-592 1.37e-17

Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. cPKCs contain a calcium-binding C2 region in their regulatory domain. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The cPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 84.37  E-value: 1.37e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKdraakpvTVAVKMLKDDAT--DKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYVLV 443
Cdd:cd05587   4 LGKGSFGKVMLAERKGTDE-------LYAIKILKKDVIiqDDDVECTMVEKRVLALSGKPPFLTQLHSCFQTMDRLYFVM 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 444 EYAAKGNLReflrarrppgldYSFDTCKppeeqlTFKDLVSCAY--QVARGMEYLASQKCIHRDLAARNVLVTEDNVMKI 521
Cdd:cd05587  77 EYVNGGDLM------------YHIQQVG------KFKEPVAVFYaaEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKI 138
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13112048 522 ADFGLARDVHNLDYYKKTTNGRlPvKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEELF 592
Cdd:cd05587 139 ADFGMCKEGIFGGKTTRTFCGT-P-DYIAPEIIAYQPYGKSVDWWAYGVLLYEMLA-GQPPFDGEDEDELF 206
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
393-632 1.41e-17

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: 83.25  E-value: 1.41e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 393 VAVKMLKDDATDKDLSD-----LVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEYAAKGNLREFLrARRPPgldysf 467
Cdd:cd06631  28 IAVKQVELDTSDKEKAEkeyekLQEEVDLLKTL-KHVNIVGYLGTCLEDNVVSIFMEFVPGGSIASIL-ARFGA------ 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 468 dtckppeeqltFKDLVSCAY--QVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARDVHNLDyyKKTTNGRL- 544
Cdd:cd06631 100 -----------LEEPVFCRYtkQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGCAKRLCINL--SSGSQSQLl 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 545 ------PVkWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGI-PVEELFKLLKEGHRMDK-PANCTHDLYMIMR 616
Cdd:cd06631 167 ksmrgtPY-WMAPEVINETGHGRKSDIWSIGCTVFEMAT-GKPPWADMnPMAAIFAIGSGRKPVPRlPDKFSPEARDFVH 244
                       250
                ....*....|....*.
gi 13112048 617 ECWHAAPSQRPTFKQL 632
Cdd:cd06631 245 ACLTRDQDERPSAEQL 260
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
366-634 1.63e-17

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: 83.38  E-value: 1.63e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKDRAAKPVTVAVKmlkDDATDKdlsdLVSEMEMMKMIgKHKNIINLLGACTQGGP------- 438
Cdd:cd14048  14 LGRGGFGVVFEAKNKVDDCNYAVKRIRLPNN---ELAREK----VLREVRALAKL-DHPGIVRYFNAWLERPPegwqekm 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 439 ----LYVLVEYAAKGNLREFLRaRRPPGLDYSFDTCKPpeeqlTFKdlvscayQVARGMEYLASQKCIHRDLAARNVLVT 514
Cdd:cd14048  86 devyLYIQMQLCRKENLKDWMN-RRCTMESRELFVCLN-----IFK-------QIASAVEYLHSKGLIHRDLKPSNVFFS 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 515 EDNVMKIADFGLARDV----------HNLDYYKKTTnGRLPVK-WMAPEALFDRVYTHQSDVWSFGVLLWEIFtlggspY 583
Cdd:cd14048 153 LDDVVKVGDFGLVTAMdqgepeqtvlTPMPAYAKHT-GQVGTRlYMSPEQIHGNQYSEKVDIFALGLILFELI------Y 225
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 13112048 584 PGIPVEELFKLLKEGHRMDKPANCTHDL---YMIMRECWHAAPSQRPTFKQLVE 634
Cdd:cd14048 226 SFSTQMERIRTLTDVRKLKFPALFTNKYpeeRDMVQQMLSPSPSERPEAHEVIE 279
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
366-578 1.63e-17

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: 83.32  E-value: 1.63e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQV--VMAEAIGiDKDRAAKPVTVAVKMLKDDATDKDLS--DLVSEMEMMKMIGKHKNIINLLGACTQGGPLYV 441
Cdd:cd08528   8 LGSGAFGCVykVRKKSNG-QTLLALKEINMTNPAFGRTEQERDKSvgDIISEVNIIKEQLRHPNIVRYYKTFLENDRLYI 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 442 LVEYAAKGNLREFlrarrppgldysFDTCKPPEEQLTFKDLVSCAYQVARGMEYLASQKCI-HRDLAARNVLVTEDNVMK 520
Cdd:cd08528  87 VMELIEGAPLGEH------------FSSLKEKNEHFTEDRIWNIFVQMVLALRYLHKEKQIvHRDLKPNNIMLGEDDKVT 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 13112048 521 IADFGLARDVHNLDYYKKTTNGRLpvKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTL 578
Cdd:cd08528 155 ITDFGLAKQKGPESSKMTSVVGTI--LYSCPEIVQNEPYGEKADIWALGCILYQMCTL 210
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
366-634 1.83e-17

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: 83.13  E-value: 1.83e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVmaeaigidKDRAAKPVTVA-VKMLkdDATDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGP------ 438
Cdd:cd06636  24 VGNGTYGQVY--------KGRHVKTGQLAaIKVM--DVTEDEEEEIKLEINMLKKYSHHRNIATYYGAFIKKSPpghddq 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 439 LYVLVEYAAKGNLREFLRARRPPGL--DYSFDTCKppeeqltfkdlvscayQVARGMEYLASQKCIHRDLAARNVLVTED 516
Cdd:cd06636  94 LWLVMEFCGAGSVTDLVKNTKGNALkeDWIAYICR----------------EILRGLAHLHAHKVIHRDIKGQNVLLTEN 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 517 NVMKIADFGLARDVHNLDYYKKTTNGRlPVkWMAPEALF-----DRVYTHQSDVWSFGVLLWEIfTLGGSPYPGI-PVEE 590
Cdd:cd06636 158 AEVKLVDFGVSAQLDRTVGRRNTFIGT-PY-WMAPEVIAcdenpDATYDYRSDIWSLGITAIEM-AEGAPPLCDMhPMRA 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 13112048 591 LFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVE 634
Cdd:cd06636 235 LFLIPRNPPPKLKSKKWSKKFIDFIEGCLVKNYLSRPSTEQLLK 278
PTK_Jak3_rpt1 cd14208
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is ...
360-637 2.01e-17

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


Pssm-ID: 271110 [Multi-domain]  Cd Length: 260  Bit Score: 82.64  E-value: 2.01e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 360 LTLGKPLGEGCFGQVVMAEAIGIDKDRAAKpVTVAVKMLkdDATDKDLSDLVSEM-EMMKMIgKHKNIINLLGACTqGGP 438
Cdd:cd14208   1 LTFMESLGKGSFTKIYRGLRTDEEDDERCE-TEVLLKVM--DPTHGNCQESFLEAaSIMSQI-SHKHLVLLHGVCV-GKD 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 439 LYVLVEYAAKGNLREFLRARRPPGLdysfdtckppeeqLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDN- 517
Cdd:cd14208  76 SIMVQEFVCHGALDLYLKKQQQKGP-------------VAISWKLQVVKQLAYALNYLEDKQLVHGNVSAKKVLLSREGd 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 518 -----VMKIADFGLARDVHNLDYYKKttngRLPvkWMAPEALFD-RVYTHQSDVWSFGVLLWEIFTLGGSPYPGIpvEEL 591
Cdd:cd14208 143 kgsppFIKLSDPGVSIKVLDEELLAE----RIP--WVAPECLSDpQNLALEADKWGFGATLWEIFSGGHMPLSAL--DPS 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 13112048 592 FKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLD 637
Cdd:cd14208 215 KKLQFYNDRKQLPAPHWIELASLIQQCMSYNPLLRPSFRAIIRDLN 260
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
425-634 2.12e-17

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: 82.78  E-value: 2.12e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 425 NIINLLGACTQGGPLYVLVEYAAKGNLREFLRARRPPgldysfdtckpPEEQLTFkdlvsCAYQVARGMEYLASQ-KCIH 503
Cdd:cd06605  60 YIVGFYGAFYSEGDISICMEYMDGGSLDKILKEVGRI-----------PERILGK-----IAVAVVKGLIYLHEKhKIIH 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 504 RDLAARNVLVTEDNVMKIADFGLARDVhnLDYYKKTTNGRLPvkWMAPEALFDRVYTHQSDVWSFGVLLWEIfTLGGSPY 583
Cdd:cd06605 124 RDVKPSNILVNSRGQVKLCDFGVSGQL--VDSLAKTFVGTRS--YMAPERISGGKYTVKSDIWSLGLSLVEL-ATGRFPY 198
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 13112048 584 PGIPVEE---LFKLLKEGHRMDKPA----NCTHDLYMIMRECWHAAPSQRPTFKQLVE 634
Cdd:cd06605 199 PPPNAKPsmmIFELLSYIVDEPPPLlpsgKFSPDFQDFVSQCLQKDPTERPSYKELME 256
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
361-635 2.31e-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: 82.39  E-value: 2.31e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 361 TLGKPLGEGCFGQVVMaeaiGI---DKDRaakpvtVAVKMLK----DDATDKDLSDLVSEMEMMKmigkHKNIINLLGAC 433
Cdd:cd14075   5 RIRGELGSGNFSQVKL----GIhqlTKEK------VAIKILDktklDQKTQRLLSREISSMEKLH----HPNIIRLYEVV 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 434 TQGGPLYVLVEYAAKGNLREFLRARRPpgldysfdtCKPPEEQLTFKDLVScayqvarGMEYLASQKCIHRDLAARNVLV 513
Cdd:cd14075  71 ETLSKLHLVMEYASGGELYTKISTEGK---------LSESEAKPLFAQIVS-------AVKHMHENNIIHRDLKAENVFY 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 514 TEDNVMKIADFG---LARDVHNLDyykkTTNGRLPvkWMAPEaLF--DRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPV 588
Cdd:cd14075 135 ASNNCVKVGDFGfstHAKRGETLN----TFCGSPP--YAAPE-LFkdEHYIGIYVDIWALGVLLYFMVT-GVMPFRAETV 206
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 13112048 589 EELFKLLKEGHrMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVED 635
Cdd:cd14075 207 AKLKKCILEGT-YTIPSYVSEPCQELIRGILQPVPSDRYSIDEIKNS 252
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
361-596 2.41e-17

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: 82.86  E-value: 2.41e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 361 TLGKpLGEGCFGQVVMAeaigidKDRAAKPVtVAVKMLKDDATDKDLSDL-VSEMEMMKMIgKHKNIINLLGACTQGGPL 439
Cdd:cd07846   5 NLGL-VGEGSYGMVMKC------RHKETGQI-VAIKKFLESEDDKMVKKIaMREIKMLKQL-RHENLVNLIEVFRRKKRW 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 440 YVLVEYAAKGNLREFLRArrPPGLDYSfdtckppeeqLTFKDLvscaYQVARGMEYLASQKCIHRDLAARNVLVTEDNVM 519
Cdd:cd07846  76 YLVFEFVDHTVLDDLEKY--PNGLDES----------RVRKYL----FQILRGIDFCHSHNIIHRDIKPENILVSQSGVV 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 520 KIADFGLARDVHN-----LDYykkttngrLPVKWM-APEALF-DRVYTHQSDVWSFGVLLWEIFTlgGSPY-PGIP-VEE 590
Cdd:cd07846 140 KLCDFGFARTLAApgevyTDY--------VATRWYrAPELLVgDTKYGKAVDVWAVGCLVTEMLT--GEPLfPGDSdIDQ 209

                ....*.
gi 13112048 591 LFKLLK 596
Cdd:cd07846 210 LYHIIK 215
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
366-632 2.62e-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: 2.62e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKDRAAKpvtvavKMLKDDATDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd14050   9 LGEGSFGEVFKVRSREDGKLYAVK------RSRSRFRGEKDRKRKLEEVERHEKLGEHPNCVRFIKAWEEKGILYIQTEL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKgNLreflrarrppgLDYSFDTCKPPEEQL--TFKDLVscayqvaRGMEYLASQKCIHRDLAARNVLVTEDNVMKIAD 523
Cdd:cd14050  83 CDT-SL-----------QQYCEETHSLPESEVwnILLDLL-------KGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGD 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 524 FGLardVHNLDYYKKTTNGRLPVKWMAPEALfDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGipveELFKLLKEGHRmdk 603
Cdd:cd14050 144 FGL---VVELDKEDIHDAQEGDPRYMAPELL-QGSFTKAADIFSLGITILELACNLELPSGG----DGWHQLRQGYL--- 212
                       250       260       270
                ....*....|....*....|....*....|...
gi 13112048 604 PANCT----HDLYMIMRECWHAAPSQRPTFKQL 632
Cdd:cd14050 213 PEEFTaglsPELRSIIKLMMDPDPERRPTAEDL 245
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
350-583 2.67e-17

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: 82.28  E-value: 2.67e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 350 DPKWELSRArltlgKPLGEGCFGQVVMAEAIGIDKDRAAKpvtvavKMLKDDATDKDLsdLVSEMEMMKMiGKHKNIINL 429
Cdd:cd06647   4 DPKKKYTRF-----EKIGQGASGTVYTAIDVATGQEVAIK------QMNLQQQPKKEL--IINEILVMRE-NKNPNIVNY 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 430 LGACTQGGPLYVLVEYAAKGNLREFLrarrppgldysfdtckpPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAAR 509
Cdd:cd06647  70 LDSYLVGDELWVVMEYLAGGSLTDVV-----------------TETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSD 132
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13112048 510 NVLVTEDNVMKIADFGLARDVhNLDYYKKTTNGRLPVkWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPY 583
Cdd:cd06647 133 NILLGMDGSVKLTDFGFCAQI-TPEQSKRSTMVGTPY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPY 203
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
363-632 2.79e-17

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: 82.48  E-value: 2.79e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 363 GKPLGEGCFGQVVMAEAIGIDKDRAAKPVTVAVKMLKDdaTDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVL 442
Cdd:cd06630   5 GPLLGTGAFSSCYQARDVKTGTLMAVKQVSFCRNSSSE--QEEVVEAIREEIRMMARL-NHPNIVRMLGATQHKSHFNIF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 443 VEYAAKGNLREFLRARRPpgldysfdtckppeeqltFKDLVSCAY--QVARGMEYLASQKCIHRDLAARNVLV-TEDNVM 519
Cdd:cd06630  82 VEWMAGGSVASLLSKYGA------------------FSENVIINYtlQILRGLAYLHDNQIIHRDLKGANLLVdSTGQRL 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 520 KIADFG----LARDVHNLDYYKkttnGRL--PVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEE--- 590
Cdd:cd06630 144 RIADFGaaarLASKGTGAGEFQ----GQLlgTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMAT-AKPPWNAEKISNhla 218
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 13112048 591 -LFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQL 632
Cdd:cd06630 219 lIFKIASATTPPPIPEHLSPGLRDVTLRCLELQPEDRPPAREL 261
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
366-596 3.13e-17

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: 82.74  E-value: 3.13e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAeaigidKDRAAKPVtVAVKMLKDDATDKDLSDL-VSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVE 444
Cdd:cd07848   9 VGEGAYGVVLKC------RHKETKEI-VAIKKFKDSEENEEVKETtLRELKMLRTL-KQENIVELKEAFRRRGKLYLVFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 445 YAAKgNLREFLRaRRPPGLdysfdtckPPEEqltfkdLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADF 524
Cdd:cd07848  81 YVEK-NMLELLE-EMPNGV--------PPEK------VRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDF 144
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13112048 525 GLARDV---HNLDYYKkttngRLPVKWM-APEALFDRVYTHQSDVWSFGVLLWEIFTlgGSP-YPG-IPVEELFKLLK 596
Cdd:cd07848 145 GFARNLsegSNANYTE-----YVATRWYrSPELLLGAPYGKAVDMWSVGCILGELSD--GQPlFPGeSEIDQLFTIQK 215
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
360-633 3.88e-17

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: 82.49  E-value: 3.88e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 360 LTLGKpLGEGCFGQVVMAEAIGIDKDRAAKPVTVavkmlkdDATDKDLSDLVSEMEMMKMIgKHKNIINLLGAC-TQGGP 438
Cdd:cd06620   8 ETLKD-LGAGNGGSVSKVLHIPTGTIMAKKVIHI-------DAKSSVRKQILRELQILHEC-HSPYIVSFYGAFlNENNN 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 439 LYVLVEYAAKGNLREFLRARRPpgldYSFDTCKppeeqltfkdlvSCAYQVARGMEYLASQ-KCIHRDLAARNVLVTEDN 517
Cdd:cd06620  79 IIICMEYMDCGSLDKILKKKGP----FPEEVLG------------KIAVAVLEGLTYLYNVhRIIHRDIKPSNILVNSKG 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 518 VMKIADFGLARDVHN--LDYYKKTTNgrlpvkWMAPEALFDRVYTHQSDVWSFGVLLWEIfTLGGSPYPGIPVEELFKLL 595
Cdd:cd06620 143 QIKLCDFGVSGELINsiADTFVGTST------YMSPERIQGGKYSVKSDVWSLGLSIIEL-ALGEFPFAGSNDDDDGYNG 215
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 13112048 596 KEG-----HRM---DKPANCTHDLY-MIMRE----CWHAAPSQRPTFKQLV 633
Cdd:cd06620 216 PMGildllQRIvnePPPRLPKDRIFpKDLRDfvdrCLLKDPRERPSPQLLL 266
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
366-578 3.98e-17

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: 82.32  E-value: 3.98e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKDraakpvtVAVKMLKDDATDKDLS-DLVSEMEMMKMIGK--HKNIINLLGACTqgGP---- 438
Cdd:cd07838   7 IGEGAYGTVYKARDLQDGRF-------VALKKVRVPLSEEGIPlSTIREIALLKQLESfeHPNVVRLLDVCH--GPrtdr 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 439 ---LYVLVEYAAKgNLREFLRARRPPGLdysfdtckPPEeqlTFKDLVscaYQVARGMEYLASQKCIHRDLAARNVLVTE 515
Cdd:cd07838  78 elkLTLVFEHVDQ-DLATYLDKCPKPGL--------PPE---TIKDLM---RQLLRGLDFLHSHRIVHRDLKPQNILVTS 142
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13112048 516 DNVMKIADFGLARdvhNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTL 578
Cdd:cd07838 143 DGQVKLADFGLAR---IYSFEMALTSVVVTLWYRAPEVLLQSSYATPVDMWSVGCIFAELFNR 202
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
364-632 4.03e-17

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: 81.67  E-value: 4.03e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVMAeaigidKDRAAKpVTVAVKMLKDDATDKD-LSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVL 442
Cdd:cd14071   6 RTIGKGNFAVVKLA------RHRITK-TEVAIKIIDKSQLDEEnLKKIYREVQIMKML-NHPHIIKLYQVMETKDMLYLV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 443 VEYAAKGNLREFLRARRppgldysfdtcKPPEEQLTFKdlvscAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIA 522
Cdd:cd14071  78 TEYASNGEIFDYLAQHG-----------RMSEKEARKK-----FWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIA 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 523 DFGLArDVHNLDYYKKTTNGRLPvkWMAPEALFDRVYTH-QSDVWSFGVLLWeIFTLGGSPYPGIPVEELFKLLKEGhRM 601
Cdd:cd14071 142 DFGFS-NFFKPGELLKTWCGSPP--YAAPEVFEGKEYEGpQLDIWSLGVVLY-VLVCGALPFDGSTLQTLRDRVLSG-RF 216
                       250       260       270
                ....*....|....*....|....*....|.
gi 13112048 602 DKPANCTHDLYMIMRECWHAAPSQRPTFKQL 632
Cdd:cd14071 217 RIPFFMSTDCEHLIRRMLVLDPSKRLTIEQI 247
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
364-635 5.06e-17

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: 81.28  E-value: 5.06e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVMAeaigIDKDRAAKPVTVAV---KMLKDDAT-DKDLSDLVSEMEMMKMIGK--HKNIINLLGACTQGG 437
Cdd:cd14004   6 KEMGEGAYGQVNLA----IYKSKGKEVVIKFIfkeRILVDTWVrDRKLGTVPLEIHILDTLNKrsHPNIVKLLDFFEDDE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 438 PLYVLVEYAAKGnLREFLRARRPPGLDysfdtckPPEEQLTFKdlvscayQVARGMEYLASQKCIHRDLAARNVLVTEDN 517
Cdd:cd14004  82 FYYLVMEKHGSG-MDLFDFIERKPNMD-------EKEAKYIFR-------QVADAVKHLHDQGIVHRDIKDENVILDGNG 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 518 VMKIADFGLARDVHN--LDYYKKTTNgrlpvkWMAPEALFDRVYTHQS-DVWSFGVLLWEIFtLGGSPYpgIPVEELFKl 594
Cdd:cd14004 147 TIKLIDFGSAAYIKSgpFDTFVGTID------YAAPEVLRGNPYGGKEqDIWALGVLLYTLV-FKENPF--YNIEEILE- 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 13112048 595 lkegHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVED 635
Cdd:cd14004 217 ----ADLRIPYAVSEDLIDLISRMLNRDVGDRPTIEELLTD 253
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
349-660 5.18e-17

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: 82.08  E-value: 5.18e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 349 ADPKWELSRArltlgKPLGEGCFGQVVMAEAIGIDKDRAAKpvtvavKMLKDDATDKDLsdLVSEMEMMKMiGKHKNIIN 428
Cdd:cd06654  16 GDPKKKYTRF-----EKIGQGASGTVYTAMDVATGQEVAIR------QMNLQQQPKKEL--IINEILVMRE-NKNPNIVN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 429 LLGACTQGGPLYVLVEYAAKGNLReflrarrppglDYSFDTCkppeeqLTFKDLVSCAYQVARGMEYLASQKCIHRDLAA 508
Cdd:cd06654  82 YLDSYLVGDELWVVMEYLAGGSLT-----------DVVTETC------MDEGQIAAVCRECLQALEFLHSNQVIHRDIKS 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 509 RNVLVTEDNVMKIADFGLARDVhNLDYYKKTTNGRLPVkWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGI-P 587
Cdd:cd06654 145 DNILLGMDGSVKLTDFGFCAQI-TPEQSKRSTMVGTPY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMIE-GEPPYLNEnP 221
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13112048 588 VEELFKLLKEGH-RMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEdldrvltvtstDEYLDLSAPFEQYSP 660
Cdd:cd06654 222 LRALYLIATNGTpELQNPEKLSAIFRDFLNRCLEMDVEKRGSAKELLQ-----------HQFLKIAKPLSSLTP 284
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
362-598 5.30e-17

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: 81.15  E-value: 5.30e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 362 LGKPLGEGCFGQVVMAeaigidKDRAAKpVTVAVKMLKDDATDKDLSDLVSEME--MMKMIgKHKNIINLLGACTQGGPL 439
Cdd:cd14081   5 LGKTLGKGQTGLVKLA------KHCVTG-QKVAIKIVNKEKLSKESVLMKVEREiaIMKLI-EHPNVLKLYDVYENKKYL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 440 YVLVEYAAKGNLREFLRARRPpgldysfdtcKPPEEQLTFkdlvscAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVM 519
Cdd:cd14081  77 YLVLEYVSGGELFDYLVKKGR----------LTEKEARKF------FRQIISALDYCHSHSICHRDLKPENLLLDEKNNI 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 520 KIADFGLARdVHNLDYYKKTTNGRLpvKWMAPEALFDRVYTHQ-SDVWSFGVLLWEIFTlGGSPYPGIPVEELFKLLKEG 598
Cdd:cd14081 141 KIADFGMAS-LQPEGSLLETSCGSP--HYACPEVIKGEKYDGRkADIWSCGVILYALLV-GALPFDDDNLRQLLEKVKRG 216
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
350-635 5.55e-17

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: 81.52  E-value: 5.55e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 350 DPKwelSRARLTLGKPLGEGCFGQVVMAEAIGIDKDRAAKPVTVAVkMLKDDATDKdlsdLVSEMEMMKMIGkHKNIINL 429
Cdd:cd14187   2 DPR---TRRRYVRGRFLGKGGFAKCYEITDADTKEVFAGKIVPKSL-LLKPHQKEK----MSMEIAIHRSLA-HQHVVGF 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 430 LGACTQGGPLYVLVEYAAKGNLREFLRARRppgldysfdTCKPPEEQLTFKdlvscayQVARGMEYLASQKCIHRDLAAR 509
Cdd:cd14187  73 HGFFEDNDFVYVVLELCRRRSLLELHKRRK---------ALTEPEARYYLR-------QIILGCQYLHRNRVIHRDLKLG 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 510 NVLVTEDNVMKIADFGLARDVHNLDYYKKTTNGrlPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFtLGGSPYPGIPVE 589
Cdd:cd14187 137 NLFLNDDMEVKIGDFGLATKVEYDGERKKTLCG--TPNYIAPEVLSKKGHSFEVDIWSIGCIMYTLL-VGKPPFETSCLK 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 13112048 590 ELFKLLKEgHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVED 635
Cdd:cd14187 214 ETYLRIKK-NEYSIPKHINPVAASLIQKMLQTDPTARPTINELLND 258
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
366-576 5.70e-17

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: 82.00  E-value: 5.70e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAeaigidKDRAAKPVTVAVKMLKDDATDKDLS-DLVSEMEMMKMIG--KHKNIINLLGACT-----QGG 437
Cdd:cd07862   9 IGEGAYGKVFKA------RDLKNGGRFVALKRVRVQTGEEGMPlSTIREVAVLRHLEtfEHPNVVRLFDVCTvsrtdRET 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 438 PLYVLVEYAAKgNLREFLRARRPPGLdysfdtckPPEeqlTFKDLVscaYQVARGMEYLASQKCIHRDLAARNVLVTEDN 517
Cdd:cd07862  83 KLTLVFEHVDQ-DLTTYLDKVPEPGV--------PTE---TIKDMM---FQLLRGLDFLHSHRVVHRDLKPQNILVTSSG 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 13112048 518 VMKIADFGLARDvhnLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIF 576
Cdd:cd07862 148 QIKLADFGLARI---YSFQMALTSVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMF 203
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
364-636 7.20e-17

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


Pssm-ID: 270887 [Multi-domain]  Cd Length: 272  Bit Score: 81.23  E-value: 7.20e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVMAEAIGIDKDRAAKpvtvavKMLKDDatDKDLSDLVSEMEMMKMIGKHKNIINLLG-ACTQGGPL--- 439
Cdd:cd13985   6 KQLGEGGFSYVYLAHDVNTGRRYALK------RMYFND--EEQLRVAIKEIEIMKRLCGHPNIVQYYDsAILSSEGRkev 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 440 YVLVEYAaKGNLREFLRaRRPPGldysfdtckppeeQLTFKDLVSCAYQVARGMEYLASQK--CIHRDLAARNVLVTEDN 517
Cdd:cd13985  78 LLLMEYC-PGSLVDILE-KSPPS-------------PLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTG 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 518 VMKIADFGlarDVHNLDYYKKTTNGRLPVK----------WMAPEA--LFDRV-YTHQSDVWSFGVLLWEI--FTLggsp 582
Cdd:cd13985 143 RFKLCDFG---SATTEHYPLERAEEVNIIEeeiqknttpmYRAPEMidLYSKKpIGEKADIWALGCLLYKLcfFKL---- 215
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 13112048 583 ypgiPVEELFKL--LKEGHRMDKPANCT---HDLYMIMREcwhAAPSQRPTFKQLVEDL 636
Cdd:cd13985 216 ----PFDESSKLaiVAGKYSIPEQPRYSpelHDLIRHMLT---PDPAERPDIFQVINII 267
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
362-585 7.53e-17

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 82.50  E-value: 7.53e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048  362 LGKPLGEGCFGQVVMAEAIGIDKDraakpvtVAVKMLKDDATDKDLSD-------------LVSEMEMMKMIgKHKNIIN 428
Cdd:PTZ00024  13 KGAHLGEGTYGKVEKAYDTLTGKI-------VAIKKVKIIEISNDVTKdrqlvgmcgihftTLRELKIMNEI-KHENIMG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048  429 LLGACTQGGPLYVLVEYAAkGNLREFLRARRppgldysfdtckppeeQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAA 508
Cdd:PTZ00024  85 LVDVYVEGDFINLVMDIMA-SDLKKVVDRKI----------------RLTESQVKCILLQILNGLNVLHKWYFMHRDLSP 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048  509 RNVLVTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVK-----------WM-APEALF-DRVYTHQSDVWSFGVLLWEI 575
Cdd:PTZ00024 148 ANIFINSKGICKIADFGLARRYGYPPYSDTLSKDETMQRreemtskvvtlWYrAPELLMgAEKYHFAVDMWSVGCIFAEL 227
                        250
                 ....*....|.
gi 13112048  576 ftLGGSP-YPG 585
Cdd:PTZ00024 228 --LTGKPlFPG 236
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
366-606 7.57e-17

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


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 80.98  E-value: 7.57e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKDRAAKPVtVAVKMLkddATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd14098   8 LGSGTFAEVKKAVEVETGKMRAIKQI-VKRKVA---GNDKNLQLFQREINILKSL-EHPGIVRLIDWYEDDQHIYLVMEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLREFLRARrpPGLDysfdtckppeEQLTfKDLVScayQVARGMEYLASQKCIHRDLAARNVLVTEDN--VMKIAD 523
Cdd:cd14098  83 VEGGDLMDFIMAW--GAIP----------EQHA-RELTK---QILEAMAYTHSMGITHRDLKPENILITQDDpvIVKISD 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 524 FGLARDVHNlDYYKKTTNGRLpvKWMAPEALFDR------VYTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEELFKLLKE 597
Cdd:cd14098 147 FGLAKVIHT-GTFLVTFCGTM--AYLAPEILMSKeqnlqgGYSNLVDMWSVGCLVYVMLT-GALPFDGSSQLPVEKRIRK 222

                ....*....
gi 13112048 598 GHRMDKPAN 606
Cdd:cd14098 223 GRYTQPPLV 231
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
348-634 7.84e-17

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: 7.84e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 348 PADpKWELSRArltlgkpLGEGCFGQVVMAeaigIDKDRAAKpvtVAVKMLkDDATDKDlSDLVSEMEMMKMIGKHKNII 427
Cdd:cd06638  16 PSD-TWEIIET-------IGKGTYGKVFKV----LNKKNGSK---AAVKIL-DPIHDID-EEIEAEYNILKALSDHPNVV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 428 NLLGA-----CTQGGPLYVLVEYAAKGNLREFLRARRPPGldysfdtckppeEQLTFKDLVSCAYQVARGMEYLASQKCI 502
Cdd:cd06638  79 KFYGMyykkdVKNGDQLWLVLELCNGGSVTDLVKGFLKRG------------ERMEEPIIAYILHEALMGLQHLHVNKTI 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 503 HRDLAARNVLVTEDNVMKIADFGLARDVHNLDYYKKTTNGRlPVkWMAPEAL-----FDRVYTHQSDVWSFGVLLWEIFT 577
Cdd:cd06638 147 HRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRLRRNTSVGT-PF-WMAPEVIaceqqLDSTYDARCDVWSLGITAIELGD 224
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 13112048 578 lGGSPYPGI-PVEELFKLLKE-GHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVE 634
Cdd:cd06638 225 -GDPPLADLhPMRALFKIPRNpPPTLHQPELWSNEFNDFIRKCLTKDYEKRPTVSDLLQ 282
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
366-610 8.13e-17

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: 80.88  E-value: 8.13e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAeaigidKDRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd14120   1 IGHGAFAVVFKG------RHRKKPDLPVAIKCITKKNLSKSQNLLGKEIKILKEL-SHENVVALLDCQETSSSVYLVMEY 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLREFLRARRppglDYSFDTCKppeeqlTFkdLVscayQVARGMEYLASQKCIHRDLAARNVLVTEDN-------- 517
Cdd:cd14120  74 CNGGDLADYLQAKG----TLSEDTIR------VF--LQ----QIAAAMKALHSKGIVHRDLKPQNILLSHNSgrkpspnd 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 518 -VMKIADFGLARDVHNlDYYKKTTNGRlPVkWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPY------------- 583
Cdd:cd14120 138 iRLKIADFGFARFLQD-GMMAATLCGS-PM-YMAPEVIMSLQYDAKADLWSIGTIVYQCLT-GKAPFqaqtpqelkafye 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 13112048 584 ------PGIPVEE-------LFKLLKEGH--RMDKPANCTHD 610
Cdd:cd14120 214 knanlrPNIPSGTspalkdlLLGLLKRNPkdRIDFEDFFSHP 255
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
359-639 8.35e-17

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: 81.17  E-value: 8.35e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 359 RLTLGKPLGEGCFGQVVMAEAIGidkdraakpvTVAVKMLKDDATDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGP 438
Cdd:cd14152   1 QIELGELIGQGRWGKVHRGRWHG----------EVAIRLLEIDGNNQDHLKLFKKEVMNYRQTRHENVVLFMGACMHPPH 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 439 LYVLVEYAAKGNLREFLRarrppgldysfdtckPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNV 518
Cdd:cd14152  71 LAIITSFCKGRTLYSFVR---------------DPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKV 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 519 MkIADFGLARDVHNLDYYKKTTNGRLPVKW---MAPEALFDRV---------YTHQSDVWSFGVLLWEIfTLGGSPYPGI 586
Cdd:cd14152 136 V-ITDFGLFGISGVVQEGRRENELKLPHDWlcyLAPEIVREMTpgkdedclpFSKAADVYAFGTIWYEL-QARDWPLKNQ 213
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 13112048 587 PVEELFKLLKEGHRMDKPANCT---HDLYMIMRECWHAAPSQRPTFKQLVEDLDRV 639
Cdd:cd14152 214 PAEALIWQIGSGEGMKQVLTTIslgKEVTEILSACWAFDLEERPSFTLLMDMLEKL 269
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
366-626 8.54e-17

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: 82.35  E-value: 8.54e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKdraakpvTVAVKMLKDDAT--DKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYVLV 443
Cdd:cd05615  18 LGKGSFGKVMLAERKGSDE-------LYAIKILKKDVViqDDDVECTMVEKRVLALQDKPPFLTQLHSCFQTVDRLYFVM 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 444 EYAAKGNLREFLRarrppgldysfDTCKPPEEQLTFKdlvscAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIAD 523
Cdd:cd05615  91 EYVNGGDLMYHIQ-----------QVGKFKEPQAVFY-----AAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIAD 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 524 FGLARDvHNLDYYKKTTNGRLPvKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEELFKLLKEgHRMDK 603
Cdd:cd05615 155 FGMCKE-HMVEGVTTRTFCGTP-DYIAPEIIAYQPYGRSVDWWAYGVLLYEMLA-GQPPFDGEDEDELFQSIME-HNVSY 230
                       250       260
                ....*....|....*....|...
gi 13112048 604 PANCTHDLYMIMRECWHAAPSQR 626
Cdd:cd05615 231 PKSLSKEAVSICKGLMTKHPAKR 253
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
151-245 9.62e-17

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 75.51  E-value: 9.62e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 151 PYWTRPErmdKKLLAVPAANTVRFRCPAAGNPTPSISWLKNGREFRGehRIGGIKLrhQQWSLVMESVVPSDRGNYTCVV 230
Cdd:cd20978   1 PKFIQKP---EKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQG--PMERATV--EDGTLTIINVQPEDTGYYGCVA 73
                        90
                ....*....|....*
gi 13112048 231 ENKFGSIRQTYTLDV 245
Cdd:cd20978  74 TNEIGDIYTETLLHV 88
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
405-632 1.11e-16

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: 80.48  E-value: 1.11e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 405 KDLSDLVSEMEMMKMIgKHKNIINLLGAC------TQGGPLYVLVEYAAKGNLREFLrarrppgldysfDTCKP-PEEQL 477
Cdd:cd14012  40 KQIQLLEKELESLKKL-RHPNLVSYLAFSierrgrSDGWKVYLLTEYAPGGSLSELL------------DSVGSvPLDTA 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 478 tfkdlvsCAY--QVARGMEYLASQKCIHRDLAARNVLV---TEDNVMKIADFGLARDVHNLDYYKKTTNGRlPVKWMAPE 552
Cdd:cd14012 107 -------RRWtlQLLEALEYLHRNGVVHKSLHAGNVLLdrdAGTGIVKLTDYSLGKTLLDMCSRGSLDEFK-QTYWLPPE 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 553 -ALFDRVYTHQSDVWSFGVLLWEIFTlggspypGIPVEELFKLLKEGHrmdKPANCTHDLYMIMRECWHAAPSQRPTFKQ 631
Cdd:cd14012 179 lAQGSKSPTRKTDVWDLGLLFLQMLF-------GLDVLEKYTSPNPVL---VSLDLSASLQDFLSKCLSLDPKKRPTALE 248

                .
gi 13112048 632 L 632
Cdd:cd14012 249 L 249
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
366-634 1.21e-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: 81.05  E-value: 1.21e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQV--VMAEAIGidkdraakpVTVAVKMLKDDATDKDLSDLVSEMEMMkmigkHK----NIINLLGACTQGGPL 439
Cdd:cd06622   9 LGKGNYGSVykVLHRPTG---------VTMAMKEIRLELDESKFNQIIMELDIL-----HKavspYIVDFYGAFFIEGAV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 440 YVLVEYAAKGNLREFLrarrppglDYSFDTCKPPEEQLTFkdlvsCAYQVARGMEYLASQ-KCIHRDLAARNVLVTEDNV 518
Cdd:cd06622  75 YMCMEYMDAGSLDKLY--------AGGVATEGIPEDVLRR-----ITYAVVKGLKFLKEEhNIIHRDVKPTNVLVNGNGQ 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 519 MKIADFGLArdvHNLDYYKKTTNGRLPvKWMAPE------ALFDRVYTHQSDVWSFGVLLWEIfTLGGSPYPGIPVEELF 592
Cdd:cd06622 142 VKLCDFGVS---GNLVASLAKTNIGCQ-SYMAPEriksggPNQNPTYTVQSDVWSLGLSILEM-ALGRYPYPPETYANIF 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 13112048 593 KLLK---EGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVE 634
Cdd:cd06622 217 AQLSaivDGDPPTLPSGYSDDAQDFVAKCLNKIPNRRPTYAQLLE 261
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
349-660 1.36e-16

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: 80.92  E-value: 1.36e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 349 ADPKWELSRArltlgKPLGEGCFGQVVMAEAIGIDKDRAAKpvtvavKMLKDDATDKDLsdLVSEMEMMKMiGKHKNIIN 428
Cdd:cd06656  15 GDPKKKYTRF-----EKIGQGASGTVYTAIDIATGQEVAIK------QMNLQQQPKKEL--IINEILVMRE-NKNPNIVN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 429 LLGACTQGGPLYVLVEYAAKGNLReflrarrppglDYSFDTCkppeeqLTFKDLVSCAYQVARGMEYLASQKCIHRDLAA 508
Cdd:cd06656  81 YLDSYLVGDELWVVMEYLAGGSLT-----------DVVTETC------MDEGQIAAVCRECLQALDFLHSNQVIHRDIKS 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 509 RNVLVTEDNVMKIADFGLARDVhNLDYYKKTTNGRLPVkWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGI-P 587
Cdd:cd06656 144 DNILLGMDGSVKLTDFGFCAQI-TPEQSKRSTMVGTPY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPYLNEnP 220
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13112048 588 VEELFKLLKEGH-RMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEdldrvltvtstDEYLDLSAPFEQYSP 660
Cdd:cd06656 221 LRALYLIATNGTpELQNPERLSAVFRDFLNRCLEMDVDRRGSAKELLQ-----------HPFLKLAKPLSSLTP 283
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
364-585 1.50e-16

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


Pssm-ID: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 81.29  E-value: 1.50e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVMAEAI-GIDKDRaakpvTVAVKMLKDdATDKDLSDLVSEMEMMKMIG-KHKNIINLLGACTQGGPLYV 441
Cdd:cd05582   1 KVLGQGSFGKVFLVRKItGPDAGT-----LYAMKVLKK-ATLKVRDRVRTKMERDILADvNHPFIVKLHYAFQTEGKLYL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 442 LVEYAAKGNLreFLRARRppglDYSFDtckppEEQLTFkdlvscaY--QVARGMEYLASQKCIHRDLAARNVLVTEDNVM 519
Cdd:cd05582  75 ILDFLRGGDL--FTRLSK----EVMFT-----EEDVKF-------YlaELALALDHLHSLGIIYRDLKPENILLDEDGHI 136
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13112048 520 KIADFGLARDvhNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPG 585
Cdd:cd05582 137 KLTDFGLSKE--SIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GSLPFQG 199
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
362-660 1.56e-16

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: 80.49  E-value: 1.56e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 362 LGKpLGEGCFGQVVMAEaigiDKDRAAkpvTVAVKML---KDDATDKDLSdlVSEMEMMKMIgKHKNIINLLGACTQGGP 438
Cdd:cd07847   6 LSK-IGEGSYGVVFKCR----NRETGQ---IVAIKKFvesEDDPVIKKIA--LREIRMLKQL-KHPNLVNLIEVFRRKRK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 439 LYVLVEYAAKGNLREFlrARRPPGLdysfdtckpPEEQLtfkdlVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNV 518
Cdd:cd07847  75 LHLVFEYCDHTVLNEL--EKNPRGV---------PEHLI-----KKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQ 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 519 MKIADFGLAR-----DVHNLDYykkttngrLPVKWM-APEALF-DRVYTHQSDVWSFGVLLWEIFTlgGSP-YPGipvee 590
Cdd:cd07847 139 IKLCDFGFARiltgpGDDYTDY--------VATRWYrAPELLVgDTQYGPPVDVWAIGCVFAELLT--GQPlWPG----- 203
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 591 lfkllkeghRMDkpancTHDLYMIMRECWHAAPSQRPTFKQlvEDLDRVLTVTSTDEYLDLSAPFEQYSP 660
Cdd:cd07847 204 ---------KSD-----VDQLYLIRKTLGDLIPRHQQIFST--NQFFKGLSIPEPETREPLESKFPNISS 257
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
366-576 2.19e-16

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: 80.01  E-value: 2.19e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAeaigidKDRAAKPVtVAVKMLKDDATDKDLS-DLVSEMEMMKMIGK--HKNIINLLGAC----TQGGP 438
Cdd:cd07863   8 IGVGAYGTVYKA------RDPHSGHF-VALKSVRVQTNEDGLPlSTVREVALLKRLEAfdHPNIVRLMDVCatsrTDRET 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 439 LYVLVEYAAKGNLREFLRARRPPGLdysfdtckPPEeqlTFKDLVScayQVARGMEYLASQKCIHRDLAARNVLVTEDNV 518
Cdd:cd07863  81 KVTLVFEHVDQDLRTYLDKVPPPGL--------PAE---TIKDLMR---QFLRGLDFLHANCIVHRDLKPENILVTSGGQ 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 13112048 519 MKIADFGLARDvhnLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIF 576
Cdd:cd07863 147 VKLADFGLARI---YSCQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMF 201
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
366-585 2.58e-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: 79.19  E-value: 2.58e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKDRAAKpvtvAVKMLKddATDKDlsDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd14103   1 LGRGKFGTVYRCVEKATGKELAAK----FIKCRK--AKDRE--DVRNEIEIMNQL-RHPRLLQLYDAFETPREMVLVMEY 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLreFLRArrppgLDYSFdtckppeeQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLV--TEDNVMKIAD 523
Cdd:cd14103  72 VAGGEL--FERV-----VDDDF--------ELTERDCILFMRQICEGVQYMHKQGILHLDLKPENILCvsRTGNQIKIID 136
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13112048 524 FGLARdvhnldyyKKTTNGRLPVKW-----MAPEAL-FDRVyTHQSDVWSFGVLLWeIFTLGGSPYPG 585
Cdd:cd14103 137 FGLAR--------KYDPDKKLKVLFgtpefVAPEVVnYEPI-SYATDMWSVGVICY-VLLSGLSPFMG 194
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
356-627 2.66e-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: 80.08  E-value: 2.66e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 356 SRARLTLGKPLGEGCFGQVVMAEAIgIDKdraakpVTVAVKMLK--DDATDKDLSDLVSEMEMMKMIgKHKNIINLLGAC 433
Cdd:cd08229  22 TLANFRIEKKIGRGQFSEVYRATCL-LDG------VPVALKKVQifDLMDAKARADCIKEIDLLKQL-NHPNVIKYYASF 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 434 TQGGPLYVLVEYAAKGNLREFLRARRPPGldysfdtcKPPEEQLTFKDLVscayQVARGMEYLASQKCIHRDLAARNVLV 513
Cdd:cd08229  94 IEDNELNIVLELADAGDLSRMIKHFKKQK--------RLIPEKTVWKYFV----QLCSALEHMHSRRVMHRDIKPANVFI 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 514 TEDNVMKIADFGLARdvhnlDYYKKTTNGRLPVK---WMAPEALFDRVYTHQSDVWSFGVLLWEIFTLgGSPYPGIPVeE 590
Cdd:cd08229 162 TATGVVKLGDLGLGR-----FFSSKTTAAHSLVGtpyYMSPERIHENGYNFKSDIWSLGCLLYEMAAL-QSPFYGDKM-N 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 13112048 591 LFKLLKEGHRMDKPA----NCTHDLYMIMRECWHAAPSQRP 627
Cdd:cd08229 235 LYSLCKKIEQCDYPPlpsdHYSEELRQLVNMCINPDPEKRP 275
PK_GC-C cd14044
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain ...
395-641 3.03e-16

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: 79.54  E-value: 3.03e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 395 VKMLKDDATDKDLSDLVSEMEMMKMIG-KHKNIINLLGACTQGGPLYVLVEYAAKGNLREFLRarrppgldysfDTCKPP 473
Cdd:cd14044  33 VVILKDLKNNEGNFTEKQKIELNKLLQiDYYNLTKFYGTVKLDTMIFGVIEYCERGSLRDVLN-----------DKISYP 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 474 EEqlTFKDL---VSCAYQVARGMEYLASQKC-IHRDLAARNVLVTEDNVMKIADFGlardvhnldyykktTNGRLPVK-- 547
Cdd:cd14044 102 DG--TFMDWefkISVMYDIAKGMSYLHSSKTeVHGRLKSTNCVVDSRMVVKITDFG--------------CNSILPPSkd 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 548 -WMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLlkegHRMDKPANCT---------------HDL 611
Cdd:cd14044 166 lWTAPEHLRQAGTSQKGDVYSYGIIAQEIILRKETFYTAACSDRKEKI----YRVQNPKGMKpfrpdlnlesagereREV 241
                       250       260       270
                ....*....|....*....|....*....|
gi 13112048 612 YMIMRECWHAAPSQRPTFKQLVEDLDRVLT 641
Cdd:cd14044 242 YGLVKNCWEEDPEKRPDFKKIENTLAKIFS 271
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
353-585 3.21e-16

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: 80.42  E-value: 3.21e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 353 WELsRARLTLGKPLGEGCFGQVVMAEAIGIDkdraakpVTVAVKMLkddatDKDLSDLV------SEMEMMKMIgKHKNI 426
Cdd:cd07851  11 WEV-PDRYQNLSPVGSGAYGQVCSAFDTKTG-------RKVAIKKL-----SRPFQSAIhakrtyRELRLLKHM-KHENV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 427 INLLGACTQGGPL------YVLVEYAAKgNLREFLRARrppgldysfdtcKPPEEQLTFkdLVscaYQVARGMEYLASQK 500
Cdd:cd07851  77 IGLLDVFTPASSLedfqdvYLVTHLMGA-DLNNIVKCQ------------KLSDDHIQF--LV---YQILRGLKYIHSAG 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 501 CIHRDLAARNVLVTEDNVMKIADFGLARDVHnldyyKKTTnGRLPVKW-MAPEALFDRV-YTHQSDVWSFGVLLWEIFTl 578
Cdd:cd07851 139 IIHRDLKPSNLAVNEDCELKILDFGLARHTD-----DEMT-GYVATRWyRAPEIMLNWMhYNQTVDIWSVGCIMAELLT- 211

                ....*...
gi 13112048 579 gGSP-YPG 585
Cdd:cd07851 212 -GKTlFPG 218
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
353-585 3.49e-16

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: 80.47  E-value: 3.49e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 353 WELSRARLTLgKPLGEGCFGQVVMAeaigIDKDRAAKpvtVAVKMLKddatdKDLSDLV------SEMEMMKMIgKHKNI 426
Cdd:cd07877  13 WEVPERYQNL-SPVGSGAYGSVCAA----FDTKTGLR---VAVKKLS-----RPFQSIIhakrtyRELRLLKHM-KHENV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 427 INLLGACTQGGPL-----YVLVEYAAKGNLREFLRArrppgldysfdtckppeEQLTFKDLVSCAYQVARGMEYLASQKC 501
Cdd:cd07877  79 IGLLDVFTPARSLeefndVYLVTHLMGADLNNIVKC-----------------QKLTDDHVQFLIYQILRGLKYIHSADI 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 502 IHRDLAARNVLVTEDNVMKIADFGLARdvHNLDyykkTTNGRLPVKWM-APEALFDRVYTHQS-DVWSFGVLLWEIFTlG 579
Cdd:cd07877 142 IHRDLKPSNLAVNEDCELKILDFGLAR--HTDD----EMTGYVATRWYrAPEIMLNWMHYNQTvDIWSVGCIMAELLT-G 214

                ....*.
gi 13112048 580 GSPYPG 585
Cdd:cd07877 215 RTLFPG 220
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
359-628 3.64e-16

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: 79.00  E-value: 3.64e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 359 RLTLGKPLGEGCFGQVVMAEAIGIDKDRAAKPVT-VAVKMLKDDATdkdlsdlVSEMEMMKMIGK--HKNIINLLGACTQ 435
Cdd:cd08222   1 RYRVVRKLGSGNFGTVYLVSDLKATADEELKVLKeISVGELQPDET-------VDANREAKLLSKldHPAIVKFHDSFVE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 436 GGPLYVLVEYAAKGNLreflrarrppglDYSFDTCKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVtE 515
Cdd:cd08222  74 KESFCIVTEYCEGGDL------------DDKISEYKKSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFL-K 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 516 DNVMKIADFGLARDVHNLDYYKKTTNGRlPVkWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLG----GSPYPGIpveeL 591
Cdd:cd08222 141 NNVIKVGDFGISRILMGTSDLATTFTGT-PY-YMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKhafdGQNLLSV----M 214
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 13112048 592 FKLLkEGHRMDKPANCTHDLYMIMRECWHAAPSQRPT 628
Cdd:cd08222 215 YKIV-EGETPSLPDKYSKELNAIYSRMLNKDPALRPS 250
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
366-628 3.71e-16

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: 79.41  E-value: 3.71e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDkdraakpvtVAVKMLkddaTDKDLSDLVSEMEMMKMIG-KHKNIINLL-------GACTQgg 437
Cdd:cd14143   3 IGKGRFGEVWRGRWRGED---------VAVKIF----SSREERSWFREAEIYQTVMlRHENILGFIaadnkdnGTWTQ-- 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 438 pLYVLVEYAAKGNLREFLRarrppgldysfdtckppEEQLTFKDLVSCAYQVARG-----MEYLASQ---KCIHRDLAAR 509
Cdd:cd14143  68 -LWLVSDYHEHGSLFDYLN-----------------RYTVTVEGMIKLALSIASGlahlhMEIVGTQgkpAIAHRDLKSK 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 510 NVLVTEDNVMKIADFGLA-RDVHNLDYYKKTTNGRLPVK-WMAPEALFDRVYTH------QSDVWSFGVLLWEIF---TL 578
Cdd:cd14143 130 NILVKKNGTCCIADLGLAvRHDSATDTIDIAPNHRVGTKrYMAPEVLDDTINMKhfesfkRADIYALGLVFWEIArrcSI 209
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13112048 579 GGS------PY----PGIP-VEELFKLL-KEGHRMDKPA-----NCTHDLYMIMRECWHAAPSQRPT 628
Cdd:cd14143 210 GGIhedyqlPYydlvPSDPsIEEMRKVVcEQKLRPNIPNrwqscEALRVMAKIMRECWYANGAARLT 276
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
361-634 4.16e-16

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: 78.74  E-value: 4.16e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 361 TLGKPLGEGCFGQVVMAEAIGIDKDRAAKPV------TVAVKMLKddatdkdlsdlvSEMEMMKMIgKHKNIINLLGACT 434
Cdd:cd14097   4 TFGRKLGQGSFGVVIEATHKETQTKWAIKKInrekagSSAVKLLE------------REVDILKHV-NHAHIIHLEEVFE 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 435 QGGPLYVLVEYAAKGNLREFLRARrppGLDYSFDTckppeeqltfKDLVSCayqVARGMEYLASQKCIHRDLAARNVLVT 514
Cdd:cd14097  71 TPKRMYLVMELCEDGELKELLLRK---GFFSENET----------RHIIQS---LASAVAYLHKNDIVHRDLKLENILVK 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 515 E---DNVM----KIADFGLARDVHNLDYYKKTTNGRLPVkWMAPEALFDRVYTHQSDVWSFGVLLWeIFTLGGSPYPGIP 587
Cdd:cd14097 135 SsiiDNNDklniKVTDFGLSVQKYGLGEDMLQETCGTPI-YMAPEVISAHGYSQQCDIWSIGVIMY-MLLCGEPPFVAKS 212
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 13112048 588 VEELFKLLKEGHrmdkpANCTHDLYMIMRECWHAA--------PSQRPTFKQLVE 634
Cdd:cd14097 213 EEKLFEEIRKGD-----LTFTQSVWQSVSDAAKNVlqqllkvdPAHRMTASELLD 262
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
366-595 4.41e-16

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: 79.01  E-value: 4.41e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAeaigidKDRAAKPVtVAVKMLKDDATDKDL-SDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVE 444
Cdd:cd07839   8 IGEGTYGTVFKA------KNRETHEI-VALKRVRLDDDDEGVpSSALREICLLKEL-KHKNIVRLYDVLHSDKKLTLVFE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 445 YAAKgNLREFlrarrppgldysFDTCKPPEEQLTFKdlvSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADF 524
Cdd:cd07839  80 YCDQ-DLKKY------------FDSCNGDIDPEIVK---SFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADF 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 525 GLARdvhnldyykkttNGRLPVK----------WMAPEALFD-RVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEE--- 590
Cdd:cd07839 144 GLAR------------AFGIPVRcysaevvtlwYRPPDVLFGaKLYSTSIDMWSAGCIFAELANAGRPLFPGNDVDDqlk 211

                ....*.
gi 13112048 591 -LFKLL 595
Cdd:cd07839 212 rIFRLL 217
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
357-632 4.57e-16

Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Drosophila melanogaster NAK, human BMP-2-inducible protein kinase (BMP2K or BIKe) and similar vertebrate proteins, as well as the Saccharomyces cerevisiae proteins Prk1, Actin-regulating kinase 1 (Ark1), and Akl1. NAK was the first characterized member of this subfamily. It plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. BMP2K contains a nuclear localization signal and a kinase domain that is capable of phosphorylating itself and myelin basic protein. The expression of the BMP2K gene is increase during BMP-2-induced osteoblast differentiation. It may function to control the rate of differentiation. Prk1, Ark1, and Akl1 comprise a subfamily of yeast proteins that are important regulators of the actin cytoskeleton and endocytosis. They share an N-terminal kinase domain but no significant homology in other regions of their sequences. The NAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 78.86  E-value: 4.57e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 357 RARLTLGKPLGEGCFGQVVMAEAIGIDKDRAAKPVTVavkmlKDDatdKDLSDLVSEMEMMKMIGKHKNIINLLG---AC 433
Cdd:cd14037   2 SHHVTIEKYLAEGGFAHVYLVKTSNGGNRAALKRVYV-----NDE---HDLNVCKREIEIMKRLSGHKNIVGYIDssaNR 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 434 TQGG--PLYVLVEYAAKGNLREFLRARRPPGLdysfdtckppEEQLTFKDLVSCAYQVARgMEYLaSQKCIHRDLAARNV 511
Cdd:cd14037  74 SGNGvyEVLLLMEYCKGGGVIDLMNQRLQTGL----------TESEILKIFCDVCEAVAA-MHYL-KPPLIHRDLKVENV 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 512 LVTEDNVMKIADFGLA----RDVHNL--------DYYKKTTngrlpVKWMAPEaLFD----RVYTHQSDVWSFGVLLWEI 575
Cdd:cd14037 142 LISDSGNYKLCDFGSAttkiLPPQTKqgvtyveeDIKKYTT-----LQYRAPE-MIDlyrgKPITEKSDIWALGCLLYKL 215
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13112048 576 --FTLggspypgiPVEELFKLLKEGHRMDKPANCTH--DLYMIMRECWHAAPSQRPTFKQL 632
Cdd:cd14037 216 cfYTT--------PFEESGQLAILNGNFTFPDNSRYskRLHKLIRYMLEEDPEKRPNIYQV 268
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
359-635 5.36e-16

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: 78.22  E-value: 5.36e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 359 RLTLGKPLGEGCFGQVVMAEAIGIDKdraakpvTVAVKML-KDDATDKDLSD-LVSEMEMMKMIgKHKNIINLLGACTQG 436
Cdd:cd14663   1 RYELGRTLGEGTFAKVKFARNTKTGE-------SVAIKIIdKEQVAREGMVEqIKREIAIMKLL-RHPNIVELHEVMATK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 437 GPLYVLVEYAAKGNLREFLRARRPpgldysfdtckppeeqltFKDLVSCAY--QVARGMEYLASQKCIHRDLAARNVLVT 514
Cdd:cd14663  73 TKIFFVMELVTGGELFSKIAKNGR------------------LKEDKARKYfqQLIDAVDYCHSRGVFHRDLKPENLLLD 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 515 EDNVMKIADFGL-ARDVHNL-DYYKKTTNGRlPvKWMAPEALFDRVYT-HQSDVWSFGVLLWEIFTlGGSPYPGIPVEEL 591
Cdd:cd14663 135 EDGNLKISDFGLsALSEQFRqDGLLHTTCGT-P-NYVAPEVLARRGYDgAKADIWSCGVILFVLLA-GYLPFDDENLMAL 211
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 13112048 592 FKLLKEGhRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVED 635
Cdd:cd14663 212 YRKIMKG-EFEYPRWFSPGAKSLIKRILDPNPSTRITVEQIMAS 254
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
392-577 5.37e-16

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: 78.91  E-value: 5.37e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 392 TVAVKMLKDdaTDKDlsDLVSEMEMMKMIG-KHKNIINLLGACTQGGPLYV---LV-EYAAKGNLREFLRARrppgldys 466
Cdd:cd14053  20 LVAVKIFPL--QEKQ--SWLTEREIYSLPGmKHENILQFIGAEKHGESLEAeywLItEFHERGSLCDYLKGN-------- 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 467 fdtckppeeQLTFKDLVSCAYQVARGMEYL---------ASQKCI-HRDLAARNVLVTEDNVMKIADFGLARdvhNLDYY 536
Cdd:cd14053  88 ---------VISWNELCKIAESMARGLAYLhedipatngGHKPSIaHRDFKSKNVLLKSDLTACIADFGLAL---KFEPG 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 13112048 537 KKTTNGRLPV---KWMAPEAL-----FDRVYTHQSDVWSFGVLLWEIFT 577
Cdd:cd14053 156 KSCGDTHGQVgtrRYMAPEVLegainFTRDAFLRIDMYAMGLVLWELLS 204
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
359-636 6.35e-16

Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GAK, also called auxilin-2, contains an N-terminal kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2. In addition, it contains an auxilin-1-like domain structure consisting of PTEN-like, clathrin-binding, and J domains. Like auxilin-1, GAK facilitates Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, unlike auxilin-1 which is nerve-specific. GAK also plays regulatory roles outside of clathrin-mediated membrane traffic including the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses through interaction with the interleukin 12 receptor. It also interacts with the androgen receptor, acting as a transcriptional coactivator, and its expression is significantly increased with the progression of prostate cancer. The GAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 78.71  E-value: 6.35e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 359 RLTLGKPLGEGCFGQVVMAEAIGIDKDRAAKPVtvavkMLKDDATDKDLsdlVSEMEMMKMIGKHKNIINLLGACT---- 434
Cdd:cd14036   1 KLRIKRVIAEGGFAFVYEAQDVGTGKEYALKRL-----LSNEEEKNKAI---IQEINFMKKLSGHPNIVQFCSAASigke 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 435 ---QGGPLYVLVEYAAKGNLREFLRARRPPGlDYSFDTckppeeqltfkdLVSCAYQVARGMEYLASQK--CIHRDLAAR 509
Cdd:cd14036  73 esdQGQAEYLLLTELCKGQLVDFVKKVEAPG-PFSPDT------------VLKIFYQTCRAVQHMHKQSppIIHRDLKIE 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 510 NVLVTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVK----------WMAPEALfdRVY-----THQSDVWSFGVLLWE 574
Cdd:cd14036 140 NLLIGNQGQIKLCDFGSATTEAHYPDYSWSAQKRSLVEdeitrnttpmYRTPEMI--DLYsnypiGEKQDIWALGCILYL 217
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13112048 575 IFtlggspYPGIPVEELFKL-LKEGH----RMDKPANCTHDLymiMRECWHAAPSQRPTFKQLVEDL 636
Cdd:cd14036 218 LC------FRKHPFEDGAKLrIINAKytipPNDTQYTVFHDL---IRSTLKVNPEERLSITEIVEQL 275
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
384-634 6.75e-16

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: 78.47  E-value: 6.75e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 384 KDRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQggPLYVLVEYAAKGNLREFLRARRPPGl 463
Cdd:cd14067  31 KKRTDGSADTMLKHLRAADAMKNFSEFRQEASMLHSL-QHPCIVYLIGISIH--PLCFALELAPLGSLNTVLEENHKGS- 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 464 dySFdtcKPPEEQLTFKdlvsCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNV-----MKIADFGLARDVHNldyykk 538
Cdd:cd14067 107 --SF---MPLGHMLTFK----IAYQIAAGLAYLHKKNIIFCDLKSDNILVWSLDVqehinIKLSDYGISRQSFH------ 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 539 ttNGRLPVK----WMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEELFKLLKEGHR--MDKPANCT-HDL 611
Cdd:cd14067 172 --EGALGVEgtpgYQAPEIRPRIVYDEKVDMFSYGMVLYELLS-GQRPSLGHHQLQIAKKLSKGIRpvLGQPEEVQfFRL 248
                       250       260
                ....*....|....*....|...
gi 13112048 612 YMIMRECWHAAPSQRPTFKQLVE 634
Cdd:cd14067 249 QALMMECWDTKPEKRPLACSVVE 271
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
364-585 9.42e-16

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: 78.99  E-value: 9.42e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVMAEAI-GIDKDRaakpvTVAVKMLKDDA---TDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPL 439
Cdd:cd05584   2 KVLGKGGYGKVFQVRKTtGSDKGK-----IFAMKVLKKASivrNQKDTAHTKAERNILEAV-KHPFIVDLHYAFQTGGKL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 440 YVLVEYAAKGNLREFLrarrppgldysfdtckppEEQLTFKDLVSCAY--QVARGMEYLASQKCIHRDLAARNVLVTEDN 517
Cdd:cd05584  76 YLILEYLSGGELFMHL------------------EREGIFMEDTACFYlaEITLALGHLHSLGIIYRDLKPENILLDAQG 137
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13112048 518 VMKIADFGLARDVHNLDYYKKTTNGrlPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPG 585
Cdd:cd05584 138 HVKLTDFGLCKESIHDGTVTHTFCG--TIEYMAPEILTRSGHGKAVDWWSLGALMYDMLT-GAPPFTA 202
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
364-628 9.78e-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: 78.29  E-value: 9.78e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVMAEAIGIDkdraakpvtVAVKMLkddATDKDLSdLVSEMEMMK-MIGKHKNIINLL-------GACTQ 435
Cdd:cd14144   1 RSVGKGRYGEVWKGKWRGEK---------VAVKIF---FTTEEAS-WFRETEIYQtVLMRHENILGFIaadikgtGSWTQ 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 436 ggpLYVLVEYAAKGNLREFLRArrppgldysfdtckppeEQLTFKDLVSCAYQVARGMEYLASQKC--------IHRDLA 507
Cdd:cd14144  68 ---LYLITDYHENGSLYDFLRG-----------------NTLDTQSMLKLAYSAACGLAHLHTEIFgtqgkpaiAHRDIK 127
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 508 ARNVLVTEDNVMKIADFGLA-RDVHNLDYYKKTTNGRLPVK-WMAPEAL--------FDRVytHQSDVWSFGVLLWEIFT 577
Cdd:cd14144 128 SKNILVKKNGTCCIADLGLAvKFISETNEVDLPPNTRVGTKrYMAPEVLdeslnrnhFDAY--KMADMYSFGLVLWEIAR 205
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13112048 578 LGGSP----------YPGIPVEELFKLLK-----EGHRMDKPANCTHDLYM-----IMRECWHAAPSQRPT 628
Cdd:cd14144 206 RCISGgiveeyqlpyYDAVPSDPSYEDMRrvvcvERRRPSIPNRWSSDEVLrtmskLMSECWAHNPAARLT 276
PTK_Jak2_rpt1 cd05078
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely ...
366-637 1.04e-15

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: 77.68  E-value: 1.04e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKDRAAKPVTVAVKMLkdDATDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd05078   7 LGQGTFTKIFKGIRREVGDYGQLHETEVLLKVL--DKAHRNYSESFFEAASMMSQLSHKHLVLNYGVCVCGDENILVQEY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLREFLRARRPPgldysfdtckppeEQLTFKdlVSCAYQVARGMEYLASQKCIHRDLAARNVLVT--EDN------ 517
Cdd:cd05078  85 VKFGSLDTYLKKNKNC-------------INILWK--LEVAKQLAWAMHFLEEKTLVHGNVCAKNILLIreEDRktgnpp 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 518 VMKIADFGLARDVHNLDYYKKttngRLPvkWMAPEALFD-RVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLK 596
Cdd:cd05078 150 FIKLSDPGISITVLPKDILLE----RIP--WVPPECIENpKNLSLATDKWSFGTTLWEICSGGDKPLSALDSQRKLQFYE 223
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 13112048 597 EGHRMdkPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLD 637
Cdd:cd05078 224 DRHQL--PAPKWTELANLINNCMDYEPDHRPSFRAIIRDLN 262
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
366-596 1.12e-15

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: 77.93  E-value: 1.12e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAeaigidKDRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd07860   8 IGEGTYGVVYKA------RNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKEL-NHPNIVKLLDVIHTENKLYLVFEF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKgNLREFLRARRPPGLDYSFdtckppeeqltfkdLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFG 525
Cdd:cd07860  81 LHQ-DLKKFMDASALTGIPLPL--------------IKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFG 145
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13112048 526 LAR--DVHNLDYykktTNGRLPVKWMAPEALFD-RVYTHQSDVWSFGVLLWEIFTLgGSPYPG-IPVEELFKLLK 596
Cdd:cd07860 146 LARafGVPVRTY----THEVVTLWYRAPEILLGcKYYSTAVDIWSLGCIFAEMVTR-RALFPGdSEIDQLFRIFR 215
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
366-628 1.37e-15

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: 77.80  E-value: 1.37e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEaigIDKDRAAKPVTVAVKMLKDD--ATDKDLSDLVSEMEMmkmigKHKNIINLLGACTQGGPL---- 439
Cdd:cd14055   3 VGKGRFAEVWKAK---LKQNASGQYETVAVKIFPYEeyASWKNEKDIFTDASL-----KHENILQFLTAEERGVGLdrqy 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 440 YVLVEYAAKGNLREFLRaRRPpgldysfdtckppeeqLTFKDLVSCAYQVARGMEYLAS-------QK--CIHRDLAARN 510
Cdd:cd14055  75 WLITAYHENGSLQDYLT-RHI----------------LSWEDLCKMAGSLARGLAHLHSdrtpcgrPKipIAHRDLKSSN 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 511 VLVTEDNVMKIADFGLARDVHNLDYYKKTTN-GRL-PVKWMAPEALFDRVYTH------QSDVWSFGVLLWEIF----TL 578
Cdd:cd14055 138 ILVKNDGTCVLADFGLALRLDPSLSVDELANsGQVgTARYMAPEALESRVNLEdlesfkQIDVYSMALVLWEMAsrceAS 217
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13112048 579 G---------GSPYPGIPVEELFK--LLKEGHRMDKPAN-CTHD----LYMIMRECWHAAPSQRPT 628
Cdd:cd14055 218 GevkpyelpfGSKVRERPCVESMKdlVLRDRGRPEIPDSwLTHQgmcvLCDTITECWDHDPEARLT 283
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
393-639 1.37e-15

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: 77.14  E-value: 1.37e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 393 VAVKMLK-DDATDKDLSDLVSEMEMMKmIGKHKNIINLLGACTQGGPLYVLVEYAAKGNLREFLRArrppGLDYSFDTCK 471
Cdd:cd14057  21 IVAKILKvRDVTTRISRDFNEEYPRLR-IFSHPNVLPVLGACNSPPNLVVISQYMPYGSLYNVLHE----GTGVVVDQSQ 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 472 ppeeqltfkdLVSCAYQVARGMEYLAS-QKCIHR-DLAARNVLVTEDNVMKIAdfglARDVHnldyYKKTTNGRL--PVk 547
Cdd:cd14057  96 ----------AVKFALDIARGMAFLHTlEPLIPRhHLNSKHVMIDEDMTARIN----MADVK----FSFQEPGKMynPA- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 548 WMAPEALF---DRVYTHQSDVWSFGVLLWEIFTLgGSPYPGI-PVEELFKLLKEGHRMDKPANCTHDLYMIMRECWHAAP 623
Cdd:cd14057 157 WMAPEALQkkpEDINRRSADMWSFAILLWELVTR-EVPFADLsNMEIGMKIALEGLRVTIPPGISPHMCKLMKICMNEDP 235
                       250
                ....*....|....*.
gi 13112048 624 SQRPTFKQLVEDLDRV 639
Cdd:cd14057 236 GKRPKFDMIVPILEKM 251
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
411-590 1.42e-15

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: 77.79  E-value: 1.42e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 411 VSEMEMMKMIG-KHKNIINLLGAC----TQGGPLYVLV-EYAAKGNLREFLRarrppgldysfdtckppEEQLTFKDLVS 484
Cdd:cd14054  35 QNEKDIYELPLmEHSNILRFIGADerptADGRMEYLLVlEYAPKGSLCSYLR-----------------ENTLDWMSSCR 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 485 CAYQVARGMEYLAS--------QKCI-HRDLAARNVLVTEDNVMKIADFGLARDVHNLDYYK--------KTTNGRLPVK 547
Cdd:cd14054  98 MALSLTRGLAYLHTdlrrgdqyKPAIaHRDLNSRNVLVKADGSCVICDFGLAMVLRGSSLVRgrpgaaenASISEVGTLR 177
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 13112048 548 WMAPEALFDRV-------YTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEE 590
Cdd:cd14054 178 YMAPEVLEGAVnlrdcesALKQVDVYALGLVLWEIAMRCSDLYPGESVPP 227
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
359-596 1.58e-15

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: 78.21  E-value: 1.58e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 359 RLTLGKPLGEGCFGQVVMAEAIGIDKDraakpVTVAVKMLKDDATDKDLSD-LVSEMEMMKMIGKHKNIINL--LGACTQ 435
Cdd:cd07857   1 RYELIKELGQGAYGIVCSARNAETSEE-----ETVAIKKITNVFSKKILAKrALRELKLLRHFRGHKNITCLydMDIVFP 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 436 GG--PLYvLVEYAAKGNLREFLRArrppgldysfdtckppEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLV 513
Cdd:cd07857  76 GNfnELY-LYEELMEADLHQIIRS----------------GQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLV 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 514 TEDNVMKIADFGLARDVH-----NLDYYKKTTNGRlpvkWM-APEALFD-RVYTHQSDVWSFGVLLWEIftLGGSP-YPG 585
Cdd:cd07857 139 NADCELKICDFGLARGFSenpgeNAGFMTEYVATR----WYrAPEIMLSfQSYTKAIDVWSVGCILAEL--LGRKPvFKG 212
                       250
                ....*....|..
gi 13112048 586 IP-VEELFKLLK 596
Cdd:cd07857 213 KDyVDQLNQILQ 224
PTK_Jak1_rpt1 cd05077
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely ...
360-637 1.62e-15

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: 77.28  E-value: 1.62e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 360 LTLGKPLGEGCFGQVVMAEAIGIDKDRA-----AKPVTVAVKMLkdDATDKDLSDLVSEM-EMMKMIgKHKNIINLLGAC 433
Cdd:cd05077   1 IVQGEHLGRGTRTQIYAGILNYKDDDEDegysyEKEIKVILKVL--DPSHRDISLAFFETaSMMRQV-SHKHIVLLYGVC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 434 TQGGPLYVLVEYAAKGNLREFLRARRPPgldysfdtckppeeqLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLV 513
Cdd:cd05077  78 VRDVENIMVEEFVEFGPLDLFMHRKSDV---------------LTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNILL 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 514 TEDNV-------MKIADFGLARDVHNldyyKKTTNGRLPvkWMAPEALFD-RVYTHQSDVWSFGVLLWEIFTLGGSPYPG 585
Cdd:cd05077 143 AREGIdgecgpfIKLSDPGIPITVLS----RQECVERIP--WIAPECVEDsKNLSIAADKWSFGTTLWEICYNGEIPLKD 216
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 13112048 586 IPVEELFKLLkEGHRMDKPANCThDLYMIMRECWHAAPSQRPTFKQLVEDLD 637
Cdd:cd05077 217 KTLAEKERFY-EGQCMLVTPSCK-ELADLMTHCMNYDPNQRPFFRAIMRDIN 266
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
469-635 1.66e-15

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: 77.40  E-value: 1.66e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 469 TCKPPEEQLT---FKDLVscayqvaRGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARDVHNLDYYKKTTNGRlP 545
Cdd:cd14118 108 TDNPLSEETArsyFRDIV-------LGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIADFGVSNEFEGDDALLSSTAGT-P 179
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 546 VkWMAPEALF---DRVYTHQSDVWSFGVLLWeIFTLGGSPYPGIPVEELFKLLKEGHRM--DKPaNCTHDLYMIMRECWH 620
Cdd:cd14118 180 A-FMAPEALSesrKKFSGKALDIWAMGVTLY-CFVFGRCPFEDDHILGLHEKIKTDPVVfpDDP-VVSEQLKDLILRMLD 256
                       170
                ....*....|....*
gi 13112048 621 AAPSQRPTFKQLVED 635
Cdd:cd14118 257 KNPSERITLPEIKEH 271
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
366-597 1.71e-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: 1.71e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKdraakpvTVAVKM--LKDDATDKDLSDLVSEMEMMKMIgKHKNIINllgACTQGGPLYVL- 442
Cdd:cd13989   1 LGSGGFGYVTLWKHQDTGE-------YVAIKKcrQELSPSDKNRERWCLEVQIMKKL-NHPNVVS---ARDVPPELEKLs 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 443 --------VEYAAKGNLREFL-RARRPPGLdysfdtckppeEQLTFKDLVScayQVARGMEYLASQKCIHRDLAARNVLV 513
Cdd:cd13989  70 pndlpllaMEYCSGGDLRKVLnQPENCCGL-----------KESEVRTLLS---DISSAISYLHENRIIHRDLKPENIVL 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 514 TEDN---VMKIADFGLARDvhnLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPY-PGIPVE 589
Cdd:cd13989 136 QQGGgrvIYKLIDLGYAKE---LDQGSLCTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECIT-GYRPFlPNWQPV 211

                ....*...
gi 13112048 590 ELFKLLKE 597
Cdd:cd13989 212 QWHGKVKQ 219
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
362-583 1.78e-15

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: 77.21  E-value: 1.78e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 362 LGKPLGEGCFGQVVMAeaigidKDRAAKpVTVAVKMLKDDATDKDLSD--LVSEMEMMKMIgKHKNIINLLGACTQGGPL 439
Cdd:cd14117  10 IGRPLGKGKFGNVYLA------REKQSK-FIVALKVLFKSQIEKEGVEhqLRREIEIQSHL-RHPNILRLYNYFHDRKRI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 440 YVLVEYAAKGNL-REFLRARRppgldysFDtckppeEQLTfkdlVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNV 518
Cdd:cd14117  82 YLILEYAPRGELyKELQKHGR-------FD------EQRT----ATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGE 144
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13112048 519 MKIADFGLArdVHNLDYYKKTTNGRLpvKWMAPEALFDRVYTHQSDVWSFGVLLWEiFTLGGSPY 583
Cdd:cd14117 145 LKIADFGWS--VHAPSLRRRTMCGTL--DYLPPEMIEGRTHDEKVDLWCIGVLCYE-LLVGMPPF 204
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
353-585 2.26e-15

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: 78.17  E-value: 2.26e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 353 WELSRaRLTLGKPLGEGCFGQVVMAeaigIDKDRAAKpvtVAVKMLKddatdKDLSDLV------SEMEMMKMIgKHKNI 426
Cdd:cd07878  11 WEVPE-RYQNLTPVGSGAYGSVCSA----YDTRLRQK---VAVKKLS-----RPFQSLIharrtyRELRLLKHM-KHENV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 427 INLLGACTQGGPLYVLVEYAAKGNLReflrarrppGLDYS-FDTCkppeEQLTFKDLVSCAYQVARGMEYLASQKCIHRD 505
Cdd:cd07878  77 IGLLDVFTPATSIENFNEVYLVTNLM---------GADLNnIVKC----QKLSDEHVQFLIYQLLRGLKYIHSAGIIHRD 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 506 LAARNVLVTEDNVMKIADFGLARDVHNldyykkTTNGRLPVKWM-APEALFDRVYTHQS-DVWSFGVLLWEIFTlGGSPY 583
Cdd:cd07878 144 LKPSNVAVNEDCELRILDFGLARQADD------EMTGYVATRWYrAPEIMLNWMHYNQTvDIWSVGCIMAELLK-GKALF 216

                ..
gi 13112048 584 PG 585
Cdd:cd07878 217 PG 218
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
360-634 2.60e-15

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: 77.08  E-value: 2.60e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 360 LTLGKpLGEGCFGQVVMAeaigidKDRAAKPVtVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACT--QGG 437
Cdd:cd06621   4 VELSS-LGEGAGGSVTKC------RLRNTKTI-FALKTITTDPNPDVQKQILRELEINKSC-ASPYIVKYYGAFLdeQDS 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 438 PLYVLVEYAAKGNLREFLRARRPPGLdysfdtckppeeQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDN 517
Cdd:cd06621  75 SIGIAMEYCEGGSLDSIYKKVKKKGG------------RIGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKG 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 518 VMKIADFGLARD-VHNLDyykKTTNGrlPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIfTLGGSPYP--GIPVEELFKL 594
Cdd:cd06621 143 QVKLCDFGVSGElVNSLA---GTFTG--TSYYMAPERIQGGPYSITSDVWSLGLTLLEV-AQNRFPFPpeGEPPLGPIEL 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 13112048 595 LKEGHRM------DKPANC---THDLYMIMRECWHAAPSQRPTFKQLVE 634
Cdd:cd06621 217 LSYIVNMpnpelkDEPENGikwSESFKDFIEKCLEKDGTRRPGPWQMLA 265
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
362-634 2.62e-15

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: 76.72  E-value: 2.62e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 362 LGKPLGEGCFGQVVMAEAIGIDKDRAAKPVTVAVK-MLKDDATDKDLSDLVSEMEMMK-----MIGKHKNIINLLGACTQ 435
Cdd:cd14077   5 FVKTIGAGSMGKVKLAKHIRTGEKCAIKIIPRASNaGLKKEREKRLEKEISRDIRTIReaalsSLLNHPHICRLRDFLRT 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 436 GGPLYVLVEYAAKGNLreflrarrppgLDYSFDTCKPPEEQLTfkdlvSCAYQVARGMEYLASQKCIHRDLAARNVLVTE 515
Cdd:cd14077  85 PNHYYMLFEYVDGGQL-----------LDYIISHGKLKEKQAR-----KFARQIASALDYLHRNSIVHRDLKIENILISK 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 516 DNVMKIADFGLArdvhNLDYYKK---TTNGRLpvKWMAPEALFDRVYTH-QSDVWSFGVLLWeIFTLGGSPYPGIPVEEL 591
Cdd:cd14077 149 SGNIKIIDFGLS----NLYDPRRllrTFCGSL--YFAAPELLQAQPYTGpEVDVWSFGVVLY-VLVCGKVPFDDENMPAL 221
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 13112048 592 FKLLKEGhRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVE 634
Cdd:cd14077 222 HAKIKKG-KVEYPSYLSSECKSLISRMLVVDPKKRATLEQVLN 263
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
366-595 2.81e-15

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: 76.97  E-value: 2.81e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKdraakpvTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd07873  10 LGEGTYATVYKGRSKLTDN-------LVALKEIRLEHEEGAPCTAIREVSLLKDL-KHANIVTLHDIIHTEKSLTLVFEY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKgNLREFLrarrppgldysfDTCKppeEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFG 525
Cdd:cd07873  82 LDK-DLKQYL------------DDCG---NSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFG 145
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13112048 526 LARdvhNLDYYKKTTNGRLPVKWMAPEALF--DRVYTHQSDVWSFGVLLWEIFTlgGSP-YPGIPVEE----LFKLL 595
Cdd:cd07873 146 LAR---AKSIPTKTYSNEVVTLWYRPPDILlgSTDYSTQIDMWGVGCIFYEMST--GRPlFPGSTVEEqlhfIFRIL 217
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
366-604 3.04e-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: 76.22  E-value: 3.04e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKdraakpvTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd14167  11 LGTGAFSEVVLAEEKRTQK-------LVAIKCIAKKALEGKETSIENEIAVLHKI-KHPNIVALDDIYESGGHLYLIMQL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLreFLRArrppgLDYSFdtckppeeqLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVL---VTEDNVMKIA 522
Cdd:cd14167  83 VSGGEL--FDRI-----VEKGF---------YTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMIS 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 523 DFGLARdVHNLDYYKKTTNGRlPvKWMAPEALFDRVYTHQSDVWSFGVLLWeIFTLGGSPYPGIPVEELF-KLLKEGHRM 601
Cdd:cd14167 147 DFGLSK-IEGSGSVMSTACGT-P-GYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDAKLFeQILKAEYEF 222

                ...
gi 13112048 602 DKP 604
Cdd:cd14167 223 DSP 225
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
366-574 3.16e-15

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: 76.88  E-value: 3.16e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEaigiDKDRAAKpvtVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINllgACTQGGPLYVLV-- 443
Cdd:cd14039   1 LGTGGFGNVCLYQ----NQETGEK---IAIKSCRLELSVKNKDRWCHEIQIMKKL-NHPNVVK---ACDVPEEMNFLVnd 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 444 ------EYAAKGNLREFLRarRPPgldysfDTCKPPEEQLtfkdlVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDN 517
Cdd:cd14039  70 vpllamEYCSGGDLRKLLN--KPE------NCCGLKESQV-----LSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEIN 136
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 518 ---VMKIADFGLARDvhnLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWE 574
Cdd:cd14039 137 gkiVHKIIDLGYAKD---LDQGSLCTSFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFE 193
I-set pfam07679
Immunoglobulin I-set domain;
171-245 3.83e-15

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 71.13  E-value: 3.83e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13112048   171 TVRFRCPAAGNPTPSISWLKNGREFRGEHRIgGIKLRHQQWSLVMESVVPSDRGNYTCVVENKFGSIRQTYTLDV 245
Cdd:pfam07679  17 SARFTCTVTGTPDPEVSWFKDGQPLRSSDRF-KVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
171-245 3.84e-15

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 71.00  E-value: 3.84e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13112048    171 TVRFRCPAAGNPTPSISWLKNGREFRGEHRIGGIKLRHQQWSLVMESVVPSDRGNYTCVVENKFGSIRQTYTLDV 245
Cdd:smart00410  11 SVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
366-634 4.00e-15

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: 76.56  E-value: 4.00e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEaigiDKDRAAKpvtVAVKMLkDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd06659  29 IGEGSTGVVCIAR----EKHSGRQ---VAVKMM-DLRKQQRRELLFNEVVIMRDY-QHPNVVEMYKSYLVGEELWVLMEY 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLREFLRARRPpGLDYSFDTCKPPEEQLTfkdlvscayqvargmeYLASQKCIHRDLAARNVLVTEDNVMKIADFG 525
Cdd:cd06659 100 LQGGALTDIVSQTRL-NEEQIATVCEAVLQALA----------------YLHSQGVIHRDIKSDSILLTLDGRVKLSDFG 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 526 LARDVHNlDYYKKTTNGRLPVkWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPY-PGIPVEELFKL-------LKE 597
Cdd:cd06659 163 FCAQISK-DVPKRKSLVGTPY-WMAPEVISRCPYGTEVDIWSLGIMVIEMVD-GEPPYfSDSPVQAMKRLrdspppkLKN 239
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 13112048 598 GHRMdKPANCTHDLYMIMREcwhaaPSQRPTFKQLVE 634
Cdd:cd06659 240 SHKA-SPVLRDFLERMLVRD-----PQERATAQELLD 270
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
364-574 4.82e-15

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: 75.87  E-value: 4.82e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVMAEAIgIDKDRaakpvtVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLV 443
Cdd:cd14046  12 QVLGKGAFGQVVKVRNK-LDGRY------YAIKKIKLRSESKNNSRILREVMLLSRL-NHQHVVRYYQAWIERANLYIQM 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 444 EYAAKGNLREFLRArrppGLDYSFDtckppeeqltfkDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIAD 523
Cdd:cd14046  84 EYCEKSTLRDLIDS----GLFQDTD------------RLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGD 147
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13112048 524 FGLARDVH------NLDYYKKTTNGRLPVK----------WMAPEAL--FDRVYTHQSDVWSFGVLLWE 574
Cdd:cd14046 148 FGLATSNKlnvelaTQDINKSTSAALGSSGdltgnvgtalYVAPEVQsgTKSTYNEKVDMYSLGIIFFE 216
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
366-596 4.84e-15

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: 76.17  E-value: 4.84e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAeaigidKDRAAKPVtVAVKMLKDDATDKDL-SDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVE 444
Cdd:cd07835   7 IGEGTYGVVYKA------RDKLTGEI-VALKKIRLETEDEGVpSTAIREISLLKEL-NHPNIVRLLDVVHSENKLYLVFE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 445 YAAKgNLREFLrarrppgldysfDTCkpPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADF 524
Cdd:cd07835  79 FLDL-DLKKYM------------DSS--PLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADF 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 525 GLARDVHnldyykkttngrLPVK---------WM-APEALF-DRVYTHQSDVWSFGVLLWEIFTlgGSP-YPG-IPVEEL 591
Cdd:cd07835 144 GLARAFG------------VPVRtythevvtlWYrAPEILLgSKHYSTPVDIWSVGCIFAEMVT--RRPlFPGdSEIDQL 209

                ....*
gi 13112048 592 FKLLK 596
Cdd:cd07835 210 FRIFR 214
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
345-634 4.86e-15

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: 76.18  E-value: 4.86e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 345 LELPADPK--WELSRArltlgkpLGEGCFGQVVmaeAIGIDKDRAakpvTVAVKMLkDDATDKDlSDLVSEMEMMKMIGK 422
Cdd:cd06639  14 LESLADPSdtWDIIET-------IGKGTYGKVY---KVTNKKDGS----LAAVKIL-DPISDVD-EEIEAEYNILRSLPN 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 423 HKNIINLLGACTQ-----GGPLYVLVEYAAKGNLREFLRA--RRPPGLDysfdtckppEEQLTFkdlvsCAYQVARGMEY 495
Cdd:cd06639  78 HPNVVKFYGMFYKadqyvGGQLWLVLELCNGGSVTELVKGllKCGQRLD---------EAMISY-----ILYGALLGLQH 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 496 LASQKCIHRDLAARNVLVTEDNVMKIADFGLARDVHNLDYYKKTTNGRlPVkWMAPEAL-----FDRVYTHQSDVWSFGV 570
Cdd:cd06639 144 LHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSARLRRNTSVGT-PF-WMAPEVIaceqqYDYSYDARCDVWSLGI 221
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13112048 571 LLWEIFTlGGSPYPGI-PVEELFKLLKE-GHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVE 634
Cdd:cd06639 222 TAIELAD-GDPPLFDMhPVKALFKIPRNpPPTLLNPEKWCRGFSHFISQCLIKDFEKRPSVTHLLE 286
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
388-633 5.10e-15

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: 76.21  E-value: 5.10e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 388 AKPVTVAVKMLkddatDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYVLVEYAAKGNLRE-FLRARrppgldys 466
Cdd:cd14178  26 ATSTEYAVKII-----DKSKRDPSEEIEILLRYGQHPNIITLKDVYDDGKFVYLVMELMRGGELLDrILRQK-------- 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 467 fdtCKPPEEqltfKDLVSCAyqVARGMEYLASQKCIHRDLAARNVLVTEDN----VMKIADFGLARDVhnldyykKTTNG 542
Cdd:cd14178  93 ---CFSERE----ASAVLCT--ITKTVEYLHSQGVVHRDLKPSNILYMDESgnpeSIRICDFGFAKQL-------RAENG 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 543 RL-----PVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIP---VEELF------KLLKEGHRMDKPANCT 608
Cdd:cd14178 157 LLmtpcyTANFVAPEVLKRQGYDAACDIWSLGILLYTMLA-GFTPFANGPddtPEEILarigsgKYALSGGNWDSISDAA 235
                       250       260
                ....*....|....*....|....*
gi 13112048 609 HDlymIMRECWHAAPSQRPTFKQLV 633
Cdd:cd14178 236 KD---IVSKMLHVDPHQRLTAPQVL 257
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
362-577 5.75e-15

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: 76.20  E-value: 5.75e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 362 LGKpLGEGCFGQVVMAEAIGIDKDRAAKPVTVAvkmlkddaTDKDLSDLVS--EMEMMKMIgKHKNIINLLGactqggpl 439
Cdd:cd07866  13 LGK-LGEGTFGEVYKARQIKTGRVVALKKILMH--------NEKDGFPITAlrEIKILKKL-KHPNVVPLID-------- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 440 yVLVEYAAKgnlreflRARRPPgldySFDTCKP------------PEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLA 507
Cdd:cd07866  75 -MAVERPDK-------SKRKRG----SVYMVTPymdhdlsgllenPSVKLTESQIKCYMLQLLEGINYLHENHILHRDIK 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 508 ARNVLVTEDNVMKIADFGLARdvhnlDYYKKTTNGRLP-------------VKWM-APEALF-DRVYTHQSDVWSFGVLL 572
Cdd:cd07866 143 AANILIDNQGILKIADFGLAR-----PYDGPPPNPKGGggggtrkytnlvvTRWYrPPELLLgERRYTTAVDIWGIGCVF 217

                ....*
gi 13112048 573 WEIFT 577
Cdd:cd07866 218 AEMFT 222
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
394-634 7.73e-15

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: 75.82  E-value: 7.73e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 394 AVKMLkddatDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYVLVEYAAKGNLRE-FLRarrppgldysfdtckp 472
Cdd:cd14177  33 AVKII-----DKSKRDPSEEIEILMRYGQHPNIITLKDVYDDGRYVYLVTELMKGGELLDrILR---------------- 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 473 pEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTED----NVMKIADFGLARDVhnldyykKTTNGRL---- 544
Cdd:cd14177  92 -QKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDDsanaDSIRICDFGFAKQL-------RGENGLLltpc 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 545 -PVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPY---PGIPVEELF------KLLKEGHRMDKPANCTHDLYMI 614
Cdd:cd14177 164 yTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLA-GYTPFangPNDTPEEILlrigsgKFSLSGGNWDTVSDAAKDLLSH 242
                       250       260
                ....*....|....*....|
gi 13112048 615 MrecWHAAPSQRPTFKQLVE 634
Cdd:cd14177 243 M---LHVDPHQRYTAEQVLK 259
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
348-635 7.80e-15

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: 75.46  E-value: 7.80e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 348 PADPkwelsRARLTLGKPLGEGCFGQVVMAEAIGIDKDRAAKpvtvavKMLKDDATDKDLsdLVSEMEMMKMIgKHKNII 427
Cdd:cd06658  17 PGDP-----REYLDSFIKIGEGSTGIVCIATEKHTGKQVAVK------KMDLRKQQRREL--LFNEVVIMRDY-HHENVV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 428 NLLGACTQGGPLYVLVEYAAKGNLREFLRARRPPgldysfdtckppEEQLTfkdlvSCAYQVARGMEYLASQKCIHRDLA 507
Cdd:cd06658  83 DMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMN------------EEQIA-----TVCLSVLRALSYLHNQGVIHRDIK 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 508 ARNVLVTEDNVMKIADFGLARDVHNLDYYKKTTNGrlPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIP 587
Cdd:cd06658 146 SDSILLTSDGRIKLSDFGFCAQVSKEVPKRKSLVG--TPYWMAPEVISRLPYGTEVDIWSLGIMVIEMID-GEPPYFNEP 222
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 13112048 588 V--------EELFKLLKEGHRMDKPANCTHDLyMIMREcwhaaPSQRPTFKQLVED 635
Cdd:cd06658 223 PlqamrrirDNLPPRVKDSHKVSSVLRGFLDL-MLVRE-----PSQRATAQELLQH 272
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
366-583 8.63e-15

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: 74.95  E-value: 8.63e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAeaigIDKDRAakpVTVAVKMLKDD-ATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYV--L 442
Cdd:cd13983   9 LGRGSFKTVYRA----FDTEEG---IEVAWNEIKLRkLPKAERQRFKQEIEILKSL-KHPNIIKFYDSWESKSKKEVifI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 443 VEYAAKGNLREFLRARRPPGLdysfdtckppeeqltfKDLVSCAYQVARGMEYLASQK--CIHRDLAARNVLVT-EDNVM 519
Cdd:cd13983  81 TELMTSGTLKQYLKRFKRLKL----------------KVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFINgNTGEV 144
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13112048 520 KIADFGLArdVHNLDYYKKTTNGRLpvKWMAPEaLFDRVYTHQSDVWSFGVLLWEIFTlGGSPY 583
Cdd:cd13983 145 KIGDLGLA--TLLRQSFAKSVIGTP--EFMAPE-MYEEHYDEKVDIYAFGMCLLEMAT-GEYPY 202
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
362-573 1.03e-14

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: 74.83  E-value: 1.03e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 362 LGKPLGEGCFGQVvmaeAIGIDKDRAAK--PVTVAVKM-LKDDATDKD-LSDLVSEMEMMKMIGkHKNIINLLGACTQGG 437
Cdd:cd14076   5 LGRTLGEGEFGKV----KLGWPLPKANHrsGVQVAIKLiRRDTQQENCqTSKIMREINILKGLT-HPNIVRLLDVLKTKK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 438 PLYVLVEYAAKGNLREFLRARRppgldysfdTCKPPEEQLTFKDLVScayqvarGMEYLASQKCIHRDLAARNVLVTEDN 517
Cdd:cd14076  80 YIGIVLEFVSGGELFDYILARR---------RLKDSVACRLFAQLIS-------GVAYLHKKGVVHRDLKLENLLLDKNR 143
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 13112048 518 VMKIADFGLARDV-HNLDYYKKTTNGRlPVkWMAPE-ALFDRVYT-HQSDVWSFGVLLW 573
Cdd:cd14076 144 NLVITDFGFANTFdHFNGDLMSTSCGS-PC-YAAPElVVSDSMYAgRKADIWSCGVILY 200
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
341-634 1.29e-14

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO1 is sometimes referred to as prostate-derived sterile 20-like kinase 2 (PSK2). TAO1 activates the p38 MAPK through direct interaction with and activation of MEK3. TAO1 is highly expressed in the brain and may play a role in neuronal apoptosis. TAO1 interacts with the checkpoint proteins BubR1 and Mad2, and plays an important role in regulating mitotic progression, which is required for both chromosome congression and checkpoint-induced anaphase delay. TAO1 may play a role in protecting genomic stability. TAO proteins possess MAPK kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 75.47  E-value: 1.29e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 341 NVSELELPADPKWELSRARltlgkPLGEGCFGQVVMAEAIGIDKDRAAKPVTVAVKMlkddaTDKDLSDLVSEMEMMKMI 420
Cdd:cd06635  13 DIAELFFKEDPEKLFSDLR-----EIGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQ-----SNEKWQDIIKEVKFLQRI 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 421 gKHKNIINLLGACTQGGPLYVLVEYAAkGNLREFLRARRPPgldysfdtckppeeqLTFKDLVSCAYQVARGMEYLASQK 500
Cdd:cd06635  83 -KHPNSIEYKGCYLREHTAWLVMEYCL-GSASDLLEVHKKP---------------LQEIEIAAITHGALQGLAYLHSHN 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 501 CIHRDLAARNVLVTEDNVMKIADFGLARDVHNLDYYKKTTngrlpvKWMAPE---ALFDRVYTHQSDVWSFGVLLWEIFT 577
Cdd:cd06635 146 MIHRDIKAGNILLTEPGQVKLADFGSASIASPANSFVGTP------YWMAPEvilAMDEGQYDGKVDVWSLGITCIELAE 219
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 13112048 578 LGGSPYPGIPVEELFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVE 634
Cdd:cd06635 220 RKPPLFNMNAMSALYHIAQNESPTLQSNEWSDYFRNFVDSCLQKIPQDRPTSEELLK 276
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
172-242 1.31e-14

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 68.90  E-value: 1.31e-14
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13112048 172 VRFRCPAAGNPTPSISWLKNGREFRGEHRiGGIKLRHQQWSLVMESVVPSDRGNYTCVVENKFGSIRQTYT 242
Cdd:cd00096   1 VTLTCSASGNPPPTITWYKNGKPLPPSSR-DSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
362-577 1.33e-14

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: 74.31  E-value: 1.33e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 362 LGKPLGEGCFGQVVMAEAIGIDKDRAAKPVTVAVKMLKddaTDKDLSDLVSEMEMMKMIgKHKNIINLLGAC--TQGGPL 439
Cdd:cd06652   6 LGKLLGQGAFGRVYLCYDADTGRELAVKQVQFDPESPE---TSKEVNALECEIQLLKNL-LHERIVQYYGCLrdPQERTL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 440 YVLVEYAAKGNLREFLRArrppgldYSFDTckppeEQLTFKdlvsCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVM 519
Cdd:cd06652  82 SIFMEYMPGGSIKDQLKS-------YGALT-----ENVTRK----YTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNV 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13112048 520 KIADFGLARDVHNLDYykkTTNGRLPVK----WMAPEALFDRVYTHQSDVWSFGVLLWEIFT 577
Cdd:cd06652 146 KLGDFGASKRLQTICL---SGTGMKSVTgtpyWMSPEVISGEGYGRKADIWSVGCTVVEMLT 204
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
367-585 1.45e-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: 74.21  E-value: 1.45e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 367 GEGCFGQVVmaeaigIDKDRAAKPVtVAVK-MLKDDATDKD-LSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVE 444
Cdd:cd05578   9 GKGSFGKVC------IVQKKDTKKM-FAMKyMNKQKCIEKDsVRNVLNELEILQEL-EHPFLVNLWYSFQDEEDMYMVVD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 445 YAAKGNLREFLRARRPpgldysFDtckppEEQLTFkdLVSCayqVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADF 524
Cdd:cd05578  81 LLLGGDLRYHLQQKVK------FS-----EETVKF--YICE---IVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDF 144
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13112048 525 GLARDVHNlDYYKKTTNGRLPvkWMAPEALFDRVYTHQSDVWSFGVLLWEiFTLGGSPYPG 585
Cdd:cd05578 145 NIATKLTD-GTLATSTSGTKP--YMAPEVFMRAGYSFAVDWWSLGVTAYE-MLRGKRPYEI 201
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
413-583 1.71e-14

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK2, also called CaMKK beta, is one of the most versatile CaMKs. It is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. CaMKK2 contains unique N- and C-terminal domains and a central catalytic kinase domain that is followed by a regulatory domain that bears overlapping autoinhibitory and CaM-binding regions. It can be activated by signaling through G-coupled receptors, IP3 receptors, plasma membrane ion channels, and Toll-like receptors. Thus, CaMKK2 acts as a molecular hub that is capable of receiving and decoding signals from diverse pathways. The CaMKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 74.62  E-value: 1.71e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 413 EMEMMKMIgKHKNIINLLGACTQGGP--LYVLVEYAAKGNLREFlrarrppgldysfDTCKPPEE---QLTFKDLVscay 487
Cdd:cd14199  75 EIAILKKL-DHPNVVKLVEVLDDPSEdhLYMVFELVKQGPVMEV-------------PTLKPLSEdqaRFYFQDLI---- 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 488 qvaRGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARDVHNLDYYKKTTNGRlPVkWMAPEALFD--RVYTHQS-D 564
Cdd:cd14199 137 ---KGIEYLHYQKIIHRDVKPSNLLVGEDGHIKIADFGVSNEFEGSDALLTNTVGT-PA-FMAPETLSEtrKIFSGKAlD 211
                       170
                ....*....|....*....
gi 13112048 565 VWSFGVLLWeIFTLGGSPY 583
Cdd:cd14199 212 VWAMGVTLY-CFVFGQCPF 229
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
366-583 1.83e-14

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: 73.74  E-value: 1.83e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKDraakpvtVAVKMLKDDATDKD--LSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLV 443
Cdd:cd14186   9 LGKGSFACVYRARSLHTGLE-------VAIKMIDKKAMQKAgmVQRVRNEVEIHCQL-KHPSILELYNYFEDSNYVYLVL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 444 EYAAKGNLREFLRARRPPgldysfdtckppeeqLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIAD 523
Cdd:cd14186  81 EMCHNGEMSRYLKNRKKP---------------FTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIAD 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 524 FGLARDVHNLDYYKKTTNGRlPvKWMAPEALFDRVYTHQSDVWSFGVLLWeIFTLGGSPY 583
Cdd:cd14186 146 FGLATQLKMPHEKHFTMCGT-P-NYISPEIATRSAHGLESDVWSLGCMFY-TLLVGRPPF 202
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
366-634 1.94e-14

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. MAP4K3 is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. mTOR regulates ribosome biogenesis and protein translation, and is frequently deregulated in cancer. MAP4Ks are involved in MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 73.93  E-value: 1.94e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKdraakpvTVAVKMLKDDATDkDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd06645  19 IGSGTYGDVYKARNVNTGE-------LAAIKVIKLEPGE-DFAVVQQEIIMMKDC-KHSNIVAYFGSYLRRDKLWICMEF 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLREFLRARRPpgldysfdtckppeeqLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFG 525
Cdd:cd06645  90 CGGGSLQDIYHVTGP----------------LSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 526 LARDVHNLDYYKKTTNGRlPVkWMAPE-ALFDRV--YTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGH--- 599
Cdd:cd06645 154 VSAQITATIAKRKSFIGT-PY-WMAPEvAAVERKggYNQLCDIWAVGITAIELAELQPPMFDLHPMRALFLMTKSNFqpp 231
                       250       260       270
                ....*....|....*....|....*....|....*
gi 13112048 600 RMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVE 634
Cdd:cd06645 232 KLKDKMKWSNSFHHFVKMALTKNPKKRPTAEKLLQ 266
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
364-583 1.99e-14

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 75.02  E-value: 1.99e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048  364 KPLGEGCFGQVVMAEAigidKDRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLV 443
Cdd:PTZ00426  36 RTLGTGSFGRVILATY----KNEDFPPVAIKRFEKSKIIKQKQVDHVFSERKILNYI-NHPFCVNLYGSFKDESYLYLVL 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048  444 EYAAKGNLREFLRARRppgldysfdtckppeeqlTFKDLVSCAY--QVARGMEYLASQKCIHRDLAARNVLVTEDNVMKI 521
Cdd:PTZ00426 111 EFVIGGEFFTFLRRNK------------------RFPNDVGCFYaaQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKM 172
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13112048  522 ADFGLARDVHNLDYYKKTTNgrlpvKWMAPEALFDRVYTHQSDVWSFGVLLWEIFtLGGSPY 583
Cdd:PTZ00426 173 TDFGFAKVVDTRTYTLCGTP-----EYIAPEILLNVGHGKAADWWTLGIFIYEIL-VGCPPF 228
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
439-591 2.28e-14

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ULK4 is a functionally uncharacterized kinase that shows similarity to ATG1/ULKs. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. The ULK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270912 [Multi-domain]  Cd Length: 269  Bit Score: 73.87  E-value: 2.28e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 439 LYVLVEYAAKGNLREFLRArrppgldysfDTCKPPEEQLTFkdlvscAYQVARGMEYLASQKCIHRDLAARNVLVTEDNV 518
Cdd:cd14010  69 LWLVVEYCTGGDLETLLRQ----------DGNLPESSVRKF------GRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGT 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 519 MKIADFGLAR--------------DVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYP 584
Cdd:cd14010 133 LKLSDFGLARregeilkelfgqfsDEGNVNKVSKKQAKRGTPYYMAPELFQGGVHSFASDLWALGCVLYEMFT-GKPPFV 211

                ....*..
gi 13112048 585 GIPVEEL 591
Cdd:cd14010 212 AESFTEL 218
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
362-577 2.29e-14

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: 73.91  E-value: 2.29e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 362 LGKPLGEGCFGQVVMAEAIGIDKDRAAKPVTVAVKmlkDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACT--QGGPL 439
Cdd:cd06653   6 LGKLLGRGAFGEVYLCYDADTGRELAVKQVPFDPD---SQETSKEVNALECEIQLLKNL-RHDRIVQYYGCLRdpEEKKL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 440 YVLVEYAAKGNLREFLRArrppgldYSFDTckppeEQLTFKdlvsCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVM 519
Cdd:cd06653  82 SIFVEYMPGGSVKDQLKA-------YGALT-----ENVTRR----YTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNV 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13112048 520 KIADFGLARDVHNLDYYK---KTTNGRlPVkWMAPEALFDRVYTHQSDVWSFGVLLWEIFT 577
Cdd:cd06653 146 KLGDFGASKRIQTICMSGtgiKSVTGT-PY-WMSPEVISGEGYGRKADVWSVACTVVEMLT 204
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
353-577 2.55e-14

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: 74.99  E-value: 2.55e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 353 WELsRARLTLGKPLGEGCFGQVVMAeaigIDKDRAAKpvtVAVKMLKDDATdkdlSDLVS-----EMEMMKMIgKHKNII 427
Cdd:cd07880  11 WEV-PDRYRDLKQVGSGAYGTVCSA----LDRRTGAK---VAIKKLYRPFQ----SELFAkrayrELRLLKHM-KHENVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 428 NLLGACTQGGPL-----YVLVEYAAKGNLREFLRARrppgldysfdtcKPPEEQLTFkdLVscaYQVARGMEYLASQKCI 502
Cdd:cd07880  78 GLLDVFTPDLSLdrfhdFYLVMPFMGTDLGKLMKHE------------KLSEDRIQF--LV---YQMLKGLKYIHAAGII 140
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13112048 503 HRDLAARNVLVTEDNVMKIADFGLARDVHNldyykkTTNGRLPVKWM-APEALFDRV-YTHQSDVWSFGVLLWEIFT 577
Cdd:cd07880 141 HRDLKPGNLAVNEDCELKILDFGLARQTDS------EMTGYVVTRWYrAPEVILNWMhYTQTVDIWSVGCIMAEMLT 211
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
394-634 2.56e-14

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: 74.67  E-value: 2.56e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 394 AVKMLkddatDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYVLVEYAAKGNLRE-FLRarrppgldysfdtckp 472
Cdd:cd14176  48 AVKII-----DKSKRDPTEEIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELLDkILR---------------- 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 473 pEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDN----VMKIADFGLARDVhnldyykKTTNGRL---- 544
Cdd:cd14176 107 -QKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGFAKQL-------RAENGLLmtpc 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 545 -PVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIP---VEELFKLLKEGHRMDKPA---NCTHDLYMIMRE 617
Cdd:cd14176 179 yTANFVAPEVLERQGYDAACDIWSLGVLLYTMLT-GYTPFANGPddtPEEILARIGSGKFSLSGGywnSVSDTAKDLVSK 257
                       250
                ....*....|....*..
gi 13112048 618 CWHAAPSQRPTFKQLVE 634
Cdd:cd14176 258 MLHVDPHQRLTAALVLR 274
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
359-635 2.60e-14

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: 73.49  E-value: 2.60e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 359 RLTLGKPLGEGCFGQVVMAeaigIDKDRAAkpvTVAVKMLK-DDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGG 437
Cdd:cd06626   1 RWQRGNKIGEGTFGKVYTA----VNLDTGE---LMAMKEIRfQDNDPKTIKEIADEMKVLEGL-DHPNLVRYYGVEVHRE 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 438 PLYVLVEYAAKGNLREFLRARRppGLDysfdtckppeEQLTfkdlVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDN 517
Cdd:cd06626  73 EVYIFMEYCQEGTLEELLRHGR--ILD----------EAVI----RVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNG 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 518 VMKIADFGLARDVHNldyyKKTTNGRLPVK-------WMAPEalfdrVYTHQ--------SDVWSFGVLLWEIFTlGGSP 582
Cdd:cd06626 137 LIKLGDFGSAVKLKN----NTTTMAPGEVNslvgtpaYMAPE-----VITGNkgeghgraADIWSLGCVVLEMAT-GKRP 206
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 13112048 583 YPGIpvEELFKLLKEGHRMDKPANCTHDL-----YMIMRECWHAAPSQRPTFKQLVED 635
Cdd:cd06626 207 WSEL--DNEWAIMYHVGMGHKPPIPDSLQlspegKDFLSRCLESDPKKRPTASELLDH 262
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
366-633 2.84e-14

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). MAP4K5 also facilitates Wnt signaling in B cells, and may therefore be implicated in the control of cell fate, proliferation, and polarity. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 73.52  E-value: 2.84e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKdraakpvTVAVKMLKDDATDkDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd06646  17 VGSGTYGDVYKARNLHTGE-------LAAVKIIKLEPGD-DFSLIQQEIFMVKEC-KHCNIVAYFGSYLSREKLWICMEY 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLREFLRARRPPGldysfdtckppEEQLTFkdlvsCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFG 525
Cdd:cd06646  88 CGGGSLQDIYHVTGPLS-----------ELQIAY-----VCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFG 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 526 LARDVHNLDYYKKTTNGRlPVkWMAPE-ALFDRV--YTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGHRMD 602
Cdd:cd06646 152 VAAKITATIAKRKSFIGT-PY-WMAPEvAAVEKNggYNQLCDIWAVGITAIELAELQPPMFDLHPMRALFLMSKSNFQPP 229
                       250       260       270
                ....*....|....*....|....*....|....
gi 13112048 603 KPANCTH---DLYMIMRECWHAAPSQRPTFKQLV 633
Cdd:cd06646 230 KLKDKTKwssTFHNFVKISLTKNPKKRPTAERLL 263
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
367-578 3.29e-14

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: 74.24  E-value: 3.29e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 367 GEGCFGQVVMAeaigIDKDRAAKPVtVAVKMLKddaTDKDLSDLVS-----EMEMMKMIgKHKNIINLLGACTQGG--PL 439
Cdd:cd07842   9 GRGTYGRVYKA----KRKNGKDGKE-YAIKKFK---GDKEQYTGISqsacrEIALLREL-KHENVVSLVEVFLEHAdkSV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 440 YVLVEYAaKGNLREFLRARRPPGLDYSfdtckPPeeqLTFKDLVscaYQVARGMEYLASQKCIHRDLAARNVLVT----E 515
Cdd:cd07842  80 YLLFDYA-EHDLWQIIKFHRQAKRVSI-----PP---SMVKSLL---WQILNGIHYLHSNWVLHRDLKPANILVMgegpE 147
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13112048 516 DNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWM-APEALFD-RVYTHQSDVWSFGVLLWEIFTL 578
Cdd:cd07842 148 RGVVKIGDLGLARLFNAPLKPLADLDPVVVTIWYrAPELLLGaRHYTKAIDIWAIGCIFAELLTL 212
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
427-634 3.91e-14

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 75.44  E-value: 3.91e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048  427 INLLGACTQGG------------PLYVLVEYAAKGNLREFLRARRPPGLDYsfdtcKPPEEQLTFkdlvscaYQVARGME 494
Cdd:PTZ00267 116 LHCLAACDHFGivkhfddfksddKLLLIMEYGSGGDLNKQIKQRLKEHLPF-----QEYEVGLLF-------YQIVLALD 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048  495 YLASQKCIHRDLAARNVLVTEDNVMKIADFGLAR---DVHNLD---------YYkkttngrlpvkwMAPEALFDRVYTHQ 562
Cdd:PTZ00267 184 EVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKqysDSVSLDvassfcgtpYY------------LAPELWERKRYSKK 251
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13112048  563 SDVWSFGVLLWEIFTLgGSPYPGIPVEELFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVE 634
Cdd:PTZ00267 252 ADMWSLGVILYELLTL-HRPFKGPSQREIMQQVLYGKYDPFPCPVSSGMKALLDPLLSKNPALRPTTQQLLH 322
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
364-585 4.63e-14

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: 73.76  E-value: 4.63e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVMAeaigidKDRAAKpVTVAVK-MLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQggPL--- 439
Cdd:cd07856  16 QPVGMGAFGLVCSA------RDQLTG-QNVAVKkIMKPFSTPVLAKRTYRELKLLKHL-RHENIISLSDIFIS--PLedi 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 440 YVLVEYAAKgNLREFLRARrppgldysfdtckPPEEQLTFKDLvscaYQVARGMEYLASQKCIHRDLAARNVLVTEDNVM 519
Cdd:cd07856  86 YFVTELLGT-DLHRLLTSR-------------PLEKQFIQYFL----YQILRGLKYVHSAGVIHRDLKPSNILVNENCDL 147
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 520 KIADFGLAR--DVHNLDYYKKTTngrlpvkWMAPEALFD-RVYTHQSDVWSFGVLLWEIftLGGSP-YPG 585
Cdd:cd07856 148 KICDFGLARiqDPQMTGYVSTRY-------YRAPEIMLTwQKYDVEVDIWSAGCIFAEM--LEGKPlFPG 208
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
366-585 5.14e-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: 5.14e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKDRAAKpvtvavKMLKDDATDKDLSDLV-SEMEMMkMIGKHKNIINLLGACTQGGPLYVLVE 444
Cdd:cd05572   1 LGVGGFGRVELVQLKSKGRTFALK------CVKKRHIVQTRQQEHIfSEKEIL-EECNSPFIVKLYRTFKDKKYLYMLME 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 445 YAAKGNLREFLRARrppGLdysFDtckppEEQLTFkdlvsCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADF 524
Cdd:cd05572  74 YCLGGELWTILRDR---GL---FD-----EYTARF-----YTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDF 137
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13112048 525 GLARDVHNldyYKKT-----TNGrlpvkWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPG 585
Cdd:cd05572 138 GFAKKLGS---GRKTwtfcgTPE-----YVAPEIILNKGYDFSVDYWSLGILLYELLT-GRPPFGG 194
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
366-575 5.30e-14

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: 73.53  E-value: 5.30e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKDRAAKPVTVAVKMlkddaTDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd06633  29 IGHGSFGAVYFATNSHTNEVVAIKKMSYSGKQ-----TNEKWQDIIKEVKFLQQL-KHPNTIEYKGCYLKDHTAWLVMEY 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAkGNLREFLRARRppgldysfdtcKPPEEQltfkDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFG 525
Cdd:cd06633 103 CL-GSASDLLEVHK-----------KPLQEV----EIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFG 166
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 13112048 526 LARDVHNLDYYKKTTngrlpvKWMAPE---ALFDRVYTHQSDVWSFGVLLWEI 575
Cdd:cd06633 167 SASIASPANSFVGTP------YWMAPEvilAMDEGQYDGKVDIWSLGITCIEL 213
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
364-592 5.57e-14

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. 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-epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 73.68  E-value: 5.57e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVMAEAIGIDKdraakpvTVAVKMLKDDAT--DKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYV 441
Cdd:cd05591   1 KVLGKGSFGKVMLAERKGTDE-------VYAIKVLKKDVIlqDDDVDCTMTEKRILALAAKHPFLTALHSCFQTKDRLFF 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 442 LVEYAAKGNLR-EFLRARRppgldysFDtckppEEQLTFKdlvscAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMK 520
Cdd:cd05591  74 VMEYVNGGDLMfQIQRARK-------FD-----EPRARFY-----AAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCK 136
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13112048 521 IADFGLARDvhNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEELF 592
Cdd:cd05591 137 LADFGMCKE--GILNGKTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPFEADNEDDLF 205
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
365-576 6.68e-14

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: 72.52  E-value: 6.68e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 365 PLGEGCFGQVVMAEAIGIDKDRAAKPVTVAVKMLKDDAtdKDLSDLvsememmkmigKHKNIINLLGACTqgGP------ 438
Cdd:cd14047  13 LIGSGGFGQVFKAKHRIDGKTYAIKRVKLNNEKAEREV--KALAKL-----------DHPNIVRYNGCWD--GFdydpet 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 439 ------------LYVLVEYAAKGNLREFLRARRPPGLDysfdtckPPEEQLTFkdlvscaYQVARGMEYLASQKCIHRDL 506
Cdd:cd14047  78 sssnssrsktkcLFIQMEFCEKGTLESWIEKRNGEKLD-------KVLALEIF-------EQITKGVEYIHSKKLIHRDL 143
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 507 AARNVLVTEDNVMKIADFGLARDVHNldyYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIF 576
Cdd:cd14047 144 KPSNIFLVDTGKVKIGDFGLVTSLKN---DGKRTKSKGTLSYMSPEQISSQDYGKEVDIYALGLILFELL 210
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
362-635 7.82e-14

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: 72.16  E-value: 7.82e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 362 LGKPLGEGCFGQVVMaeaiGIDKDRAAKpvtVAVKMLKDDATDKD---LSDLVSEMEMMKMIgKHKNIINLLGACTQGGP 438
Cdd:cd14070   6 IGRKLGEGSFAKVRE----GLHAVTGEK---VAIKVIDKKKAKKDsyvTKNLRREGRIQQMI-RHPNITQLLDILETENS 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 439 LYVLVEYAAKGNLREFLrarrppgldysfdtCKppEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNV 518
Cdd:cd14070  78 YYLVMELCPGGNLMHRI--------------YD--KKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDN 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 519 MKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIP--VEELFKLLK 596
Cdd:cd14070 142 IKLIDFGLSNCAGILGYSDPFSTQCGSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLT-GTLPFTVEPfsLRALHQKMV 220
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 13112048 597 EGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVED 635
Cdd:cd14070 221 DKEMNPLPTDLSPGAISFLRSLLEPDPLKRPNIKQALAN 259
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
366-577 9.60e-14

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: 72.79  E-value: 9.60e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAeaigidKDRAAKPVtVAVKMLKDDATDKDLS-DLVSEMEMMKMIgKHKNIINLLGAC----TQG---- 436
Cdd:cd07865  20 IGQGTFGEVFKA------RHRKTGQI-VALKKVLMENEKEGFPiTALREIKILQLL-KHENVVNLIEICrtkaTPYnryk 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 437 GPLYVLVEYAAKgNLREFLrarrppglDYSFDTCKPPEEQLTFKDLVScayqvarGMEYLASQKCIHRDLAARNVLVTED 516
Cdd:cd07865  92 GSIYLVFEFCEH-DLAGLL--------SNKNVKFTLSEIKKVMKMLLN-------GLYYIHRNKILHRDMKAANILITKD 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13112048 517 NVMKIADFGLARDVH--NLDYYKKTTNgRLPVKWM-APEALF-DRVYTHQSDVWSFGVLLWEIFT 577
Cdd:cd07865 156 GVLKLADFGLARAFSlaKNSQPNRYTN-RVVTLWYrPPELLLgERDYGPPIDMWGAGCIMAEMWT 219
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
362-578 9.83e-14

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: 72.30  E-value: 9.83e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 362 LGKpLGEGCFGQVVMAEAIgidKDRAakpvTVAVKMLKDDATDKDLSDLVSEMEMMKMIGKHKNIINLL--------GAC 433
Cdd:cd07831   4 LGK-IGEGTFSEVLKAQSR---KTGK----YYAIKCMKKHFKSLEQVNNLREIQALRRLSPHPNILRLIevlfdrktGRL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 434 TqggplyvLVEYAAKGNLREFLRARRPPgldysfdtckPPEEQLTfkdlvSCAYQVARGMEYLASQKCIHRDLAARNVLV 513
Cdd:cd07831  76 A-------LVFELMDMNLYELIKGRKRP----------LPEKRVK-----NYMYQLLKSLDHMHRNGIFHRDIKPENILI 133
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13112048 514 tEDNVMKIADFGLARDVHNLDYYKKTTNGRlpvkWM-APEALF-DRVYTHQSDVWSFGVLLWEIFTL 578
Cdd:cd07831 134 -KDDILKLADFGSCRGIYSKPPYTEYISTR----WYrAPECLLtDGYYGPKMDIWAVGCVFFEILSL 195
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
366-585 1.03e-13

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: 71.53  E-value: 1.03e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKdraakpvTVAVKMLKDDATDKDlsDLVSEMEMMKMIgKHKNIINLLGAcTQGGPLYVLV-E 444
Cdd:cd14006   1 LGRGRFGVVKRCIEKATGR-------EFAAKFIPKRDKKKE--AVLREISILNQL-QHPRIIQLHEA-YESPTELVLIlE 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 445 YAAKGNLREFLRarrppgldysfdtckpPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTE--DNVMKIA 522
Cdd:cd14006  70 LCSGGELLDRLA----------------ERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADrpSPQIKII 133
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13112048 523 DFGLARDVhNLDYYKKTTNGRLpvKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPG 585
Cdd:cd14006 134 DFGLARKL-NPGEELKEIFGTP--EFVAPEIVNGEPVSLATDMWSIGVLTYVLLS-GLSPFLG 192
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
366-632 1.07e-13

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: 71.69  E-value: 1.07e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEaigidkdRAAKPVTVAVKMLK-DDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVE 444
Cdd:cd08220   8 VGRGAYGTVYLCR-------RKDDNKLVIIKQIPvEQMTKEERQAALNEVKVLSML-HHPNIIEYYESFLEDKALMIVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 445 YAAKGNLREFLRARRPPGLDysfdtckppEEQLtfkdlVSCAYQVARGMEYLASQKCIHRDLAARNVLVTED-NVMKIAD 523
Cdd:cd08220  80 YAPGGTLFEYIQQRKGSLLS---------EEEI-----LHFFVQILLALHHVHSKQILHRDLKTQNILLNKKrTVVKIGD 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 524 FGLARDVHNLDyyKKTTNGRLPVkWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLG----GSPYPGIpveeLFKLLKeGH 599
Cdd:cd08220 146 FGISKILSSKS--KAYTVVGTPC-YISPELCEGKPYNQKSDIWALGCVLYELASLKrafeAANLPAL----VLKIMR-GT 217
                       250       260       270
                ....*....|....*....|....*....|...
gi 13112048 600 RMDKPANCTHDLYMIMRECWHAAPSQRPTFKQL 632
Cdd:cd08220 218 FAPISDRYSEELRHLILSMLHLDPNKRPTLSEI 250
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
393-585 1.13e-13

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: 72.13  E-value: 1.13e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 393 VAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEYAAKgNLREFLRARRPPGldysfdtckp 472
Cdd:cd07836  28 VALKEIHLDAEEGTPSTAIREISLMKEL-KHENIVRLHDVIHTENKLMLVFEYMDK-DLKKYMDTHGVRG---------- 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 473 PEEQLTFKDLVscaYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARDVH---NldyykKTTNGRLPVKWM 549
Cdd:cd07836  96 ALDPNTVKSFT---YQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLARAFGipvN-----TFSNEVVTLWYR 167
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 13112048 550 APEALF-DRVYTHQSDVWSFGVLLWEIFTlgGSP-YPG 585
Cdd:cd07836 168 APDVLLgSRTYSTSIDIWSVGCIMAEMIT--GRPlFPG 203
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
359-585 1.17e-13

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: 72.15  E-value: 1.17e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 359 RLTLGKPLGEGCFGQVVmaEAIGIDKDRaakpvTVAVKMLKDDATDKDLsdlvsEMEMMKMIgKHKNIINLLGAC-TQGG 437
Cdd:cd14137   5 SYTIEKVIGSGSFGVVY--QAKLLETGE-----VVAIKKVLQDKRYKNR-----ELQIMRRL-KHPNIVKLKYFFySSGE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 438 P-----LYVLVEYAAKgNLREFLRarrppglDYSFDtckppEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVL 512
Cdd:cd14137  72 KkdevyLNLVMEYMPE-TLYRVIR-------HYSKN-----KQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLL 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 513 V-TEDNVMKIADFGLArdvhnldyyKKTTNGRLPVKWM------APEALFD-RVYTHQSDVWSFGVLLWEIFTlgGSP-Y 583
Cdd:cd14137 139 VdPETGVLKLCDFGSA---------KRLVPGEPNVSYIcsryyrAPELIFGaTDYTTAIDIWSAGCVLAELLL--GQPlF 207

                ..
gi 13112048 584 PG 585
Cdd:cd14137 208 PG 209
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
364-593 1.19e-13

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: 71.74  E-value: 1.19e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVMAEaigidkdraaKPVT---VAVKMLKDDATD--KDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGP 438
Cdd:cd05611   2 KPISKGAFGSVYLAK----------KRSTgdyFAIKVLKKSDMIakNQVTNVKAERAIMMIQGESPYVAKLYYSFQSKDY 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 439 LYVLVEYAAKGNLREFLRARRPPGLDYSfdtckppeeqltfkdlvsCAY--QVARGMEYLASQKCIHRDLAARNVLVTED 516
Cdd:cd05611  72 LYLVMEYLNGGDCASLIKTLGGLPEDWA------------------KQYiaEVVLGVEDLHQRGIIHRDIKPENLLIDQT 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 517 NVMKIADFGLARDV----HNLDYYkKTTNgrlpvkWMAPEALFDRVYTHQSDVWSFGVLLWEiFTLGGSPYPGIPVEELF 592
Cdd:cd05611 134 GHLKLTDFGLSRNGlekrHNKKFV-GTPD------YLAPETILGVGDDKMSDWWSLGCVIFE-FLFGYPPFHAETPDAVF 205

                .
gi 13112048 593 K 593
Cdd:cd05611 206 D 206
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
364-626 1.31e-13

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: 72.05  E-value: 1.31e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVMAEAIGIDKDRAAKPVTV--AVKMlkddatdKDLSDLVSEMEMMKMIGkHKNIINLLGACTQGGPLYV 441
Cdd:cd14209   7 KTLGTGSFGRVMLVRHKETGNYYAMKILDKqkVVKL-------KQVEHTLNEKRILQAIN-FPFLVKLEYSFKDNSNLYM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 442 LVEYAAKGNLREFLRARRppgldysfdtcKPPEEQLTFKdlvscAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKI 521
Cdd:cd14209  79 VMEYVPGGEMFSHLRRIG-----------RFSEPHARFY-----AAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKV 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 522 ADFGLARDVHNldyyKKTTNGRLPvKWMAPEALFDRVYTHQSDVWSFGVLLWEiFTLGGSPYPGIPVEELFKLLKEGhRM 601
Cdd:cd14209 143 TDFGFAKRVKG----RTWTLCGTP-EYLAPEIILSKGYNKAVDWWALGVLIYE-MAAGYPPFFADQPIQIYEKIVSG-KV 215
                       250       260
                ....*....|....*....|....*
gi 13112048 602 DKPANCTHDLYMIMRECWHAAPSQR 626
Cdd:cd14209 216 RFPSHFSSDLKDLLRNLLQVDLTKR 240
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
366-585 1.35e-13

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: 72.01  E-value: 1.35e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAeaigidKDRAAKPVtVAVKMLKDDaTDKDLSDLVSEMEMMKMIG-KHKNIINLLGACT--QGGPLYVL 442
Cdd:cd07845  15 IGEGTYGIVYRA------RDTTSGEI-VALKKVRMD-NERDGIPISSLREITLLLNlRHPNIVELKEVVVgkHLDSIFLV 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 443 VEYAAKgNLREFLRARRPPgldysFdtckpPEEQltfkdlVSC-AYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKI 521
Cdd:cd07845  87 MEYCEQ-DLASLLDNMPTP-----F-----SESQ------VKClMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKI 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13112048 522 ADFGLARDVHNLdyYKKTTNGRLPVKWMAPEALF-DRVYTHQSDVWSFGVLLWEIftLGGSP-YPG 585
Cdd:cd07845 150 ADFGLARTYGLP--AKPMTPKVVTLWYRAPELLLgCTTYTTAIDMWAVGCILAEL--LAHKPlLPG 211
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
364-597 1.42e-13

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also called ERK4) and 6 (also called ERK3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK4 (also called ERK4 or p63MAPK) and MAPK6 (also called ERK3 or p97MAPK) are atypical MAPKs that are not regulated by MAPK kinases. MAPK6 is expressed ubiquitously with highest amounts in brain and skeletal muscle. It may be involved in the control of cell differentiation by negatively regulating cell cycle progression in certain conditions. It may also play a role in glucose-induced insulin secretion. MAPK6 and MAPK4 cooperate to regulate the activity of MAPK-activated protein kinase 5 (MK5), leading to its relocation to the cytoplasm and exclusion from the nucleus. The MAPK6/MK5 and MAPK4/MK5 pathways may play critical roles in embryonic and post-natal development. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143359 [Multi-domain]  Cd Length: 342  Bit Score: 72.50  E-value: 1.42e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVMAeaigIDKdRAAKPVTVAVKMLKDDatdKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGG-----P 438
Cdd:cd07854  11 RPLGCGSNGLVFSA----VDS-DCDKRVAVKKIVLTDP---QSVKHALREIKIIRRL-DHDNIVKVYEVLGPSGsdlteD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 439 LYVLVEYAAKGNLREFLRArrppgldysfDTCKPPEEQLTFKDLVSC-AYQVARGMEYLASQKCIHRDLAARNVLV-TED 516
Cdd:cd07854  82 VGSLTELNSVYIVQEYMET----------DLANVLEQGPLSEEHARLfMYQLLRGLKYIHSANVLHRDLKPANVFInTED 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 517 NVMKIADFGLARDVHNLDYYKKTTNGRLPVKWM-APEALFD-RVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEELFKL 594
Cdd:cd07854 152 LVLKIGDFGLARIVDPHYSHKGYLSEGLVTKWYrSPRLLLSpNNYTKAIDMWAAGCIFAEMLT-GKPLFAGAHELEQMQL 230

                ...
gi 13112048 595 LKE 597
Cdd:cd07854 231 ILE 233
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
364-634 1.72e-13

Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K8 is also called Tumor progression locus 2 (Tpl2) or Cancer Osaka thyroid (Cot), and was first identified as a proto-oncogene in T-cell lymphoma induced by MoMuL virus and in breast carcinoma induced by MMTV. Activated MAP3K8 induces various MAPK pathways including Extracellular Regulated Kinase (ERK) 1/2, c-Jun N-terminal kinase (JNK), and p38. It plays a pivotal role in innate immunity, linking Toll-like receptors to the production of TNF and the activation of ERK in macrophages. It is also required in interleukin-1beta production and is critical in host defense against Gram-positive bacteria. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K8 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 70.81  E-value: 1.72e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLG-----EGCFGQVVMAEAIGIDKDRAAKpvTVAVKMLKDdatdkdlsdlvSEMEMMKMIgKHKNIINLLGACTQGGP 438
Cdd:cd13995   5 RNIGsdfipRGAFGKVYLAQDTKTKKRMACK--LIPVEQFKP-----------SDVEIQACF-RHENIAELYGALLWEET 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 439 LYVLVEYAAKGNLREFLrarrppgldysfDTCKPPEEqltfKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNV 518
Cdd:cd13995  71 VHLFMEAGEGGSVLEKL------------ESCGPMRE----FEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKA 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 519 MkIADFGLARDVHNLDYYKKTTNGrlPVKWMAPEALFDRVYTHQSDVWSFGVLLweIFTLGGSP-----YP--GIPvEEL 591
Cdd:cd13995 135 V-LVDFGLSVQMTEDVYVPKDLRG--TEIYMSPEVILCRGHNTKADIYSLGATI--IHMQTGSPpwvrrYPrsAYP-SYL 208
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 13112048 592 FKLLKEGHRM-DKPANCTHDLYMIMRECWHAAPSQRPTFKQLVE 634
Cdd:cd13995 209 YIIHKQAPPLeDIAQDCSPAMRELLEAALERNPNHRSSAAELLK 252
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
364-582 2.11e-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: 71.31  E-value: 2.11e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVMAeaigidKDRAAKPVTVAVKMLKDDATD-KDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVL 442
Cdd:cd05612   7 KTIGTGTFGRVHLV------RDRISEHYYALKVMAIPEVIRlKQEQHVHNEKRVLKEV-SHPFIIRLFWTEHDQRFLYML 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 443 VEYAAKGNLREFLRARRppgldySFDTckppEEQLTFKDLVSCAyqvargMEYLASQKCIHRDLAARNVLVTEDNVMKIA 522
Cdd:cd05612  80 MEYVPGGELFSYLRNSG------RFSN----STGLFYASEIVCA------LEYLHSKEIVYRDLKPENILLDKEGHIKLT 143
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 523 DFGLARDVHNLDYykkTTNGRlPvKWMAPEALFDRVYTHQSDVWSFGVLLWEIftLGGSP 582
Cdd:cd05612 144 DFGFAKKLRDRTW---TLCGT-P-EYLAPEVIQSKGHNKAVDWWALGILIYEM--LVGYP 196
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
356-592 2.14e-13

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: 71.12  E-value: 2.14e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 356 SRARLTLGKPLGEGCFGQVVMAeaigIDKDRAAKpvtVAVKMLKDDATDKDL-SDLVSEMEMMKMIGKHKNIINLLGACT 434
Cdd:cd14197   7 ERYSLSPGRELGRGKFAVVRKC----VEKDSGKE---FAAKFMRKRRKGQDCrMEIIHEIAVLELAQANPWVINLHEVYE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 435 QGGPLYVLVEYAAKGNLreflrarrppgldysFDTC-KPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLV 513
Cdd:cd14197  80 TASEMILVLEYAAGGEI---------------FNQCvADREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILL 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 514 TEDNVM---KIADFGLARDVHNLDYYKKTTNgrLPvKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEE 590
Cdd:cd14197 145 TSESPLgdiKIVDFGLSRILKNSEELREIMG--TP-EYVAPEILSYEPISTATDMWSIGVLAYVMLT-GISPFLGDDKQE 220

                ..
gi 13112048 591 LF 592
Cdd:cd14197 221 TF 222
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
394-636 2.14e-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: 71.28  E-value: 2.14e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 394 AVKMLKDDATDKDLSD----LVSEMEMMKMIgKHKNIINLLG-ACTQGGPLYVLVEYAAKgNLREFLRARRPPGLDySFd 468
Cdd:cd14001  32 AVKKINSKCDKGQRSLyqerLKEEAKILKSL-NHPNIVGFRAfTKSEDGSLCLAMEYGGK-SLNDLIEERYEAGLG-PF- 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 469 tckPPeeqltfKDLVSCAYQVARGMEYLASQKCI-HRDLAARNVLVTED-NVMKIADFGLA-RDVHNLDYYKKTTN---G 542
Cdd:cd14001 108 ---PA------ATILKVALSIARALEYLHNEKKIlHGDIKSGNVLIKGDfESVKLCDFGVSlPLTENLEVDSDPKAqyvG 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 543 RLPvkWMAPEALF-DRVYTHQSDVWSFGVLLWEIFTLgGSPYPGIPVEELFKLLKEGHRMD------------KPA---N 606
Cdd:cd14001 179 TEP--WKAKEALEeGGVITDKADIFAYGLVLWEMMTL-SVPHLNLLDIEDDDEDESFDEDEedeeayygtlgtRPAlnlG 255
                       250       260       270
                ....*....|....*....|....*....|....
gi 13112048 607 CTHDLYMIMRE----CWHAAPSQRPTFKQLVEDL 636
Cdd:cd14001 256 ELDDSYQKVIElfyaCTQEDPKDRPSAAHIVEAL 289
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
485-592 2.24e-13

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: 70.71  E-value: 2.24e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 485 CAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLAR----DVHNLDYYKKTTNGRLPVK---------WMAP 551
Cdd:cd05579  98 YIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSKvglvRRQIKLSIQKKSNGAPEKEdrrivgtpdYLAP 177
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 13112048 552 EALFDRVYTHQSDVWSFGVLLWEiFTLGGSPYPGIPVEELF 592
Cdd:cd05579 178 EILLGQGHGKTVDWWSLGVILYE-FLVGIPPFHAETPEEIF 217
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
361-599 2.45e-13

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: 70.43  E-value: 2.45e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 361 TLGKPLGEGCFGqvVMAEAigidKDRAAKPvTVAVKMLkDDATDKDLSDLV-SEMEMMKMIgKHKNIINLLGACTQGGPL 439
Cdd:cd14095   3 DIGRVIGDGNFA--VVKEC----RDKATDK-EYALKII-DKAKCKGKEHMIeNEVAILRRV-KHPNIVQLIEEYDTDTEL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 440 YVLVEYAAKGNLreflrarrppgldysFD----TCKPPEEqltfkDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTE 515
Cdd:cd14095  74 YLVMELVKGGDL---------------FDaitsSTKFTER-----DASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVE 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 516 DN----VMKIADFGLARDVHNLDYykkTTNGRlPVkWMAPEALFDRVYTHQSDVWSFGVLLWeIFTLGGSPY--PGIPVE 589
Cdd:cd14095 134 HEdgskSLKLADFGLATEVKEPLF---TVCGT-PT-YVAPEILAETGYGLKVDIWAAGVITY-ILLCGFPPFrsPDRDQE 207
                       250
                ....*....|
gi 13112048 590 ELFKLLKEGH 599
Cdd:cd14095 208 ELFDLILAGE 217
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
363-577 2.75e-13

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: 70.50  E-value: 2.75e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 363 GKPLGEGCFGQVVMAEAIGIDKDRAAKPVTVAVKmlkDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGG--PLY 440
Cdd:cd06651  12 GKLLGQGAFGRVYLCYDVDTGRELAAKQVQFDPE---SPETSKEVSALECEIQLLKNL-QHERIVQYYGCLRDRAekTLT 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 441 VLVEYAAKGNLREFLRArrppgldYSFDTckppeEQLTFKdlvsCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMK 520
Cdd:cd06651  88 IFMEYMPGGSVKDQLKA-------YGALT-----ESVTRK----YTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVK 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13112048 521 IADFGLARDVHNLdyyKKTTNGRLPVK----WMAPEALFDRVYTHQSDVWSFGVLLWEIFT 577
Cdd:cd06651 152 LGDFGASKRLQTI---CMSGTGIRSVTgtpyWMSPEVISGEGYGRKADVWSLGCTVVEMLT 209
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
364-631 2.82e-13

Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), is an ER-localized type I transmembrane protein with kinase and endoribonuclease domains in the cytoplasmic side. It acts as an ER stress sensor and is the oldest and most conserved component of the unfolded protein response (UPR) in eukaryotes. The UPR is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. During ER stress, IRE1 dimerizes and forms oligomers, allowing the kinase domain to undergo trans-autophosphorylation. This leads to a conformational change that stimulates its endoribonuclease activity and results in the cleavage of its mRNA substrate, HAC1 in yeast and XBP1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. Mammals contain two IRE1 proteins, IRE1alpha (or ERN1) and IRE1beta (or ERN2). The Ire1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 70.38  E-value: 2.82e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVMAeaiGIDKDRAakpvtVAVK-MLKD--DATDKDLSDLVSEMEmmkmigkHKNIINLLgaCTQGGP-- 438
Cdd:cd13982   7 KVLGYGSEGTIVFR---GTFDGRP-----VAVKrLLPEffDFADREVQLLRESDE-------HPNVIRYF--CTEKDRqf 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 439 LYVLVEYAAkGNLREFLRARRPpgldysfdtcKPPEEQLTFkDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNV 518
Cdd:cd13982  70 LYIALELCA-ASLQDLVESPRE----------SKLFLRPGL-EPVRLLRQIASGLAHLHSLNIVHRDLKPQNILISTPNA 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 519 -----MKIADFGLARdvhNLDY----YKKTTNGRLPVKWMAPEALFDRVYTHQS---DVWSFGVLLWEIFTLGGSPYpGI 586
Cdd:cd13982 138 hgnvrAMISDFGLCK---KLDVgrssFSRRSGVAGTSGWIAPEMLSGSTKRRQTravDIFSLGCVFYYVLSGGSHPF-GD 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 13112048 587 PVEELFKLLKEGHRMDKP---ANCTHDLYMIMRECWHAAPSQRPTFKQ 631
Cdd:cd13982 214 KLEREANILKGKYSLDKLlslGEHGPEAQDLIERMIDFDPEKRPSAEE 261
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
171-232 3.50e-13

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 65.28  E-value: 3.50e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13112048   171 TVRFRCPAAGNPTPSISWLKNGREFRGEHRIGGIKLRHQQwSLVMESVVPSDRGNYTCVVEN 232
Cdd:pfam13927  18 TVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNS-TLTISNVTRSDAGTYTCVASN 78
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
366-585 3.57e-13

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: 69.99  E-value: 3.57e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKDRAAKPVTVAvkmlkddaTDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd14192  12 LGGGRFGQVHKCTELSTGLTLAAKIIKVK--------GAKEREEVKNEINIMNQL-NHVNLIQLYDAFESKTNLTLIMEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLreflrarrppgldysFDTCKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTED--NVMKIAD 523
Cdd:cd14192  83 VDGGEL---------------FDRITDESYQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILCVNStgNQIKIID 147
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13112048 524 FGLARDVHNLDYYKktTNGRLPvKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPG 585
Cdd:cd14192 148 FGLARRYKPREKLK--VNFGTP-EFLAPEVVNYDFVSFPTDMWSVGVITYMLLS-GLSPFLG 205
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
422-628 3.92e-13

Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin receptor-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR1, also called Activin receptor-Like Kinase 2 (ALK2), and ALK1 act as receptors for bone morphogenetic proteins (BMPs) and they activate SMAD1/5/8. ACVR1 is widely expressed while ALK1 is limited mainly to endothelial cells. The specificity of BMP binding to type I receptors is affected by type II receptors. ACVR1 binds BMP6/7/9/10 and can also bind anti-Mullerian hormone (AMH) in the presence of AMHR2. ALK1 binds BMP9/10 as well as TGFbeta in endothelial cells. A missense mutation in the GS domain of ACVR1 causes fibrodysplasia ossificans progressiva, a complex and disabling disease characterized by congenital skeletal malformations and extraskeletal bone formation. ACVR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like ACVR1 and ALK1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The ACVR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271044 [Multi-domain]  Cd Length: 298  Bit Score: 70.55  E-value: 3.92e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 422 KHKNIINLLGA-------CTQggpLYVLVEYAAKGNLREFLRarrppgldysfdtckppEEQLTFKDLVSCAYQVARGME 494
Cdd:cd14142  57 RHENILGFIASdmtsrnsCTQ---LWLITHYHENGSLYDYLQ-----------------RTTLDHQEMLRLALSAASGLV 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 495 YLASQ--------KCIHRDLAARNVLVTEDNVMKIADFGLA-RDVHNLDYYKKTTNGRLPVK-WMAPEALFDRVYT---- 560
Cdd:cd14142 117 HLHTEifgtqgkpAIAHRDLKSKNILVKSNGQCCIADLGLAvTHSQETNQLDVGNNPRVGTKrYMAPEVLDETINTdcfe 196
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 561 --HQSDVWSFGVLLWEI---FTLGG-----SP--YPGIPVEELFKLLK-----EGHRMDKPANCTHD-----LYMIMREC 618
Cdd:cd14142 197 syKRVDIYAFGLVLWEVarrCVSGGiveeyKPpfYDVVPSDPSFEDMRkvvcvDQQRPNIPNRWSSDptltaMAKLMKEC 276
                       250
                ....*....|
gi 13112048 619 WHAAPSQRPT 628
Cdd:cd14142 277 WYQNPSARLT 286
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
353-605 4.31e-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: 70.04  E-value: 4.31e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 353 WELSRARLtlgkpLGEGCFGQVVMAeaigidKDRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGA 432
Cdd:cd14201   6 FEYSRKDL-----VGHGAFAVVFKG------RHRKKTDWEVAIKSINKKNLSKSQILLGKEIKILKEL-QHENIVALYDV 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 433 CTQGGPLYVLVEYAAKGNLREFLRARRPpgldYSFDTCKppeeqlTFkdlvscAYQVARGMEYLASQKCIHRDLAARNVL 512
Cdd:cd14201  74 QEMPNSVFLVMEYCNGGDLADYLQAKGT----LSEDTIR------VF------LQQIAAAMRILHSKGIIHRDLKPQNIL 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 513 VTEDNV---------MKIADFGLARDVHNlDYYKKTTNGRlPVkWMAPEALFDRVYTHQSDVWSFGVLLWEIFtLGGSPY 583
Cdd:cd14201 138 LSYASRkkssvsgirIKIADFGFARYLQS-NMMAATLCGS-PM-YMAPEVIMSQHYDAKADLWSIGTVIYQCL-VGKPPF 213
                       250       260
                ....*....|....*....|..
gi 13112048 584 PGIPVEELfKLLKEGHRMDKPA 605
Cdd:cd14201 214 QANSPQDL-RMFYEKNKNLQPS 234
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
353-596 4.41e-13

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: 71.09  E-value: 4.41e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 353 WELSRaRLTLGKPLGEGCFGQVVMAeaigIDKDRAAKpvtVAVKMLKDDATDKDLSDLV-SEMEMMKMIgKHKNIINLLG 431
Cdd:cd07879  11 WELPE-RYTSLKQVGSGAYGSVCSA----IDKRTGEK---VAIKKLSRPFQSEIFAKRAyRELTLLKHM-QHENVIGLLD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 432 ACTQGGPL------YVLVEYAakgnlreFLRARRPPGLDYSfdtckppEEQLTFkdLVscaYQVARGMEYLASQKCIHRD 505
Cdd:cd07879  82 VFTSAVSGdefqdfYLVMPYM-------QTDLQKIMGHPLS-------EDKVQY--LV---YQMLCGLKYIHSAGIIHRD 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 506 LAARNVLVTEDNVMKIADFGLARdvhnldYYKKTTNGRLPVKWM-APEALFDRV-YTHQSDVWSFGVLLWEIFTlGGSPY 583
Cdd:cd07879 143 LKPGNLAVNEDCELKILDFGLAR------HADAEMTGYVVTRWYrAPEVILNWMhYNQTVDIWSVGCIMAEMLT-GKTLF 215
                       250
                ....*....|....
gi 13112048 584 PGIP-VEELFKLLK 596
Cdd:cd07879 216 KGKDyLDQLTQILK 229
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
366-595 5.59e-13

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: 70.41  E-value: 5.59e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKdraakpvTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd07872  14 LGEGTYATVFKGRSKLTEN-------LVALKEIRLEHEEGAPCTAIREVSLLKDL-KHANIVTLHDIVHTDKSLTLVFEY 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKgNLREFLrarrppgldysfDTCKppeEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFG 525
Cdd:cd07872  86 LDK-DLKQYM------------DDCG---NIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFG 149
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13112048 526 LARdvhNLDYYKKTTNGRLPVKWMAPE--ALFDRVYTHQSDVWSFGVLLWEIFTlgGSP-YPGIPVEE----LFKLL 595
Cdd:cd07872 150 LAR---AKSVPTKTYSNEVVTLWYRPPdvLLGSSEYSTQIDMWGVGCIFFEMAS--GRPlFPGSTVEDelhlIFRLL 221
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
366-577 5.81e-13

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: 70.24  E-value: 5.81e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAeaigidkdrAAKPVTVAVKMLKDDAtDKDLS----DLVSEMEMMKMIgKHKNIINLLGACTQGGPLYV 441
Cdd:cd14159   1 IGEGGFGCVYQA---------VMRNTEYAVKRLKEDS-ELDWSvvknSFLTEVEKLSRF-RHPNIVDLAGYSAQQGNYCL 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 442 LVEYAAKGNLREFLRarrppgldysfdtCKPPEEQLTFKDLVSCAYQVARGMEYL--ASQKCIHRDLAARNVLVTEDNVM 519
Cdd:cd14159  70 IYVYLPNGSLEDRLH-------------CQVSCPCLSWSQRLHVLLGTARAIQYLhsDSPSLIHGDVKSSNILLDAALNP 136
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13112048 520 KIADFGLAR------DVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFT 577
Cdd:cd14159 137 KLGDFGLARfsrrpkQPGMSSTLARTQTVRGTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELLT 200
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
364-632 5.88e-13

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: 69.55  E-value: 5.88e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQV--VMAEAIGIdkdraakpvtVAVKMLK-DDATDKDLSDLVSEMEMMKMIGKHKNIINLLGA--CTQGGP 438
Cdd:cd14131   7 KQLGKGGSSKVykVLNPKKKI----------YALKRVDlEGADEQTLQSYKNEIELLKKLKGSDRIIQLYDYevTDEDDY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 439 LYVLVEYAaKGNLREFLRARRPPGLDYSFdtckppeEQLTFKDLVSCAYQVARgmeylasQKCIHRDLAARN-VLVteDN 517
Cdd:cd14131  77 LYMVMECG-EIDLATILKKKRPKPIDPNF-------IRYYWKQMLEAVHTIHE-------EGIVHSDLKPANfLLV--KG 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 518 VMKIADFGLARDVHNldyykKTTN-------GRLpvKWMAPEALFDRVYTHQ----------SDVWSFGVLLWEiFTLGG 580
Cdd:cd14131 140 RLKLIDFGIAKAIQN-----DTTSivrdsqvGTL--NYMSPEAIKDTSASGEgkpkskigrpSDVWSLGCILYQ-MVYGK 211
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 13112048 581 SPYPGI--PVEELFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQL 632
Cdd:cd14131 212 TPFQHItnPIAKLQAIIDPNHEIEFPDIPNPDLIDVMKRCLQRDPKKRPSIPEL 265
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
362-595 6.92e-13

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: 69.65  E-value: 6.92e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 362 LGKpLGEGCFGQVVmaeaigidKDRAA-KPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLY 440
Cdd:cd07871  10 LDK-LGEGTYATVF--------KGRSKlTENLVALKEIRLEHEEGAPCTAIREVSLLKNL-KHANIVTLHDIIHTERCLT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 441 VLVEYAaKGNLREFLrarrppgldysfDTCKppeEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMK 520
Cdd:cd07871  80 LVFEYL-DSDLKQYL------------DNCG---NLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELK 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 521 IADFGLARdvhNLDYYKKTTNGRLPVKWMAPE--ALFDRVYTHQSDVWSFGVLLWEIFTlgGSP-YPGIPVEE----LFK 593
Cdd:cd07871 144 LADFGLAR---AKSVPTKTYSNEVVTLWYRPPdvLLGSTEYSTPIDMWGVGCILYEMAT--GRPmFPGSTVKEelhlIFR 218

                ..
gi 13112048 594 LL 595
Cdd:cd07871 219 LL 220
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
486-598 6.93e-13

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: 69.67  E-value: 6.93e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 486 AYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLArdVHNLDyyKKTTNGRL-PVKWMAPEALFDRVYTHQSD 564
Cdd:cd05630 108 AAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLA--VHVPE--GQTIKGRVgTVGYMAPEVVKNERYTFSPD 183
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 13112048 565 VWSFGVLLWEIFTlGGSPY----PGIPVEELFKLLKEG 598
Cdd:cd05630 184 WWALGCLLYEMIA-GQSPFqqrkKKIKREEVERLVKEV 220
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
364-639 7.27e-13

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: 69.68  E-value: 7.27e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVMAEAIGidkdraaKPVTVAVKMLKDDATdkdlsdLVSEMEMMK-MIGKHKNIINLLGACTQGG----P 438
Cdd:cd14220   1 RQIGKGRYGEVWMGKWRG-------EKVAVKVFFTTEEAS------WFRETEIYQtVLMRHENILGFIAADIKGTgswtQ 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 439 LYVLVEYAAKGNLREFLRARrppgldySFDTckppeeqltfKDLVSCAYQVARGMEYLASQ--------KCIHRDLAARN 510
Cdd:cd14220  68 LYLITDYHENGSLYDFLKCT-------TLDT----------RALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKN 130
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 511 VLVTEDNVMKIADFGLA----RDVHNLDYYKKTTNGrlPVKWMAPEALFDRVYTHQ------SDVWSFGVLLWEIF---T 577
Cdd:cd14220 131 ILIKKNGTCCIADLGLAvkfnSDTNEVDVPLNTRVG--TKRYMAPEVLDESLNKNHfqayimADIYSFGLIIWEMArrcV 208
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13112048 578 LGG-------SPYPGIPVEELFKLLKEGHRMD--KPA--------NCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRV 639
Cdd:cd14220 209 TGGiveeyqlPYYDMVPSDPSYEDMREVVCVKrlRPTvsnrwnsdECLRAVLKLMSECWAHNPASRLTALRIKKTLAKM 287
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
341-575 7.33e-13

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: 70.05  E-value: 7.33e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 341 NVSELELPADPKWELSRARltlgkPLGEGCFGQVVMAEAIGIDKDRAAKPVTVAVKMlkddaTDKDLSDLVSEMEMMKMI 420
Cdd:cd06634   3 EVAELFFKDDPEKLFSDLR-----EIGHGSFGAVYFARDVRNNEVVAIKKMSYSGKQ-----SNEKWQDIIKEVKFLQKL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 421 gKHKNIINLLGACTQGGPLYVLVEYAAkGNLREFLRARRppgldysfdtcKPPEEQltfkDLVSCAYQVARGMEYLASQK 500
Cdd:cd06634  73 -RHPNTIEYRGCYLREHTAWLVMEYCL-GSASDLLEVHK-----------KPLQEV----EIAAITHGALQGLAYLHSHN 135
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13112048 501 CIHRDLAARNVLVTEDNVMKIADFGLARDVHNLDYYKKTTngrlpvKWMAPE---ALFDRVYTHQSDVWSFGVLLWEI 575
Cdd:cd06634 136 MIHRDVKAGNILLTEPGLVKLGDFGSASIMAPANSFVGTP------YWMAPEvilAMDEGQYDGKVDVWSLGITCIEL 207
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
345-583 7.53e-13

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 70.23  E-value: 7.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048  345 LELPADPKWELSRarLTLGKPLGEGCFGQVVMAEAIGIDKdraakpvTVAVKMLKDDAT--DKDLSDLVSEMEMMKMIgK 422
Cdd:PTZ00263   7 FTKPDTSSWKLSD--FEMGETLGTGSFGRVRIAKHKGTGE-------YYAIKCLKKREIlkMKQVQHVAQEKSILMEL-S 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048  423 HKNIINLLGACTQGGPLYVLVEYAAKGNLREFLR-ARRPPGldysfDTCKppeeqltfkdlVSCAyQVARGMEYLASQKC 501
Cdd:PTZ00263  77 HPFIVNMMCSFQDENRVYFLLEFVVGGELFTHLRkAGRFPN-----DVAK-----------FYHA-ELVLAFEYLHSKDI 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048  502 IHRDLAARNVLVTEDNVMKIADFGLARDVHNLDYykkTTNGRlPvKWMAPEALFDRVYTHQSDVWSFGVLLWEiFTLGGS 581
Cdd:PTZ00263 140 IYRDLKPENLLLDNKGHVKVTDFGFAKKVPDRTF---TLCGT-P-EYLAPEVIQSKGHGKAVDWWTMGVLLYE-FIAGYP 213

                 ..
gi 13112048  582 PY 583
Cdd:PTZ00263 214 PF 215
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
366-634 7.90e-13

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: 69.38  E-value: 7.90e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVvmaeaigiDKDRAAKPVTV-AVKMLKDDATDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYVLVE 444
Cdd:cd06617   9 LGRGAYGVV--------DKMRHVPTGTImAVKRIRATVNSQEQKRLLMDLDISMRSVDCPYTVTFYGALFREGDVWICME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 445 yAAKGNLREFLRARRPPGLdysfdtcKPPEEQLTfkdlvSCAYQVARGMEYLASQ-KCIHRDLAARNVLVTEDNVMKIAD 523
Cdd:cd06617  81 -VMDTSLDKFYKKVYDKGL-------TIPEDILG-----KIAVSIVKALEYLHSKlSVIHRDVKPSNVLINRNGQVKLCD 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 524 FGLARdvHNLDYYKKTTN-GRLPvkWMAPE----ALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYP--GIPVEELfKLLK 596
Cdd:cd06617 148 FGISG--YLVDSVAKTIDaGCKP--YMAPErinpELNQKGYDVKSDVWSLGITMIELAT-GRFPYDswKTPFQQL-KQVV 221
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 13112048 597 EGHRMDKPANC-THDLYMIMRECWHAAPSQRPTFKQLVE 634
Cdd:cd06617 222 EEPSPQLPAEKfSPEFQDFVNKCLKKNYKERPNYPELLQ 260
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
366-570 9.22e-13

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: 69.02  E-value: 9.22e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAeaigidKDRAAKPVtVAVKMLK---DDATDKdLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVL 442
Cdd:cd06607   9 IGHGSFGAVYYA------RNKRTSEV-VAIKKMSysgKQSTEK-WQDIIKEVKFLRQL-RHPNTIEYKGCYLREHTAWLV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 443 VEYAAkGNLREFLRARRppgldysfdtcKPPEEQltfkDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIA 522
Cdd:cd06607  80 MEYCL-GSASDIVEVHK-----------KPLQEV----EIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLA 143
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 13112048 523 DFGLARDVHNLDYYKKTtngrlPVkWMAPE---ALFDRVYTHQSDVWSFGV 570
Cdd:cd06607 144 DFGSASLVCPANSFVGT-----PY-WMAPEvilAMDEGQYDGKVDVWSLGI 188
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
407-583 1.01e-12

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK1, also called CaMKK alpha, is involved in the regulation of glucose uptake in skeletal muscles, independently of AMPK and PKB activation. It also play roles in learning and memory. Studies on CaMKK1 knockout mice reveal deficits in fear conditioning. The CaMKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 69.21  E-value: 1.01e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 407 LSDLVSEMEMMKMIgKHKNIINLLGACTQGGP--LYVLVEYAAKGNLREFlrarrPPGLDYSFDtckppEEQLTFKDLVs 484
Cdd:cd14200  67 LERVYQEIAILKKL-DHVNIVKLIEVLDDPAEdnLYMVFDLLRKGPVMEV-----PSDKPFSED-----QARLYFRDIV- 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 485 cayqvaRGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARDVHNLDYYKKTTNGRlPVkWMAPEALFDrvyTHQS- 563
Cdd:cd14200 135 ------LGIEYLHYQKIVHRDIKPSNLLLGDDGHVKIADFGVSNQFEGNDALLSSTAGT-PA-FMAPETLSD---SGQSf 203
                       170       180
                ....*....|....*....|....*
gi 13112048 564 -----DVWSFGVLLWeIFTLGGSPY 583
Cdd:cd14200 204 sgkalDVWAMGVTLY-CFVYGKCPF 227
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
364-575 1.02e-12

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: 70.12  E-value: 1.02e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVMAEAIGIDKDRAAKpvtvavKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTqggPLYVLV 443
Cdd:cd07874  23 KPIGSGAQGIVCAAYDAVLDRNVAIK------KLSRPFQNQTHAKRAYRELVLMKCV-NHKNIISLLNVFT---PQKSLE 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 444 EYAAKGNLREFLRArrppgldysfDTCKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIAD 523
Cdd:cd07874  93 EFQDVYLVMELMDA----------NLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILD 162
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 13112048 524 FGLARDVHNLDYYKKTTNGRLpvkWMAPEALFDRVYTHQSDVWSFGVLLWEI 575
Cdd:cd07874 163 FGLARTAGTSFMMTPYVVTRY---YRAPEVILGMGYKENVDIWSVGCIMGEM 211
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
362-599 1.14e-12

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: 68.44  E-value: 1.14e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 362 LGKPLGEGCFGQVVMAEAIGIDKDRAAKPVTVAVKMLKDDATDkdlsdlvSEMEMMKMIgKHKNIINLLGACTQGGPLYV 441
Cdd:cd14185   4 IGRTIGDGNFAVVKECRHWNENQEYAMKIIDKSKLKGKEDMIE-------SEILIIKSL-SHPNIVKLFEVYETEKEIYL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 442 LVEYAAKGNLreflrarrppgLDYSFDTCKPPEEQ--LTFKDLvscayqvARGMEYLASQKCIHRDLAARNVLVTED--- 516
Cdd:cd14185  76 ILEYVRGGDL-----------FDAIIESVKFTEHDaaLMIIDL-------CEALVYIHSKHIVHRDLKPENLLVQHNpdk 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 517 -NVMKIADFGLARDVHNLDYykkTTNGRlPVkWMAPEALFDRVYTHQSDVWSFGVLLWeIFTLGGSPY--PGIPVEELFK 593
Cdd:cd14185 138 sTTLKLADFGLAKYVTGPIF---TVCGT-PT-YVAPEILSEKGYGLEVDMWAAGVILY-ILLCGFPPFrsPERDQEELFQ 211

                ....*.
gi 13112048 594 LLKEGH 599
Cdd:cd14185 212 IIQLGH 217
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
487-575 1.23e-12

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: 69.77  E-value: 1.23e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 487 YQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARdVHNLDYYKKTTNGRLPVKWMAPEALF-DRVYTHQSDV 565
Cdd:cd07853 110 YQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLAR-VEEPDESKHMTQEVVTQYYRAPEILMgSRHYTSAVDI 188
                        90
                ....*....|
gi 13112048 566 WSFGVLLWEI 575
Cdd:cd07853 189 WSVGCIFAEL 198
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
364-595 1.28e-12

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: 69.26  E-value: 1.28e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVMAEAIGIDKDRAAKPVTVAVKMLKDDatdkdLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLV 443
Cdd:cd05595   1 KLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDE-----VAHTVTESRVLQNT-RHPFLTALKYAFQTHDRLCFVM 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 444 EYAAKGNLREFLRARRppgldySFDtckppEEQLTFKdlvscAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIAD 523
Cdd:cd05595  75 EYANGGELFFHLSRER------VFT-----EDRARFY-----GAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITD 138
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13112048 524 FGLARDVHNLDYYKKTTNGRlPvKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEELFKLL 595
Cdd:cd05595 139 FGLCKEGITDGATMKTFCGT-P-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHERLFELI 207
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
361-604 1.54e-12

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271071 [Multi-domain]  Cd Length: 277  Bit Score: 68.38  E-value: 1.54e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 361 TLGKPLGEGCFGQVVMAEAIGIDKdraakpvTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLY 440
Cdd:cd14169   6 ELKEKLGEGAFSEVVLAQERGSQR-------LVALKCIPKKALRGKEAMVENEIAVLRRI-NHENIVSLEDIYESPTHLY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 441 VLVEYAAKGNLREFLRARrppgldysfdtckppeEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVT---EDN 517
Cdd:cd14169  78 LAMELVTGGELFDRIIER----------------GSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYAtpfEDS 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 518 VMKIADFGLAR-DVHNLDYYKKTTNGrlpvkWMAPEALFDRVYTHQSDVWSFGVLLWeIFTLGGSPYPGIPVEELFKL-L 595
Cdd:cd14169 142 KIMISDFGLSKiEAQGMLSTACGTPG-----YVAPELLEQKPYGKAVDVWAIGVISY-ILLCGYPPFYDENDSELFNQiL 215

                ....*....
gi 13112048 596 KEGHRMDKP 604
Cdd:cd14169 216 KAEYEFDSP 224
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
364-592 1.54e-12

The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2 (also called STK17B). Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. DRAK2 has been implicated in inducing or enhancing apoptosis in beta cells, fibroblasts, and lymphoid cells, where it is highly expressed. It is involved in regulating many immune processes including the germinal center (GC) reaction, responses to thymus-dependent antigens, activated T cell survival, memory T cell responses. It may be involved in the development of autoimmunity. The DRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271100 [Multi-domain]  Cd Length: 270  Bit Score: 68.41  E-value: 1.54e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVMAEAIGIDKDRAAKpvtvavkMLKDDATDKDL-SDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYVL 442
Cdd:cd14198  14 KELGRGKFAVVRQCISKSTGQEYAAK-------FLKKRRRGQDCrAEILHEIAVLELAKSNPRVVNLHEVYETTSEIILI 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 443 VEYAAKGNLreflrarrppgldysFDTCKPPE-EQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVM-- 519
Cdd:cd14198  87 LEYAAGGEI---------------FNLCVPDLaEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIYPLgd 151
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13112048 520 -KIADFGLARDVHNLDYYKKTTNgrlPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEELF 592
Cdd:cd14198 152 iKIVDFGMSRKIGHACELREIMG---TPEYLAPEILNYDPITTATDMWNIGVIAYMLLT-HESPFVGEDNQETF 221
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
364-585 1.83e-12

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: 68.98  E-value: 1.83e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVMAEAIGIDKDRAAKP-------VTVAVKMLKddatdkdlsdlvsEMEMMKMIgKHKNIINLLGACTqg 436
Cdd:cd07850   6 KPIGSGAQGIVCAAYDTVTGQNVAIKKlsrpfqnVTHAKRAYR-------------ELVLMKLV-NHKNIIGLLNVFT-- 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 437 gPLYVLVEYAAKGNLREFLRArrppgldysfDTCKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTED 516
Cdd:cd07850  70 -PQKSLEEFQDVYLVMELMDA----------NLCQVIQMDLDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSD 138
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13112048 517 NVMKIADFGLARDVHN---------LDYYKkttngrlpvkwmAPEALFDRVYTHQSDVWSFGVLLWEIFtLGGSPYPG 585
Cdd:cd07850 139 CTLKILDFGLARTAGTsfmmtpyvvTRYYR------------APEVILGMGYKENVDIWSVGCIMGEMI-RGTVLFPG 203
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
366-577 2.59e-12

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: 68.29  E-value: 2.59e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEaigiDKDRAAkpvTVAVKMLKDDATDKDLS-DLVSEMEMMKMIgKHKNIINLLGACT---------- 434
Cdd:cd07864  15 IGEGTYGQVYKAK----DKDTGE---LVALKKVRLDNEKEGFPiTAIREIKILRQL-NHRSVVNLKEIVTdkqdaldfkk 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 435 QGGPLYVLVEYAAKgNLREFLRArrppGL-DYSfdtckppEEQLTfkdlvSCAYQVARGMEYLASQKCIHRDLAARNVLV 513
Cdd:cd07864  87 DKGAFYLVFEYMDH-DLMGLLES----GLvHFS-------EDHIK-----SFMKQLLEGLNYCHKKNFLHRDIKCSNILL 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13112048 514 TEDNVMKIADFGLARdVHNLDYYKKTTNGRLPVKWMAPEALF-DRVYTHQSDVWSFGVLLWEIFT 577
Cdd:cd07864 150 NNKGQIKLADFGLAR-LYNSEESRPYTNKVITLWYRPPELLLgEERYGPAIDVWSCGCILGELFT 213
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
486-585 2.77e-12

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: 68.35  E-value: 2.77e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 486 AYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARDVHNLDyyKKTTNGRL----PVKWM-APEALF-DRVY 559
Cdd:cd07852 113 MYQLLKALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGLARSLSQLE--EDDENPVLtdyvATRWYrAPEILLgSTRY 190
                        90       100
                ....*....|....*....|....*..
gi 13112048 560 THQSDVWSFGVLLWEIftLGGSP-YPG 585
Cdd:cd07852 191 TKGVDMWSVGCILGEM--LLGKPlFPG 215
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
363-592 2.81e-12

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs, also called STK17, were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. They may play a role in apoptotic signaling. The DRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271008 [Multi-domain]  Cd Length: 268  Bit Score: 67.38  E-value: 2.81e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 363 GKPLGEGCFGQVVMAeaigIDKDRAakpVTVAVKMLKDDATDKDLS-DLVSEMEMMKMIGKHKNIINLLGACTQGGPLYV 441
Cdd:cd14106  13 STPLGRGKFAVVRKC----IHKETG---KEYAAKFLRKRRRGQDCRnEILHEIAVLELCKDCPRVVNLHEVYETRSELIL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 442 LVEYAAKGNLreflrarrppgldysFDTCKPpEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNV--- 518
Cdd:cd14106  86 ILELAAGGEL---------------QTLLDE-EECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEFPlgd 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 519 MKIADFGLARDVHN----------LDYykkttngrlpvkwMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPV 588
Cdd:cd14106 150 IKLCDFGISRVIGEgeeireilgtPDY-------------VAPEILSYEPISLATDMWSIGVLTYVLLT-GHSPFGGDDK 215

                ....
gi 13112048 589 EELF 592
Cdd:cd14106 216 QETF 219
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
366-596 3.19e-12

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 67.92  E-value: 3.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048  366 LGEGCFGQVVMAeaigidKDRAAKPvTVAVKMLKDDATDKDL-SDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVE 444
Cdd:PLN00009  10 IGEGTYGVVYKA------RDRVTNE-TIALKKIRLEQEDEGVpSTAIREISLLKEM-QHGNIVRLQDVVHSEKRLYLVFE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048  445 YAAKgNLREFLrarrppglDYSFDTCKPPEEQLTFkdlvscAYQVARGMEYLASQKCIHRDLAARNVLVTE-DNVMKIAD 523
Cdd:PLN00009  82 YLDL-DLKKHM--------DSSPDFAKNPRLIKTY------LYQILRGIAYCHSHRVLHRDLKPQNLLIDRrTNALKLAD 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13112048  524 FGLARdvhNLDYYKKTTNGRLPVKWM-APEALF-DRVYTHQSDVWSFGVLLWEIFTlgGSP-YPG-IPVEELFKLLK 596
Cdd:PLN00009 147 FGLAR---AFGIPVRTFTHEVVTLWYrAPEILLgSRHYSTPVDIWSVGCIFAEMVN--QKPlFPGdSEIDELFKIFR 218
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
366-585 3.27e-12

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: 67.25  E-value: 3.27e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEaigidkdRAAKPVTVAVKMLKDDATdKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd14193  12 LGGGRFGQVHKCE-------EKSSGLKLAAKIIKARSQ-KEKEEVKNEIEVMNQL-NHANLIQLYDAFESRNDIVLVMEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLreflrarrppgldysFDTCKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVT--EDNVMKIAD 523
Cdd:cd14193  83 VDGGEL---------------FDRIIDENYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCVsrEANQVKIID 147
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13112048 524 FGLARDvhnldyYKKTTngRLPVKWMAPEALFDRVYTHQ-----SDVWSFGVLLWEIFTlGGSPYPG 585
Cdd:cd14193 148 FGLARR------YKPRE--KLRVNFGTPEFLAPEVVNYEfvsfpTDMWSLGVIAYMLLS-GLSPFLG 205
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
366-593 3.36e-12

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: 68.01  E-value: 3.36e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKdraakpvTVAVKMLKDDA--TDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYVLV 443
Cdd:cd05590   3 LGKGSFGKVMLARLKESGR-------LYAVKVLKKDVilQDDDVECTMTEKRILSLARNHPFLTQLYCCFQTPDRLFFVM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 444 EYAAKGNLREFLRARRppgldySFDtckppEEQLTFKdlvscAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIAD 523
Cdd:cd05590  76 EFVNGGDLMFHIQKSR------RFD-----EARARFY-----AAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLAD 139
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13112048 524 FGLARD-VHNldyyKKTTNGRLPV-KWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEELFK 593
Cdd:cd05590 140 FGMCKEgIFN----GKTTSTFCGTpDYIAPEILQEMLYGPSVDWWAMGVLLYEMLC-GHAPFEAENEDDLFE 206
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
359-585 3.51e-12

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 69.44  E-value: 3.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048  359 RLTLGKPLGEGcfGqvvMAEA-IGIDK--DRaakpvTVAVKMLKDD-ATDKD--------------LSdlvsememmkmi 420
Cdd:NF033483   8 RYEIGERIGRG--G---MAEVyLAKDTrlDR-----DVAVKVLRPDlARDPEfvarfrreaqsaasLS------------ 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048  421 gkHKNIINLL--GactQGGPLYVLV-EYAAKGNLREFLRARRPpgldysfdtckppeeqLTFKDLVSCAYQVARGMEYLA 497
Cdd:NF033483  66 --HPNIVSVYdvG---EDGGIPYIVmEYVDGRTLKDYIREHGP----------------LSPEEAVEIMIQILSALEHAH 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048  498 SQKCIHRDLAARNVLVTEDNVMKIADFGLAR--DVHNLDYykktTNGRL-PVKWMAPE-ALFDRVyTHQSDVWSFGVLLW 573
Cdd:NF033483 125 RNGIVHRDIKPQNILITKDGRVKVTDFGIARalSSTTMTQ----TNSVLgTVHYLSPEqARGGTV-DARSDIYSLGIVLY 199
                        250
                 ....*....|..
gi 13112048  574 EIFTlGGSPYPG 585
Cdd:NF033483 200 EMLT-GRPPFDG 210
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
364-585 3.96e-12

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: 68.53  E-value: 3.96e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVMAEAIGIDKDRAAKpvtvavKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTqggPLYVLV 443
Cdd:cd07875  30 KPIGSGAQGIVCAAYDAILERNVAIK------KLSRPFQNQTHAKRAYRELVLMKCV-NHKNIIGLLNVFT---PQKSLE 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 444 EYAAKGNLREFLRArrppgldysfDTCKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIAD 523
Cdd:cd07875 100 EFQDVYIVMELMDA----------NLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILD 169
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13112048 524 FGLARDVHNLDYYKKTTNGRLpvkWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPG 585
Cdd:cd07875 170 FGLARTAGTSFMMTPYVVTRY---YRAPEVILGMGYKENVDIWSVGCIMGEMIK-GGVLFPG 227
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
409-634 4.07e-12

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: 67.57  E-value: 4.07e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 409 DLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEYAAkgnlreflrarrppGLDYSFDTCKPPEEQLTFKDLVSCAY- 487
Cdd:cd14094  51 DLKREASICHML-KHPHIVELLETYSSDGMLYMVFEFMD--------------GADLCFEIVKRADAGFVYSEAVASHYm 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 488 -QVARGMEYLASQKCIHRDLAARN-VLVTEDNV--MKIADFGLARDvhnLDYYKKTTNGRLPV-KWMAPEALFDRVYTHQ 562
Cdd:cd14094 116 rQILEALRYCHDNNIIHRDVKPHCvLLASKENSapVKLGGFGVAIQ---LGESGLVAGGRVGTpHFMAPEVVKREPYGKP 192
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13112048 563 SDVWSFGVLLWeIFTLGGSPYPGIPVEELFKLLKEGHRMDKP-----ANCTHDLYMIMREcwhAAPSQRPTFKQLVE 634
Cdd:cd14094 193 VDVWGCGVILF-ILLSGCLPFYGTKERLFEGIIKGKYKMNPRqwshiSESAKDLVRRMLM---LDPAERITVYEALN 265
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
481-583 4.69e-12

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: 66.77  E-value: 4.69e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 481 DLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARDVHNLDYYKKTTN-GRLpvKWMAPEALFDRVY 559
Cdd:cd14111 100 DVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGSAQSFNPLSLRQLGRRtGTL--EYMAPEMVKGEPV 177
                        90       100
                ....*....|....*....|....
gi 13112048 560 THQSDVWSFGVLLWeIFTLGGSPY 583
Cdd:cd14111 178 GPPADIWSIGVLTY-IMLSGRSPF 200
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
394-634 5.01e-12

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: 67.27  E-value: 5.01e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 394 AVKMLkddatDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYVLVEYAAKGNLreflrarrppgLDYSFDtckpp 473
Cdd:cd14091  29 AVKII-----DKSKRDPSEEIEILLRYGQHPNIITLRDVYDDGNSVYLVTELLRGGEL-----------LDRILR----- 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 474 EEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTED----NVMKIADFGLARDVhnldyykKTTNGRL--P-- 545
Cdd:cd14091  88 QKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADEsgdpESLRICDFGFAKQL-------RAENGLLmtPcy 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 546 -VKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPY---PGIPVEELFKLLKEGH-RMDKP--ANCTHDLYMIMREC 618
Cdd:cd14091 161 tANFVAPEVLKKQGYDAACDIWSLGVLLYTMLA-GYTPFasgPNDTPEVILARIGSGKiDLSGGnwDHVSDSAKDLVRKM 239
                       250
                ....*....|....*.
gi 13112048 619 WHAAPSQRPTFKQLVE 634
Cdd:cd14091 240 LHVDPSQRPTAAQVLQ 255
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
366-604 5.08e-12

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: 66.63  E-value: 5.08e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEaigidkDRAAKPVtVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd14083  11 LGTGAFSEVVLAE------DKATGKL-VAIKCIDKKALKGKEDSLENEIAVLRKI-KHPNIVQLLDIYESKSHLYLVMEL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLreflrarrppgldysFDTCKPpEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLV---TEDNVMKIA 522
Cdd:cd14083  83 VTGGEL---------------FDRIVE-KGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYyspDEDSKIMIS 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 523 DFGLArdvhnldyyKKTTNGRLPVK-----WMAPEALFDRVYTHQSDVWSFGVLLWeIFTLGGSPYPGIPVEELF-KLLK 596
Cdd:cd14083 147 DFGLS---------KMEDSGVMSTAcgtpgYVAPEVLAQKPYGKAVDCWSIGVISY-ILLCGYPPFYDENDSKLFaQILK 216

                ....*...
gi 13112048 597 EGHRMDKP 604
Cdd:cd14083 217 AEYEFDSP 224
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
366-599 5.80e-12

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: 66.94  E-value: 5.80e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAeaigidKDRAAKPVtVAVKMLKDDATDKDlSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd14166  11 LGSGAFSEVYLV------KQRSTGKL-YALKCIKKSPLSRD-SSLENEIAVLKRI-KHENIVTLEDIYESTTHYYLVMQL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLREFLRARrppGLdysfdtckppeeqLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLV---TEDNVMKIA 522
Cdd:cd14166  82 VSGGELFDRILER---GV-------------YTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYltpDENSKIMIT 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 523 DFGLArdvhnldyyKKTTNGRLPVK-----WMAPEALFDRVYTHQSDVWSFGVLLWeIFTLGGSPYPGIPVEELFKLLKE 597
Cdd:cd14166 146 DFGLS---------KMEQNGIMSTAcgtpgYVAPEVLAQKPYSKAVDCWSIGVITY-ILLCGYPPFYEETESRLFEKIKE 215

                ..
gi 13112048 598 GH 599
Cdd:cd14166 216 GY 217
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
359-639 5.94e-12

Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR2 interacts with the protein phosphatase calcineurin and functions in calcium-mediated ERK signaling. It also functions in energy metabolism by regulating AMP kinase and AMPK-dependent processes such as glucose uptake and fatty acid oxidation. KSR proteins act as scaffold proteins that function downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases. The KSR2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 66.57  E-value: 5.94e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 359 RLTLGKPLGEGCFGQVVMAEAIGidkdraakpvTVAVKMLKDDATDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGP 438
Cdd:cd14153   1 QLEIGELIGKGRFGQVYHGRWHG----------EVAIRLIDIERDNEEQLKAFKREVMAYRQTRHENVVLFMGACMSPPH 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 439 LYVLVEYAAKGNLREFLRARRppgldYSFDTCKPPEeqltfkdlvsCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNV 518
Cdd:cd14153  71 LAIITSLCKGRTLYSVVRDAK-----VVLDVNKTRQ----------IAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKV 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 519 MkIADFGLARDVHNLDYYKKTTNGRLPVKW-----------MAPEALFDRV-YTHQSDVWSFGVLLWEIFTLGGsPYPGI 586
Cdd:cd14153 136 V-ITDFGLFTISGVLQAGRREDKLRIQSGWlchlapeiirqLSPETEEDKLpFSKHSDVFAFGTIWYELHAREW-PFKTQ 213
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 13112048 587 PVEELFKLLKEGHRMD-KPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRV 639
Cdd:cd14153 214 PAEAIIWQVGSGMKPNlSQIGMGKEISDILLFCWAYEQEERPTFSKLMEMLEKL 267
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
348-634 8.94e-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: 66.58  E-value: 8.94e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 348 PADPkwelsRARLTLGKPLGEGCFGQVVMAEAIGIDKdraakpvTVAVKMLkDDATDKDLSDLVSEMEMMKMIgKHKNII 427
Cdd:cd06657  15 PGDP-----RTYLDNFIKIGEGSTGIVCIATVKSSGK-------LVAVKKM-DLRKQQRRELLFNEVVIMRDY-QHENVV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 428 NLLGACTQGGPLYVLVEYAAKGNLREFLRARRPPgldysfdtckppEEQLTfkdlvSCAYQVARGMEYLASQKCIHRDLA 507
Cdd:cd06657  81 EMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMN------------EEQIA-----AVCLAVLKALSVLHAQGVIHRDIK 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 508 ARNVLVTEDNVMKIADFGLARDVHNLDYYKKTTNGrlPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIP 587
Cdd:cd06657 144 SDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVG--TPYWMAPELISRLPYGPEVDIWSLGIMVIEMVD-GEPPYFNEP 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 13112048 588 VEELFKLLKEG--HRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVE 634
Cdd:cd06657 221 PLKAMKMIRDNlpPKLKNLHKVSPSLKGFLDRLLVRDPAQRATAAELLK 269
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
366-583 1.05e-11

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: 66.14  E-value: 1.05e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMaeaiGIDKDRAAKpvtVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNII-------NLLGACTQGGP 438
Cdd:cd14038   2 LGTGGFGNVLR----WINQETGEQ---VAIKQCRQELSPKNRERWCLEIQIMKRL-NHPNVVaardvpeGLQKLAPNDLP 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 439 LYVLvEYAAKGNLREFLRarrppgldySFDTCKPPEEQlTFKDLVScayQVARGMEYLASQKCIHRDLAARNVLVTEDN- 517
Cdd:cd14038  74 LLAM-EYCQGGDLRKYLN---------QFENCCGLREG-AILTLLS---DISSALRYLHENRIIHRDLKPENIVLQQGEq 139
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13112048 518 --VMKIADFGLARDvhnLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPY 583
Cdd:cd14038 140 rlIHKIIDLGYAKE---LDQGSLCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECIT-GFRPF 203
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
393-646 1.08e-11

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 5; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK5 (also called MEK5) is a dual-specificity PK that phosphorylates its downstream target, extracellular signal-regulated kinase 5 (ERK5), on specific threonine and tyrosine residues. MKK5 is activated by MEKK2 and MEKK3 in response to mitogenic and stress stimuli. The ERK5 cascade promotes cell proliferation, differentiation, neuronal survival, and neuroprotection. This cascade plays an essential role in heart development. Mice deficient in either ERK5 or MKK5 die around embryonic day 10 due to cardiovascular defects including underdevelopment of the myocardium. In addition, MKK5 is associated with metastasis and unfavorable prognosis in prostate cancer. The MKK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 66.06  E-value: 1.08e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 393 VAVKMLKDDATDKDLSDLVSEMEMMKMIGKhKNIINLLGACTQGGPLYVLVEYAAKGNLREFLRArrppgldysfdtckp 472
Cdd:cd06619  29 LAVKVIPLDITVELQKQIMSELEILYKCDS-PYIIGFYGAFFVENRISICTEFMDGGSLDVYRKI--------------- 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 473 PEEQLTfkdlvSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARDVHNldYYKKT---TNGrlpvkWM 549
Cdd:cd06619  93 PEHVLG-----RIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQLVN--SIAKTyvgTNA-----YM 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 550 APEALFDRVYTHQSDVWSFGVLLWEIfTLGGSPYPGI--------PVEELFKLLKEGHRMDKPANCTHDLYMIMRECWHA 621
Cdd:cd06619 161 APERISGEQYGIHSDVWSLGISFMEL-ALGRFPYPQIqknqgslmPLQLLQCIVDEDPPVLPVGQFSEKFVHFITQCMRK 239
                       250       260
                ....*....|....*....|....*
gi 13112048 622 APSQRPTFKQLvedLDRVLTVTSTD 646
Cdd:cd06619 240 QPKERPAPENL---MDHPFIVQYND 261
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
366-577 1.10e-11

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: 65.90  E-value: 1.10e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAeaigidKDRAAKPVtVAVKMLKDDATDKDL-SDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVE 444
Cdd:cd07861   8 IGEGTYGVVYKG------RNKKTGQI-VAMKKIRLESEEEGVpSTAIREISLLKEL-QHPNIVCLEDVLMQENRLYLVFE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 445 YAAKgNLREFLrarrppgldysfDTCkPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADF 524
Cdd:cd07861  80 FLSM-DLKKYL------------DSL-PKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADF 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13112048 525 GLARDVHnldyykkttngrLPVK----------WMAPEALFDRV-YTHQSDVWSFGVLLWEIFT 577
Cdd:cd07861 146 GLARAFG------------IPVRvythevvtlwYRAPEVLLGSPrYSTPVDIWSIGTIFAEMAT 197
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
487-585 1.15e-11

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: 66.63  E-value: 1.15e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 487 YQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARdvhnldyykkTTNGR-------LPVKWM-APEALFD-R 557
Cdd:cd07858 115 YQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLAR----------TTSEKgdfmteyVVTRWYrAPELLLNcS 184
                        90       100
                ....*....|....*....|....*....
gi 13112048 558 VYTHQSDVWSFGVLLWEIftLGGSP-YPG 585
Cdd:cd07858 185 EYTTAIDVWSVGCIFAEL--LGRKPlFPG 211
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
366-585 1.46e-11

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase; Protein Kinases (PKs), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK) subfamily, catalytic (c) domain. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. The DYRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein S/T PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. Vertebrates contain multiple DYRKs (DYRK1-4) and mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A is involved in neuronal differentiation and is implicated in the pathogenesis of DS (Down syndrome). DYRK1B plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRK2 promotes apoptosis in response to DNA damage by phosphorylating the tumor suppressor p53, while DYRK3 promotes cell survival by phosphorylating SIRT1 and promoting p53 deacetylation. DYRK4 is a testis-specific kinase that may function during spermiogenesis.


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 66.03  E-value: 1.46e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAeaigidKDRAAKpVTVAVKMLKDdaTDKDLSDLVSEMEMMKMIGKHK-----NIINLLGACTQGGPLY 440
Cdd:cd14210  21 LGKGSFGQVVKC------LDHKTG-QLVAIKIIRN--KKRFHQQALVEVKILKHLNDNDpddkhNIVRYKDSFIFRGHLC 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 441 VLVEYAAKgNLREFLRARRPPGLDYSfdtckppeeqltfkdLV-SCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVM 519
Cdd:cd14210  92 IVFELLSI-NLYELLKSNNFQGLSLS---------------LIrKFAKQILQALQFLHKLNIIHCDLKPENILLKQPSKS 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13112048 520 --KIADFGLARDVHNLDY-------YKkttngrlpvkwmAPEALFDRVYTHQSDVWSFGVLLWEIFTlgGSP-YPG 585
Cdd:cd14210 156 siKVIDFGSSCFEGEKVYtyiqsrfYR------------APEVILGLPYDTAIDMWSLGCILAELYT--GYPlFPG 217
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
487-575 1.47e-11

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: 66.24  E-value: 1.47e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 487 YQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARDV-HNLDYYKKTTNGRLPVKWM-APEALF--DRvYTHQ 562
Cdd:cd07855 116 YQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGMARGLcTSPEEHKYFMTEYVATRWYrAPELMLslPE-YTQA 194
                        90
                ....*....|...
gi 13112048 563 SDVWSFGVLLWEI 575
Cdd:cd07855 195 IDMWSVGCIFAEM 207
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
487-585 1.49e-11

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: 66.17  E-value: 1.49e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 487 YQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLAR-DVHNLDYYKKTTNgRLPVKWM-APE-ALFDRVYTHQS 563
Cdd:cd07849 113 YQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLARiADPEHDHTGFLTE-YVATRWYrAPEiMLNSKGYTKAI 191
                        90       100
                ....*....|....*....|...
gi 13112048 564 DVWSFGVLLWEIFTlgGSP-YPG 585
Cdd:cd07849 192 DIWSVGCILAEMLS--NRPlFPG 212
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
366-585 1.99e-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: 1.99e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQV--VMAEAIGIDkdRAAKPVTvavkmlKDDATDKDLsdLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLV 443
Cdd:cd14190  12 LGGGKFGKVhtCTEKRTGLK--LAAKVIN------KQNSKDKEM--VLLEIQVMNQL-NHRNLIQLYEAIETPNEIVLFM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 444 EYAAKGNLREFLrarrppgLDYSFdtckppeeQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLV--TEDNVMKI 521
Cdd:cd14190  81 EYVEGGELFERI-------VDEDY--------HLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCvnRTGHQVKI 145
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 522 ADFGLARdvhnldyyKKTTNGRLPVKWMAPEAL------FDRVyTHQSDVWSFGVLLWEIFTlGGSPYPG 585
Cdd:cd14190 146 IDFGLAR--------RYNPREKLKVNFGTPEFLspevvnYDQV-SFPTDMWSMGVITYMLLS-GLSPFLG 205
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
441-633 2.24e-11

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 66.82  E-value: 2.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048  441 VLVEYAAKGNLREFLRARRPPGLDYsfdtcKPPEEQLTFkdlvscaYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMK 520
Cdd:PTZ00283 116 LVLDYANAGDLRQEIKSRAKTNRTF-----REHEAGLLF-------IQVLLAVHHVHSKHMIHRDIKSANILLCSNGLVK 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048  521 IADFGLARDVHNL--DYYKKTTNGRlPVkWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLgGSPYPGIPVEELFKLLKEG 598
Cdd:PTZ00283 184 LGDFGFSKMYAATvsDDVGRTFCGT-PY-YVAPEIWRRKPYSKKADMFSLGVLLYELLTL-KRPFDGENMEEVMHKTLAG 260
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 13112048  599 HRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLV 633
Cdd:PTZ00283 261 RYDPLPPSISPEMQEIVTALLSSDPKRRPSSSKLL 295
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
392-623 2.51e-11

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: 65.06  E-value: 2.51e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 392 TVAVKMLKDdatdKDLSDLVSEMEMMKMIG-KHKNIINLLGACTQGG----PLYVLVEYAAKGNLREFLRArrppgldys 466
Cdd:cd14141  20 YVAVKIFPI----QDKLSWQNEYEIYSLPGmKHENILQFIGAEKRGTnldvDLWLITAFHEKGSLTDYLKA--------- 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 467 fdtckppeEQLTFKDLVSCAYQVARGMEYLASQ----------KCIHRDLAARNVLVTEDNVMKIADFGLARDVHNLDYY 536
Cdd:cd14141  87 --------NVVSWNELCHIAQTMARGLAYLHEDipglkdghkpAIAHRDIKSKNVLLKNNLTACIADFGLALKFEAGKSA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 537 KKTTNGRLPVKWMAPEAL-----FDRVYTHQSDVWSFGVLLWEIF---TLGGSPYPG--IPVEE------LFKLLKE--G 598
Cdd:cd14141 159 GDTHGQVGTRRYMAPEVLegainFQRDAFLRIDMYAMGLVLWELAsrcTASDGPVDEymLPFEEevgqhpSLEDMQEvvV 238
                       250       260
                ....*....|....*....|....*
gi 13112048 599 HRMDKPancthdlymIMRECWHAAP 623
Cdd:cd14141 239 HKKKRP---------VLRECWQKHA 254
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
364-595 2.87e-11

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: 65.49  E-value: 2.87e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVMAEAIGIDKDRAAKPVTVAVKMLKDDatdkdLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLV 443
Cdd:cd05593  21 KLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDE-----VAHTLTESRVLKNT-RHPFLTSLKYSFQTKDRLCFVM 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 444 EYAAKGNLREFLRARRPpgldYSfdtckppEEQLTFKdlvscAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIAD 523
Cdd:cd05593  95 EYVNGGELFFHLSRERV----FS-------EDRTRFY-----GAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITD 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13112048 524 FGLARDVHNLDYYKKTTNGrlPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEELFKLL 595
Cdd:cd05593 159 FGLCKEGITDAATMKTFCG--TPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELI 227
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
366-646 2.89e-11

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: 64.48  E-value: 2.89e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEaigidkDRAAKPvTVAVKMLKDDATDKDLSDlvSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd14087   9 IGRGSFSRVVRVE------HRVTRQ-PYAIKMIETKCRGREVCE--SELNVLRRV-RHTNIIQLIEVFETKERVYMVMEL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLREFLRARRppgldySFdtckppeeqlTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLV----TEDNVMkI 521
Cdd:cd14087  79 ATGGELFDRIIAKG------SF----------TERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYyhpgPDSKIM-I 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 522 ADFGLARDVHNLDYYKKTTNGRLPvKWMAPEALFDRVYTHQSDVWSFGVLLWeIFTLGGSPYPGIPVEELFKLLKEGHrm 601
Cdd:cd14087 142 TDFGLASTRKKGPNCLMKTTCGTP-EYIAPEILLRKPYTQSVDMWAVGVIAY-ILLSGTMPFDDDNRTRLYRQILRAK-- 217
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 13112048 602 dkpancthdlYMIMRECWhaaPSQRPTFKQLVedlDRVLTVTSTD 646
Cdd:cd14087 218 ----------YSYSGEPW---PSVSNLAKDFI---DRLLTVNPGE 246
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
468-597 3.33e-11

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: 64.55  E-value: 3.33e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 468 DTCKPPEEQLTFKDLVscaYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARDV-HNLdyyKKTTNGRLPV 546
Cdd:cd07843  97 ETMKQPFLQSEVKCLM---LQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGLAREYgSPL---KPYTQLVVTL 170
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 13112048 547 KWMAPEALFD-RVYTHQSDVWSFGVLLWEIFTlgGSP-YPGI-PVEELFKLLKE 597
Cdd:cd07843 171 WYRAPELLLGaKEYSTAIDMWSVGCIFAELLT--KKPlFPGKsEIDQLNKIFKL 222
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
387-582 3.34e-11

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: 64.30  E-value: 3.34e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 387 AAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYVLVEYAAKGNLreflrarrppgLDYS 466
Cdd:cd14093  32 AVKIIDITGEKSSENEAEELREATRREIEILRQVSGHPNIIELHDVFESPTFIFLVFELCRKGEL-----------FDYL 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 467 FDTCKPPEEQ--LTFKDLVScayqvarGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARDVHNLDYYKKT--TNG 542
Cdd:cd14093 101 TEVVTLSEKKtrRIMRQLFE-------AVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFATRLDEGEKLRELcgTPG 173
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 13112048 543 rlpvkWMAPEAL----FDRV--YTHQSDVWSFGVLLWEIftLGGSP 582
Cdd:cd14093 174 -----YLAPEVLkcsmYDNApgYGKEVDMWACGVIMYTL--LAGCP 212
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
171-245 3.68e-11

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 59.54  E-value: 3.68e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13112048 171 TVRFRCPAAGNPTPSISWLKNGREFRGEHRI---GGiKLRHQQWSLvmesvvpSDRGNYTCVVENKFGSIRQTYTLDV 245
Cdd:cd05728  16 SLRWECKASGNPRPAYRWLKNGQPLASENRIeveAG-DLRITKLSL-------SDSGMYQCVAENKHGTIYASAELAV 85
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
487-633 4.93e-11

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: 64.27  E-value: 4.93e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 487 YQVARGMEYL-ASQKCIHRDLAARNVLVTEDNVMKIADFGLARDVHN---LDYYKKTTNGRLPV------KWMAPEALFD 556
Cdd:cd14011 121 LQISEALSFLhNDVKLVHGNICPESVVINSNGEWKLAGFDFCISSEQatdQFPYFREYDPNLPPlaqpnlNYLAPEYILS 200
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 557 RVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFK-------LLKEGHRMDKPANCTHDLymimRECWHAAPSQRPTF 629
Cdd:cd14011 201 KTCDPASDMFSLGVLIYAIYNKGKPLFDCVNNLLSYKknsnqlrQLSLSLLEKVPEELRDHV----KTLLNVTPEVRPDA 276

                ....
gi 13112048 630 KQLV 633
Cdd:cd14011 277 EQLS 280
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
365-577 5.93e-11

Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PRP4 phosphorylates a number of factors involved in the formation of active spliceosomes, which catalyze pre-mRNA splicing. It phosphorylates PRP6 and PRP31, components of the U4/U6-U5 tri-small nuclear ribonucleoprotein (snRNP), during spliceosomal complex formation. In fission yeast, PRP4 phosphorylates the splicing factor PRP1 (U5-102 kD in mammals). Thus, PRP4 plays a key role in regulating spliceosome assembly and pre-mRNA splicing. It also plays an important role in mitosis by acting as a spindle assembly checkpoint kinase that is required for chromosome alignment and the recruitment of the checkpoint proteins MPS1, MAD1, and MAD2 at kinetochores. The PRP4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 64.17  E-value: 5.93e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 365 PLGEGCFGQVVMAEaigidkDRAAKPVTVAVKMLKDDATDKDLSDLvsEMEMMKMIGKH-----KNIINLLGACTQGGPL 439
Cdd:cd14135   7 YLGKGVFSNVVRAR------DLARGNQEVAIKIIRNNELMHKAGLK--ELEILKKLNDAdpddkKHCIRLLRHFEHKNHL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 440 YVLVEYAAkGNLREFLRarrppglDYSFDTckppeeQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTED-NV 518
Cdd:cd14135  79 CLVFESLS-MNLREVLK-------KYGKNV------GLNIKAVRSYAQQLFLALKHLKKCNILHADIKPDNILVNEKkNT 144
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13112048 519 MKIADFGLARDVHNLD--------YYKkttngrlpvkwmAPEALFDRVYTHQSDVWSFGVLLWEIFT 577
Cdd:cd14135 145 LKLCDFGSASDIGENEitpylvsrFYR------------APEIILGLPYDYPIDMWSVGCTLYELYT 199
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
486-583 1.01e-10

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. GRKs play important roles in the cardiovascular, immune, respiratory, skeletal, and nervous systems. They contain a central catalytic domain, flanked by N- and C-terminal extensions. The N-terminus contains an RGS (regulator of G protein signaling) homology (RH) domain and several motifs. The C-terminus diverges among different groups of GRKs. There are seven types of GRKs, named GRK1 to GRK7, which are subdivided into three main groups: visual (GRK1/7); beta-adrenergic receptor kinases (GRK2/3); and GRK4-like (GRK4/5/6). Expression of GRK2/3/5/6 is widespread while GRK1/4/7 show a limited tissue distribution. The substrate spectrum of the widely expressed GRKs partially overlaps. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 62.93  E-value: 1.01e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 486 AYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARDVHNldyyKKTTNGRL-PVKWMAPEALFDRV-YTHQS 563
Cdd:cd05577 101 AAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAVEFKG----GKKIKGRVgTHGYMAPEVLQKEVaYDFSV 176
                        90       100
                ....*....|....*....|
gi 13112048 564 DVWSFGVLLWEIFTlGGSPY 583
Cdd:cd05577 177 DWFALGCMLYEMIA-GRSPF 195
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
366-604 1.06e-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: 63.14  E-value: 1.06e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKdraakpvTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd14168  18 LGTGAFSEVVLAEERATGK-------LFAVKCIPKKALKGKESSIENEIAVLRKI-KHENIVALEDIYESPNHLYLVMQL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLREFLrarrppgLDYSFdtckppeeqLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLV---TEDNVMKIA 522
Cdd:cd14168  90 VSGGELFDRI-------VEKGF---------YTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYfsqDEESKIMIS 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 523 DFGLARDVHNLDYYkkTTNGRLPvKWMAPEALFDRVYTHQSDVWSFGVLLWeIFTLGGSPYPGIPVEELF-KLLKEGHRM 601
Cdd:cd14168 154 DFGLSKMEGKGDVM--STACGTP-GYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFeQILKADYEF 229

                ...
gi 13112048 602 DKP 604
Cdd:cd14168 230 DSP 232
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
366-585 1.10e-10

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: 63.45  E-value: 1.10e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKDRAAKpvTVAVKMLKddaTDKDLSDLVSEMEMMKMIGKhKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd05632  10 LGKGGFGEVCACQVRATGKMYACK--RLEKKRIK---KRKGESMALNEKQILEKVNS-QFVVNLAYAYETKDALCLVLTI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLREFLRARRPPGLDysfdtckppEEQLTFKdlvscAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFG 525
Cdd:cd05632  84 MNGGDLKFHIYNMGNPGFE---------EERALFY-----AAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLG 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13112048 526 LARDVHNLDYYKkttnGRL-PVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPG 585
Cdd:cd05632 150 LAVKIPEGESIR----GRVgTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIE-GQSPFRG 205
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
362-583 1.34e-10

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: 62.82  E-value: 1.34e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 362 LGKPLGEGCFGQVVMAEAIGIDKDRAAKpvTVAVKMLkddaTDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYV 441
Cdd:cd14086   5 LKEELGKGAFSVVRRCVQKSTGQEFAAK--IINTKKL----SARDHQKLEREARICRLL-KHPNIVRLHDSISEEGFHYL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 442 LVEYAAKGNLREFLRARrppgldysfdtckppeEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLV---TEDNV 518
Cdd:cd14086  78 VFDLVTGGELFEDIVAR----------------EFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLaskSKGAA 141
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13112048 519 MKIADFGLARDVH--NLDYYK-KTTNGrlpvkWMAPEALFDRVYTHQSDVWSFGVLLWeIFTLGGSPY 583
Cdd:cd14086 142 VKLADFGLAIEVQgdQQAWFGfAGTPG-----YLSPEVLRKDPYGKPVDIWACGVILY-ILLVGYPPF 203
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
362-624 1.61e-10

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


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 62.05  E-value: 1.61e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 362 LGKPLGEGCFGQVVMAEAIGIDKdraakpvTVAVKMLkdDATDKD---LSDLVSEMEMMKMIgKHKNIINLLGACTQGGP 438
Cdd:cd14074   7 LEETLGRGHFAVVKLARHVFTGE-------KVAVKVI--DKTKLDdvsKAHLFQEVRCMKLV-QHPNVVRLYEVIDTQTK 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 439 LYVLVEYAAKGNLREFLrARRPPGLDysfdtckppeeqltfKDLVSCAY-QVARGMEYLASQKCIHRDLAARNVLVTEDN 517
Cdd:cd14074  77 LYLILELGDGGDMYDYI-MKHENGLN---------------EDLARKYFrQIVSAISYCHKLHVVHRDLKPENVVFFEKQ 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 518 VM-KIADFGLARDV---HNLDyykkTTNGRLpvKWMAPEALFDRVYTHQS-DVWSFGVLLWEIftLGGSPypgiPVEElf 592
Cdd:cd14074 141 GLvKLTDFGFSNKFqpgEKLE----TSCGSL--AYSAPEILLGDEYDAPAvDIWSLGVILYML--VCGQP----PFQE-- 206
                       250       260       270
                ....*....|....*....|....*....|..
gi 13112048 593 kllkeghrmdkpANCTHDLYMIMrECWHAAPS 624
Cdd:cd14074 207 ------------ANDSETLTMIM-DCKYTVPA 225
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
359-628 2.26e-10

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: 62.37  E-value: 2.26e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 359 RLTLGKPLGEGCFGQVVMAEAIGidkdraaKPVTVAVKMLKDDATdkdlsdLVSEMEMMK-MIGKHKNIINLLGACTQGG 437
Cdd:cd14219   6 QIQMVKQIGKGRYGEVWMGKWRG-------EKVAVKVFFTTEEAS------WFRETEIYQtVLMRHENILGFIAADIKGT 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 438 ----PLYVLVEYAAKGNLREFLRArrppgldysfdtckppeEQLTFKDLVSCAYQVARGMEYLASQ--------KCIHRD 505
Cdd:cd14219  73 gswtQLYLITDYHENGSLYDYLKS-----------------TTLDTKAMLKLAYSSVSGLCHLHTEifstqgkpAIAHRD 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 506 LAARNVLVTEDNVMKIADFGLA----RDVHNLDYYKKTTNGrlPVKWMAPEALFDRVYTHQ------SDVWSFGVLLWEI 575
Cdd:cd14219 136 LKSKNILVKKNGTCCIADLGLAvkfiSDTNEVDIPPNTRVG--TKRYMPPEVLDESLNRNHfqsyimADMYSFGLILWEV 213
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13112048 576 F---TLGGS------PYPG-IPVEELFKLLKEGHRMDK--PA--------NCTHDLYMIMRECWHAAPSQRPT 628
Cdd:cd14219 214 ArrcVSGGIveeyqlPYHDlVPSDPSYEDMREIVCIKRlrPSfpnrwssdECLRQMGKLMTECWAHNPASRLT 286
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
359-585 2.38e-10

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: 61.93  E-value: 2.38e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 359 RLTLGKPLGEGCFGqvVMAEAIGIDKDRAakpvtVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGP 438
Cdd:cd14183   7 RYKVGRTIGDGNFA--VVKECVERSTGRE-----YALKIINKSKCRGKEHMIQNEVSILRRV-KHPNIVLLIEEMDMPTE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 439 LYVLVEYAAKGNLreflrarrppgldysFDTCKPpEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTE--- 515
Cdd:cd14183  79 LYLVMELVKGGDL---------------FDAITS-TNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEhqd 142
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13112048 516 -DNVMKIADFGLARDVHNLDYykkTTNGRlPVkWMAPEALFDRVYTHQSDVWSFGVLLWeIFTLGGSPYPG 585
Cdd:cd14183 143 gSKSLKLGDFGLATVVDGPLY---TVCGT-PT-YVAPEIIAETGYGLKVDIWAAGVITY-ILLCGFPPFRG 207
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
426-584 2.48e-10

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: 62.07  E-value: 2.48e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 426 IINLLGACTQGGPLYVLVEYAAKGNLREFL-RARRPPgldysfdtckppeEQLtfkdLVSCAYQVARGMEYLASQ-KCIH 503
Cdd:cd06615  61 IVGFYGAFYSDGEISICMEHMDGGSLDQVLkKAGRIP-------------ENI----LGKISIAVLRGLTYLREKhKIMH 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 504 RDLAARNVLVTEDNVMKIADFGLARDVHNldyykKTTNGRLPVK-WMAPEALFDRVYTHQSDVWSFGVLLWEIfTLGGSP 582
Cdd:cd06615 124 RDVKPSNILVNSRGEIKLCDFGVSGQLID-----SMANSFVGTRsYMSPERLQGTHYTVQSDIWSLGLSLVEM-AIGRYP 197

                ..
gi 13112048 583 YP 584
Cdd:cd06615 198 IP 199
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
364-575 2.61e-10

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: 62.74  E-value: 2.61e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVMA--EAIGIDkdraakpvtVAVKMLKDDATDKDLSDLV-SEMEMMKMIgKHKNIINLLGACTqggPLY 440
Cdd:cd07876  27 KPIGSGAQGIVCAAfdTVLGIN---------VAVKKLSRPFQNQTHAKRAyRELVLLKCV-NHKNIISLLNVFT---PQK 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 441 VLVEYAAKGNLREFLRArrppgldysfDTCKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMK 520
Cdd:cd07876  94 SLEEFQDVYLVMELMDA----------NLCQVIHMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLK 163
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 13112048 521 IADFGLARDVHN---LDYYKKTTNGRlpvkwmAPEALFDRVYTHQSDVWSFGVLLWEI 575
Cdd:cd07876 164 ILDFGLARTACTnfmMTPYVVTRYYR------APEVILGMGYKENVDIWSVGCIMGEL 215
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
362-660 2.68e-10

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 63.13  E-value: 2.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048  362 LGKPLGEGCFGqvVMAEAIGIDKDRaakpvTVAVKMLKDDATDKDlsdlvSEMEMMKMIgKHKNIINL----LGACTQGG 437
Cdd:PTZ00036  70 LGNIIGNGSFG--VVYEAICIDTSE-----KVAIKKVLQDPQYKN-----RELLIMKNL-NHINIIFLkdyyYTECFKKN 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048  438 P----LYVLVEYAAKgNLREFLRArrppgldYSFDTCKPPeeqLTFKDLVScaYQVARGMEYLASQKCIHRDLAARNVLV 513
Cdd:PTZ00036 137 EknifLNVVMEFIPQ-TVHKYMKH-------YARNNHALP---LFLVKLYS--YQLCRALAYIHSKFICHRDLKPQNLLI 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048  514 TED-NVMKIADFGLARdvhNLDYYKKTTNGRLPVKWMAPEALFDRV-YTHQSDVWSFGVLLWEIFtLGGSPYPG-IPVEE 590
Cdd:PTZ00036 204 DPNtHTLKLCDFGSAK---NLLAGQRSVSYICSRFYRAPELMLGATnYTTHIDLWSLGCIIAEMI-LGYPIFSGqSSVDQ 279
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048  591 LFKLLKEghrMDKPancTHDLYMIMRECWhaAPSQRPTFKQlvEDLDRVLTVTSTDEYLDLSAPFEQYSP 660
Cdd:PTZ00036 280 LVRIIQV---LGTP---TEDQLKEMNPNY--ADIKFPDVKP--KDLKKVFPKGTPDDAINFISQFLKYEP 339
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
165-245 3.15e-10

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 57.02  E-value: 3.15e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 165 AVPAANTVRFRCPAAGNPTPSISWLKNGrefrGEHRIGGIKLRHQQwSLVMESVVPSDRGNYTCVVENKFGSIRQTYTLD 244
Cdd:cd05725   8 VVLVDDSAEFQCEVGGDPVPTVRWRKED----GELPKGRYEILDDH-SLKIRKVTAGDMGSYTCVAENMVGKIEASATLT 82

                .
gi 13112048 245 V 245
Cdd:cd05725  83 V 83
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
487-595 3.24e-10

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: 61.63  E-value: 3.24e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 487 YQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARdvhnldyYK----KTTNGRLPVKWMAPE--ALFDRVYT 560
Cdd:cd07844 105 FQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLAR-------AKsvpsKTYSNEVVTLWYRPPdvLLGSTEYS 177
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 13112048 561 HQSDVWSFGVLLWEIFTlgGSP-YPGI--PVEEL---FKLL 595
Cdd:cd07844 178 TSLDMWGVGCIFYEMAT--GRPlFPGStdVEDQLhkiFRVL 216
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
364-594 3.25e-10

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: 61.52  E-value: 3.25e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVMaeaiGIDKDRAAkpvTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLV 443
Cdd:cd07870   6 EKLGEGSYATVYK----GISRINGQ---LVALKVISMKTEEGVPFTAIREASLLKGL-KHANIVLLHDIIHTKETLTFVF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 444 EYAaKGNLREFLrARRPPGLDysfdtckpPEEQLTFkdlvscAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIAD 523
Cdd:cd07870  78 EYM-HTDLAQYM-IQHPGGLH--------PYNVRLF------MFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLAD 141
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13112048 524 FGLARdvhNLDYYKKTTNGRLPVKWM-APEALFDRV-YTHQSDVWSFGVLLWEIFTlgGSP-YPGIP--VEELFKL 594
Cdd:cd07870 142 FGLAR---AKSIPSQTYSSEVVTLWYrPPDVLLGATdYSSALDIWGAGCIFIEMLQ--GQPaFPGVSdvFEQLEKI 212
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
362-583 3.26e-10

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: 61.20  E-value: 3.26e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 362 LGKPLGEGCFGqvVMAEAIgidkDRAAKPvTVAVKMLkDDATDKDLSDLV-SEMEMMKMIgKHKNIINLLGACTQGGPLY 440
Cdd:cd14184   5 IGKVIGDGNFA--VVKECV----ERSTGK-EFALKII-DKAKCCGKEHLIeNEVSILRRV-KHPNIIMLIEEMDTPAELY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 441 VLVEYAAKGNLreflrarrppgldysFDTCKPpEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTE----D 516
Cdd:cd14184  76 LVMELVKGGDL---------------FDAITS-STKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVCEypdgT 139
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13112048 517 NVMKIADFGLARDVHNLDYykkTTNGRlPVkWMAPEALFDRVYTHQSDVWSFGVLLWeIFTLGGSPY 583
Cdd:cd14184 140 KSLKLGDFGLATVVEGPLY---TVCGT-PT-YVAPEIIAETGYGLKVDIWAAGVITY-ILLCGFPPF 200
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
393-591 3.53e-10

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: 61.81  E-value: 3.53e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 393 VAVKMLK-DDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEYAAKGNLREFLRARRPPGLDYSFdtck 471
Cdd:cd08226  28 VTVKITNlDNCSEEHLKALQNEVVLSHFF-RHPNIMTHWTVFTEGSWLWVISPFMAYGSARGLLKTYFPEGMNEAL---- 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 472 ppeeqltfkdLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIAdfGLardvHNLdyYKKTTNGR-------- 543
Cdd:cd08226 103 ----------IGNILYGAIKALNYLHQNGCIHRSVKASHILISGDGLVSLS--GL----SHL--YSMVTNGQrskvvydf 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 13112048 544 -------LPvkWMAPEALFDRV--YTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEEL 591
Cdd:cd08226 165 pqfstsvLP--WLSPELLRQDLhgYNVKSDIYSVGITACELAR-GQVPFQDMRRTQM 218
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
487-585 3.94e-10

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: 62.11  E-value: 3.94e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 487 YQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARDVHN--------LDYykkttngrLPVKWM-APE---AL 554
Cdd:cd07859 110 YQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGLARVAFNdtptaifwTDY--------VATRWYrAPElcgSF 181
                        90       100       110
                ....*....|....*....|....*....|..
gi 13112048 555 FDRvYTHQSDVWSFGVLLWEIFTlgGSP-YPG 585
Cdd:cd07859 182 FSK-YTPAIDIWSIGCIFAEVLT--GKPlFPG 210
PTK_Tyk2_rpt1 cd05076
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; Tyk2 is ...
423-636 5.41e-10

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: 60.69  E-value: 5.41e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 423 HKNIINLLGACTQGGPLYVLVEYAAKGNLREFLRARRppgldysfdTCKPPEEQLTfkdlvsCAYQVARGMEYLASQKCI 502
Cdd:cd05076  74 HTHLVFVHGVCVRGSENIMVEEFVEHGPLDVWLRKEK---------GHVPMAWKFV------VARQLASALSYLENKNLV 138
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 503 HRDLAARNVLVT----EDNV---MKIADFGLARDVHNldyyKKTTNGRLPvkWMAPEALFD-RVYTHQSDVWSFGVLLWE 574
Cdd:cd05076 139 HGNVCAKNILLArlglEEGTspfIKLSDPGVGLGVLS----REERVERIP--WIAPECVPGgNSLSTAADKWGFGATLLE 212
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13112048 575 IFTLGGSPYPGIPVEELFKLLKEGHRMDKPAncTHDLYMIMRECWHAAPSQRPTFKQLVEDL 636
Cdd:cd05076 213 ICFNGEAPLQSRTPSEKERFYQRQHRLPEPS--CPELATLISQCLTYEPTQRPSFRTILRDL 272
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
502-582 5.82e-10

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS was originally identified in Drosophila using a screen for genes whose inactivation led to overproliferation of cells. In tetrapods, there are two LATS isoforms, LATS1 and LATS2. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. LATS functions as a tumor suppressor and is implicated in cell cycle regulation. The LATS subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 61.18  E-value: 5.82e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 502 IHRDLAARNVLVTEDNVMKIADFGLA---RDVHNLDYYKK-----TTNgrlpvkWMAPEALFDRVYTHQSDVWSFGVLLW 573
Cdd:cd05598 123 IHRDIKPDNILIDRDGHIKLTDFGLCtgfRWTHDSKYYLAhslvgTPN------YIAPEVLLRTGYTQLCDWWSVGVILY 196

                ....*....
gi 13112048 574 EIftLGGSP 582
Cdd:cd05598 197 EM--LVGQP 203
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
349-595 5.88e-10

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-alpha is predominantly expressed in endothelial cells. It is critical for the regulation of angiogenesis and the maintenance of vascular integrity. It also plays a role in adipocyte differentiation. Mice deficient in PKB-alpha exhibit perinatal morbidity, growth retardation, reduction in body weight accompanied by reduced sizes of multiple organs, and enhanced apoptosis in some cell types. PKB-alpha activity has been reported to be frequently elevated in breast and prostate cancers. In some cancer cells, PKB-alpha may act as a suppressor of metastasis. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 61.58  E-value: 5.88e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 349 ADPKWELSRARLTLGKPLGEGCFGQVVMAEAIGIDKDRAAKPVTVAVKMLKDDatdkdLSDLVSEMEMMKMiGKHKNIIN 428
Cdd:cd05594  16 TKPKHKVTMNDFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDE-----VAHTLTENRVLQN-SRHPFLTA 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 429 LLGACTQGGPLYVLVEYAAKGNLreFLRARRppglDYSFDtckppEEQLTFKdlvscAYQVARGMEYLASQK-CIHRDLA 507
Cdd:cd05594  90 LKYSFQTHDRLCFVMEYANGGEL--FFHLSR----ERVFS-----EDRARFY-----GAEIVSALDYLHSEKnVVYRDLK 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 508 ARNVLVTEDNVMKIADFGLARDVHNLDYYKKTTNGrlPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIP 587
Cdd:cd05594 154 LENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCG--TPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQD 230

                ....*...
gi 13112048 588 VEELFKLL 595
Cdd:cd05594 231 HEKLFELI 238
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
166-245 5.92e-10

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 56.35  E-value: 5.92e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 166 VPAANTVRFRCPAAGNPTPSISWLKNGREFRGEH-RIGGIklrhQQWSLVMESVVPSDRGNYTCVVENKFGSIRQTYTLD 244
Cdd:cd20952  11 VAVGGTVVLNCQATGEPVPTISWLKDGVPLLGKDeRITTL----ENGSLQIKGAEKSDTGEYTCVALNLSGEATWSAVLD 86

                .
gi 13112048 245 V 245
Cdd:cd20952  87 V 87
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
351-575 6.07e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 61.43  E-value: 6.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048  351 PKWELSRARLTLG----KPLGEGCFGQVVMAEaigidkdRAAKPVTVAVKMLKDDATdkdlsdLVSEMeMMKMIgKHKNI 426
Cdd:PHA03209  55 TKQKAREVVASLGytviKTLTPGSEGRVFVAT-------KPGQPDPVVLKIGQKGTT------LIEAM-LLQNV-NHPSV 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048  427 INLLGACTQGgPLYVLVEYAAKGNLREFLRARRPPgldysfdtckppeeqLTFKDLVSCAYQVARGMEYLASQKCIHRDL 506
Cdd:PHA03209 120 IRMKDTLVSG-AITCMVLPHYSSDLYTYLTKRSRP---------------LPIDQALIIEKQILEGLRYLHAQRIIHRDV 183
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048  507 AARNVLVTEDNVMKIADFGLAR-DVHNLDYYKKTTNgrlpVKWMAPEALFDRVYTHQSDVWSFGVLLWEI 575
Cdd:PHA03209 184 KTENIFINDVDQVCIGDLGAAQfPVVAPAFLGLAGT----VETNAPEVLARDKYNSKADIWSAGIVLFEM 249
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
492-592 6.24e-10

Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine/threonine kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. There are four mammalian MAST kinases, named MAST1-MAST4. MAST1 is also called syntrophin-associated STK (SAST) while MAST2 is also called MAST205. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MAST1, MAST2, and MAST3 bind and phosphorylate the tumor suppressor PTEN, and may contribute to the regulation and stabilization of PTEN. MAST2 is involved in the regulation of the Fc-gamma receptor of the innate immune response in macrophages, and may also be involved in the regulation of the Na+/H+ exchanger NHE3. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 60.88  E-value: 6.24e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 492 GMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARdvhnLDYYKKTTN---GRLPV--------------KWMAPEAL 554
Cdd:cd05609 112 ALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLSK----IGLMSLTTNlyeGHIEKdtrefldkqvcgtpEYIAPEVI 187
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 13112048 555 FDRVYTHQSDVWSFGVLLWEiFTLGGSPYPGIPVEELF 592
Cdd:cd05609 188 LRQGYGKPVDWWAMGIILYE-FLVGCVPFFGDTPEELF 224
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
393-577 6.31e-10

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: 60.81  E-value: 6.31e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 393 VAVKMLKDdatdKDLSDLVSEMEMMKMIG-KHKNIINLLGACTQGG----PLYVLVEYAAKGNLREFLRArrppgldysf 467
Cdd:cd14140  21 VAVKIFPI----QDKQSWQSEREIFSTPGmKHENLLQFIAAEKRGSnlemELWLITAFHDKGSLTDYLKG---------- 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 468 dtckppeEQLTFKDLVSCAYQVARGMEYLASQ--KC---------IHRDLAARNVLVTEDNVMKIADFGLARDVHNlDYY 536
Cdd:cd14140  87 -------NIVSWNELCHIAETMARGLSYLHEDvpRCkgeghkpaiAHRDFKSKNVLLKNDLTAVLADFGLAVRFEP-GKP 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 13112048 537 KKTTNGRLPV-KWMAPEAL-----FDRVYTHQSDVWSFGVLLWEIFT 577
Cdd:cd14140 159 PGDTHGQVGTrRYMAPEVLegainFQRDSFLRIDMYAMGLVLWELVS 205
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
364-576 6.84e-10

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK1 is ubiquitously expressed and is under transcriptional control of numerous stimuli including cell stress (cell shrinkage), serum, hormones (gluco- and mineralocorticoids), gonadotropins, growth factors, interleukin-6, and other cytokines. It plays roles in sodium retention and potassium elimination in the kidney, nutrient transport, salt sensitivity, memory consolidation, and cardiac repolarization. A common SGK1 variant is associated with increased blood pressure and body weight. SGK1 may also contribute to tumor growth, neurodegeneration, fibrosing disease, and ischemia. The SGK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270753 [Multi-domain]  Cd Length: 339  Bit Score: 61.19  E-value: 6.84e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVMAEaigidkdRAAKPVTVAVKMLKDDA--TDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYV 441
Cdd:cd05602  13 KVIGKGSFGKVLLAR-------HKSDEKFYAVKVLQKKAilKKKEEKHIMSERNVLLKNVKHPFLVGLHFSFQTTDKLYF 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 442 LVEYAAKGNLREFLRARR----PPGLDYsfdtckppeeqltfkdlvscAYQVARGMEYLASQKCIHRDLAARNVLVTEDN 517
Cdd:cd05602  86 VLDYINGGELFYHLQRERcflePRARFY--------------------AAEIASALGYLHSLNIVYRDLKPENILLDSQG 145
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 13112048 518 VMKIADFGLARDvhNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIF 576
Cdd:cd05602 146 HIVLTDFGLCKE--NIEPNGTTSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEML 202
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
361-570 7.61e-10

Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. There are two forms of STRAD, alpha and beta, that complex with LKB1 and MO25. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha stabilized through ATP and MO25 may be needed to activate LKB1. The STRAD subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 60.77  E-value: 7.61e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 361 TLGKPLGEGCFGQVVMAeaigidkdrAAKPVT----VAVK-MLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQ 435
Cdd:cd08216   1 ELLYEIGKCFKGGGVVH---------LAKHKPtntlVAVKkINLESDSKEDLKFLQQEILTSRQL-QHPNILPYVTSFVV 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 436 GGPLYVLVEYAAKGNLREFLRARRPPGLdysfdtckpPEE--QLTFKDlvscayqVARGMEYLASQKCIHRDLAARNVLV 513
Cdd:cd08216  71 DNDLYVVTPLMAYGSCRDLLKTHFPEGL---------PELaiAFILRD-------VLNALEYIHSKGYIHRSVKASHILI 134
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13112048 514 TEDNVMKIADFGLARDVHNLDYYKKTTNGrLPV------KWMAPEALFD--RVYTHQSDVWSFGV 570
Cdd:cd08216 135 SGDGKVVLSGLRYAYSMVKHGKRQRVVHD-FPKsseknlPWLSPEVLQQnlLGYNEKSDIYSVGI 198
pknD PRK13184
serine/threonine-protein kinase PknD;
366-583 8.30e-10

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 62.10  E-value: 8.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048  366 LGEGCFGQVVMAEaigiDKDRAAKpvtVAVKMLKDDATDKDL------------SDLVsememmkmigkHKNIINLLGAC 433
Cdd:PRK13184  10 IGKGGMGEVYLAY----DPVCSRR---VALKKIREDLSENPLlkkrflreakiaADLI-----------HPGIVPVYSIC 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048  434 TQGGPLYVLVEYAAKGNLREFLRA-RRPPGLDysfdtcKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVL 512
Cdd:PRK13184  72 SDGDPVYYTMPYIEGYTLKSLLKSvWQKESLS------KELAEKTSVGAFLSIFHKICATIEYVHSKGVLHRDLKPDNIL 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048  513 VTEDNVMKIADFGLAR--------------DVHNLDYYKKTTNGRL--PVKWMAPEALFDRVYTHQSDVWSFGVLLWEIF 576
Cdd:PRK13184 146 LGLFGEVVILDWGAAIfkkleeedlldidvDERNICYSSMTIPGKIvgTPDYMAPERLLGVPASESTDIYALGVILYQML 225

                 ....*..
gi 13112048  577 TLgGSPY 583
Cdd:PRK13184 226 TL-SFPY 231
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
363-585 9.91e-10

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase signal-integrating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 60.12  E-value: 9.91e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 363 GKPLGEGCFGQVVMAEAIGIDKDraakpvtVAVKMLKDDATDKDlSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYVL 442
Cdd:cd14090   7 GELLGEGAYASVQTCINLYTGKE-------YAVKIIEKHPGHSR-SRVFREVETLHQCQGHPNILQLIEYFEDDERFYLV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 443 VEYAAKGNLREFLRARRppgldySFDTCkppEEQLTFKDlvscayqVARGMEYLASQKCIHRDLAARNVL-VTEDNV--M 519
Cdd:cd14090  79 FEKMRGGPLLSHIEKRV------HFTEQ---EASLVVRD-------IASALDFLHDKGIAHRDLKPENILcESMDKVspV 142
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13112048 520 KIADFGLARDVHNLDYYK---KTTNGRLPV---KWMAPE---ALFDR--VYTHQSDVWSFGVLLWeIFTLGGSPYPG 585
Cdd:cd14090 143 KICDFDLGSGIKLSSTSMtpvTTPELLTPVgsaEYMAPEvvdAFVGEalSYDKRCDLWSLGVILY-IMLCGYPPFYG 218
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
366-583 9.95e-10

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK4 has a limited tissue distribution. It is mainly found in the testis, but is also present in the cerebellum and kidney. It is expressed as multiple splice variants with different domain architectures and is post-translationally palmitoylated and localized in the membrane. GRK4 polymorphisms are associated with hypertension and salt sensitivity, as they cause hyperphosphorylation, desensitization, and internalization of the dopamine 1 (D1) receptor while increasing the expression of the angiotensin II type 1 receptor. GRK4 plays a crucial role in the D1 receptor regulation of sodium excretion and blood pressure. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 60.01  E-value: 9.95e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKDRAAKPVTVA-VKMLKDDATdkdlsdLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVE 444
Cdd:cd05631   8 LGKGGFGEVCACQVRATGKMYACKKLEKKrIKKRKGEAM------ALNEKRILEKV-NSRFVVSLAYAYETKDALCLVLT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 445 YAAKGNLREFLRARRPPGLDysfdtckppEEQLTFKdlvscAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADF 524
Cdd:cd05631  81 IMNGGDLKFHIYNMGNPGFD---------EQRAIFY-----AAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDL 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 525 GLARDVHNldyyKKTTNGRL-PVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPY 583
Cdd:cd05631 147 GLAVQIPE----GETVRGRVgTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQ-GQSPF 201
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
366-597 1.03e-09

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC-zeta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270768 [Multi-domain]  Cd Length: 357  Bit Score: 60.81  E-value: 1.03e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMaeaIGIDKDRAAKPVTVAVKMLKDDatDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd05617  23 IGRGSYAKVLL---VRLKKNDQIYAMKVVKKELVHD--DEDIDWVQTEKHVFEQASSNPFLVGLHSCFQTTSRLFLVIEY 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLREFLRARRppgldysfdtcKPPEEQLTFKdlvscAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFG 525
Cdd:cd05617  98 VNGGDLMFHMQRQR-----------KLPEEHARFY-----AAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYG 161
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13112048 526 LARDvhNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPY------PGIPVEE-LFKLLKE 597
Cdd:cd05617 162 MCKE--GLGPGDTTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMA-GRSPFdiitdnPDMNTEDyLFQVILE 237
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
366-577 1.06e-09

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Cdc7 kinase (or Hsk1 in fission yeast) is a critical regulator in the initiation of DNA replication. It forms a complex with a Dbf4-related regulatory subunit, a cyclin-like molecule that activates the kinase in late G1 phase, and is also referred to as Dbf4-dependent kinase (DDK). Its main targets are mini-chromosome maintenance (MCM) proteins. Cdc7 kinase may also have additional roles in meiosis, checkpoint responses, the maintenance and repair of chromosome structures, and cancer progression. The Cdc7 kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 59.54  E-value: 1.06e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKDRAAKPVTVAVKMLKDDATDKDLSDlvsEMEMMKMIGKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd14019   9 IGEGTFSSVYKAEDKLHDLYDRNKGRLVALKHIYPTSSPSRILN---ELECLERLGGSNNVSGLITAFRNEDQVVAVLPY 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLREFLRarrppgldysfdtckppeeQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDN-VMKIADF 524
Cdd:cd14019  86 IEHDDFRDFYR-------------------KMSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNRETgKGVLVDF 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13112048 525 GLARDVHnldyYKKT-------TNGrlpvkWMAPEALFDrvYTHQS---DVWSFGVLLWEIFT 577
Cdd:cd14019 147 GLAQREE----DRPEqrapragTRG-----FRAPEVLFK--CPHQTtaiDIWSAGVILLSILS 198
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
451-634 1.16e-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: 59.83  E-value: 1.16e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 451 LREFLRARRPPGLDYSFDTCKPPEEQLTFkdLVSCAYQVARGMEYLASQKCIHRDLAARNVLVT-EDNVMKIADFGLA-- 527
Cdd:cd14049  93 LWDWIVERNKRPCEEEFKSAPYTPVDVDV--TTKILQQLLEGVTYIHSMGIVHRDLKPRNIFLHgSDIHVRIGDFGLAcp 170
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 528 ------RDVHNLDYYK--KTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFtlggSPYpGIPVE--ELFKLLKE 597
Cdd:cd14049 171 dilqdgNDSTTMSRLNglTHTSGVGTCLYAAPEQLEGSHYDFKSDMYSIGVILLELF----QPF-GTEMEraEVLTQLRN 245
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 13112048 598 GHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVE 634
Cdd:cd14049 246 GQIPKSLCKRWPVQAKYIKLLTSTEPSERPSASQLLE 282
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
366-660 1.17e-09

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: 60.23  E-value: 1.17e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAeaigidKDRAAKPVtVAVKMLKDDATDKDL-SDLVSEMEMMKMIGKHKNIINLLG---ACTQGGP-LY 440
Cdd:cd07837   9 IGEGTYGKVYKA------RDKNTGKL-VALKKTRLEMEEEGVpSTALREVSLLQMLSQSIYIVRLLDvehVEENGKPlLY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 441 VLVEYAAKgNLREFLRARRppgldysfdtcKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTED-NVM 519
Cdd:cd07837  82 LVFEYLDT-DLKKFIDSYG-----------RGPHNPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQkGLL 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 520 KIADFGLARDVHNLdyYKKTTNGRLPVKWMAPEALFDRV-YTHQSDVWSFGVLLWEIFTLgGSPYPGipVEELFKLLKEG 598
Cdd:cd07837 150 KIADLGLGRAFTIP--IKSYTHEIVTLWYRAPEVLLGSThYSTPVDMWSVGCIFAEMSRK-QPLFPG--DSELQQLLHIF 224
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13112048 599 HRMDKPANCTHDLYMIMREcWHAAPSQRPtfkqlvEDLDRVLTVTSTdEYLDLSAPFEQYSP 660
Cdd:cd07837 225 RLLGTPNEEVWPGVSKLRD-WHEYPQWKP------QDLSRAVPDLEP-EGVDLLTKMLAYDP 278
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
366-637 1.21e-09

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: 60.00  E-value: 1.21e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKDRAAKPVTVAVKmlkddatdKDLSDLVSEMEMMKMIgKHKNIINLLGAC--TQGGP---LY 440
Cdd:cd13986   8 LGEGGFSFVYLVEDLSTGRLYALKKILCHSK--------EDVKEAMREIENYRLF-NHPNILRLLDSQivKEAGGkkeVY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 441 VLVEYAAKGNLREFLRARRPPGldysfdtckppeEQLTFKDLVSCAYQVARGMEYLASQKCI---HRDLAARNVLVTEDN 517
Cdd:cd13986  79 LLLPYYKRGSLQDEIERRLVKG------------TFFPEDRILHIFLGICRGLKAMHEPELVpyaHRDIKPGNVLLSEDD 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 518 VMKIADFG-------LARDVHNLDYYKKTTNGRLPVKWMAPEaLFDrVYTHQ-----SDVWSFGVLLWEIFtLGGSPY-- 583
Cdd:cd13986 147 EPILMDLGsmnpariEIEGRREALALQDWAAEHCTMPYRAPE-LFD-VKSHCtidekTDIWSLGCTLYALM-YGESPFer 223
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 13112048 584 ---PGIPVeelfKLLKEGHRMDKPANCTH--DLYMIMRECWHAAPSQRPTFKQLVEDLD 637
Cdd:cd13986 224 ifqKGDSL----ALAVLSGNYSFPDNSRYseELHQLVKSMLVVNPAERPSIDDLLSRVH 278
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
474-580 1.35e-09

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK1 (also called rhodopsin kinase) belongs to the visual group of GRKs and is expressed in retinal cells. It phosphorylates rhodopsin in rod cells, which leads to termination of the phototransduction cascade. Mutations in GRK1 are associated to a recessively inherited form of stationary nightblindness called Oguchi disease. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 59.90  E-value: 1.35e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 474 EEQLTFKDLVSCAY--QVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLArdVHNLDYYKKTTNGRLPVKWMAP 551
Cdd:cd05608  97 EENPGFQEPRACFYtaQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLA--VELKDGQTKTKGYAGTPGFMAP 174
                        90       100
                ....*....|....*....|....*....
gi 13112048 552 EALFDRVYTHQSDVWSFGVLLWEIFTLGG 580
Cdd:cd05608 175 ELLLGEEYDYSVDYFTLGVTLYEMIAARG 203
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
410-598 1.55e-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: 59.06  E-value: 1.55e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 410 LVSEMEMMKMIgKHKNIINLLGAC-TQGGPLYVLVEYAAKGnlrEFLRARRPPGLDYSFDTCkppeeqltfkdLVSCAYQ 488
Cdd:cd14109  43 LMREVDIHNSL-DHPNIVQMHDAYdDEKLAVTVIDNLASTI---ELVRDNLLPGKDYYTERQ-----------VAVFVRQ 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 489 VARGMEYLASQKCIHRDLAARNVLVTEDNvMKIADFGLARdvhNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSF 568
Cdd:cd14109 108 LLLALKHMHDLGIAHLDLRPEDILLQDDK-LKLADFGQSR---RLLRGKLTTLIYGSPEFVSPEIVNSYPVTLATDMWSV 183
                       170       180       190
                ....*....|....*....|....*....|
gi 13112048 569 GVLLWEIFTlGGSPYPGIPVEELFKLLKEG 598
Cdd:cd14109 184 GVLTYVLLG-GISPFLGDNDRETLTNVRSG 212
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
359-632 1.66e-09

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


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 59.23  E-value: 1.66e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 359 RLTLGKPLGEGCFGQVVMAeaigidKDRAAKPVtVAVKML-KDDATDKDLS-DLVSEMEMmkmigKHKNIINLLGACTQG 436
Cdd:cd14665   1 RYELVKDIGSGNFGVARLM------RDKQTKEL-VAVKYIeRGEKIDENVQrEIINHRSL-----RHPNIVRFKEVILTP 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 437 GPLYVLVEYAAKGNLREFL-RARRppgldYSFDtckppEEQLTFKDLVScayqvarGMEYLASQKCIHRDLAARNVLVTE 515
Cdd:cd14665  69 THLAIVMEYAAGGELFERIcNAGR-----FSED-----EARFFFQQLIS-------GVSYCHSMQICHRDLKLENTLLDG 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 516 DNV--MKIADFGLARDvHNLDYYKKTTNGRlPVkWMAPEALFDRVYTHQ-SDVWSFGVLLWeIFTLGGspYPGIPVEELF 592
Cdd:cd14665 132 SPAprLKICDFGYSKS-SVLHSQPKSTVGT-PA-YIAPEVLLKKEYDGKiADVWSCGVTLY-VMLVGA--YPFEDPEEPR 205
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 13112048 593 KLLKEGHRMDKPANCTHDLYMIMRECWH-------AAPSQRPTFKQL 632
Cdd:cd14665 206 NFRKTIQRILSVQYSIPDYVHISPECRHlisrifvADPATRITIPEI 252
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
353-585 1.74e-09

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: 59.30  E-value: 1.74e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 353 WELSRARLT-LGKpLGEGCFGQVvmaeaigiDKDRAAKPVTV-AVKMLKDDATDKDLSDLVSEMEMMKMIGKHKNIINLL 430
Cdd:cd06616   1 YEFTAEDLKdLGE-IGRGAFGTV--------NKMLHKPSGTImAVKRIRSTVDEKEQKRLLMDLDVVMRSSDCPYIVKFY 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 431 GACTQGGPLYVLVEYaakgnlreflrarrppgLDYSFDTC----------KPPEEQLTfkdlvSCAYQVARGMEYLASQ- 499
Cdd:cd06616  72 GALFREGDCWICMEL-----------------MDISLDKFykyvyevldsVIPEEILG-----KIAVATVKALNYLKEEl 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 500 KCIHRDLAARNVLVTEDNVMKIADFGLARdvHNLDYYKKTTN-GRLPvkWMAPEAL----FDRVYTHQSDVWSFGVLLWE 574
Cdd:cd06616 130 KIIHRDVKPSNILLDRNGNIKLCDFGISG--QLVDSIAKTRDaGCRP--YMAPERIdpsaSRDGYDVRSDVWSLGITLYE 205
                       250
                ....*....|.
gi 13112048 575 IFTlGGSPYPG 585
Cdd:cd06616 206 VAT-GKFPYPK 215
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
392-584 1.82e-09

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: 59.16  E-value: 1.82e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 392 TVAVKMLKDDATDKDLsdLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEYAAKGNLREFLRARRppglDYSfdtck 471
Cdd:cd14110  30 MLAAKIIPYKPEDKQL--VLREYQVLRRL-SHPRIAQLHSAYLSPRHLVLIEELCSGPELLYNLAERN----SYS----- 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 472 ppeeQLTFKDLVscaYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARDvHNLDYYKKTTNGRLPVKWMAP 551
Cdd:cd14110  98 ----EAEVTDYL---WQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLGNAQP-FNQGKVLMTDKKGDYVETMAP 169
                       170       180       190
                ....*....|....*....|....*....|...
gi 13112048 552 EALFDRVYTHQSDVWSFGVLlweIFTLGGSPYP 584
Cdd:cd14110 170 ELLEGQGAGPQTDIWAIGVT---AFIMLSADYP 199
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
486-634 1.89e-09

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 7; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK7 is a dual-specificity PK that phosphorylates and activates its downstream target, c-Jun N-terminal kinase (JNK), on specific threonine and tyrosine residues. Although MKK7 is capable of dual phosphorylation, it prefers to phosphorylate the threonine residue of JNK. Thus, optimal activation of JNK requires both MKK4 and MKK7. MKK7 is primarily activated by cytokines. MKK7 is essential for liver formation during embryogenesis. It plays roles in G2/M cell cycle arrest and cell growth. In addition, it is involved in the control of programmed cell death, which is crucial in oncogenesis, cancer chemoresistance, and antagonism to TNFalpha-induced killing, through its inhibition by Gadd45beta and the subsequent suppression of the JNK cascade. The MKK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270791 [Multi-domain]  Cd Length: 295  Bit Score: 59.31  E-value: 1.89e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 486 AYQVARGMEYLA-SQKCIHRDLAARNVLVTEDNVMKIADFGLA-RDVhnlDYYKKTTNGRLPVkWMAPEAL----FDRvY 559
Cdd:cd06618 120 TVSIVKALHYLKeKHGVIHRDVKPSNILLDESGNVKLCDFGISgRLV---DSKAKTRSAGCAA-YMAPERIdppdNPK-Y 194
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13112048 560 THQSDVWSFGVLLWEIFTlGGSPYPGIPVE--ELFKLLKEG-HRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVE 634
Cdd:cd06618 195 DIRADVWSLGISLVELAT-GQFPYRNCKTEfeVLTKILNEEpPSLPPNEGFSPDFCSFVDLCLTKDHRYRPKYRELLQ 271
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
170-245 2.89e-09

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 54.34  E-value: 2.89e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13112048 170 NTVRFRCPAAGNPTPSISWLKNGrefrGEHRIGGIKLRHQQWSLVMESVVPSDRGNYTCVVENKFGSIRQTYTLDV 245
Cdd:cd05731  11 GVLLLECIAEGLPTPDIRWIKLG----GELPKGRTKFENFNKTLKIENVSEADSGEYQCTASNTMGSARHTISVTV 82
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
332-634 3.23e-09

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 59.07  E-value: 3.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048  332 SSGEGPTLANVSELELPADPKW--ELSRARLtlgkpLGEGCFGQVVMAEAIGIDKdraakpvTVAVKMLKDDATDKDLSD 409
Cdd:PLN00034  51 SSSSSSSSSSSASGSAPSAAKSlsELERVNR-----IGSGAGGTVYKVIHRPTGR-------LYALKVIYGNHEDTVRRQ 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048  410 LVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEYAAKGnlreflrarrppgldySFDTCKPPEEQLtfkdLVSCAYQV 489
Cdd:PLN00034 119 ICREIEILRDV-NHPNVVKCHDMFDHNGEIQVLLEFMDGG----------------SLEGTHIADEQF----LADVARQI 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048  490 ARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARDV-HNLDYYKKTTNgrlPVKWMAPEA----LFDRVYT-HQS 563
Cdd:PLN00034 178 LSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRILaQTMDPCNSSVG---TIAYMSPERintdLNHGAYDgYAG 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048  564 DVWSFGVLLWEiFTLGGSPypgipveelFKLLKEG------------HRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQ 631
Cdd:PLN00034 255 DIWSLGVSILE-FYLGRFP---------FGVGRQGdwaslmcaicmsQPPEAPATASREFRHFISCCLQREPAKRWSAMQ 324

                 ...
gi 13112048  632 LVE 634
Cdd:PLN00034 325 LLQ 327
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
426-591 3.41e-09

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: 58.91  E-value: 3.41e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 426 IINLLGACTQGGPLYVLVEYAAKGNLREFLR-ARRPPgldysfdtckppeEQLTFKdlVSCAyqVARGMEYLASQ-KCIH 503
Cdd:cd06650  65 IVGFYGAFYSDGEISICMEHMDGGSLDQVLKkAGRIP-------------EQILGK--VSIA--VIKGLTYLREKhKIMH 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 504 RDLAARNVLVTEDNVMKIADFGLARDVhnLDYYKKTTNGRLpvKWMAPEALFDRVYTHQSDVWSFGVLLWEIfTLGGSPY 583
Cdd:cd06650 128 RDVKPSNILVNSRGEIKLCDFGVSGQL--IDSMANSFVGTR--SYMSPERLQGTHYSVQSDIWSMGLSLVEM-AVGRYPI 202

                ....*...
gi 13112048 584 PGIPVEEL 591
Cdd:cd06650 203 PPPDAKEL 210
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
362-583 3.58e-09

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 59.28  E-value: 3.58e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 362 LGKPLGEGCFGQVVMAEAIGIDKDRAAKpvtVAVKMLKDDatDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYV 441
Cdd:cd05618  24 LLRVIGRGSYAKVLLVRLKKTERIYAMK---VVKKELVND--DEDIDWVQTEKHVFEQASNHPFLVGLHSCFQTESRLFF 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 442 LVEYAAKGNLREFLRARRppgldysfdtcKPPEEQLTFkdlvsCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKI 521
Cdd:cd05618  99 VIEYVNGGDLMFHMQRQR-----------KLPEEHARF-----YSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKL 162
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13112048 522 ADFGLARDvhNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPY 583
Cdd:cd05618 163 TDYGMCKE--GLRPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMA-GRSPF 221
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
164-245 4.12e-09

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 54.11  E-value: 4.12e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 164 LAVPAANTVRFRCPAAGNPTPSISWLKNGREFRGEHRiggiKLRHQQWSLVMESVVP-SDRGNYTCVVENKFG-SIRQTY 241
Cdd:cd20958  10 LTAVAGQTLRLHCPVAGYPISSITWEKDGRRLPLNHR----QRVFPNGTLVIENVQRsSDEGEYTCTARNQQGqSASRSV 85

                ....
gi 13112048 242 TLDV 245
Cdd:cd20958  86 FVKV 89
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
154-243 4.17e-09

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 54.28  E-value: 4.17e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 154 TRPERMdkkllAVPAANTVRFRCPAAGNPTPSISWLKNGREFRGEHRIGGIKLRHQQwSLVMESVVPSDRGNYTCVVENK 233
Cdd:cd05747   8 TKPRSL-----TVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKS-TFEISKVQMSDEGNYTVVVENS 81
                        90
                ....*....|
gi 13112048 234 FGSIRQTYTL 243
Cdd:cd05747  82 EGKQEAQFTL 91
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
364-626 4.20e-09

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. There are three PKB isoforms from different genes, PKB-alpha (or Akt1), PKB-beta (or Akt2), and PKB-gamma (or Akt3). PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. It is activated downstream of phosphoinositide 3-kinase (PI3K) and plays important roles in diverse cellular functions including cell survival, growth, proliferation, angiogenesis, motility, and migration. PKB also has a central role in a variety of human cancers, having been implicated in tumor initiation, progression, and metastasis. The PKB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 58.52  E-value: 4.20e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVMAeaigidKDRAAKPVtVAVKMLKDDA-TDKD-LSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYV 441
Cdd:cd05571   1 KVLGKGTFGKVILC------REKATGEL-YAIKILKKEViIAKDeVAHTLTENRVLQNT-RHPFLTSLKYSFQTNDRLCF 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 442 LVEYAAKGNLreFLRARRppglDYSFDtckppEEQLTFKdlvscAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKI 521
Cdd:cd05571  73 VMEYVNGGEL--FFHLSR----ERVFS-----EDRTRFY-----GAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKI 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 522 ADFGLARDvhNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEELFKL-LKEGHR 600
Cdd:cd05571 137 TDFGLCKE--EISYGATTKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNRDHEVLFELiLMEEVR 213
                       250       260
                ....*....|....*....|....*.
gi 13112048 601 MdkPANCTHDLYMIMRECWHAAPSQR 626
Cdd:cd05571 214 F--PSTLSPEAKSLLAGLLKKDPKKR 237
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
164-246 4.59e-09

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 53.78  E-value: 4.59e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 164 LAVPAANTVRFRCPAAGNPTPSISWLKNG-------REFRgehriggIKLRHQQWSLVMESVVPSDRGNYTCVVENKFGS 236
Cdd:cd05763   9 ITIRAGSTARLECAATGHPTPQIAWQKDGgtdfpaaRERR-------MHVMPEDDVFFIVDVKIEDTGVYSCTAQNSAGS 81
                        90
                ....*....|
gi 13112048 237 IRQTYTLDVL 246
Cdd:cd05763  82 ISANATLTVL 91
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
486-583 4.91e-09

Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the GRK4-like group include GRK4, GRK5, GRK6, and similar GRKs. They contain an N-terminal RGS homology (RH) domain and a catalytic domain, but lack a G protein betagamma-subunit binding domain. They are localized to the plasma membrane through post-translational lipid modification or direct binding to PIP2. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270756 [Multi-domain]  Cd Length: 285  Bit Score: 58.14  E-value: 4.91e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 486 AYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARDVHNldyyKKTTNGRL-PVKWMAPEALFDRVYTHQSD 564
Cdd:cd05605 108 AAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVEIPE----GETIRGRVgTVGYMAPEVVKNERYTFSPD 183
                        90
                ....*....|....*....
gi 13112048 565 VWSFGVLLWEIFTlGGSPY 583
Cdd:cd05605 184 WWGLGCLIYEMIE-GQAPF 201
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
364-592 4.97e-09

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: 58.44  E-value: 4.97e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVMAEaigidkdRAAKPVTVAVKMLKDDA--TDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYV 441
Cdd:cd05603   1 KVIGKGSFGKVLLAK-------RKCDGKFYAVKVLQKKTilKKKEQNHIMAERNVLLKNLKHPFLVGLHYSFQTSEKLYF 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 442 LVEYAAKGNLreFLRARRppgldysfDTC-KPPEEQLTfkdlvscAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMK 520
Cdd:cd05603  74 VLDYVNGGEL--FFHLQR--------ERCfLEPRARFY-------AAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVV 136
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13112048 521 IADFGLARDvhNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFtLGGSPYPGIPVEELF 592
Cdd:cd05603 137 LTDFGLCKE--GMEPEETTSTFCGTPEYLAPEVLRKEPYDRTVDWWCLGAVLYEML-YGLPPFYSRDVSQMY 205
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
439-638 1.13e-08

Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDIK1L is also called STK35 or CLIK-1. It is predominantly a nuclear protein which is capable of autophosphorylation. Through its interaction with the PDZ-LIM protein CLP-36, it is localized to actin stress fibers. The PDIK1L 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: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 57.18  E-value: 1.13e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 439 LYVLVEYAAKGNLREFLRARRP-PGLDYSFdtckppeeqltfkdlvscAYQVARGMEYLASQKCIHRDLAARNVLVTEDN 517
Cdd:cd13977 110 LWFVMEFCDGGDMNEYLLSRRPdRQTNTSF------------------MLQLSSALAFLHRNQIVHRDLKPDNILISHKR 171
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 518 ---VMKIADFGLARDVHNldyykKTTNGRLPVK--------------WMAPEaLFDRVYTHQSDVWSFGVLLWEI----- 575
Cdd:cd13977 172 gepILKVADFGLSKVCSG-----SGLNPEEPANvnkhflssacgsdfYMAPE-VWEGHYTAKADIFALGIIIWAMverit 245
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13112048 576 FT--------LGGSPYPGIPVEELFKLLKEGHRMD------KPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDR 638
Cdd:cd13977 246 FRdgetkkelLGTYIQQGKEIVPLGEALLENPKLElqiplkKKKSMNDDMKQLLRDMLAANPQERPDAFQLELRLRQ 322
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
426-591 1.21e-08

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: 57.37  E-value: 1.21e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 426 IINLLGACTQGGPLYVLVEYAAKGNLREFLRARRppgldysfdtcKPPEEQLtfkDLVSCAyqVARGMEYLASQ-KCIHR 504
Cdd:cd06649  65 IVGFYGAFYSDGEISICMEHMDGGSLDQVLKEAK-----------RIPEEIL---GKVSIA--VLRGLAYLREKhQIMHR 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 505 DLAARNVLVTEDNVMKIADFGLARDVhnLDYYKKTTNGRLpvKWMAPEALFDRVYTHQSDVWSFGVLLWEIfTLGGSPYP 584
Cdd:cd06649 129 DVKPSNILVNSRGEIKLCDFGVSGQL--IDSMANSFVGTR--SYMSPERLQGTHYSVQSDIWSMGLSLVEL-AIGRYPIP 203

                ....*..
gi 13112048 585 GIPVEEL 591
Cdd:cd06649 204 PPDAKEL 210
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
366-590 1.33e-08

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: 56.52  E-value: 1.33e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKDRAAKpvTVAVKMLKDDATDKDLSDLVSEmemmkmigKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd14113  15 LGRGRFSVVKKCDQRGTKRAVATK--FVNKKLMKRDQVTHELGVLQSL--------QHPQLVGLLDTFETPTSYILVLEM 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLreflrarrppgLDYSFDTCKPPEEQLTFKdlvscAYQVARGMEYLASQKCIHRDLAARNVLVTEDN---VMKIA 522
Cdd:cd14113  85 ADQGRL-----------LDYVVRWGNLTEEKIRFY-----LREILEALQYLHNCRIAHLDLKPENILVDQSLskpTIKLA 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13112048 523 DFGLARDVhNLDYYKKTTNGRlpVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEE 590
Cdd:cd14113 149 DFGDAVQL-NTTYYIHQLLGS--PEFAAPEIILGNPVSLTSDLWSIGVLTYVLLS-GVSPFLDESVEE 212
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
418-628 1.55e-08

Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PINK1 contains an N-terminal mitochondrial targeting sequence, a catalytic domain, and a C-terminal regulatory region. It plays an important role in maintaining mitochondrial homeostasis. It protects cells against oxidative stress-induced apoptosis by phosphorylating the chaperone TNFR-associated protein 1 (TRAP1), also called Hsp75. Phosphorylated TRAP1 prevents cytochrome c release and peroxide-induced apoptosis. PINK1 interacts with Omi/HtrA2, a serine protease, and Parkin, an E3 ubiquitin ligase, in different pathways to promote mitochondrial health. The parkin gene is the most commonly mutated gene in autosomal recessive familial parkinsonism. Mutations within the catalytic domain of PINK1 are also associated with Parkinson's disease. The PINK1 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: 270920 [Multi-domain]  Cd Length: 313  Bit Score: 56.73  E-value: 1.55e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 418 KMIGKHKNIINLLGACTQGGPLY--VLVEY-----------AAKGNLREFLRARR-PPGLDYSFDTCKPPEEQLTFKDLv 483
Cdd:cd14018  67 KLLAPHPNIIRVQRAFTDSVPLLpgAIEDYpdvlparlnpsGLGHNRTLFLVMKNyPCTLRQYLWVNTPSYRLARVMIL- 145
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 484 scayQVARGMEYLASQKCIHRDLAARNVLVTEDN----VMKIADFG--LARDVHNL------DYYKKTTNGRLpvkwMAP 551
Cdd:cd14018 146 ----QLLEGVDHLVRHGIAHRDLKSDNILLELDFdgcpWLVIADFGccLADDSIGLqlpfssWYVDRGGNACL----MAP 217
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 552 EAL------FDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQ 625
Cdd:cd14018 218 EVStavpgpGVVINYSKADAWAVGAIAYEIFGLSNPFYGLGDTMLESRSYQESQLPALPSAVPPDVRQVVKDLLQRDPNK 297

                ...
gi 13112048 626 RPT 628
Cdd:cd14018 298 RVS 300
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
364-582 1.57e-08

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: 56.89  E-value: 1.57e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGQVVMAEaigidKDRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYVLV 443
Cdd:cd05604   2 KVIGKGSFGKVLLAK-----RKRDGKYYAVKVLQKKVILNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTDKLYFVL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 444 EYAAKGNLREFLRARRppgldySFdtckpPEEQLTFKdlvscAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIAD 523
Cdd:cd05604  77 DFVNGGELFFHLQRER------SF-----PEPRARFY-----AAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTD 140
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 524 FGLARD-VHNLDyyKKTTNGRLPvKWMAPEALFDRVYTHQSDVWSFGVLLWEIftLGGSP 582
Cdd:cd05604 141 FGLCKEgISNSD--TTTTFCGTP-EYLAPEVIRKQPYDNTVDWWCLGSVLYEM--LYGLP 195
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
493-598 2.03e-08

Catalytic domain of Suppressor of loss of cAMP-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 Schizosaccharomyces pombe Sck1 and similar fungal proteins. Sck1 plays a role in trehalase activation triggered by glucose and a nitrogen source. Trehalase catalyzes the cleavage of the disaccharide trehalose to glucose. Trehalose, as a carbohydrate reserve and stress metabolite, plays an important role in the response of yeast to environmental changes. The Sck1-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: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 56.42  E-value: 2.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 493 MEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARDvhNLDYYKKTTNGRLPVKWMAPEALFDRV-YTHQSDVWSFGVL 571
Cdd:cd05586 109 LEHLHKNDIVYRDLKPENILLDANGHIALCDFGLSKA--DLTDNKTTNTFCGTTEYLAPEVLLDEKgYTKMVDFWSLGVL 186
                        90       100
                ....*....|....*....|....*..
gi 13112048 572 LWEIfTLGGSPYPGIPVEELFKLLKEG 598
Cdd:cd05586 187 VFEM-CCGWSPFYAEDTQQMYRNIAFG 212
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
366-585 2.07e-08

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: 55.74  E-value: 2.07e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKDraakpvtVAVKMLKDDatdKDLSDL-VSEMEMMKMIGKH-----KNIINLLGACTQGGPL 439
Cdd:cd14133   7 LGKGTFGQVVKCYDLLTGEE-------VALKIIKNN---KDYLDQsLDEIRLLELLNKKdkadkYHIVRLKDVFYFKNHL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 440 yVLVEYAAKGNLREFLRARRPPGLdysfdtckppeeqlTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTE--DN 517
Cdd:cd14133  77 -CIVFELLSQNLYEFLKQNKFQYL--------------SLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASysRC 141
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 518 VMKIADFGLARDVHN-LDYYKKTTNGRlpvkwmAPEALFDRVYTHQSDVWSFGVLLWEIFTlgGSP-YPG 585
Cdd:cd14133 142 QIKIIDFGSSCFLTQrLYSYIQSRYYR------APEVILGLPYDEKIDMWSLGCILAELYT--GEPlFPG 203
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
366-633 2.24e-08

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: 55.88  E-value: 2.24e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMaeaiGIDKDRAakpVTVAVKMLKD-DATDKDLSDLVSEMEMMKMIgKHKNIINLLGA---CTQGGPLYV 441
Cdd:cd14031  18 LGRGAFKTVYK----GLDTETW---VEVAWCELQDrKLTKAEQQRFKEEAEMLKGL-QHPNIVRFYDSwesVLKGKKCIV 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 442 LV-EYAAKGNLREFLRarrppgldySFDTCKPpeeqltfKDLVSCAYQVARGMEYLASQK--CIHRDLAARNVLVT-EDN 517
Cdd:cd14031  90 LVtELMTSGTLKTYLK---------RFKVMKP-------KVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITgPTG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 518 VMKIADFGLARDVHNldYYKKTTNGrlPVKWMAPEaLFDRVYTHQSDVWSFGVLLWEIFTlggSPYPGIPVEELFKLLKE 597
Cdd:cd14031 154 SVKIGDLGLATLMRT--SFAKSVIG--TPEFMAPE-MYEEHYDESVDVYAFGMCMLEMAT---SEYPYSECQNAAQIYRK 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 13112048 598 GHRMDKPANCTH----DLYMIMRECWHAAPSQRPTFKQLV 633
Cdd:cd14031 226 VTSGIKPASFNKvtdpEVKEIIEGCIRQNKSERLSIKDLL 265
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
164-238 2.81e-08

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 51.78  E-value: 2.81e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 164 LAVPAANTVRFRCPAAGNPTPSISWLKNGREFR------GEHRI---GGiklrhqqwSLVMESVVP-----SDRGNYTCV 229
Cdd:cd07693  10 LIVSKGDPATLNCKAEGRPTPTIQWLKNGQPLEtdkddpRSHRIvlpSG--------SLFFLRVVHgrkgrSDEGVYVCV 81

                ....*....
gi 13112048 230 VENKFGSIR 238
Cdd:cd07693  82 AHNSLGEAV 90
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
413-584 2.97e-08

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: 55.39  E-value: 2.97e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 413 EMEMMKMIgKHKNIINLLGA---CTQGGPLYVLV-EYAAKGNLREFLRARRppgldysfdtckppeeQLTFKDLVSCAYQ 488
Cdd:cd14033  50 EVEMLKGL-QHPNIVRFYDSwksTVRGHKCIILVtELMTSGTLKTYLKRFR----------------EMKLKLLQRWSRQ 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 489 VARGMEYLASQ--KCIHRDLAARNVLVT-EDNVMKIADFGLArdVHNLDYYKKTTNGRlPvKWMAPEaLFDRVYTHQSDV 565
Cdd:cd14033 113 ILKGLHFLHSRcpPILHRDLKCDNIFITgPTGSVKIGDLGLA--TLKRASFAKSVIGT-P-EFMAPE-MYEEKYDEAVDV 187
                       170
                ....*....|....*....
gi 13112048 566 WSFGVLLWEIFTlggSPYP 584
Cdd:cd14033 188 YAFGMCILEMAT---SEYP 203
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
164-245 2.97e-08

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 51.42  E-value: 2.97e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 164 LAVPAANTVRFRCPAAGNPTPSISWLKNGREFRGEHRIGGIKLRHQQWSLVMESVVPSDRGNYTCVVENKFGSIRQTYTL 243
Cdd:cd20973   7 KEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAEL 86

                ..
gi 13112048 244 DV 245
Cdd:cd20973  87 TV 88
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
161-236 3.07e-08

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 51.43  E-value: 3.07e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13112048   161 KKLLAVPAANTVRFRCPA-AGNPTPSISWLKNGREFRGEHRIGGIKLRHQQWSLVMESVVPSDRGNYTCVVENKFGS 236
Cdd:pfam00047   3 PPTVTVLEGDSATLTCSAsTGSPGPDVTWSKEGGTLIESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGS 79
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here ...
171-245 3.50e-08

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains, five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM.


Pssm-ID: 409460 [Multi-domain]  Cd Length: 83  Bit Score: 51.07  E-value: 3.50e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13112048 171 TVRFRCPAAGNPTPSISWLKNGREFRGEHrigGIKLRHQQWsLVMESVVPSDRGNYTCVVENKFGSIRQTYTLDV 245
Cdd:cd05876  12 SLVLECIAEGLPTPTVKWLRPSGPLPPDR---VKYQNHNKT-LQLLNVGESDDGEYVCLAENSLGSARHAYYVTV 82
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
366-585 3.57e-08

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 55.42  E-value: 3.57e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKDraakpvtVAVKMLKDDAtDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd14174  10 LGEGAYAKVQGCVSLQNGKE-------YAVKIIEKNA-GHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLREFLRARRppgldySFDTckpPEEQLTFKDlvscayqVARGMEYLASQKCIHRDLAARNVLV-TEDNV--MKIA 522
Cdd:cd14174  82 LRGGSILAHIQKRK------HFNE---REASRVVRD-------IASALDFLHTKGIAHRDLKPENILCeSPDKVspVKIC 145
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13112048 523 DFGLARDVHNLDYYKKTTNGRL-----PVKWMAPEALfdRVYTHQS-------DVWSFGVLLWeIFTLGGSPYPG 585
Cdd:cd14174 146 DFDLGSGVKLNSACTPITTPELttpcgSAEYMAPEVV--EVFTDEAtfydkrcDLWSLGVILY-IMLSGYPPFVG 217
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
366-585 3.73e-08

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: 55.01  E-value: 3.73e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKDRAAKPVTVAVKMLKDDATDkdlsdlvsEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd14191  10 LGSGKFGQVFRLVEKKTKKVWAGKFFKAYSAKEKENIRQ--------EISIMNCL-HHPKLVQCVDAFEEKANIVMVLEM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLreflrarrppgldysFDTCKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTED--NVMKIAD 523
Cdd:cd14191  81 VSGGEL---------------FERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKtgTKIKLID 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13112048 524 FGLARDVHNLdyykkttnGRLPV-----KWMAPEALFDRVYTHQSDVWSFGVLLWeIFTLGGSPYPG 585
Cdd:cd14191 146 FGLARRLENA--------GSLKVlfgtpEFVAPEVINYEPIGYATDMWSIGVICY-ILVSGLSPFMG 203
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
494-583 4.12e-08

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: 55.75  E-value: 4.12e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 494 EYLASQKCIHRDLAARNVLVTEDNVMKIADFGLA---RDVHNLDYYK---KTTNGRLPVK-------------------- 547
Cdd:cd05573 115 DSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCtkmNKSGDRESYLndsVNTLFQDNVLarrrphkqrrvraysavgtp 194
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 13112048 548 -WMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPY 583
Cdd:cd05573 195 dYIAPEVLRGTGYGPECDWWSLGVILYEMLY-GFPPF 230
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
161-245 5.17e-08

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 50.92  E-value: 5.17e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 161 KKLLAVPAANTVRFRCPAAGNPTPSISWLKNGREFRGEHRIGGIKLRhqqwSLVMESVVPSDRGNYTCVVENKFGSIRQT 240
Cdd:cd04969   9 KKKILAAKGGDVIIECKPKASPKPTISWSKGTELLTNSSRICILPDG----SLKIKNVTKSDEGKYTCFAVNFFGKANST 84

                ....*
gi 13112048 241 YTLDV 245
Cdd:cd04969  85 GSLSV 89
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
164-245 5.74e-08

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 50.96  E-value: 5.74e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 164 LAVPAANTVRFRCPAAGNPTPSISWLKNGREFRGEHRIGGIKLRHQQWSLVMESVVPSDRGNYTCVVENKFGSIRQTYTL 243
Cdd:cd05744  10 LEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENGRHSLIIEPVTKRDAGIYTCIARNRAGENSFNAEL 89

                ..
gi 13112048 244 DV 245
Cdd:cd05744  90 VV 91
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
362-583 6.26e-08

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: 54.62  E-value: 6.26e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 362 LGKPLGEGCFGQVVMAEAI-GIDKDRaakpvTVAVKMLKDdAT----DKDLSDLVSEMEMMKMIGKHKNIINLLGACTQG 436
Cdd:cd05613   4 LLKVLGTGAYGKVFLVRKVsGHDAGK-----LYAMKVLKK-ATivqkAKTAEHTRTERQVLEHIRQSPFLVTLHYAFQTD 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 437 GPLYVLVEYAAKGNLREFLRARrppgldysfdtckppeEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTED 516
Cdd:cd05613  78 TKLHLILDYINGGELFTHLSQR----------------ERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSS 141
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13112048 517 NVMKIADFGLARDVHnLDYYKKTTNGRLPVKWMAPEALF--DRVYTHQSDVWSFGVLLWEIFTlGGSPY 583
Cdd:cd05613 142 GHVVLTDFGLSKEFL-LDENERAYSFCGTIEYMAPEIVRggDSGHDKAVDWWSLGVLMYELLT-GASPF 208
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
422-632 6.44e-08

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


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 54.39  E-value: 6.44e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 422 KHKNIINLLGACTQGGPLYVLVEYAAKGNLREFL-RARRppgldYSFDtckppEEQLTFKDLVScayqvarGMEYLASQK 500
Cdd:cd14662  54 RHPNIIRFKEVVLTPTHLAIVMEYAAGGELFERIcNAGR-----FSED-----EARYFFQQLIS-------GVSYCHSMQ 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 501 CIHRDLAARNVLV--TEDNVMKIADFGLARDvHNLDYYKKTTNGRlPVkWMAPEALFDRVYTHQ-SDVWSFGVLLWEIft 577
Cdd:cd14662 117 ICHRDLKLENTLLdgSPAPRLKICDFGYSKS-SVLHSQPKSTVGT-PA-YIAPEVLSRKEYDGKvADVWSCGVTLYVM-- 191
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13112048 578 LGGSpYPGIPVEELFKLLKEGHRMDKPANCTHDLYMIMRECWH-------AAPSQRPTFKQL 632
Cdd:cd14662 192 LVGA-YPFEDPDDPKNFRKTIQRIMSVQYKIPDYVRVSQDCRHllsrifvANPAKRITIPEI 252
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
486-577 6.50e-08

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. They play important roles in mediating pre-mRNA processing and mRNA maturation, as well as other cellular functions such as chromatin reorganization, cell cycle and p53 regulation, and metabolic signaling. Vertebrates contain three distinct SRPKs, called SRPK1-3. The SRPK homolog in budding yeast, Sky1p, recognizes and phosphorylates its substrate Npl3p, which lacks a classic RS domain but contains a single RS dipeptide at the C-terminus of its RGG domain. Npl3p is a shuttling heterogeneous nuclear ribonucleoprotein (hnRNP) that exports a distinct class of mRNA from the nucleus to the cytoplasm. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 54.89  E-value: 6.50e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 486 AYQVARGMEYLASQ-KCIHRDLAARNVLVTEDNV-MKIADFGLARDVHnldyyKKTTNGRLPVKWMAPEALFDRVYTHQS 563
Cdd:cd14136 125 ARQVLQGLDYLHTKcGIIHTDIKPENVLLCISKIeVKIADLGNACWTD-----KHFTEDIQTRQYRSPEVILGAGYGTPA 199
                        90
                ....*....|....
gi 13112048 564 DVWSFGVLLWEIFT 577
Cdd:cd14136 200 DIWSTACMAFELAT 213
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
362-634 6.99e-08

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: 54.16  E-value: 6.99e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 362 LGKPLGEGCFGQVVMAEaigidkdRAAKPVTVAVK-MLKDDATDK----DLSDLVSEMEMMKMI--GKHKNIINLLG--A 432
Cdd:cd14005   4 VGDLLGKGGFGTVYSGV-------RIRDGLPVAVKfVPKSRVTEWaminGPVPVPLEIALLLKAskPGVPGVIRLLDwyE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 433 CTQGgplYVLV-EYAAkgnlreflrarrpPGLDYsFDTCK---PPEEQLT---FKDLVSCAYQVArgmeylaSQKCIHRD 505
Cdd:cd14005  77 RPDG---FLLImERPE-------------PCQDL-FDFITergALSENLAriiFRQVVEAVRHCH-------QRGVLHRD 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 506 LAARNVLVT-EDNVMKIADFGLARDVHnlDYYKKTTNGRlPVkWMAPEALFDRVYtH--QSDVWSFGVLLWEIftLGGSp 582
Cdd:cd14005 133 IKDENLLINlRTGEVKLIDFGCGALLK--DSVYTDFDGT-RV-YSPPEWIRHGRY-HgrPATVWSLGILLYDM--LCGD- 204
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 13112048 583 ypgIPVEELFKLLKEG--HRMDKPANCtHDLymiMRECWHAAPSQRPTFKQLVE 634
Cdd:cd14005 205 ---IPFENDEQILRGNvlFRPRLSKEC-CDL---ISRCLQFDPSKRPSLEQILS 251
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
359-582 7.21e-08

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: 54.75  E-value: 7.21e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 359 RLTLGKPLGEGCFGQVVMAeaigIDKDRAAKPVTVAV---KMLKDDATDKDLSD-LVSEMEMMKMIgKHKNIINLLGACT 434
Cdd:cd14096   2 NYRLINKIGEGAFSNVYKA----VPLRNTGKPVAIKVvrkADLSSDNLKGSSRAnILKEVQIMKRL-SHPNIVKLLDFQE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 435 QGGPLYVLVEYAAKGNLreFLRARRppgLDYsFdtckppEEQLTfKDLVScayQVARGMEYLASQKCIHRDLAARNVLVT 514
Cdd:cd14096  77 SDEYYYIVLELADGGEI--FHQIVR---LTY-F------SEDLS-RHVIT---QVASAVKYLHEIGVVHRDIKPENLLFE 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 515 -----------------EDNV----------------MKIADFGLARDVHnlDYYKKTTNGrlPVKWMAPEALFDRVYTH 561
Cdd:cd14096 141 pipfipsivklrkadddETKVdegefipgvggggigiVKLADFGLSKQVW--DSNTKTPCG--TVGYTAPEVVKDERYSK 216
                       250       260
                ....*....|....*....|.
gi 13112048 562 QSDVWSFGVLLWEIftLGGSP 582
Cdd:cd14096 217 KVDMWALGCVLYTL--LCGFP 235
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
411-634 8.18e-08

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 55.00  E-value: 8.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048  411 VSEMEMMKMIgKHKNIINLLGACTQGG-PLYVLVEYaaKGNLREFLRARRppgldysfdtckppeeQLTFKDLVSCAYQV 489
Cdd:PHA03212 131 ATEAHILRAI-NHPSIIQLKGTFTYNKfTCLILPRY--KTDLYCYLAAKR----------------NIAICDILAIERSV 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048  490 ARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLA---RDVHNLDYY----KKTTNgrlpvkwmAPEALFDRVYTHQ 562
Cdd:PHA03212 192 LRAIQYLHENRIIHRDIKAENIFINHPGDVCLGDFGAAcfpVDINANKYYgwagTIATN--------APELLARDPYGPA 263
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048  563 SDVWSFGVLLWEIFTLGGSPYP------GIPVEELFKLL--KEG-HRMDKPANCTHDLYMI-MRECWHAA--PSQRPTFK 630
Cdd:PHA03212 264 VDIWSAGIVLFEMATCHDSLFEkdgldgDCDSDRQIKLIirRSGtHPNEFPIDAQANLDEIyIGLAKKSSrkPGSRPLWT 343

                 ....
gi 13112048  631 QLVE 634
Cdd:PHA03212 344 NLYE 347
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
366-585 8.78e-08

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: 54.13  E-value: 8.78e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAeaigidKDRAAKPVTVAVKMLKDDATDKDLsdLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd14114  10 LGTGAFGVVHRC------TERATGNNFAAKFIMTPHESDKET--VRKEIQIMNQL-HHPKLINLHDAFEDDNEMVLILEF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLreflrarrppgldysFDTCKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVT--EDNVMKIAD 523
Cdd:cd14114  81 LSGGEL---------------FERIAAEHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTtkRSNEVKLID 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13112048 524 FGLARDVHNLDYYKKTTNgrlPVKWMAPEALFDRVYTHQSDVWSFGVLLWeIFTLGGSPYPG 585
Cdd:cd14114 146 FGLATHLDPKESVKVTTG---TAEFAAPEIVEREPVGFYTDMWAVGVLSY-VLLSGLSPFAG 203
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
175-245 1.07e-07

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 50.20  E-value: 1.07e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13112048 175 RCPAAG-NPTPSISWLKNGREFrGEHRIGGIKLRHQQWS--LVMESVVPSDRGNYTCVVENKFGSIRQTYTLDV 245
Cdd:cd05750  20 KCEATSeNPSPRYRWFKDGKEL-NRKRPKNIKIRNKKKNseLQINKAKLEDSGEYTCVVENILGKDTVTGNVTV 92
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
366-585 1.11e-07

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 53.88  E-value: 1.11e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKDRAAKPVtvavkmlkDDATDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd14173  10 LGEGAYARVQTCINLITNKEYAVKII--------EKRPGHSRSRVFREVEMLYQCQGHRNVLELIEFFEEEDKFYLVFEK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLREFLRARRppgldySFDTckpPEEQLTFKDlvscayqVARGMEYLASQKCIHRDLAARNVLVTEDNVM---KIA 522
Cdd:cd14173  82 MRGGSILSHIHRRR------HFNE---LEASVVVQD-------IASALDFLHNKGIAHRDLKPENILCEHPNQVspvKIC 145
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13112048 523 DFGLARDVH-NLDYYKKTTNGRL----PVKWMAPEAL--FDR---VYTHQSDVWSFGVLLWeIFTLGGSPYPG 585
Cdd:cd14173 146 DFDLGSGIKlNSDCSPISTPELLtpcgSAEYMAPEVVeaFNEeasIYDKRCDLWSLGVILY-IMLSGYPPFVG 217
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
366-585 1.12e-07

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: 53.71  E-value: 1.12e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKDRAAKPVTVavkmlkdDATDKDLsdLVSEMEMMKmIGKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd14104   8 LGRGQFGIVHRCVETSSKKTYMAKFVKV-------KGADQVL--VKKEISILN-IARHRNILRLHESFESHEELVMIFEF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLREFLRarrppglDYSFdtckppeeQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVT--EDNVMKIAD 523
Cdd:cd14104  78 ISGVDIFERIT-------TARF--------ELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCtrRGSYIKIIE 142
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13112048 524 FGLARDVHNLDYYKKTTngrLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPG 585
Cdd:cd14104 143 FGQSRQLKPGDKFRLQY---TSAEFYAPEVHQHESVSTATDMWSLGCLVYVLLS-GINPFEA 200
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
175-245 1.49e-07

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 49.56  E-value: 1.49e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13112048 175 RCPAAGNPTPSISWLKNGRE--FRGEHriggIKLRHQQWSLVMESVVPSDRGNYTCVVENKFGSIRQTYTLDV 245
Cdd:cd20976  22 QCSARGKPVPRITWIRNAQPlqYAADR----STCEAGVGELHIQDVLPEDHGTYTCLAKNAAGQVSCSAWVTV 90
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
372-577 1.55e-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: 53.40  E-value: 1.55e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 372 GQVVMAEAIGIDKDRAAKPVTVAVKMLKDDATDKDLSD---LVSEMEMMKMIGKHKNIINLLGACTQ----GGPLYVLVE 444
Cdd:cd14020   9 GQGSSASVYRVSSGRGADQPTSALKEFQLDHQGSQESGdygFAKERAALEQLQGHRNIVTLYGVFTNhysaNVPSRCLLL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 445 YAAKGNLREFLRARRPPGLDYSFdtckppeeqltfkdLVSCAYQVARGMEYLASQKCIHRDLAARNVLVT-EDNVMKIAD 523
Cdd:cd14020  89 ELLDVSVSELLLRSSNQGCSMWM--------------IQHCARDVLEALAFLHHEGYVHADLKPRNILWSaEDECFKLID 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13112048 524 FGLARDVHNLDYYKKTTNGrlpvkWMAPEALF-----------DRVYTHQSDVWSFGVLLWEIFT 577
Cdd:cd14020 155 FGLSFKEGNQDVKYIQTDG-----YRAPEAELqnclaqaglqsETECTSAVDLWSLGIVLLEMFS 214
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
366-586 1.68e-07

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: 53.54  E-value: 1.68e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAigidkdrAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEY 445
Cdd:cd07869  13 LGEGSYATVYKGKS-------KVNGKLVALKVIRLQEEEGTPFTAIREASLLKGL-KHANIVLLHDIIHTKETLTLVFEY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKgNLREFLRaRRPPGLDysfdtckpPEEQLTFkdlvscAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFG 525
Cdd:cd07869  85 VHT-DLCQYMD-KHPGGLH--------PENVKLF------LFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFG 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13112048 526 LAR--DVHNLDYykktTNGRLPVKWMAPEALFDRV-YTHQSDVWSFGVLLWEIFTlGGSPYPGI 586
Cdd:cd07869 149 LARakSVPSHTY----SNEVVTLWYRPPDVLLGSTeYSTCLDMWGVGCIFVEMIQ-GVAAFPGM 207
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
362-573 1.72e-07

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: 53.07  E-value: 1.72e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 362 LGKPLGEGCFGQVvmAEAIGIDKDRaakpvTVAVKMLKDDATDKDLSD--LVSEMEMMKMIgKHKNIINLLGAC-TQGGP 438
Cdd:cd14163   4 LGKTIGEGTYSKV--KEAFSKKHQR-----KVAIKIIDKSGGPEEFIQrfLPRELQIVERL-DHKNIIHVYEMLeSADGK 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 439 LYVLVEYAAKGNLreflrarrppgLDYSFDTCKPPEEQLT--FKDLVScayqvarGMEYLASQKCIHRDLAARNVLVTED 516
Cdd:cd14163  76 IYLVMELAEDGDV-----------FDCVLHGGPLPEHRAKalFRQLVE-------AIRYCHGCGVAHRDLKCENALLQGF 137
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13112048 517 NVmKIADFGLARDV-HNLDYYKKTTNGRlpVKWMAPEALfdRVYTHQS---DVWSFGVLLW 573
Cdd:cd14163 138 TL-KLTDFGFAKQLpKGGRELSQTFCGS--TAYAAPEVL--QGVPHDSrkgDIWSMGVVLY 193
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
366-585 2.10e-07

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK3 is a Fas-interacting protein that induces FADD (Fas-associated death domain) phosphorylation and mediates FasL-induced JNK activation. Overexpression of HIPK3 does not affect cell death, however its expression in prostate cancer cells contributes to increased resistance to Fas receptor-mediated apoptosis. HIPK3 also plays a role in regulating steroidogenic gene expression. In response to cAMP, HIPK3 activates the phosphorylation of JNK and c-Jun, leading to increased activity of the transcription factor SF-1 (Steroidogenic factor 1), a key regulator for steroid biosynthesis in the gonad and adrenal gland. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 53.49  E-value: 2.10e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKdraakpvTVAVKMLKDDATDKDLSDLvsEMEMM-KMIGKHKNIINLLGA--CTQGGPLYVL 442
Cdd:cd14229   8 LGRGTFGQVVKCWKRGTNE-------IVAVKILKNHPSYARQGQI--EVGILaRLSNENADEFNFVRAyeCFQHRNHTCL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 443 VEYAAKGNLREFLRARRppgldYSfdtckppeeQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVL----VTEDNV 518
Cdd:cd14229  79 VFEMLEQNLYDFLKQNK-----FS---------PLPLKVIRPILQQVATALKKLKSLGLIHADLKPENIMlvdpVRQPYR 144
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13112048 519 MKIADFGLARDVHnldyyKKTTNGRLPVKWM-APEALFDRVYTHQSDVWSFGVLLWEIFtLGGSPYPG 585
Cdd:cd14229 145 VKVIDFGSASHVS-----KTVCSTYLQSRYYrAPEIILGLPFCEAIDMWSLGCVIAELF-LGWPLYPG 206
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
364-631 2.22e-07

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 54.36  E-value: 2.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048   364 KPLGEGCFGQVVMAEAIGIDKDRAAKpvTVAVKMLKDdatdKDLSDLVSEMEMMKMIgKHKNIIN----LLGACTQggPL 439
Cdd:PTZ00266   19 KKIGNGRFGEVFLVKHKRTQEFFCWK--AISYRGLKE----REKSQLVIEVNVMREL-KHKNIVRyidrFLNKANQ--KL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048   440 YVLVEYAAKGNLREflrarrppgldySFDTCKPPEEQLTFKDLVSCAYQVARGMEYLAS-------QKCIHRDLAARNVL 512
Cdd:PTZ00266   90 YILMEFCDAGDLSR------------NIQKCYKMFGKIEEHAIVDITRQLLHALAYCHNlkdgpngERVLHRDLKPQNIF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048   513 VTE------------DN-----VMKIADFGLARDVhNLDYYKKTTNGRlPVKWmAPEALF--DRVYTHQSDVWSFGVLLW 573
Cdd:PTZ00266  158 LSTgirhigkitaqaNNlngrpIAKIGDFGLSKNI-GIESMAHSCVGT-PYYW-SPELLLheTKSYDDKSDMWALGCIIY 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 13112048   574 EIFTlGGSPY-PGIPVEELFKLLKEGHRMDKPANcTHDLYMIMRECWHAAPSQRPTFKQ 631
Cdd:PTZ00266  235 ELCS-GKTPFhKANNFSQLISELKRGPDLPIKGK-SKELNILIKNLLNLSAKERPSALQ 291
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
364-598 2.35e-07

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 53.12  E-value: 2.35e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 364 KPLGEGCFGqvvMAEAIGIDKDRAAKPVTVAVKMLKddatdkdlSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYVLV 443
Cdd:cd14179  13 KPLGEGSFS---ICRKCLHKKTNQEYAVKIVSKRME--------ANTQREIAALKLCEGHPNIVKLHEVYHDQLHTFLVM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 444 EYAAKGNLREFLRARRppglDYSfdtckPPEEQLTFKDLVScayqvarGMEYLASQKCIHRDLAARNVLVTEDN---VMK 520
Cdd:cd14179  82 ELLKGGELLERIKKKQ----HFS-----ETEASHIMRKLVS-------AVSHMHDVGVVHRDLKPENLLFTDESdnsEIK 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 521 IADFGLARdvhnldyYKKTTNGRLP-----VKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPG-------IPV 588
Cdd:cd14179 146 IIDFGFAR-------LKPPDNQPLKtpcftLHYAAPELLNYNGYDESCDLWSLGVILYTMLS-GQVPFQChdksltcTSA 217
                       250
                ....*....|
gi 13112048 589 EELFKLLKEG 598
Cdd:cd14179 218 EEIMKKIKQG 227
IgI_1_FGFR cd04973
First immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of ...
37-109 2.46e-07

First immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR). Fibroblast growth factors (FGFs) participate in morphogenesis, development, angiogenesis, and wound healing. These FGF-stimulated processes are mediated by four FGFR tyrosine kinases (FGRF1-4). FGFRs are comprised of an extracellular portion consisting of three Ig-like domains, a transmembrane helix, and a cytoplasmic portion having protein tyrosine kinase activity. The highly conserved Ig-like domains 2 and 3, and the linker region between D2 and D3 define a general binding site for all FGFs.


Pssm-ID: 409362  Cd Length: 94  Bit Score: 49.12  E-value: 2.46e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13112048  37 EVPGPEPGQQEQLVFGSGDAVELSCPPPGGGPMGPtvWVKDGTGLVPSERVLVGPQRLQVLNASHEDSGAYSC 109
Cdd:cd04973   7 APPTYQISEVESYSAHPGDLLQLRCRLRDDVQSIN--WTKDGVQLGENNRTRITGEEVQIKDAVPRDSGLYAC 77
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
371-583 2.54e-07

Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to Calcium/calmodulin-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 uncharacterized STKs with similarity to CaMKs, which are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. This uncharacterized 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: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 52.72  E-value: 2.54e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 371 FGQVVMAEA---IGIDKDRAAKPVTVAVKMLKDDATdKDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLYVLVEYAA 447
Cdd:cd14088   5 LGQVIKTEEfceIFRAKDKTTGKLYTCKKFLKRDGR-KVRKAAKNEINILKMV-KHPNILQLVDVFETRKEYFIFLELAT 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 448 KgnlREFLrarrppglDYSFDTCKPPEeqltfKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTedNVMK-----IA 522
Cdd:cd14088  83 G---REVF--------DWILDQGYYSE-----RDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYY--NRLKnskivIS 144
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13112048 523 DFGLArdvhnldyykKTTNGRL--PV---KWMAPEALFDRVYTHQSDVWSFGVLLWeIFTLGGSPY 583
Cdd:cd14088 145 DFHLA----------KLENGLIkePCgtpEYLAPEVVGRQRYGRPVDCWAIGVIMY-ILLSGNPPF 199
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
361-635 2.94e-07

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: 52.16  E-value: 2.94e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 361 TLGKPLGEGCFGQVVMAEaigidkdRAAKPVTVAVKMLKDDATDK--DLSDLVS---EMEMMKMIGK---HKNIINLLGA 432
Cdd:cd14101   3 TMGNLLGKGGFGTVYAGH-------RISDGLQVAIKQISRNRVQQwsKLPGVNPvpnEVALLQSVGGgpgHRGVIRLLDW 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 433 C-TQGGPLYVLVEYAAKGNLREFLRARRPpgLDYSFDTCkppeeqlTFKdlvscayQVARGMEYLASQKCIHRDLAARNV 511
Cdd:cd14101  76 FeIPEGFLLVLERPQHCQDLFDYITERGA--LDESLARR-------FFK-------QVVEAVQHCHSKGVVHRDIKDENI 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 512 LV-TEDNVMKIADFGLARDVHNLDYYK-KTTNGRLPVKWMapeaLFDRVYTHQSDVWSFGVLLWEIFTlggspyPGIPVE 589
Cdd:cd14101 140 LVdLRTGDIKLIDFGSGATLKDSMYTDfDGTRVYSPPEWI----LYHQYHALPATVWSLGILLYDMVC------GDIPFE 209
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 13112048 590 ELFKLLKEghRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVED 635
Cdd:cd14101 210 RDTDILKA--KPSFNKRVSNDCRSLIRSCLAYNPSDRPSLEQILLH 253
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
366-583 3.07e-07

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: 52.60  E-value: 3.07e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 366 LGEGCFGQVVMAEAIGIDKDRAAKPVTVavKMLKDDATDKdlsdlvseMEMMKmigkhKNIINLLGActqggPLYVLVEY 445
Cdd:cd05607  10 LGKGGFGEVCAVQVKNTGQMYACKKLDK--KRLKKKSGEK--------MALLE-----KEILEKVNS-----PFIVSLAY 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 446 AAKGNLREFLRARRPPGLDYSFDTCKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFG 525
Cdd:cd05607  70 AFETKTHLCLVMSLMNGGDLKYHIYNVGERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLG 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 13112048 526 LARDVHNldyyKKTTNGRLPVK-WMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPY 583
Cdd:cd05607 150 LAVEVKE----GKPITQRAGTNgYMAPEILKEESYSYPVDWFAMGCSIYEMVA-GRTPF 203
IgI_VEGFR cd04976
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor (VEGFR); member ...
158-246 3.17e-07

Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor (VEGFR); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor (VEGFR). The VEGFRs have an extracellular component with seven Ig-like domains, a transmembrane segment, and an intracellular tyrosine kinase domain interrupted by a kinase-insert domain. The VEGFR family consists of three members, VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). VEGFRs bind VEGFs with high affinity at the Ig-like domains. VEGF-A is important to the growth and maintenance of vascular endothelial cells and to the development of new blood- and lymphatic-vessels in physiological and pathological states. VEGFR-2 is a major mediator of the mitogenic, angiogenic, and microvascular permeability-enhancing effects of VEGF-A. VEGFR-1 may play an inhibitory part in these processes by binding VEGF and interfering with its interaction with VEGFR-2. VEGFR-1 has a signaling role in mediating monocyte chemotaxis. VEGFR-1 and VEGFR-2 may mediate a chemotactic and a survival signal in hematopoietic stem cells or leukemia cells. VEGFR-3 has been shown to be involved in tumor angiogenesis and growth. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409365  Cd Length: 90  Bit Score: 48.75  E-value: 3.17e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 158 RMDKKLLAVPAANTVRFRCPAAGNPTPSISWLKNGREFRGEHRiggiklRHQQWSLVMESVVPSDRGNYTCVVENKFGSI 237
Cdd:cd04976   7 RKQQVLEATAGKRSVRLPMKVKAYPPPEVVWYKDGLPLTEKAR------YLTRHSLIIKEVTEEDTGNYTILLSNKQSNV 80

                ....*....
gi 13112048 238 RQTYTLDVL 246
Cdd:cd04976  81 FKNLTATLV 89
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
361-576 3.19e-07

Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK2 is a tetrameric protein with two catalytic (alpha) and two regulatory (beta) subunits. It is constitutively active and ubiquitously expressed, and is found in the cytoplasm, nucleus, as well as in the plasma membrane. It phosphorylates a wide variety of substrates including gylcogen synthase, cell cycle proteins, nuclear proteins (e.g. DNA topoisomerase II), and ion channels (e.g. ENaC), among others. It may be considered a master kinase controlling the activity or lifespan of many other kinases and exerting its effect over cell fate, gene expression, protein synthesis and degradation, and viral infection. CK2 is implicated in every stage of the cell cycle and is required for cell cycle progression. It plays crucial roles in cell differentiation, proliferation, and survival, and is thus implicated in cancer. CK2 is not an oncogene by itself but elevated CK2 levels create an environment that enhances the survival of tumor cells. The CK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 52.54  E-value: 3.19e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 361 TLGKPLGEGCFGQVVmaEAIGIDKDRAakpvtVAVKMLKDDATDKdlsdLVSEMEMMKMIGKHKNIINLLGA----CTQg 436
Cdd:cd14132  21 EIIRKIGRGKYSEVF--EGINIGNNEK-----VVIKVLKPVKKKK----IKREIKILQNLRGGPNIVKLLDVvkdpQSK- 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 437 gpLYVLV-EYAAKGNLREFLrarrppgldysfdtckppeEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTE 515
Cdd:cd14132  89 --TPSLIfEYVNNTDFKTLY-------------------PTLTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMIDH 147
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13112048 516 DN-VMKIADFGLArdvhnlDYY--KKTTNGRLPVKWM-APEALFD-RVYTHQSDVWSFGVLLWE-IF 576
Cdd:cd14132 148 EKrKLRLIDWGLA------EFYhpGQEYNVRVASRYYkGPELLVDyQYYDYSLDMWSLGCMLASmIF 208
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
387-582 3.35e-07

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: 52.28  E-value: 3.35e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 387 AAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYVLVEYAAKGNLREFLRARrppgldys 466
Cdd:cd14181  39 AVKIIEVTAERLSPEQLEEVRSSTLKEIHILRQVSGHPSIITLIDSYESSTFIFLVFDLMRRGELFDYLTEK-------- 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 467 fdtckppeEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARDVHNLDYYKKT--TNGrl 544
Cdd:cd14181 111 --------VTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGFSCHLEPGEKLRELcgTPG-- 180
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 13112048 545 pvkWMAPEAL---FDRV---YTHQSDVWSFGVLLWEIftLGGSP 582
Cdd:cd14181 181 ---YLAPEILkcsMDEThpgYGKEVDLWACGVILFTL--LAGSP 219
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
411-582 3.66e-07

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: 52.22  E-value: 3.66e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 411 VSEMEMMKMIGKHKNIINLLGACTQGGPLYVLVEYAAKGNLREFLrarrppgldysfdtckppEEQLTF--KDLVSCAYQ 488
Cdd:cd14182  57 LKEIDILRKVSGHPNIIQLKDTYETNTFFFLVFDLMKKGELFDYL------------------TEKVTLseKETRKIMRA 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 489 VARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARDVHNLDYYKKT--TNGrlpvkWMAPEALFDRV------YT 560
Cdd:cd14182 119 LLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFSCQLDPGEKLREVcgTPG-----YLAPEIIECSMddnhpgYG 193
                       170       180
                ....*....|....*....|..
gi 13112048 561 HQSDVWSFGVLLWEIftLGGSP 582
Cdd:cd14182 194 KEVDMWSTGVIMYTL--LAGSP 213
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
360-587 5.28e-07

Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like kinase (also called greatwall kinase); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MASTL kinases in this group carry only a catalytic domain, which contains a long insertion relative to MAST kinases. MASTL, also called greatwall kinase (Gwl), is involved in the regulation of mitotic entry, which is controlled by the coordinated activities of protein kinases and opposing protein phosphatases (PPs). The cyclin B/CDK1 complex induces entry into M-phase while PP2A-B55 shows anti-mitotic activity. MASTL/Gwl is activated downstream of cyclin B/CDK1 and indirectly inhibits PP2A-B55 by phosphorylating the small protein alpha-endosulfine (Ensa) or the cAMP-regulated phosphoprotein 19 (Arpp19), resulting in M-phase progression. Gwl kinase may also play roles in mRNA stabilization and DNA checkpoint recovery. The human MASTL gene has also been named FLJ14813; a missense mutation in FLJ14813 is associated with autosomal dominant thrombocytopenia. The MASTL 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: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 52.19  E-value: 5.28e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 360 LTLGKPLGEGCFGQVVMAEaigidKDRAAKPVTVAVkMLKDDATDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPL 439
Cdd:cd05610   6 FVIVKPISRGAFGKVYLGR-----KKNNSKLYAVKV-VKKADMINKNMVHQVQAERDALALSKSPFIVHLYYSLQSANNV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 440 YVLVEYAAKGNLREFLRArrppgldYSFdtckppeeqltFKDLVSCAY--QVARGMEYLASQKCIHRDLAARNVLVTEDN 517
Cdd:cd05610  80 YLVMEYLIGGDVKSLLHI-------YGY-----------FDEEMAVKYisEVALALDYLHRHGIIHRDLKPDNMLISNEG 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 518 VMKIADFGLA-----RDVHNLDYY-------------------------------------KKTTNGRLPVK-------- 547
Cdd:cd05610 142 HIKLTDFGLSkvtlnRELNMMDILttpsmakpkndysrtpgqvlslisslgfntptpyrtpKSVRRGAARVEgerilgtp 221
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 13112048 548 -WMAPEALFDRVYTHQSDVWSFGVLLWEIFTlggspypGIP 587
Cdd:cd05610 222 dYLAPELLLGKPHGPAVDWWALGVCLFEFLT-------GIP 255
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
164-240 5.46e-07

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 47.91  E-value: 5.46e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13112048 164 LAVPAANTVRFRCPAAGNPTPSISWLKNGREFRGEHRIGGIKLRhqqwSLVMESVVPSDRGNYTCVVENKFGSIRQT 240
Cdd:cd20957  11 QTVDFGRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQILSED----VLVIPSVKREDKGMYQCFVRNDGDSAQAT 83
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
489-633 6.29e-07

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 3 (MAPKAP3 or MK3) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK3 is a bonafide substrate for the MAPK p38. It is closely related to MK2 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK3 activity is only significant when MK2 is absent. The MK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 51.53  E-value: 6.29e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 489 VARGMEYLASQKCIHRDLAARNVLVT---EDNVMKIADFGLARD--VHNldyyKKTTNGRLPVkWMAPEALFDRVYTHQS 563
Cdd:cd14172 112 IGTAIQYLHSMNIAHRDVKPENLLYTskeKDAVLKLTDFGFAKEttVQN----ALQTPCYTPY-YVAPEVLGPEKYDKSC 186
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13112048 564 DVWSFGVLLWeIFTLGGSPYPGIPVEELFKLLKEGHRMDK---P----ANCTHDLYMIMRECWHAAPSQRPTFKQLV 633
Cdd:cd14172 187 DMWSLGVIMY-ILLCGFPPFYSNTGQAISPGMKRRIRMGQygfPnpewAEVSEEAKQLIRHLLKTDPTERMTITQFM 262
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
426-567 6.64e-07

Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIK, also called mitogen activated protein kinase kinase kinase 14 (MAP3K14), phosphorylates and activates Inhibitor of NF-KappaB Kinase (IKK) alpha, which is a regulator of 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. NIK is essential in the IKKalpha-mediated non-canonical NF-kB signaling pathway, in which IKKalpha processes the IkB-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus where it regulates gene transcription. NIK also plays an important role in Toll-like receptor 7/9 signaling cascades. The NIK 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: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 51.36  E-value: 6.64e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 426 IINLLGACTQGGPLYVLVEYAAKGNLREFLRARrppgldysfdTCKPPEEQLTFKdlvscaYQVARGMEYLASQKCIHRD 505
Cdd:cd13991  60 VVPLYGAVREGPWVNIFMDLKEGGSLGQLIKEQ----------GCLPEDRALHYL------GQALEGLEYLHSRKILHGD 123
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13112048 506 LAARNVLVTED-NVMKIADFGLARDVHNLDYYKKTTNGRLPV---KWMAPEALFDRVYTHQSDVWS 567
Cdd:cd13991 124 VKADNVLLSSDgSDAFLCDFGHAECLDPDGLGKSLFTGDYIPgteTHMAPEVVLGKPCDAKVDVWS 189
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
359-590 7.64e-07

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. 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 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: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 50.99  E-value: 7.64e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 359 RLTLGKPLGEGCFGQVVMaeaiGIDKDRAAKPVtVAVKMLKddaTDKDLSDLVSEMEMMKMiGKHKNIINLLGACTQGGP 438
Cdd:cd14112   4 RFSFGSEIFRGRFSVIVK----AVDSTTETDAH-CAVKIFE---VSDEASEAVREFESLRT-LQHENVQRLIAAFKPSNF 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 439 LYVLVEyaakgNLREFLRARRPPGLDYSfdtckppEEQLTfkdlvSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDN- 517
Cdd:cd14112  75 AYLVME-----KLQEDVFTRFSSNDYYS-------EEQVA-----TTVRQILDALHYLHFKGIAHLDVQPDNIMFQSVRs 137
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13112048 518 -VMKIADFGLARDVHNLDyyKKTTNGRlpVKWMAPEALFDRVY-THQSDVWSFGVLLWeIFTLGGSPYPGIPVEE 590
Cdd:cd14112 138 wQVKLVDFGRAQKVSKLG--KVPVDGD--TDWASPEFHNPETPiTVQSDIWGLGVLTF-CLLSGFHPFTSEYDDE 207
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
166-245 8.16e-07

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 47.42  E-value: 8.16e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 166 VPAANTVRFRCPAAGNPTPSISWLKNGREFRGEHRIGGIKLRHQQW--SLVMESVVPSDRGNYTCVVENKFGSIRQTYTL 243
Cdd:cd20951  12 VWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIPGKYKIESEYGvhVLHIRRVTVEDSAVYSAVAKNIHGEASSSASV 91

                ..
gi 13112048 244 DV 245
Cdd:cd20951  92 VV 93
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
361-583 8.26e-07

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: 51.36  E-value: 8.26e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 361 TLGKPLGEGCFGQVVMAEAIGIDKDraakpvtVAVKMLKDDAtdkDLSDLVSEMEMMKMIgKHKNIINLLGACTQGGPLY 440
Cdd:cd14085   6 EIESELGRGATSVVYRCRQKGTQKP-------YAVKKLKKTV---DKKIVRTEIGVLLRL-SHPNIIKLKEIFETPTEIS 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13112048 441 VLVEYAAKGNLREFLRARrppGLdYSFdtckppeeqltfKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVT---EDN 517
Cdd:cd14085  75 LVLELVTGGELFDRIVEK---GY-YSE------------RDAADAVKQILEAVAYLHENGIVHRDLKPENLLYAtpaPDA 138
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13112048 518 VMKIADFGLARDVHNlDYYKKTTNGRlPvKWMAPEALFDRVYTHQSDVWSFGVLLWeIFTLGGSPY 583
Cdd:cd14085 139 PLKIADFGLSKIVDQ-QVTMKTVCGT-P-GYCAPEILRGCAYGPEVDMWSVGVITY-ILLCGFEPF 200
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
171-245 8.73e-07

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 47.59  E-value: 8.73e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13112048 171 TVRFRCPAAGNPTPSISWLKNGREFRGEHRIgGIKLRHQQW-SLVMESVVPSDRGNYTCVVENKFGSIRQTYTLDV 245
Cdd:cd05737  18 TLNLTCNVWGDPPPEVSWLKNDQALAFLDHC-NLKVEAGRTvYFTINGVSSEDSGKYGLVVKNKYGSETSDVTVSV 92
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
48-110 1.04e-04

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 41.41  E-value: 1.04e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13112048    48 QLVFGSGDAVELSCPPPGGGPMGPTVWVKDGTGLVPSERVLVGPQR-----LQVLNASHEDSGAYSCR 110
Cdd:pfam00047   5 TVTVLEGDSATLTCSASTGSPGPDVTWSKEGGTLIESLKVKHDNGRttqssLLISNVTKEDAGTYTCV 72
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
253-288 1.17e-03

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 38.53  E-value: 1.17e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 13112048 253 PILQAGLPANQTAVLGSDVEFHCKVYSDAQPHIQWL 288
Cdd:cd20978   1 PKFIQKPEKNVVVKGGQDVTLPCQVTGVPQPKITWL 36
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
260-289 1.24e-03

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 38.26  E-value: 1.24e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 13112048    260 PANQTAVLGSDVEFHCKVYSDAQPHIQWLK 289
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVTWYK 30
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
260-289 1.97e-03

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 37.76  E-value: 1.97e-03
                        10        20        30
                ....*....|....*....|....*....|
gi 13112048 260 PANQTAVLGSDVEFHCKVYSDAQPHIQWLK 289
Cdd:cd05725   4 PQNQVVLVDDSAEFQCEVGGDPVPTVRWRK 33
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
260-308 2.21e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 37.55  E-value: 2.21e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 13112048   260 PANQTAVLGSDVEFHCKVYSDAQPHIQWLKhvevNGSKVGPDGTPYVTV 308
Cdd:pfam13927   8 PSSVTVREGETVTLTCEATGSPPPTITWYK----NGEPISSGSTRSRSL 52
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
54-125 3.34e-03

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 37.10  E-value: 3.34e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13112048     54 GDAVELSCPPPGGGPMGPTvWVKDGTGLV-PSERVLV----GPQRLQVLNASHEDSGAYSCRQRLTQRVL-CHFSVRV 125
Cdd:smart00410   9 GESVTLSCEASGSPPPEVT-WYKQGGKLLaESGRFSVsrsgSTSTLTISNVTPEDSGTYTCAATNSSGSAsSGTTLTV 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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