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Conserved domains on  [gi|1379623326|ref|XP_024635580|]
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probable inactive leucine-rich repeat receptor-like protein kinase At3g03770 [Medicago truncatula]

Protein Classification

protein kinase family protein( domain architecture ID 1000044)

protein kinase family protein containing leucine-rich repeat(s), may catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine and/or tyrosine residues on protein substrates; similar to plant LRR receptor-like kinases

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 ...
 487-742 4.71e-38

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 cd14066:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 272  Bit Score: 142.80  E-value: 4.71e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLENGIPVVIRCI-PLSKKYSIRNFKLRLDLLAKLRHTHLISLLGHCIDGilGERndskvFLIYECVS 565
Cdd:cd14066     1 IGSGGFGTVYKGVLENGTVVAVKRLnEMNCAASKKEFLTELEMLGRLRHPNLVRLLGYCLES--DEK-----LLVYEYMP 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 566 NGNFQTYLSGDSCGKIFNWSERLSVLISVAKAIHFLHTGMIPGFFRNRLKTNNILFNENWMAKLSDYGLS-------IVS 638
Cdd:cd14066    74 NGSLEDRLHCHKGSPPLPWPQRLKIAKGIARGLEYLHEECPPPIIHGDIKSSNILLDEDFEPKLTDFGLArlippseSVS 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 639 EETDASGVIGESPNSW-QMKKLED--DIYSFGFIILEALVG-PSMFAKREAAVLNAMASF---SSQDEWKQIVDP----- 706
Cdd:cd14066   154 KTSAVKGTIGYLAPEYiRTGRVSTksDVYSFGVVLLELLTGkPAVDENRENASRKDLVEWvesKGKEELEDILDKrlvdd 233

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1379623326 707 -VVQATCCKESLSIVISitnkCISTESWSRPSIEDVL 742
Cdd:cd14066   234 dGVEEEEVEALLRLALL----CTRSDPSLRPSMKEVV 266
PLN00113 super family cl33413
leucine-rich repeat receptor-like protein kinase; Provisional
 113-750 1.62e-36

leucine-rich repeat receptor-like protein kinase; Provisional


The actual alignment was detected with superfamily member PLN00113:

Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 148.07  E-value: 1.62e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 113 LARLTSLRVLHLVSLGIWGPFPDRIHRLFSLEQLDLSSNYLYGSIPPKISTMVSLQILMLGDNFFNGTIPNLFDSSSNLT 192
Cdd:PLN00113  304 VIQLQNLEILHLFSNNFTGKIPVALTSLPRLQVLQLWSNKFSGEIPKNLGKHNNLTVLDLSTNNLTGEIPEGLCSSGNLF 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 193 VFSLKNNKLKGPFPFSILSITTLTNIDMSRNQISGSL-QDFTGL------------------------SSLEHLDLRENE 247
Cdd:PLN00113  384 KLILFSNSLEGEIPKSLGACRSLRRVRLQDNSFSGELpSEFTKLplvyfldisnnnlqgrinsrkwdmPSLQMLSLARNK 463

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 248 LDSDLPAL--PKGLISLFLNRNSFSGQIPKSYGQLNSLQHLDISFNTLTGATPSELFSLPNIIYLNLGSNMLSGTLQNSL 325
Cdd:PLN00113  464 FFGGLPDSfgSKRLENLDLSRNQFSGAVPRKLGSLSELMQLKLSENKLSGEIPDELSSCKKLVSLDLSHNQLSGQIPASF 543

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 326 RCGRNLSFVDISNNRLIGALPYSLSNVSENRAVESDGNCLSGTLQHQHAvsYCAEAPDKKKSNrvgifvgvivgilviiv 405
Cdd:PLN00113  544 SEMPVLSQLDLSQNQLSGEIPKNLGNVESLVQVNISHNHLHGSLPSTGA--FLAINASAVAGN----------------- 604

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 406 lfglciVVICKRYYSRGIAEQHLLHKS------VQDSYSAGFSCELIANA------RYVSEAAKLGRED---------LP 464
Cdd:PLN00113  605 ------IDLCGGDTTSGLPPCKRVRKTpswwfyITCTLGAFLVLALVAFGfvfirgRNNLELKRVENEDgtwelqffdSK 678

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 465 SCRSYSLEELMEATNnfdNSTFLGENIYGKLYKGK-LENGIPVVIRCIplsKKY-SIRnfKLRLDLLAKLRHTHLISLLG 542
Cdd:PLN00113  679 VSKSITINDILSSLK---EENVISRGKKGASYKGKsIKNGMQFVVKEI---NDVnSIP--SSEIADMGKLQHPNIVKLIG 750

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 543 HCidgilgeRNDSKVFLIYECVSNGNFQTYLSGDScgkifnWSERLSVLISVAKAIHFLHTGMIPGFFRNRLKTNNILFN 622
Cdd:PLN00113  751 LC-------RSEKGAYLIHEYIEGKNLSEVLRNLS------WERRRKIAIGIAKALRFLHCRCSPAVVVGNLSPEKIIID 817

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 623 ENWMAKLSdygLSIVSEE-TDASGVIGE---SPNSWQMKKL--EDDIYSFGFIILEALVGPS----MFAKREAAVLNAMA 692
Cdd:PLN00113  818 GKDEPHLR---LSLPGLLcTDTKCFISSayvAPETRETKDIteKSDIYGFGLILIELLTGKSpadaEFGVHGSIVEWARY 894

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1379623326 693 SFSS--QDEWkqiVDPVV--QATCCKESLSIVISITNKCISTESWSRPSIEDVLWNLQYASQ 750
Cdd:PLN00113  895 CYSDchLDMW---IDPSIrgDVSVNQNEIVEVMNLALHCTATDPTARPCANDVLKTLESASR 953
 
Name Accession Description Interval E-value
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
 487-742 4.71e-38

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: 142.80  E-value: 4.71e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLENGIPVVIRCI-PLSKKYSIRNFKLRLDLLAKLRHTHLISLLGHCIDGilGERndskvFLIYECVS 565
Cdd:cd14066     1 IGSGGFGTVYKGVLENGTVVAVKRLnEMNCAASKKEFLTELEMLGRLRHPNLVRLLGYCLES--DEK-----LLVYEYMP 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 566 NGNFQTYLSGDSCGKIFNWSERLSVLISVAKAIHFLHTGMIPGFFRNRLKTNNILFNENWMAKLSDYGLS-------IVS 638
Cdd:cd14066    74 NGSLEDRLHCHKGSPPLPWPQRLKIAKGIARGLEYLHEECPPPIIHGDIKSSNILLDEDFEPKLTDFGLArlippseSVS 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 639 EETDASGVIGESPNSW-QMKKLED--DIYSFGFIILEALVG-PSMFAKREAAVLNAMASF---SSQDEWKQIVDP----- 706
Cdd:cd14066   154 KTSAVKGTIGYLAPEYiRTGRVSTksDVYSFGVVLLELLTGkPAVDENRENASRKDLVEWvesKGKEELEDILDKrlvdd 233

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1379623326 707 -VVQATCCKESLSIVISitnkCISTESWSRPSIEDVL 742
Cdd:cd14066   234 dGVEEEEVEALLRLALL----CTRSDPSLRPSMKEVV 266
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 113-750 1.62e-36

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 148.07  E-value: 1.62e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 113 LARLTSLRVLHLVSLGIWGPFPDRIHRLFSLEQLDLSSNYLYGSIPPKISTMVSLQILMLGDNFFNGTIPNLFDSSSNLT 192
Cdd:PLN00113  304 VIQLQNLEILHLFSNNFTGKIPVALTSLPRLQVLQLWSNKFSGEIPKNLGKHNNLTVLDLSTNNLTGEIPEGLCSSGNLF 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 193 VFSLKNNKLKGPFPFSILSITTLTNIDMSRNQISGSL-QDFTGL------------------------SSLEHLDLRENE 247
Cdd:PLN00113  384 KLILFSNSLEGEIPKSLGACRSLRRVRLQDNSFSGELpSEFTKLplvyfldisnnnlqgrinsrkwdmPSLQMLSLARNK 463

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 248 LDSDLPAL--PKGLISLFLNRNSFSGQIPKSYGQLNSLQHLDISFNTLTGATPSELFSLPNIIYLNLGSNMLSGTLQNSL 325
Cdd:PLN00113  464 FFGGLPDSfgSKRLENLDLSRNQFSGAVPRKLGSLSELMQLKLSENKLSGEIPDELSSCKKLVSLDLSHNQLSGQIPASF 543

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 326 RCGRNLSFVDISNNRLIGALPYSLSNVSENRAVESDGNCLSGTLQHQHAvsYCAEAPDKKKSNrvgifvgvivgilviiv 405
Cdd:PLN00113  544 SEMPVLSQLDLSQNQLSGEIPKNLGNVESLVQVNISHNHLHGSLPSTGA--FLAINASAVAGN----------------- 604

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 406 lfglciVVICKRYYSRGIAEQHLLHKS------VQDSYSAGFSCELIANA------RYVSEAAKLGRED---------LP 464
Cdd:PLN00113  605 ------IDLCGGDTTSGLPPCKRVRKTpswwfyITCTLGAFLVLALVAFGfvfirgRNNLELKRVENEDgtwelqffdSK 678

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 465 SCRSYSLEELMEATNnfdNSTFLGENIYGKLYKGK-LENGIPVVIRCIplsKKY-SIRnfKLRLDLLAKLRHTHLISLLG 542
Cdd:PLN00113  679 VSKSITINDILSSLK---EENVISRGKKGASYKGKsIKNGMQFVVKEI---NDVnSIP--SSEIADMGKLQHPNIVKLIG 750

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 543 HCidgilgeRNDSKVFLIYECVSNGNFQTYLSGDScgkifnWSERLSVLISVAKAIHFLHTGMIPGFFRNRLKTNNILFN 622
Cdd:PLN00113  751 LC-------RSEKGAYLIHEYIEGKNLSEVLRNLS------WERRRKIAIGIAKALRFLHCRCSPAVVVGNLSPEKIIID 817

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 623 ENWMAKLSdygLSIVSEE-TDASGVIGE---SPNSWQMKKL--EDDIYSFGFIILEALVGPS----MFAKREAAVLNAMA 692
Cdd:PLN00113  818 GKDEPHLR---LSLPGLLcTDTKCFISSayvAPETRETKDIteKSDIYGFGLILIELLTGKSpadaEFGVHGSIVEWARY 894

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1379623326 693 SFSS--QDEWkqiVDPVV--QATCCKESLSIVISITNKCISTESWSRPSIEDVLWNLQYASQ 750
Cdd:PLN00113  895 CYSDchLDMW---IDPSIrgDVSVNQNEIVEVMNLALHCTATDPTARPCANDVLKTLESASR 953
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
108-351 1.32e-22

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 101.16  E-value: 1.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 108 SFVATLARLTSLRVLHLVSLGIwGPFPDRIHRLFSLEQLDLSSNYLyGSIPPKISTMVSLQILMLGDNFFNgTIPNLFDS 187
Cdd:COG4886   104 SGNEELSNLTNLESLDLSGNQL-TDLPEELANLTNLKELDLSNNQL-TDLPEPLGNLTNLKSLDLSNNQLT-DLPEELGN 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 188 SSNLTVFSLKNNKLKgPFPFSILSITTLTNIDMSRNQISGSLQDFTGLSSLEHLDLRENELdSDLPALP--KGLISLFLN 265
Cdd:COG4886   181 LTNLKELDLSNNQIT-DLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQL-TDLPELGnlTNLEELDLS 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 266 RNSFSGqIPKSyGQLNSLQHLDISFNTLTGATPSELFSLPNIIYLNLGSNMLSGTLQNSLRCGRNLSFVDISNNRLIGAL 345
Cdd:COG4886   259 NNQLTD-LPPL-ANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVT 336


                  ....*.
gi 1379623326 346 PYSLSN 351
Cdd:COG4886   337 LTTLAL 342
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
 486-742 5.70e-15

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 75.26  E-value: 5.70e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326  486 FLGENIYGKLYKGK-LENGIPVVIRCIPLSKKYSIRNFKLR-LDLLAKLRHTHLISLLGHCIDgilgernDSKVFLIYEC 563
Cdd:smart00220   6 KLGEGSFGKVYLARdKKTGKLVAIKVIKKKKIKKDRERILReIKILKKLKHPNIVRLYDVFED-------EDKLYLVMEY 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326  564 VSNGNFQTYLSGDscgKIFNWSERLSVLISVAKAIHFLHT-GMIpgffrNR-LKTNNILFNENWMAKLSDYGLS-IVSEE 640
Cdd:smart00220  79 CEGGDLFDLLKKR---GRLSEDEARFYLRQILSALEYLHSkGIV-----HRdLKPENILLDEDGHVKLADFGLArQLDPG 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326  641 TDASGVIGeSPN-------SWQMKKLEDDIYSFGFIILEALVGpsmfakreaavlnaMASFSSQDEWKQIVDPVVQATCC 713
Cdd:smart00220 151 EKLTTFVG-TPEymapevlLGKGYGKAVDIWSLGVILYELLTG--------------KPPFPGDDQLLELFKKIGKPKPP 215

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1379623326  714 KESLSIVIS-----ITNKCISTESWSRPSIEDVL 742
Cdd:smart00220 216 FPPPEWDISpeakdLIRKLLVKDPEKRLTAEEAL 249
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
 487-667 1.41e-11

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: 65.60  E-value: 1.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKL-----ENGIPVVIRCI-PLSKKYSIRNFKLRLDLLAKLRHTHLISLLGHCIDGilgerndSKVFLI 560
Cdd:pfam07714   7 LGEGAFGEVYKGTLkgegeNTKIKVAVKTLkEGADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQG-------EPLYIV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 561 YECVSNGNFQTYLSgdSCGKIFNWSERLSVLISVAKAIHFLHT-GMIpgfFRNrLKTNNILFNENWMAKLSDYGLSIVSE 639
Cdd:pfam07714  80 TEYMPGGDLLDFLR--KHKRKLTLKDLLSMALQIAKGMEYLESkNFV---HRD-LAARNCLVSENLVVKISDFGLSRDIY 153

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1379623326 640 ETDASGVIGE--------SPNSWQMKKL--EDDIYSFG 667
Cdd:pfam07714 154 DDDYYRKRGGgklpikwmAPESLKDGKFtsKSDVWSFG 191
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
487-676 2.09e-10

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 63.88  E-value: 2.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGK-LENGIPVVIRCIPLSKKYS---IRNFKLRLDLLAKLRHTHLISLLGHcidgilGERNDSkVFLIYE 562
Cdd:COG0515    15 LGRGGMGVVYLARdLRLGRPVALKVLRPELAADpeaRERFRREARALARLNHPNIVRVYDV------GEEDGR-PYLVME 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 563 CVSNGNFQTYLSGdscGKIFNWSERLSVLISVAKAIHFLHT-GMIpgfFRNrLKTNNILFNENWMAKLSDYGLSIV---S 638
Cdd:COG0515    88 YVEGESLADLLRR---RGPLPPAEALRILAQLAEALAAAHAaGIV---HRD-IKPANILLTPDGRVKLIDFGIARAlggA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1379623326 639 EETDASGVIGE----SPNSWQMKKLE--DDIYSFGFIILEALVG 676
Cdd:COG0515   161 TLTQTGTVVGTpgymAPEQARGEPVDprSDVYSLGVTLYELLTG 204
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 166-339 1.46e-08

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 55.95  E-value: 1.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 166 SLQILMLGDNFFNgTIPNLfDSSSNLTVFSLKNNKLKgpfpfSILSITTLTN---IDMSRNQISgSLQDFTGLSSLEHLD 242
Cdd:cd21340    25 NLKVLYLYDNKIT-KIENL-EFLTNLTHLYLQNNQIE-----KIENLENLVNlkkLYLGGNRIS-VVEGLENLTNLEELH 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 243 LrENEldsdlpALPKGLISLFLNRNSFSgqipksygQLNSLQHLDISFNTLTgaTPSELFSLPNIIYLNLGSNMLS--GT 320
Cdd:cd21340    97 I-ENQ------RLPPGEKLTFDPRSLAA--------LSNSLRVLNISGNNID--SLEPLAPLRNLEQLDASNNQISdlEE 159

                         170
                  ....*....|....*....
gi 1379623326 321 LQNSLRCGRNLSFVDISNN 339
Cdd:cd21340   160 LLDLLSSWPSLRELDLTGN 178
PHA02988 PHA02988
hypothetical protein; Provisional
 482-745 9.92e-06

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 48.20  E-value: 9.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 482 DNSTFLGENIYGKLYKGKLeNGIPVVIR---CIPLSKKYSIRNFKLRLDLLAKLRHTHLISLLGHCIDGIlgernDS--K 556
Cdd:PHA02988   23 YTSVLIKENDQNSIYKGIF-NNKEVIIRtfkKFHKGHKVLIDITENEIKNLRRIDSNNILKIYGFIIDIV-----DDlpR 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 557 VFLIYECVSNGNFQTYLSGDscgKIFNWSERLSVLISVAKAIHFLHTgmipgfFRNR----LKTNNILFNENWMAKLSDY 632
Cdd:PHA02988   97 LSLILEYCTRGYLREVLDKE---KDLSFKTKLDMAIDCCKGLYNLYK------YTNKpyknLTSVSFLVTENYKLKIICH 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 633 GLSIVSEETDASGVIGESPNSWQMKK-------LEDDIYSFGFIILEALVGPSMFAkreaavlnamaSFSSQDEWKQIVD 705
Cdd:PHA02988  168 GLEKILSSPPFKNVNFMVYFSYKMLNdifseytIKDDIYSLGVVLWEIFTGKIPFE-----------NLTTKEIYDLIIN 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1379623326 706 PVVQATCCKESLSIVISITNKCISTESWSRPSIEDVLWNL 745
Cdd:PHA02988  237 KNNSLKLPLDCPLEIKCIVEACTSHDSIKRPNIKEILYNL 276
LRR_8 pfam13855
Leucine rich repeat;
282-341 1.14e-05

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 43.28  E-value: 1.14e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 282 SLQHLDISFNTLTGATPSELFSLPNIIYLNLGSNMLSGTLQNSLRCGRNLSFVDISNNRL 341
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
 
Name Accession Description Interval E-value
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
 487-742 4.71e-38

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: 142.80  E-value: 4.71e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLENGIPVVIRCI-PLSKKYSIRNFKLRLDLLAKLRHTHLISLLGHCIDGilGERndskvFLIYECVS 565
Cdd:cd14066     1 IGSGGFGTVYKGVLENGTVVAVKRLnEMNCAASKKEFLTELEMLGRLRHPNLVRLLGYCLES--DEK-----LLVYEYMP 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 566 NGNFQTYLSGDSCGKIFNWSERLSVLISVAKAIHFLHTGMIPGFFRNRLKTNNILFNENWMAKLSDYGLS-------IVS 638
Cdd:cd14066    74 NGSLEDRLHCHKGSPPLPWPQRLKIAKGIARGLEYLHEECPPPIIHGDIKSSNILLDEDFEPKLTDFGLArlippseSVS 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 639 EETDASGVIGESPNSW-QMKKLED--DIYSFGFIILEALVG-PSMFAKREAAVLNAMASF---SSQDEWKQIVDP----- 706
Cdd:cd14066   154 KTSAVKGTIGYLAPEYiRTGRVSTksDVYSFGVVLLELLTGkPAVDENRENASRKDLVEWvesKGKEELEDILDKrlvdd 233

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1379623326 707 -VVQATCCKESLSIVISitnkCISTESWSRPSIEDVL 742
Cdd:cd14066   234 dGVEEEEVEALLRLALL----CTRSDPSLRPSMKEVV 266
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 113-750 1.62e-36

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 148.07  E-value: 1.62e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 113 LARLTSLRVLHLVSLGIWGPFPDRIHRLFSLEQLDLSSNYLYGSIPPKISTMVSLQILMLGDNFFNGTIPNLFDSSSNLT 192
Cdd:PLN00113  304 VIQLQNLEILHLFSNNFTGKIPVALTSLPRLQVLQLWSNKFSGEIPKNLGKHNNLTVLDLSTNNLTGEIPEGLCSSGNLF 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 193 VFSLKNNKLKGPFPFSILSITTLTNIDMSRNQISGSL-QDFTGL------------------------SSLEHLDLRENE 247
Cdd:PLN00113  384 KLILFSNSLEGEIPKSLGACRSLRRVRLQDNSFSGELpSEFTKLplvyfldisnnnlqgrinsrkwdmPSLQMLSLARNK 463

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 248 LDSDLPAL--PKGLISLFLNRNSFSGQIPKSYGQLNSLQHLDISFNTLTGATPSELFSLPNIIYLNLGSNMLSGTLQNSL 325
Cdd:PLN00113  464 FFGGLPDSfgSKRLENLDLSRNQFSGAVPRKLGSLSELMQLKLSENKLSGEIPDELSSCKKLVSLDLSHNQLSGQIPASF 543

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 326 RCGRNLSFVDISNNRLIGALPYSLSNVSENRAVESDGNCLSGTLQHQHAvsYCAEAPDKKKSNrvgifvgvivgilviiv 405
Cdd:PLN00113  544 SEMPVLSQLDLSQNQLSGEIPKNLGNVESLVQVNISHNHLHGSLPSTGA--FLAINASAVAGN----------------- 604

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 406 lfglciVVICKRYYSRGIAEQHLLHKS------VQDSYSAGFSCELIANA------RYVSEAAKLGRED---------LP 464
Cdd:PLN00113  605 ------IDLCGGDTTSGLPPCKRVRKTpswwfyITCTLGAFLVLALVAFGfvfirgRNNLELKRVENEDgtwelqffdSK 678

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 465 SCRSYSLEELMEATNnfdNSTFLGENIYGKLYKGK-LENGIPVVIRCIplsKKY-SIRnfKLRLDLLAKLRHTHLISLLG 542
Cdd:PLN00113  679 VSKSITINDILSSLK---EENVISRGKKGASYKGKsIKNGMQFVVKEI---NDVnSIP--SSEIADMGKLQHPNIVKLIG 750

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 543 HCidgilgeRNDSKVFLIYECVSNGNFQTYLSGDScgkifnWSERLSVLISVAKAIHFLHTGMIPGFFRNRLKTNNILFN 622
Cdd:PLN00113  751 LC-------RSEKGAYLIHEYIEGKNLSEVLRNLS------WERRRKIAIGIAKALRFLHCRCSPAVVVGNLSPEKIIID 817

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 623 ENWMAKLSdygLSIVSEE-TDASGVIGE---SPNSWQMKKL--EDDIYSFGFIILEALVGPS----MFAKREAAVLNAMA 692
Cdd:PLN00113  818 GKDEPHLR---LSLPGLLcTDTKCFISSayvAPETRETKDIteKSDIYGFGLILIELLTGKSpadaEFGVHGSIVEWARY 894

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1379623326 693 SFSS--QDEWkqiVDPVV--QATCCKESLSIVISITNKCISTESWSRPSIEDVLWNLQYASQ 750
Cdd:PLN00113  895 CYSDchLDMW---IDPSIrgDVSVNQNEIVEVMNLALHCTATDPTARPCANDVLKTLESASR 953
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 103-351 3.18e-30

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 128.04  E-value: 3.18e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 103 SFSMDSFVATLAR--LTSLRVLHLVSLGIWGPFPDRIHRLFSLEQLDLSSNYLYGSIPPKISTMVSLQILMLGDNFFNGT 180
Cdd:PLN00113  124 NLSNNNFTGSIPRgsIPNLETLDLSNNMLSGEIPNDIGSFSSLKVLDLGGNVLVGKIPNSLTNLTSLEFLTLASNQLVGQ 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 181 IPNLFDSSSNLTVFSLKNNKLKGPFPFSILSITTLTNIDMSRNQISGSLQDFTG-LSSLEHLDLRENELDSDLP----AL 255
Cdd:PLN00113  204 IPRELGQMKSLKWIYLGYNNLSGEIPYEIGGLTSLNHLDLVYNNLTGPIPSSLGnLKNLQYLFLYQNKLSGPIPpsifSL 283

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 256 PKgLISLFLNRNSFSGQIPKSYGQLNSLQHLDISFNTLTGATPSELFSLPNIIYLNLGSNMLSGTLQNSLRCGRNLSFVD 335
Cdd:PLN00113  284 QK-LISLDLSDNSLSGEIPELVIQLQNLEILHLFSNNFTGKIPVALTSLPRLQVLQLWSNKFSGEIPKNLGKHNNLTVLD 362

                         250
                  ....*....|....*.
gi 1379623326 336 ISNNRLIGALPYSLSN 351
Cdd:PLN00113  363 LSTNNLTGEIPEGLCS 378
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 129-346 5.23e-30

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 127.27  E-value: 5.23e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 129 IWGPFPDRIHRLFSLEQLDLSSNYLYGSIPPKISTMV-SLQILMLGDNFFNGTIPNlfDSSSNLTVFSLKNNKLKGPFPF 207
Cdd:PLN00113   81 ISGKISSAIFRLPYIQTINLSNNQLSGPIPDDIFTTSsSLRYLNLSNNNFTGSIPR--GSIPNLETLDLSNNMLSGEIPN 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 208 SILSITTLTNIDMSRNQISGSLQDF-TGLSSLEHLDLRENELDSDLPA---LPKGLISLFLNRNSFSGQIPKSYGQLNSL 283
Cdd:PLN00113  159 DIGSFSSLKVLDLGGNVLVGKIPNSlTNLTSLEFLTLASNQLVGQIPRelgQMKSLKWIYLGYNNLSGEIPYEIGGLTSL 238

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1379623326 284 QHLDISFNTLTGATPSELFSLPNIIYLNLGSNMLSGTLQNSLRCGRNLSFVDISNNRLIGALP 346
Cdd:PLN00113  239 NHLDLVYNNLTGPIPSSLGNLKNLQYLFLYQNKLSGPIPPSIFSLQKLISLDLSDNSLSGEIP 301
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 117-367 2.27e-27

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 119.18  E-value: 2.27e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 117 TSLRVLHLVSLGIWGPFPDriHRLFSLEQLDLSSNYLYGSIPPKISTMVSLQILMLGDNFFNGTIPNLFDSSSNLTVFSL 196
Cdd:PLN00113  118 SSLRYLNLSNNNFTGSIPR--GSIPNLETLDLSNNMLSGEIPNDIGSFSSLKVLDLGGNVLVGKIPNSLTNLTSLEFLTL 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 197 KNNKLKGPFPFSILSITTLTNIDMSRNQISGSL-QDFTGLSSLEHLDLRENELdsdlpalpkglislflnrnsfSGQIPK 275
Cdd:PLN00113  196 ASNQLVGQIPRELGQMKSLKWIYLGYNNLSGEIpYEIGGLTSLNHLDLVYNNL---------------------TGPIPS 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 276 SYGQLNSLQHLDISFNTLTGATPSELFSLPNIIYLNLGSNMLSGTLQNSLRCGRNLSFVDISNNRLIGALPYSLSNVSEN 355
Cdd:PLN00113  255 SLGNLKNLQYLFLYQNKLSGPIPPSIFSLQKLISLDLSDNSLSGEIPELVIQLQNLEILHLFSNNFTGKIPVALTSLPRL 334

                         250
                  ....*....|..
gi 1379623326 356 RAVESDGNCLSG 367
Cdd:PLN00113  335 QVLQLWSNKFSG 346
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
 487-742 7.12e-26

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: 106.85  E-value: 7.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLeNGIPVVIR--CIPLSKKYSIRNFKLRLDLLAKLRHTHLISLLGHCIDgilgernDSKVFLIYECV 564
Cdd:cd13999     1 IGSGSFGEVYKGKW-RGTDVAIKklKVEDDNDELLKEFRREVSILSKLRHPNIVQFIGACLS-------PPPLCIVTEYM 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 565 SNGNFQTYLSGDScgKIFNWSERLSVLISVAKAIHFLHTGMIPgfFRNrLKTNNILFNENWMAKLSDYGLS--IVSEETD 642
Cdd:cd13999    73 PGGSLYDLLHKKK--IPLSWSLRLKIALDIARGMNYLHSPPII--HRD-LKSLNILLDENFTVKIADFGLSriKNSTTEK 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 643 ASGVIG----ESPNSWQMKK--LEDDIYSFGFIILEalvgpsMFAKRE--AAVLNAMASFSSQDEWKQivdPVVQATCCK 714
Cdd:cd13999   148 MTGVVGtprwMAPEVLRGEPytEKADVYSFGIVLWE------LLTGEVpfKELSPIQIAAAVVQKGLR---PPIPPDCPP 218

                         250       260
                  ....*....|....*....|....*...
gi 1379623326 715 EslsiVISITNKCISTESWSRPSIEDVL 742
Cdd:cd13999   219 E----LSKLIKRCWNEDPEKRPSFSEIV 242
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
 471-746 1.05e-24

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: 104.89  E-value: 1.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 471 LEELMEATNNFDNSTF------LGENIYGKLYKGKLENGIPVVIRCIPLSKKYS---IRNFKLRLDLLAKLRHTHLISLL 541
Cdd:cd14158     1 FHELKNMTNNFDERPIsvggnkLGEGGFGVVFKGYINDKNVAVKKLAAMVDISTedlTKQFEQEIQVMAKCQHENLVELL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 542 GHCIDGilgerndSKVFLIYECVSNGNFQTYLSGDSCGKIFNWSERLSVLISVAKAIHFLHTGmipGFFRNRLKTNNILF 621
Cdd:cd14158    81 GYSCDG-------PQLCLVYTYMPNGSLLDRLACLNDTPPLSWHMRCKIAQGTANGINYLHEN---NHIHRDIKSANILL 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 622 NENWMAKLSDYGLSIVSeETDASGVIGE---------SPNSWQMK-KLEDDIYSFGFIILEALVG-PSMFAKREAAVLNA 690
Cdd:cd14158   151 DETFVPKISDFGLARAS-EKFSQTIMTErivgttaymAPEALRGEiTPKSDIFSFGVVLLEIITGlPPVDENRDPQLLLD 229

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1379623326 691 MASfSSQDEWKQIVD--PVVQATCCKESLSIVISITNKCISTESWSRPSIEDVLWNLQ 746
Cdd:cd14158   230 IKE-EIEDEEKTIEDyvDKKMGDWDSTSIEAMYSVASQCLNDKKNRRPDIAKVQQLLQ 286
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
108-351 1.32e-22

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 101.16  E-value: 1.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 108 SFVATLARLTSLRVLHLVSLGIwGPFPDRIHRLFSLEQLDLSSNYLyGSIPPKISTMVSLQILMLGDNFFNgTIPNLFDS 187
Cdd:COG4886   104 SGNEELSNLTNLESLDLSGNQL-TDLPEELANLTNLKELDLSNNQL-TDLPEPLGNLTNLKSLDLSNNQLT-DLPEELGN 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 188 SSNLTVFSLKNNKLKgPFPFSILSITTLTNIDMSRNQISGSLQDFTGLSSLEHLDLRENELdSDLPALP--KGLISLFLN 265
Cdd:COG4886   181 LTNLKELDLSNNQIT-DLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQL-TDLPELGnlTNLEELDLS 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 266 RNSFSGqIPKSyGQLNSLQHLDISFNTLTGATPSELFSLPNIIYLNLGSNMLSGTLQNSLRCGRNLSFVDISNNRLIGAL 345
Cdd:COG4886   259 NNQLTD-LPPL-ANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVT 336


                  ....*.
gi 1379623326 346 PYSLSN 351
Cdd:COG4886   337 LTTLAL 342
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
 487-672 3.93e-22

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: 95.42  E-value: 3.93e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGK-LENGIPVVIRCIPLSKKYSIRNFKLR-LDLLAKLRHTHLISLLGHCIDgilgernDSKVFLIYECV 564
Cdd:cd00180     1 LGKGSFGKVYKARdKETGKKVAVKVIPKEKLKKLLEELLReIEILKKLNHPNIVKLYDVFET-------ENFLYLVMEYC 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 565 SNGNFQTYLsgDSCGKIFNWSERLSVLISVAKAIHFLHT-GMIpgfFRNrLKTNNILFNENWMAKLSDYGLSIVSEETDA 643
Cdd:cd00180    74 EGGSLKDLL--KENKGPLSEEEALSILRQLLSALEYLHSnGII---HRD-LKPENILLDSDGTVKLADFGLAKDLDSDDS 147

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1379623326 644 SGVIGESPNSWQMKKLE----------DDIYSFGFIILE 672
Cdd:cd00180   148 LLKTTGGTTPPYYAPPEllggryygpkVDIWSLGVILYE 186
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
 487-742 5.39e-22

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: 96.41  E-value: 5.39e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLENGIPVVI-RCIPLSKKYSIRNFKLRLDLLAKLRHTHLISLLGHCIdgilgerNDSKVFLIYECVS 565
Cdd:cd14664     1 IGRGGAGTVYKGVMPNGTLVAVkRLKGEGTQGGDHGFQAEIQTLGMIRHRNIVRLRGYCS-------NPTTNLLVYEYMP 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 566 NGNFQTYLSGDSCGKI-FNWSERLSVLISVAKAIHFLHTGMIPGFFRNRLKTNNILFNENWMAKLSDYGLSIVSEETDA- 643
Cdd:cd14664    74 NGSLGELLHSRPESQPpLDWETRQRIALGSARGLAYLHHDCSPLIIHRDVKSNNILLDEEFEAHVADFGLAKLMDDKDSh 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 644 -----SGVIGE-SPNSWQMKKLED--DIYSFGFIILEALVGP----SMFAKREAAVLNAMASFSSQDEWKQIVDPVVQAT 711
Cdd:cd14664   154 vmssvAGSYGYiAPEYAYTGKVSEksDVYSYGVVLLELITGKrpfdEAFLDDGVDIVDWVRGLLEEKKVEALVDPDLQGV 233

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1379623326 712 CCKESLSIVISITNKCISTESWSRPSIEDVL 742
Cdd:cd14664   234 YKLEEVEQVFQVALLCTQSSPMERPTMREVV 264
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
 487-746 6.97e-17

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: 81.80  E-value: 6.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLENGIPVVIRCIPLSK-KYSI--RNFKLRLDLLAKLRHTHLISLLGHCIDGilgerndSKVFLIYEC 563
Cdd:cd14159     1 IGEGGFGCVYQAVMRNTEYAVKRLKEDSElDWSVvkNSFLTEVEKLSRFRHPNIVDLAGYSAQQ-------GNYCLIYVY 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 564 VSNGNFQTYLSGDSCGKIFNWSERLSVLISVAKAIHFLHTGMiPGFFRNRLKTNNILFNENWMAKLSDYGL--------- 634
Cdd:cd14159    74 LPNGSLEDRLHCQVSCPCLSWSQRLHVLLGTARAIQYLHSDS-PSLIHGDVKSSNILLDAALNPKLGDFGLarfsrrpkq 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 635 ----SIVSEETDASGVIGESPNSW-QMKKL--EDDIYSFGFIILEALVG----------PSMFAK-----REAAVLNAMA 692
Cdd:cd14159   153 pgmsSTLARTQTVRGTLAYLPEEYvKTGTLsvEIDVYSFGVVLLELLTGrramevdscsPTKYLKdlvkeEEEAQHTPTT 232

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1379623326 693 SFSSQDEW---------KQIVDPvvQATCCKESLSIVIS-ITNKCISTESWSRPSIEDVLWNLQ 746
Cdd:cd14159   233 MTHSAEAQaaqlatsicQKHLDP--QAGPCPPELGIEISqLACRCLHRRAKKRPPMTEVFQELE 294
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 187-369 8.38e-17

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 84.90  E-value: 8.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 187 SSSNLTVFSLKNNKLKGPFPFSILSITTLTNIDMSRNQISGSLQD--FTGLSSLEHLDLRENELDSDLP--ALPkGLISL 262
Cdd:PLN00113   67 NSSRVVSIDLSGKNISGKISSAIFRLPYIQTINLSNNQLSGPIPDdiFTTSSSLRYLNLSNNNFTGSIPrgSIP-NLETL 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 263 FLNRNSFSGQIPKSYGQLNSLQHLDISFNTLTGATPSELFSLPNIIYLNLGSNMLSGTLQNSLRCGRNLSFVDISNNRLI 342
Cdd:PLN00113  146 DLSNNMLSGEIPNDIGSFSSLKVLDLGGNVLVGKIPNSLTNLTSLEFLTLASNQLVGQIPRELGQMKSLKWIYLGYNNLS 225

                         170       180
                  ....*....|....*....|....*..
gi 1379623326 343 GALPYSLSNVSENRAVESDGNCLSGTL 369
Cdd:PLN00113  226 GEIPYEIGGLTSLNHLDLVYNNLTGPI 252
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
 486-742 5.70e-15

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 75.26  E-value: 5.70e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326  486 FLGENIYGKLYKGK-LENGIPVVIRCIPLSKKYSIRNFKLR-LDLLAKLRHTHLISLLGHCIDgilgernDSKVFLIYEC 563
Cdd:smart00220   6 KLGEGSFGKVYLARdKKTGKLVAIKVIKKKKIKKDRERILReIKILKKLKHPNIVRLYDVFED-------EDKLYLVMEY 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326  564 VSNGNFQTYLSGDscgKIFNWSERLSVLISVAKAIHFLHT-GMIpgffrNR-LKTNNILFNENWMAKLSDYGLS-IVSEE 640
Cdd:smart00220  79 CEGGDLFDLLKKR---GRLSEDEARFYLRQILSALEYLHSkGIV-----HRdLKPENILLDEDGHVKLADFGLArQLDPG 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326  641 TDASGVIGeSPN-------SWQMKKLEDDIYSFGFIILEALVGpsmfakreaavlnaMASFSSQDEWKQIVDPVVQATCC 713
Cdd:smart00220 151 EKLTTFVG-TPEymapevlLGKGYGKAVDIWSLGVILYELLTG--------------KPPFPGDDQLLELFKKIGKPKPP 215

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1379623326  714 KESLSIVIS-----ITNKCISTESWSRPSIEDVL 742
Cdd:smart00220 216 FPPPEWDISpeakdLIRKLLVKDPEKRLTAEEAL 249
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
 487-746 1.24e-14

Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK3 (or IRAK-M) is the only IRAK that does not show kinase activity. It is found only in monocytes and macrophages in humans, and functions as a negative regulator of TLR signaling including TLR-2 induced p38 activation. It also negatively regulates the alternative NFkB pathway in a TLR-2 specific manner. IRAK3 is downregulated in the monocytes of obese people, and is associated with high SOD2, a marker of mitochondrial oxidative stress. It is an important inhibitor of inflammation in association with obesity and metabolic syndrome. The IRAK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271062 [Multi-domain]  Cd Length: 276  Bit Score: 74.92  E-value: 1.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLENgIPVVIRCIPLSKKYSIR----NFKLRLDLLAKLRHTHLISLLGHCIDgilgernDSKVFLIYE 562
Cdd:cd14160     1 IGEGEIFEVYRVRIGN-RSYAVKLFKQEKKMQWKkhwkRFLSELEVLLLFQHPNILELAAYFTE-------TEKFCLVYP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 563 CVSNGNFQTYLSGDSCGKIFNWSERLSVLISVAKAIHFLHTGMIPGFFRNRLKTNNILFNENWMAKLSDYGLS-IVSEET 641
Cdd:cd14160    73 YMQNGTLFDRLQCHGVTKPLSWHERINILIGIAKAIHYLHNSQPCTVICGNISSANILLDDQMQPKLTDFALAhFRPHLE 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 642 DASGVI----GESPNSWQMKK---------LEDDIYSFGFIILEALVG-------PSMFAKREaaVLNAMASFSSQDEWK 701
Cdd:cd14160   153 DQSCTInmttALHKHLWYMPEeyirqgklsVKTDVYSFGIVIMEVLTGckvvlddPKHLQLRD--LLHELMEKRGLDSCL 230

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1379623326 702 QIVDPVVQAtcCKESLSI-VISITNKCISTESWSRPSIEDVLWNLQ 746
Cdd:cd14160   231 SFLDLKFPP--CPRNFSAkLFRLAGRCTATKAKLRPDMDEVLQRLE 274
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
105-341 1.72e-14

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 76.13  E-value: 1.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 105 SMDSFVATLARLTSLRVLHLVSLGIWGPFPDRIHRLFSLEQLDLSSNYLYGSIPPKISTMVSLQILMLGDNFFNGtiPNL 184
Cdd:COG4886    14 LLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLG--LTD 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 185 FDSSSNLTVFSLKNNKlkgpfpfSILSITTLTNIDMSRNQISGSLQDFTGLSSLEHLDLREN---ELDSDLPALPKgLIS 261
Cdd:COG4886    92 LGDLTNLTELDLSGNE-------ELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNqltDLPEPLGNLTN-LKS 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 262 LFLNRNSFSGqIPKSYGQLNSLQHLDISFNTLTgATPSELFSLPNIIYLNLGSNMLSgTLQNSLRCGRNLSFVDISNNRL 341
Cdd:COG4886   164 LDLSNNQLTD-LPEELGNLTNLKELDLSNNQIT-DLPEPLGNLTNLEELDLSGNQLT-DLPEPLANLTNLETLDLSNNQL 240
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
 487-742 2.31e-14

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: 73.64  E-value: 2.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGK-LENGIPVVIRCIPLSKKYSIRNFKL--RLDLLAKLRHTHLISLLGHCIDGIlgerndsKVFLIYEC 563
Cdd:cd13978     1 LGSGGFGTVSKARhVSWFGMVAIKCLHSSPNCIEERKALlkEAEKMERARHSYVLPLLGVCVERR-------SLGLVMEY 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 564 VSNGNFQTYLsgDSCGKIFNWSERLSVLISVAKAIHFLHtGMIPGFFRNRLKTNNILFNENWMAKLSDYGLSIV------ 637
Cdd:cd13978    74 MENGSLKSLL--EREIQDVPWSLRFRIIHEIALGMNFLH-NMDPPLLHHDLKPENILLDNHFHVKISDFGLSKLgmksis 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 638 -SEETDASGVIG-------ESPNSWQMKKLE-DDIYSFGFIILEALVGPSMFA-KREAAVLnaMASFSSQDewkQIVDPV 707
Cdd:cd13978   151 aNRRRGTENLGGtpiymapEAFDDFNKKPTSkSDVYSFAIVIWAVLTRKEPFEnAINPLLI--MQIVSKGD---RPSLDD 225

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1379623326 708 VQATCCKESLSIVISITNKCISTESWSRPSIEDVL 742
Cdd:cd13978   226 IGRLKQIENVQELISLMIRCWDGNPDARPTFLECL 260
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
 487-672 4.27e-13

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: 70.16  E-value: 4.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLENGIPVVIRCIPLSKKYSIRNFKLRLDLLAKLRHTHLISLLGHCIDGilgerndSKVFLIYECVSN 566
Cdd:cd05148    14 LGSGYFGEVWEGLWKNRVRVAIKILKSDDLLKQQDFQKEVQALKRLRHKHLISLFAVCSVG-------EPVYIITELMEK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 567 GNFQTYLsGDSCGKIFNWSERLSVLISVAKAIHFLHTGMIpgfFRNRLKTNNILFNENWMAKLSDYGLSIVSEETDASGV 646
Cdd:cd05148    87 GSLLAFL-RSPEGQVLPVASLIDMACQVAEGMAYLEEQNS---IHRDLAARNILVGEDLVCKVADFGLARLIKEDVYLSS 162

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1379623326 647 IGESPNSW--------QMKKLEDDIYSFGFIILE 672
Cdd:cd05148   163 DKKIPYKWtapeaashGTFSTKSDVWSFGILLYE 196
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
 487-667 1.25e-12

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: 68.72  E-value: 1.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLENGI----PVVIRCIPLSKKYS-IRNFKLRLDLLAKLRHTHLISLLGHCIDgilgernDSKVFLIY 561
Cdd:cd00192     3 LGEGAFGEVYKGKLKGGDgktvDVAVKTLKEDASESeRKDFLKEARVMKKLGHPNVVRLLGVCTE-------EEPLYLVM 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 562 ECVSNGNFQTYL------SGDSCGKIFNWSERLSVLISVAKAIHFLHtgmipgffRNR-----LKTNNILFNENWMAKLS 630
Cdd:cd00192    76 EYMEGGDLLDFLrksrpvFPSPEPSTLSLKDLLSFAIQIAKGMEYLA--------SKKfvhrdLAARNCLVGEDLVVKIS 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1379623326 631 DYGLS--IVSEETDASGVIGESPNSWqMKK--LED-------DIYSFG 667
Cdd:cd00192   148 DFGLSrdIYDDDYYRKKTGGKLPIRW-MAPesLKDgiftsksDVWSFG 194
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
 484-674 1.38e-12

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: 68.57  E-value: 1.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 484 STFLGENIYGKlyKGKLENGIPVVIRCIPLsKKYSIRNFKLRLDLLAKLRHTHLISLLGHCIdgilgerNDSKVFLIYEC 563
Cdd:cd13992     8 SSHTGEPKYVK--KVGVYGGRTVAIKHITF-SRTEKRTILQELNQLKELVHDNLNKFIGICI-------NPPNIAVVTEY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 564 VSNGNFQTYLSGDSCGkiFNWSERLSVLISVAKAIHFLHTGmiPGFFRNRLKTNNILFNENWMAKLSDYGL-SIVSEETD 642
Cdd:cd13992    78 CTRGSLQDVLLNREIK--MDWMFKSSFIKDIVKGMNYLHSS--SIGYHGRLKSSNCLVDSRWVVKLTDFGLrNLLEEQTN 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1379623326 643 ---------------ASGVIGESPNSWQMkKLEDDIYSFGFIILEAL 674
Cdd:cd13992   154 hqldedaqhkkllwtAPELLRGSLLEVRG-TQKGDVYSFAIILYEIL 199
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
 486-674 3.03e-12

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: 68.02  E-value: 3.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 486 FLGENIYGKLYKGKLEN-GIPVVIRC--IPLSKKYSIRNFKLR-LDLLAKLRHTHLISLLGHCidgilgerNDSKVF-LI 560
Cdd:cd14026     4 YLSRGAFGTVSRARHADwRVTVAIKClkLDSPVGDSERNCLLKeAEILHKARFSYILPILGIC--------NEPEFLgIV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 561 YECVSNGNFQTYLSGDSCGKIFNWSERLSVLISVAKAIHFLHTgMIPGFFRNRLKTNNILFNENWMAKLSDYGL------ 634
Cdd:cd14026    76 TEYMTNGSLNELLHEKDIYPDVAWPLRLRILYEIALGVNYLHN-MSPPLLHHDLKTQNILLDGEFHVKIADFGLskwrql 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1379623326 635 SIVSEETDASGVIGES----------PNSWQMKKLEDDIYSFGFIILEAL 674
Cdd:cd14026   155 SISQSRSSKSAPEGGTiiymppeeyePSQKRRASVKHDIYSYAIIMWEVL 204
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
 487-642 6.00e-12

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: 66.42  E-value: 6.00e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326  487 LGENIYGKLYKGKL-----ENGIPVVIRCIPLSKKYS-IRNFKLRLDLLAKLRHTHLISLLGHCIDgilgernDSKVFLI 560
Cdd:smart00221   7 LGEGAFGEVYKGTLkgkgdGKEVEVAVKTLKEDASEQqIEEFLREARIMRKLDHPNIVKLLGVCTE-------EEPLMIV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326  561 YECVSNGNFQTYLSgDSCGKIFNWSERLSVLISVAKAIHFLHT-GMIpgffrNR-LKTNNILFNENWMAKLSDYGLSIVS 638
Cdd:smart00221  80 MEYMPGGDLLDYLR-KNRPKELSLSDLLSFALQIARGMEYLESkNFI-----HRdLAARNCLVGENLVVKISDFGLSRDL 153


                   ....
gi 1379623326  639 EETD 642
Cdd:smart00221 154 YDDD 157
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
 487-667 1.41e-11

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: 65.60  E-value: 1.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKL-----ENGIPVVIRCI-PLSKKYSIRNFKLRLDLLAKLRHTHLISLLGHCIDGilgerndSKVFLI 560
Cdd:pfam07714   7 LGEGAFGEVYKGTLkgegeNTKIKVAVKTLkEGADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQG-------EPLYIV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 561 YECVSNGNFQTYLSgdSCGKIFNWSERLSVLISVAKAIHFLHT-GMIpgfFRNrLKTNNILFNENWMAKLSDYGLSIVSE 639
Cdd:pfam07714  80 TEYMPGGDLLDFLR--KHKRKLTLKDLLSMALQIAKGMEYLESkNFV---HRD-LAARNCLVSENLVVKISDFGLSRDIY 153

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1379623326 640 ETDASGVIGE--------SPNSWQMKKL--EDDIYSFG 667
Cdd:pfam07714 154 DDDYYRKRGGgklpikwmAPESLKDGKFtsKSDVWSFG 191
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
 487-667 1.49e-11

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 65.24  E-value: 1.49e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326  487 LGENIYGKLYKGKLE-----NGIPVVIRCIPLSKKYS-IRNFKLRLDLLAKLRHTHLISLLGHCIDgilgernDSKVFLI 560
Cdd:smart00219   7 LGEGAFGEVYKGKLKgkggkKKVEVAVKTLKEDASEQqIEEFLREARIMRKLDHPNVVKLLGVCTE-------EEPLYIV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326  561 YECVSNGNFQTYLSgdSCGKIFNWSERLSVLISVAKAIHFLHT-GMIpgffrNR-LKTNNILFNENWMAKLSDYGLSIVS 638
Cdd:smart00219  80 MEYMEGGDLLSYLR--KNRPKLSLSDLLSFALQIARGMEYLESkNFI-----HRdLAARNCLVGENLVVKISDFGLSRDL 152

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1379623326  639 EETDASGVIGE-------SPNSWQMKKL--EDDIYSFG 667
Cdd:smart00219 153 YDDDYYRKRGGklpirwmAPESLKEGKFtsKSDVWSFG 190
PLN03150 PLN03150
hypothetical protein; Provisional
 122-209 2.08e-11

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 67.15  E-value: 2.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 122 LHLVSLGIWGPFPDRIHRLFSLEQLDLSSNYLYGSIPPKISTMVSLQILMLGDNFFNGTIPNLFDSSSNLTVFSLKNNKL 201
Cdd:PLN03150  423 LGLDNQGLRGFIPNDISKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNGNSL 502


                  ....*...
gi 1379623326 202 KGPFPFSI 209
Cdd:PLN03150  503 SGRVPAAL 510
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
 487-746 2.85e-11

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: 64.99  E-value: 2.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLENGIP------VVIRCIPLSKKYSIRNFKLRLDLLAKLRHTHLISLLGHCIDGilgerndSKVFLI 560
Cdd:cd05092    13 LGEGAFGKVFLAECHNLLPeqdkmlVAVKALKEATESARQDFQREAELLTVLQHQHIVRFYGVCTEG-------EPLIMV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 561 YECVSNGNFQTYL-------------SGDSCGKIfNWSERLSVLISVAK------AIHFLHtgmipgffrNRLKTNNILF 621
Cdd:cd05092    86 FEYMRHGDLNRFLrshgpdakildggEGQAPGQL-TLGQMLQIASQIASgmvylaSLHFVH---------RDLATRNCLV 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 622 NENWMAKLSDYGLSIVSEETDASGVIGES--------PNSWQMKKL--EDDIYSFGFIILEALVgpsmFAKREAAVLNAM 691
Cdd:cd05092   156 GQGLVVKIGDFGMSRDIYSTDYYRVGGRTmlpirwmpPESILYRKFttESDIWSFGVVLWEIFT----YGKQPWYQLSNT 231

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1379623326 692 ASFSSQDEWKQIVDPvvqATCCKEslsiVISITNKCISTESWSRPSIEDVLWNLQ 746
Cdd:cd05092   232 EAIECITQGRELERP---RTCPPE----VYAIMQGCWQREPQQRHSIKDIHSRLQ 279
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
 482-667 3.12e-11

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: 64.71  E-value: 3.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 482 DNSTFLGENIYGKLYKGKLEnGIPVVIRCIPLSKKYSIRNFKLRLDL-LAKLRHTHLISLLGhcidGILGERNDSKVFLI 560
Cdd:cd13979     6 RLQEPLGSGGFGSVYKATYK-GETVAVKIVRRRRKNRASRQSFWAELnAARLRHENIVRVLA----AETGTDFASLGLII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 561 YECVSNGNFQTYLSGDScgKIFNWSERLSVLISVAKAIHFLHTGmipGFFRNRLKTNNILFNENWMAKLSDYGLSIVSEE 640
Cdd:cd13979    81 MEYCGNGTLQQLIYEGS--EPLPLAHRILISLDIARALRFCHSH---GIVHLDVKPANILISEQGVCKLCDFGCSVKLGE 155

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1379623326 641 TDASG----VIGESPN--SWQMKKLED-----DIYSFG 667
Cdd:cd13979   156 GNEVGtprsHIGGTYTyrAPELLKGERvtpkaDIYSFG 193
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
 487-672 4.86e-11

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: 64.32  E-value: 4.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKL------ENGIPVVIRCIPLSKKYSIRN-FKLRLDLLAKLRHTHLISLLGHCIdgilgerNDSKVFL 559
Cdd:cd05048    13 LGEGAFGKVYKGELlgpsseESAISVAIKTLKENASPKTQQdFRREAELMSDLQHPNIVCLLGVCT-------KEQPQCM 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 560 IYECVSNGNFQTYL-------------SGDSCGKIFNWSERLSVLISVAKAIHFLHTgmipGFFRNR-LKTNNILFNENW 625
Cdd:cd05048    86 LFEYMAHGDLHEFLvrhsphsdvgvssDDDGTASSLDQSDFLHIAIQIAAGMEYLSS----HHYVHRdLAARNCLVGDGL 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1379623326 626 MAKLSDYGLSIVSEETDASGVIGES--PNSWQMKK--------LEDDIYSFGFIILE 672
Cdd:cd05048   162 TVKISDFGLSRDIYSSDYYRVQSKSllPVRWMPPEailygkftTESDVWSFGVVLWE 218
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
 487-692 9.49e-11

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


Pssm-ID: 270966 [Multi-domain]  Cd Length: 254  Bit Score: 62.93  E-value: 9.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLENGIPVV--IRCIPLSKKYSIRNFKLRLDLLAKLRHTHLISLLGHCIDgilgerNDSKVFLIYECV 564
Cdd:cd14064     1 IGSGSFGKVYKGRCRNKIVAIkrYRANTYCSKSDVDMFCREVSILCRLNHPCVIQFVGACLD------DPSQFAIVTQYV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 565 SNGNFQTYLSGDScgKIFNWSERLSVLISVAKAIHFLHTGMIPGFFRNrLKTNNILFNENWMAKLSDYGLSIVSEETDAS 644
Cdd:cd14064    75 SGGSLFSLLHEQK--RVIDLQSKLIIAVDVAKGMEYLHNLTQPIIHRD-LNSHNILLYEDGHAVVADFGESRFLQSLDED 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1379623326 645 GVIGESPNSWQMK----------KLEDDIYSFGFIILEALVGPSMFAK-REAAVLNAMA 692
Cdd:cd14064   152 NMTKQPGNLRWMApevftqctrySIKADVFSYALCLWELLTGEIPFAHlKPAAAAADMA 210
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
487-676 2.09e-10

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 63.88  E-value: 2.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGK-LENGIPVVIRCIPLSKKYS---IRNFKLRLDLLAKLRHTHLISLLGHcidgilGERNDSkVFLIYE 562
Cdd:COG0515    15 LGRGGMGVVYLARdLRLGRPVALKVLRPELAADpeaRERFRREARALARLNHPNIVRVYDV------GEEDGR-PYLVME 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 563 CVSNGNFQTYLSGdscGKIFNWSERLSVLISVAKAIHFLHT-GMIpgfFRNrLKTNNILFNENWMAKLSDYGLSIV---S 638
Cdd:COG0515    88 YVEGESLADLLRR---RGPLPPAEALRILAQLAEALAAAHAaGIV---HRD-IKPANILLTPDGRVKLIDFGIARAlggA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1379623326 639 EETDASGVIGE----SPNSWQMKKLE--DDIYSFGFIILEALVG 676
Cdd:COG0515   161 TLTQTGTVVGTpgymAPEQARGEPVDprSDVYSLGVTLYELLTG 204
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 211-372 4.21e-10

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 63.33  E-value: 4.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 211 SITTLTNIDMSRNQISGSLQDFT-GLSSLEHLDLRENELdsdlpalpkglislflnrnsfSGQIPKS-YGQLNSLQHLDI 288
Cdd:PLN00113   67 NSSRVVSIDLSGKNISGKISSAIfRLPYIQTINLSNNQL---------------------SGPIPDDiFTTSSSLRYLNL 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 289 SFNTLTGATPSElfSLPNIIYLNLGSNMLSGTLQNSLRCGRNLSFVDISNNRLIGALPYSLSNVSENRAVESDGNCLSGT 368
Cdd:PLN00113  126 SNNNFTGSIPRG--SIPNLETLDLSNNMLSGEIPNDIGSFSSLKVLDLGGNVLVGKIPNSLTNLTSLEFLTLASNQLVGQ 203


                  ....
gi 1379623326 369 LQHQ 372
Cdd:PLN00113  204 IPRE 207
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
 487-672 1.12e-09

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: 60.17  E-value: 1.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLENGIP------VVIRCIPLSKKYSIR-NFKLRLDLLAKLRHTHLISLLGHCIDGilgerndSKVFL 559
Cdd:cd05049    13 LGEGAFGKVFLGECYNLEPeqdkmlVAVKTLKDASSPDARkDFEREAELLTNLQHENIVKFYGVCTEG-------DPLLM 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 560 IYECVSNGNFQTYL-----------SGDSCGKIFNWSERLSVLISVAKAI------HFLHtgmipgffRNrLKTNNILFN 622
Cdd:cd05049    86 VFEYMEHGDLNKFLrshgpdaaflaSEDSAPGELTLSQLLHIAVQIASGMvylasqHFVH--------RD-LATRNCLVG 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 623 ENWMAKLSDYGLSIVSEETDASGVIGE--------SPNSWQMKKL--EDDIYSFGFIILE 672
Cdd:cd05049   157 TNLVVKIGDFGMSRDIYSTDYYRVGGHtmlpirwmPPESILYRKFttESDVWSFGVVLWE 216
PLN03150 PLN03150
hypothetical protein; Provisional
 184-305 2.66e-09

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 60.60  E-value: 2.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 184 LFDSSSNLTVFS---LKNNKLKGPFPFSILSITTLTNIDMSRNQISGSLQDFTG-LSSLEHLDLreneldsdlpalpkgl 259
Cdd:PLN03150  410 QFDSTKGKWFIDglgLDNQGLRGFIPNDISKLRHLQSINLSGNSIRGNIPPSLGsITSLEVLDL---------------- 473

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1379623326 260 islflNRNSFSGQIPKSYGQLNSLQHLDISFNTLTGATPSELFSLP 305
Cdd:PLN03150  474 -----SYNSFNGSIPESLGQLTSLRILNLNGNSLSGRVPAALGGRL 514
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
 487-676 3.37e-09

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: 58.37  E-value: 3.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGK-LENGIPVVI---RCIPLSKKYSIRNFKLRLDLLAKLRHTHLISLLGHCIDGILgerndskVFLIYE 562
Cdd:cd14014     8 LGRGGMGEVYRARdTLLGRPVAIkvlRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGR-------PYIVME 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 563 CVSNGNFQTYLSGdscGKIFNWSERLSVLISVAKAIHFLHT-GMIpgffrNR-LKTNNILFNENWMAKLSDYGLSIV--- 637
Cdd:cd14014    81 YVEGGSLADLLRE---RGPLPPREALRILAQIADALAAAHRaGIV-----HRdIKPANILLTEDGRVKLTDFGIARAlgd 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1379623326 638 SEETDASGVIGE----SPNSWQMKKL--EDDIYSFGFIILEALVG 676
Cdd:cd14014   153 SGLTQTGSVLGTpaymAPEQARGGPVdpRSDIYSLGVVLYELLTG 197
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
 486-737 4.57e-09

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: 58.04  E-value: 4.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 486 FLGENIYGKLYKGKLEnGIPVVIRCipLSKKYSIRNFKLRLDLLAKLRHTHLISLLGHCIdgilgerndSKVFLIYECVS 565
Cdd:cd14068     1 LLGDGGFGSVYRAVYR-GEDVAVKI--FNKHTSFRLLRQELVVLSHLHHPSLVALLAAGT---------APRMLVMELAP 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 566 NGNFQTYLSGDSCGKIFNWSERLSvlISVAKAIHFLHTGMIpgFFRNrLKTNNILF-----NENWMAKLSDYGLS----- 635
Cdd:cd14068    69 KGSLDALLQQDNASLTRTLQHRIA--LHVADGLRYLHSAMI--IYRD-LKPHNVLLftlypNCAIIAKIADYGIAqyccr 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 636 --IVSEETDASGVIGESPNSWQMKKLEDDIYSFGFIILEALVGpsmfAKREAAVLNAMASFSSQDEWKQIVDPVVQATCC 713
Cdd:cd14068   144 mgIKTSEGTPGFRAPEVARGNVIYNQQADVYSFGLLLYDILTC----GERIVEGLKFPNEFDELAIQGKLPDPVKEYGCA 219

                         250       260
                  ....*....|....*....|....
gi 1379623326 714 keSLSIVISITNKCISTESWSRPS 737
Cdd:cd14068   220 --PWPGVEALIKDCLKENPQCRPT 241
PLN03150 PLN03150
hypothetical protein; Provisional
 248-325 4.57e-09

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 59.83  E-value: 4.57e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1379623326 248 LDSDLPALPKgLISLFLNRNSFSGQIPKSYGQLNSLQHLDISFNTLTGATPSELFSLPNIIYLNLGSNMLSGTLQNSL 325
Cdd:PLN03150  434 IPNDISKLRH-LQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNGNSLSGRVPAAL 510
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
 487-639 8.44e-09

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: 57.14  E-value: 8.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGK-LENGIPVVIRCIPLSKKYSIRNFKLR--LDLLAKLRHTHLISLLGHCidgilgeRNDSKVFLIYEC 563
Cdd:cd14003     8 LGEGSFGKVKLARhKLTGEKVAIKIIDKSKLKEEIEEKIKreIEIMKLLNHPNIIKLYEVI-------ETENKIYLVMEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 564 VSNGNFQTY------LSGDSCGKIFnwserlSVLISvakAIHFLHTGMIpgFFRNrLKTNNILFNENWMAKLSDYGLSIV 637
Cdd:cd14003    81 ASGGELFDYivnngrLSEDEARRFF------QQLIS---AVDYCHSNGI--VHRD-LKLENILLDKNGNLKIIDFGLSNE 148


                  ..
gi 1379623326 638 SE 639
Cdd:cd14003   149 FR 150
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
 487-672 9.72e-09

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: 57.37  E-value: 9.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLENgIPVVIRCIPLSKKysiRNFKLRLDL--LAKLRHTHLISLLGhcIDGILGERNDSKVFLIYECV 564
Cdd:cd14054     3 IGQGRYGTVWKGSLDE-RPVAVKVFPARHR---QNFQNEKDIyeLPLMEHSNILRFIG--ADERPTADGRMEYLLVLEYA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 565 SNGNFQTYLSGDScgkiFNWSERLSVLISVAKAIHFLHTGMI------PGFFRNRLKTNNILFNENWMAKLSDYGLSIVS 638
Cdd:cd14054    77 PKGSLCSYLRENT----LDWMSSCRMALSLTRGLAYLHTDLRrgdqykPAIAHRDLNSRNVLVKADGSCVICDFGLAMVL 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1379623326 639 eeTDASGVIGESP---------------------------NSWQMKKLEDDIYSFGFIILE 672
Cdd:cd14054   153 --RGSSLVRGRPGaaenasisevgtlrymapevlegavnlRDCESALKQVDVYALGLVLWE 211
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
 487-676 1.03e-08

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: 56.85  E-value: 1.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENI----YGKLYKG-KLENGIPVVIRCIPLSK--KYSIRNFKLRLDLLAKLRHTHLISLLGHcidgilgERNDSKVFL 559
Cdd:cd06627     4 LGDLIgrgaFGSVYKGlNLNTGEFVAIKQISLEKipKSDLKSVMGEIDLLKKLNHPNIVKYIGS-------VKTKDSLYI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 560 IYECVSNGNFQTYLsgdscgKIF-NWSERL-SVLIS-VAKAIHFLHT-GMIpgffrNR-LKTNNILFNENWMAKLSDYGL 634
Cdd:cd06627    77 ILEYVENGSLASII------KKFgKFPESLvAVYIYqVLEGLAYLHEqGVI-----HRdIKGANILTTKDGLVKLADFGV 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1379623326 635 SIV--SEETDASGVIGeSPNsW------QMKKL--EDDIYSFGFIILEALVG 676
Cdd:cd06627   146 ATKlnEVEKDENSVVG-TPY-WmapeviEMSGVttASDIWSVGCTVIELLTG 195
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
 487-672 1.13e-08

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: 56.97  E-value: 1.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLENGIPVVIRCIPLSKKYSI----RNFKLRLDLLAKL-RHTHLISLLGHCidgilgeRNDSKVFLIY 561
Cdd:cd05047     3 IGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASkddhRDFAGELEVLCKLgHHPNIINLLGAC-------EHRGYLYLAI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 562 ECVSNGNFQTYLS-------------GDSCGKIFNWSERLSVLISVAKAIHFLHTGMipgFFRNRLKTNNILFNENWMAK 628
Cdd:cd05047    76 EYAPHGNLLDFLRksrvletdpafaiANSTASTLSSQQLLHFAADVARGMDYLSQKQ---FIHRDLAARNILVGENYVAK 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1379623326 629 LSDYGLSiVSEETDASGVIGESPNSW--------QMKKLEDDIYSFGFIILE 672
Cdd:cd05047   153 IADFGLS-RGQEVYVKKTMGRLPVRWmaieslnySVYTTNSDVWSYGVLLWE 203
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
 487-746 1.25e-08

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: 56.65  E-value: 1.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLENGIPVVIRCIPLSKkYSIRNFKLRLDLLAKLRHTHLISLLGHCIDgilgernDSKVFLIYECVSN 566
Cdd:cd05068    16 LGSGQFGEVWEGLWNNTTPVAVKTLKPGT-MDPEDFLREAQIMKKLRHPKLIQLYAVCTL-------EEPIYIITELMKH 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 567 GNFQTYLSGDscGKIFNWSERLSVLISVAKAIHFLHTgmiPGFFRNRLKTNNILFNENWMAKLSDYGLS--IVSEETDAS 644
Cdd:cd05068    88 GSLLEYLQGK--GRSLQLPQLIDMAAQVASGMAYLES---QNYIHRDLAARNVLVGENNICKVADFGLArvIKVEDEYEA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 645 GVIGESPNSW------QMKK--LEDDIYSFGfIILEALVG------PSMfakREAAVLnamasfssqdewkQIVDPVVQA 710
Cdd:cd05068   163 REGAKFPIKWtapeaaNYNRfsIKSDVWSFG-ILLTEIVTygripyPGM---TNAEVL-------------QQVERGYRM 225

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1379623326 711 TC---CKESLsivISITNKCISTESWSRPSIEDVLWNLQ 746
Cdd:cd05068   226 PCppnCPPQL---YDIMLECWKADPMERPTFETLQWKLE 261
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
 495-672 1.25e-08

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


Pssm-ID: 270944 [Multi-domain]  Cd Length: 279  Bit Score: 56.83  E-value: 1.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 495 LYKGKLengipVVIRCIPLSKKYSIRNFKLRLDLLAKLRHTHLISLLGHCIDgilgernDSKVFLIYECVSNGNFQTYLS 574
Cdd:cd14042    27 YYKGNL-----VAIKKVNKKRIDLTREVLKELKHMRDLQHDNLTRFIGACVD-------PPNICILTEYCPKGSLQDILE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 575 GDScgkI-FNWSERLSVLISVAKAIHFLHTGMIPgfFRNRLKTNNILFNENWMAKLSDYGLSIVSEETDASgvIGESpNS 653
Cdd:cd14042    95 NED---IkLDWMFRYSLIHDIVKGMHYLHDSEIK--SHGNLKSSNCVVDSRFVLKITDFGLHSFRSGQEPP--DDSH-AY 166

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1379623326 654 WQmKKL------------------EDDIYSFGFIILE 672
Cdd:cd14042   167 YA-KLLwtapellrdpnppppgtqKGDVYSFGIILQE 202
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 166-339 1.46e-08

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 55.95  E-value: 1.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 166 SLQILMLGDNFFNgTIPNLfDSSSNLTVFSLKNNKLKgpfpfSILSITTLTN---IDMSRNQISgSLQDFTGLSSLEHLD 242
Cdd:cd21340    25 NLKVLYLYDNKIT-KIENL-EFLTNLTHLYLQNNQIE-----KIENLENLVNlkkLYLGGNRIS-VVEGLENLTNLEELH 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 243 LrENEldsdlpALPKGLISLFLNRNSFSgqipksygQLNSLQHLDISFNTLTgaTPSELFSLPNIIYLNLGSNMLS--GT 320
Cdd:cd21340    97 I-ENQ------RLPPGEKLTFDPRSLAA--------LSNSLRVLNISGNNID--SLEPLAPLRNLEQLDASNNQISdlEE 159

                         170
                  ....*....|....*....
gi 1379623326 321 LQNSLRCGRNLSFVDISNN 339
Cdd:cd21340   160 LLDLLSSWPSLRELDLTGN 178
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
 487-679 2.82e-08

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: 55.47  E-value: 2.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGK-LENGIPVVIRCIPLSK---KYSIRNFKLRLDLLAKLRHTHLISLLghcidgilgE--RNDSKVFLI 560
Cdd:cd14073     9 LGKGTYGKVKLAIeRATGREVAIKSIKKDKiedEQDMVRIRREIEIMSSLNHPHIIRIY---------EvfENKDKIVIV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 561 YECVSNGNFQTYLSgdSCGKIFNWSERlSVLISVAKAIHFLHTGmipGFFRNRLKTNNILFNENWMAKLSDYGLSIVSEE 640
Cdd:cd14073    80 MEYASGGELYDYIS--ERRRLPEREAR-RIFRQIVSAVHYCHKN---GVVHRDLKLENILLDQNGNAKIADFGLSNLYSK 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1379623326 641 TDASGVIGESP--------NSWQMKKLEDDIYSFGfIILEALVGPSM 679
Cdd:cd14073   154 DKLLQTFCGSPlyaspeivNGTPYQGPEVDCWSLG-VLLYTLVYGTM 199
PLN03150 PLN03150
hypothetical protein; Provisional
 85-182 3.08e-08

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 57.13  E-value: 3.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326  85 NKGRGF-DGFAIPNQTLSQSFSMDsfvatLARLTSLRVLHLVSLGIWGPFPDRIHRLFSLEQLDLSSNYLYGSIPPKIST 163
Cdd:PLN03150  414 TKGKWFiDGLGLDNQGLRGFIPND-----ISKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQ 488

                          90
                  ....*....|....*....
gi 1379623326 164 MVSLQILMLGDNFFNGTIP 182
Cdd:PLN03150  489 LTSLRILNLNGNSLSGRVP 507
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
 532-672 3.80e-08

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: 55.25  E-value: 3.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 532 LRHTHLISLLGHCIDgilgernDSKVFLIYECVSNGNFQTYLSGDSCGkiFNWSERLSVLISVAKAIHFLHTGMIpgfFR 611
Cdd:cd14045    59 LDHPNLCKFIGGCIE-------VPNVAIITEYCPKGSLNDVLLNEDIP--LNWGFRFSFATDIARGMAYLHQHKI---YH 126

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1379623326 612 NRLKTNNILFNENWMAKLSDYGLSIVSEETDASGVIG--------------ESPNSWQMKKLeDDIYSFGFIILE 672
Cdd:cd14045   127 GRLKSSNCVIDDRWVCKIADYGLTTYRKEDGSENASGyqqrlmqvylppenHSNTDTEPTQA-TDVYSYAIILLE 200
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
 512-741 4.07e-08

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: 55.71  E-value: 4.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 512 PLSKKYSIRNFKLRLDLLAKLRHTHLISLLGHCIDgilgernDSKVFLIYECVSNGNFQTYLSG---------------- 575
Cdd:cd05096    56 PDANKNARNDFLKEVKILSRLKDPNIIRLLGVCVD-------EDPLCMITEYMENGDLNQFLSShhlddkeengndavpp 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 576 DSCGKIFNWSERLSVLISVAKAIHFLHTgmiPGFFRNRLKTNNILFNENWMAKLSDYGLSIVSEETDASGVIGES--PNS 653
Cdd:cd05096   129 AHCLPAISYSSLLHVALQIASGMKYLSS---LNFVHRDLATRNCLVGENLTIKIADFGMSRNLYAGDYYRIQGRAvlPIR 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 654 WQ------MKKL--EDDIYSFGFIILEALV----GPSMFAKREAAVLNAMASFssQDEWKQIVdpVVQATCCKESLsivI 721
Cdd:cd05096   206 WMawecilMGKFttASDVWAFGVTLWEILMlckeQPYGELTDEQVIENAGEFF--RDQGRQVY--LFRPPPCPQGL---Y 278

                         250       260
                  ....*....|....*....|
gi 1379623326 722 SITNKCISTESWSRPSIEDV 741
Cdd:cd05096   279 ELMLQCWSRDCRERPSFSDI 298
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
 487-672 4.21e-08

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: 54.99  E-value: 4.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLEnGIPVVIRCIplSKKYSIRNFKLRLDLLAKLRHTHLISLLGhcidgILGERNDSkVFLIYECVSN 566
Cdd:cd05082    14 IGKGEFGDVMLGDYR-GNKVAVKCI--KNDATAQAFLAEASVMTQLRHSNLVQLLG-----VIVEEKGG-LYIVTEYMAK 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 567 GNFQTYLSgdSCGKIFNWSERL-SVLISVAKAIHFLHTGmipGFFRNRLKTNNILFNENWMAKLSDYGLSIVSEETDASG 645
Cdd:cd05082    85 GSLVDYLR--SRGRSVLGGDCLlKFSLDVCEAMEYLEGN---NFVHRDLAARNVLVSEDNVAKVSDFGLTKEASSTQDTG 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1379623326 646 ---VIGESPNSWQMKKL--EDDIYSFGFIILE 672
Cdd:cd05082   160 klpVKWTAPEALREKKFstKSDVWSFGILLWE 191
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
 487-741 4.66e-08

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: 55.19  E-value: 4.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLEN-GIPVVIRCIPL--SKKYSIRNFKLRLDLLAKLRHTHLISLLGHCIDgilgerndsKVFLIYEC 563
Cdd:cd14025     4 VGSGGFGQVYKVRHKHwKTWLAIKCPPSlhVDDSERMELLEEAKKMEMAKFRHILPVYGICSE---------PVGLVMEY 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 564 VSNGNFQTYLSGDScgkiFNWSERLSVLISVAKAIHFLHTgMIPGFFRNRLKTNNILFNENWMAKLSDYGLSI---VSEE 640
Cdd:cd14025    75 METGSLEKLLASEP----LPWELRFRIIHETAVGMNFLHC-MKPPLLHLDLKPANILLDAHYHVKISDFGLAKwngLSHS 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 641 TDAS-----GVIGESPNSWQMKK-----LEDDIYSFGFIILEALVGPSMFAKrEAAVLNAMASFSsqdewkQIVDPVVQA 710
Cdd:cd14025   150 HDLSrdglrGTIAYLPPERFKEKnrcpdTKHDVYSFAIVIWGILTQKKPFAG-ENNILHIMVKVV------KGHRPSLSP 222

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1379623326 711 TCCK--ESLSIVISITNKCISTESWSRPSIEDV 741
Cdd:cd14025   223 IPRQrpSECQQMICLMKRCWDQDPRKRPTFQDI 255
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
 487-672 4.66e-08

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: 55.43  E-value: 4.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLENGIP------VVIRCIPLSKKYSIRNFKLRLDLLAKLRHTHLISLLGHCIDGilgerndSKVFLI 560
Cdd:cd05093    13 LGEGAFGKVFLAECYNLCPeqdkilVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEG-------DPLIMV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 561 YECVSNGNFQTYLSGDSCGKIFNWSERLSVLISVAKAIHF---LHTGMI----PGFFRNRLKTNNILFNENWMAKLSDYG 633
Cdd:cd05093    86 FEYMKHGDLNKFLRAHGPDAVLMAEGNRPAELTQSQMLHIaqqIAAGMVylasQHFVHRDLATRNCLVGENLLVKIGDFG 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1379623326 634 LSIVSEETDASGVIGES--------PNSWQMKKL--EDDIYSFGFIILE 672
Cdd:cd05093   166 MSRDVYSTDYYRVGGHTmlpirwmpPESIMYRKFttESDVWSLGVVLWE 214
STKc_IRAK2 cd14157
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; ...
 489-676 6.14e-08

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK2 plays a role in mediating NFkB activation by TLR3, TLR4, and TLR8. It is specifically targeted by the viral protein A52, which is important for virulence, to inhibit all IL-1/TLR pathways, indicating that IRAK2 has a predominant role in NFkB activation. It is redundant with IRAK1 in early signaling but is critical for late and sustained activation. The IRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271059 [Multi-domain]  Cd Length: 289  Bit Score: 54.84  E-value: 6.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 489 ENIYGKLYKGKLENGIPVVIRC---IPLSKKYSIRNFKLRLDLLAKLRHTHLISLLGHCIDGILGErndskvfLIYECVS 565
Cdd:cd14157     3 EGTFADIYKGYRHGKQYVIKRLketECESPKSTERFFQTEVQICFRCCHPNILPLLGFCVESDCHC-------LIYPYMP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 566 NGNFQTYLSGDSCGKIFNWSERLSVLISVAKAIHFLHTGmipGFFRNRLKTNNILFNENWMAKLSDYGLSIVSEETDASG 645
Cdd:cd14157    76 NGSLQDRLQQQGGSHPLPWEQRLSISLGLLKAVQHLHNF---GILHGNIKSSNVLLDGNLLPKLGHSGLRLCPVDKKSVY 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1379623326 646 VIGES----------PNSW----QMKKlEDDIYSFGFIILEALVG 676
Cdd:cd14157   153 TMMKTkvlqislaylPEDFvrhgQLTE-KVDIFSCGVVLAEILTG 196
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
 487-672 8.05e-08

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: 54.63  E-value: 8.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLENGIP------VVIRCIPLSKKYSIRNFKLRLDLLAKLRHTHLISLLGHCIDGilgerndSKVFLI 560
Cdd:cd05094    13 LGEGAFGKVFLAECYNLSPtkdkmlVAVKTLKDPTLAARKDFQREAELLTNLQHDHIVKFYGVCGDG-------DPLIMV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 561 YECVSNGNFQTYLSG---------DSCGKIFNWSERLSVLISVAKAIhflHTGMI----PGFFRNRLKTNNILFNENWMA 627
Cdd:cd05094    86 FEYMKHGDLNKFLRAhgpdamilvDGQPRQAKGELGLSQMLHIATQI---ASGMVylasQHFVHRDLATRNCLVGANLLV 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1379623326 628 KLSDYGLSIVSEETDASGVIGES--------PNSWQMKKL--EDDIYSFGFIILE 672
Cdd:cd05094   163 KIGDFGMSRDVYSTDYYRVGGHTmlpirwmpPESIMYRKFttESDVWSFGVILWE 217
PLN03150 PLN03150
hypothetical protein; Provisional
 179-269 1.22e-07

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 55.21  E-value: 1.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 179 GTIPNLFDSSSNLTVFSLKNNKLKGPFPFSILSITTLTNIDMSRNQISGSLQDFTG-LSSLEHLDLRENELDSDLPALPK 257
Cdd:PLN03150  432 GFIPNDISKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGqLTSLRILNLNGNSLSGRVPAALG 511

                          90
                  ....*....|..
gi 1379623326 258 GLIslfLNRNSF 269
Cdd:PLN03150  512 GRL---LHRASF 520
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
 487-635 1.46e-07

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: 53.42  E-value: 1.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLENGIPVVIRCIplsKKYSIRN------FKLRLDLLAKLRHTHLISLlgHCIdgilgERNDSKVFLI 560
Cdd:cd14161    11 LGKGTYGRVKKARDSSGRLVAIKSI---RKDRIKDeqdllhIRREIEIMSSLNHPHIISV--YEV-----FENSSKIVIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 561 YECVSNGNFQTYLSGdscgkifnwSERLSVLIS------VAKAIHFLHTGmipGFFRNRLKTNNILFNENWMAKLSDYGL 634
Cdd:cd14161    81 MEYASRGDLYDYISE---------RQRLSELEArhffrqIVSAVHYCHAN---GIVHRDLKLENILLDANGNIKIADFGL 148


                  .
gi 1379623326 635 S 635
Cdd:cd14161   149 S 149
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
 520-742 1.48e-07

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: 53.47  E-value: 1.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 520 RNFKLRLDLLAKLRHTHLISLLGHCIDGILGERNdskVFLIYECVSNGNFQTYLSGDSCGK---IFNWSERlsvlisVAK 596
Cdd:cd14033    45 QRFSEEVEMLKGLQHPNIVRFYDSWKSTVRGHKC---IILVTELMTSGTLKTYLKRFREMKlklLQRWSRQ------ILK 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 597 AIHFLHTGMIPGFFRNrLKTNNILFN-ENWMAKLSDYGLSIVSEETDASGVIGE----SPNSWQMKKLED-DIYSFGFII 670
Cdd:cd14033   116 GLHFLHSRCPPILHRD-LKCDNIFITgPTGSVKIGDLGLATLKRASFAKSVIGTpefmAPEMYEEKYDEAvDVYAFGMCI 194

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1379623326 671 LEALVG--PSMFAKREAAVLNAMASFSSQDEWKQIVDPVVQatcckeslsiviSITNKCISTESWSRPSIEDVL 742
Cdd:cd14033   195 LEMATSeyPYSECQNAAQIYRKVTSGIKPDSFYKVKVPELK------------EIIEGCIRTDKDERFTIQDLL 256
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
 486-674 1.49e-07

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: 53.47  E-value: 1.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 486 FLGENIYGKLYKGKLENGIPVVIRCIP--LSKKYSIRnFKLRLDLLAKLRHTHLISLLGHCIdgilgerNDSKVFLIYEC 563
Cdd:cd05085     3 LLGKGNFGEVYKGTLKDKTPVAVKTCKedLPQELKIK-FLSEARILKQYDHPNIVKLIGVCT-------QRQPIYIVMEL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 564 VSNGNFQTYLSGDScgKIFNWSERLSVLISVAKAIHFLHTgmiPGFFRNRLKTNNILFNENWMAKLSDYGLSivSEETD- 642
Cdd:cd05085    75 VPGGDFLSFLRKKK--DELKTKQLVKFSLDAAAGMAYLES---KNCIHRDLAARNCLVGENNALKISDFGMS--RQEDDg 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1379623326 643 --ASGVIGESPNSWQMKKL--------EDDIYSFGFIILEAL 674
Cdd:cd05085   148 vySSSGLKQIPIKWTAPEAlnygryssESDVWSFGILLWETF 189
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
 487-672 1.51e-07

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: 53.12  E-value: 1.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENI----YGKLYKGKLENGiPVVIRCIPLSKKySIRNFKLRLDLLAKLRHTHLISLLGHCIDGilgerndSKVFLIYE 562
Cdd:cd05039    10 LGELIgkgeFGDVMLGDYRGQ-KVAVKCLKDDST-AAQAFLAEASVMTTLRHPNLVQLLGVVLEG-------NGLYIVTE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 563 CVSNGNFQTYLSgdSCGK-IFNWSERLSVLISVAKAIHFLHTgmiPGFFRNRLKTNNILFNENWMAKLSDYGLSIVSEET 641
Cdd:cd05039    81 YMAKGSLVDYLR--SRGRaVITRKDQLGFALDVCEGMEYLES---KKFVHRDLAARNVLVSEDNVAKVSDFGLAKEASSN 155

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1379623326 642 DASG---VIGESPNSWQMKKL--EDDIYSFGFIILE 672
Cdd:cd05039   156 QDGGklpIKWTAPEALREKKFstKSDVWSFGILLWE 191
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
 487-676 1.58e-07

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: 53.48  E-value: 1.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLENGIPVVIRCIPLSKKYSIRNFKLRLDLLAKLRHTHLISLLGHCID---GILGERNDSKVFLIYEC 563
Cdd:cd14150     8 IGTGSFGTVFRGKWHGDVAVKILKVTEPTPEQLQAFKNEMQVLRKTRHVNILLFMGFMTRpnfAIITQWCEGSSLYRHLH 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 564 VSNGNFQTYlsgdscgkifnwsERLSVLISVAKAIHFLHTGMIpgfFRNRLKTNNILFNENWMAKLSDYGLSIVSE---- 639
Cdd:cd14150    88 VTETRFDTM-------------QLIDVARQTAQGMDYLHAKNI---IHRDLKSNNIFLHEGLTVKIGDFGLATVKTrwsg 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1379623326 640 ----ETDASGVIGESPNSWQMKK-----LEDDIYSFGFIILEALVG 676
Cdd:cd14150   152 sqqvEQPSGSILWMAPEVIRMQDtnpysFQSDVYAYGVVLYELMSG 197
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
 487-635 1.58e-07

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: 53.26  E-value: 1.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKgkLENGIPVVIRCIPLSKKYSIRNFKLR-LDLLAKLRHTHLISLLGHCIdgilgerNDSKVFLIYECVS 565
Cdd:cd14065     1 LGKGFFGEVYK--VTHRETGKVMVMKELKRFDEQRSFLKeVKLMRRLSHPNILRFIGVCV-------KDNKLNFITEYVN 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1379623326 566 NGNFQTYLSgdSCGKIFNWSERLSVLISVAKAIHFLHTgmiPGFFRNRLKTNNILF---NENWMAKLSDYGLS 635
Cdd:cd14065    72 GGTLEELLK--SMDEQLPWSQRVSLAKDIASGMAYLHS---KNIIHRDLNSKNCLVreaNRGRNAVVADFGLA 139
PLN03150 PLN03150
hypothetical protein; Provisional
 135-229 1.92e-07

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 54.44  E-value: 1.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 135 DRIHRLFSLEQLDLSSNYLYGSIPPKISTMVSLQILMLGDNFFNGTIPNLFDSSSNLTVFSLKNNKLKGPFPFSILSITT 214
Cdd:PLN03150  412 DSTKGKWFIDGLGLDNQGLRGFIPNDISKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTS 491

                          90
                  ....*....|....*
gi 1379623326 215 LTNIDMSRNQISGSL 229
Cdd:PLN03150  492 LRILNLNGNSLSGRV 506
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
 486-676 2.12e-07

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: 52.79  E-value: 2.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 486 FLGENIYGKLYKGK-LENGIPVVIRCIPLSKKYSIR---NFKLRLDLLAKLRHTHLISLLGhcidgILGERNdsKVFLIY 561
Cdd:cd14663     7 TLGEGTFAKVKFARnTKTGESVAIKIIDKEQVAREGmveQIKREIAIMKLLRHPNIVELHE-----VMATKT--KIFFVM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 562 ECVSNGN-FQTYLSG-----DSCGKIFNWserlsvLISvakAIHFLHTgmiPGFFRNRLKTNNILFNENWMAKLSDYGLS 635
Cdd:cd14663    80 ELVTGGElFSKIAKNgrlkeDKARKYFQQ------LID---AVDYCHS---RGVFHRDLKPENLLLDEDGNLKISDFGLS 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1379623326 636 IVSEETDASGVIGE---SPNSWQMKKLED--------DIYSFGFIILEALVG 676
Cdd:cd14663   148 ALSEQFRQDGLLHTtcgTPNYVAPEVLARrgydgakaDIWSCGVILFVLLAG 199
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
 487-635 2.57e-07

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: 52.87  E-value: 2.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGK-LENGIPVVIrciplsKKYSIRNFK-------LR-LDLLAKLRHTHLISLLghciDGILGERndsKV 557
Cdd:cd07829     7 LGEGTYGVVYKAKdKKTGEIVAL------KKIRLDNEEegipstaLReISLLKELKHPNIVKLL----DVIHTEN---KL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 558 FLIYECVSNgNFQTYLsgDSCGKIFNWSERLSVLISVAKAIHFLHtgmipgffRNR-----LKTNNILFNENWMAKLSDY 632
Cdd:cd07829    74 YLVFEYCDQ-DLKKYL--DKRPGPLPPNLIKSIMYQLLRGLAYCH--------SHRilhrdLKPQNLLINRDGVLKLADF 142


                  ...
gi 1379623326 633 GLS 635
Cdd:cd07829   143 GLA 145
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
 487-746 3.06e-07

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: 52.24  E-value: 3.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLE-NGIPVVIRCIPLSKKYSIRN-FKLRLDLLAKLRHTHLISLLGHCIdgilgerNDSKVFLIYECV 564
Cdd:cd05084     4 IGRGNFGEVFSGRLRaDNTPVAVKSCRETLPPDLKAkFLQEARILKQYSHPNIVRLIGVCT-------QKQPIYIVMELV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 565 SNGNFQTYLSGDscGKIFNWSERLSVLISVAKAIHFLHTGMIpgfFRNRLKTNNILFNENWMAKLSDYGLSivSEETD-- 642
Cdd:cd05084    77 QGGDFLTFLRTE--GPRLKVKELIRMVENAAAGMEYLESKHC---IHRDLAARNCLVTEKNVLKISDFGMS--REEEDgv 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 643 --ASGVIGESPNSWQMKKL--------EDDIYSFGFIILEALvgpsmfaKREAAVLNAMASFSSQDEWKQIVDPVVQATC 712
Cdd:cd05084   150 yaATGGMKQIPVKWTAPEAlnygryssESDVWSFGILLWETF-------SLGAVPYANLSNQQTREAVEQGVRLPCPENC 222

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1379623326 713 CKEslsiVISITNKCISTESWSRPSIEDVLWNLQ 746
Cdd:cd05084   223 PDE----VYRLMEQCWEYDPRKRPSFSTVHQDLQ 252
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
 487-674 3.58e-07

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: 52.05  E-value: 3.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLENGIpVVIRCIPLSKKysIRNFKLRLDLLAKLRHTHLISLLGHCIdgilgerNDSKVFLIYECVSN 566
Cdd:cd14058     1 VGRGSFGVVCKARWRNQI-VAVKIIESESE--KKAFEVEVRQLSRVDHPNIIKLYGACS-------NQKPVCLVMEYAEG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 567 GNFQTYLSGDSCGKIFNWSERLSVLISVAKAIHFLHtGMIPGFFRNR-LKTNNIL-FNENWMAKLSDYGLS--IVSEETD 642
Cdd:cd14058    71 GSLYNVLHGKEPKPIYTAAHAMSWALQCAKGVAYLH-SMKPKALIHRdLKPPNLLlTNGGTVLKICDFGTAcdISTHMTN 149

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1379623326 643 ASGVIG-ESPNSWQMKKLED--DIYSFGFIILEAL 674
Cdd:cd14058   150 NKGSAAwMAPEVFEGSKYSEkcDVFSWGIILWEVI 184
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
 488-746 4.08e-07

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: 51.88  E-value: 4.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 488 GENIYGKLYKGKLengipvvircIPLSKKYSIRNFkLRLD----LLAKLRHTHLISLLGHCIDGilgeRNDSkvfLIYEC 563
Cdd:cd14060     2 GGGSFGSVYRAIW----------VSQDKEVAVKKL-LKIEkeaeILSVLSHRNIIQFYGAILEA----PNYG---IVTEY 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 564 VSNGNFQTYLSGDSCGKIfNWSERLSVLISVAKAIHFLHTGMIPGFFRNRLKTNNILFNENWMAKLSDYGLSIVSEETDA 643
Cdd:cd14060    64 ASYGSLFDYLNSNESEEM-DMDQIMTWATDIAKGMHYLHMEAPVKVIHRDLKSRNVVIAADGVLKICDFGASRFHSHTTH 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 644 SGVIGESPnsWQMKKLED--------DIYSFGFIILEALVGPSMFAKREAAvlnamasfssQDEWkQIVDPVVQAT---C 712
Cdd:cd14060   143 MSLVGTFP--WMAPEVIQslpvsetcDTYSYGVVLWEMLTREVPFKGLEGL----------QVAW-LVVEKNERPTipsS 209

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1379623326 713 CKESLSiviSITNKCISTESWSRPSIEDVLWNLQ 746
Cdd:cd14060   210 CPRSFA---ELMRRCWEADVKERPSFKQIIGILE 240
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
143-349 4.71e-07

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 53.55  E-value: 4.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 143 LEQLDLSSnyLYGSIPPKISTMV--SLQILMLGDNFfNGTIPNLFDSSSNLTvfslknnKLKGPFPfsilsiTTLTNIDM 220
Cdd:PRK15370  185 LKILGLTT--IPACIPEQITTLIldNNELKSLPENL-QGNIKTLYANSNQLT-------SIPATLP------DTIQEMEL 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 221 SRNQISGSLQDFTglSSLEHLDLRENELdSDLP-ALPKGLISLFLNRNSFSGqIPKSYGqlNSLQHLDISFNTLTgATPS 299
Cdd:PRK15370  249 SINRITELPERLP--SALQSLDLFHNKI-SCLPeNLPEELRYLSVYDNSIRT-LPAHLP--SGITHLNVQSNSLT-ALPE 321

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1379623326 300 ELfsLPNIIYLNLGSNMLSgTLQNSLRcgRNLSFVDISNNRlIGALPYSL 349
Cdd:PRK15370  322 TL--PPGLKTLEAGENALT-SLPASLP--PELQVLDVSKNQ-ITVLPETL 365
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
 487-640 4.96e-07

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: 51.51  E-value: 4.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLENGIPVVIRCIPlSKKYSIRNFKLRLDLLAKLRHTHLISLLGHCIDGilgerndSKVFLIYECVSN 566
Cdd:cd05034     3 LGAGQFGEVWMGVWNGTTKVAVKTLK-PGTMSPEAFLQEAQIMKKLRHDKLVQLYAVCSDE-------EPIYIVTELMSK 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 567 GNFQTYLSGDSCGKIfnwseRLSVLISVAKAIHflhTGMipGFFRNR------LKTNNILFNENWMAKLSDYGLSIVSEE 640
Cdd:cd05034    75 GSLLDYLRTGEGRAL-----RLPQLIDMAAQIA---SGM--AYLESRnyihrdLAARNILVGENNVCKVADFGLARLIED 144
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
 486-635 7.86e-07

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: 51.42  E-value: 7.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 486 FLGENIYGKLYKGK-LENGIPVVIRCIPLSKKYSIR---NFK-LR-LDLLAKLRHTHLISLL---GHcidgilgernDSK 556
Cdd:cd07841     7 KLGEGTYAVVYKARdKETGRIVAIKKIKLGERKEAKdgiNFTaLReIKLLQELKHPNIIGLLdvfGH----------KSN 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 557 VFLIYEcvsngnfqtYLSGDSCGKIFNWSERLSV------LISVAKAIHFLHTGmipgFFRNR-LKTNNILFNENWMAKL 629
Cdd:cd07841    77 INLVFE---------FMETDLEKVIKDKSIVLTPadiksyMLMTLRGLEYLHSN----WILHRdLKPNNLLIASDGVLKL 143


                  ....*.
gi 1379623326 630 SDYGLS 635
Cdd:cd07841   144 ADFGLA 149
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
 487-742 8.11e-07

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: 51.28  E-value: 8.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGK--LYKgKLENGIPVVIRCIPLSK--KYSIRNFKLRLDLLAKLRHTHLISLLGHCIDGilgerndSKVFLIYE 562
Cdd:cd08221     8 LGRGAFGEavLYR-KTEDNSLVVWKEVNLSRlsEKERRDALNEIDILSLLNHDNIITYYNHFLDG-------ESLFIEME 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 563 CVSNGNFQTYLSgDSCGKIFNWSERLSVLISVAKAIHFLHTGmipGFFRNRLKTNNILFNENWMAKLSDYGLSIV--SEE 640
Cdd:cd08221    80 YCNGGNLHDKIA-QQKNQLFPEEVVLWYLYQIVSAVSHIHKA---GILHRDIKTLNIFLTKADLVKLGDFGISKVldSES 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 641 TDASGVIGE----SPNSWQMKK--LEDDIYSFGFIILEALVGPSMFakrEAAVLNAMASFSSQDEWKQIVDPVVQAtcck 714
Cdd:cd08221   156 SMAESIVGTpyymSPELVQGVKynFKSDIWAVGCVLYELLTLKRTF---DATNPLRLAVKIVQGEYEDIDEQYSEE---- 228

                         250       260
                  ....*....|....*....|....*...
gi 1379623326 715 eslsiVISITNKCISTESWSRPSIEDVL 742
Cdd:cd08221   229 -----IIQLVHDCLHQDPEDRPTAEELL 251
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
 487-672 8.72e-07

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: 51.20  E-value: 8.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLENGIPVVIRCIPlSKKYSIRNFKLRLDLLAKLRHTHLISLLGHCIdgilgerNDSKVFLIYECVSN 566
Cdd:cd05072    15 LGAGQFGEVWMGYYNNSTKVAVKTLK-PGTMSVQAFLEEANLMKTLQHDKLVRLYAVVT-------KEEPIYIITEYMAK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 567 GNFQTYLSGDSCGKIFnwserLSVLISVAKAIHflhTGMI----PGFFRNRLKTNNILFNENWMAKLSDYGLSIVSEETD 642
Cdd:cd05072    87 GSLLDFLKSDEGGKVL-----LPKLIDFSAQIA---EGMAyierKNYIHRDLRAANVLVSESLMCKIADFGLARVIEDNE 158

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1379623326 643 ASGVIGES-PNSWQMKK--------LEDDIYSFGFIILE 672
Cdd:cd05072   159 YTAREGAKfPIKWTAPEainfgsftIKSDVWSFGILLYE 197
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
 487-742 1.33e-06

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: 50.49  E-value: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLENGIPVVIRCIPLSKKYSI---RNFKLRLDLLAKLRHTHLISLLGHCIDGILGERNdskVFLIYEC 563
Cdd:cd14031    18 LGRGAFKTVYKGLDTETWVEVAWCELQDRKLTKaeqQRFKEEAEMLKGLQHPNIVRFYDSWESVLKGKKC---IVLVTEL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 564 VSNGNFQTYLSGDSCGK---IFNWSERlsvlisVAKAIHFLHTGMIPGFFRNrLKTNNILFN-ENWMAKLSDYGLSIVSE 639
Cdd:cd14031    95 MTSGTLKTYLKRFKVMKpkvLRSWCRQ------ILKGLQFLHTRTPPIIHRD-LKCDNIFITgPTGSVKIGDLGLATLMR 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 640 ETDASGVIGE----SPNSWQMKKLED-DIYSFGFIILEALVG--PSMFAKREAAVLNAMASFSSQDEWKQIVDPVVQatc 712
Cdd:cd14031   168 TSFAKSVIGTpefmAPEMYEEHYDESvDVYAFGMCMLEMATSeyPYSECQNAAQIYRKVTSGIKPASFNKVTDPEVK--- 244

                         250       260       270
                  ....*....|....*....|....*....|
gi 1379623326 713 ckeslsiviSITNKCISTESWSRPSIEDVL 742
Cdd:cd14031   245 ---------EIIEGCIRQNKSERLSIKDLL 265
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
 484-676 1.45e-06

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: 50.80  E-value: 1.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 484 STFLGENIYGKLYKGKLENGIPVVIRCIPLSKKYSIRNFKLRLDLLAKLRHTHLISLLGHCIDG---ILGERNDSKVFLI 560
Cdd:cd14149    17 STRIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGYMTKDnlaIVTQWCEGSSLYK 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 561 YECVSNGNFQTYlsgdscgkifnwsERLSVLISVAKAIHFLHTGMIpgfFRNRLKTNNILFNENWMAKLSDYGLSIVSE- 639
Cdd:cd14149    97 HLHVQETKFQMF-------------QLIDIARQTAQGMDYLHAKNI---IHRDMKSNNIFLHEGLTVKIGDFGLATVKSr 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1379623326 640 -------ETDASGVIGESPNSWQMK-----KLEDDIYSFGFIILEALVG 676
Cdd:cd14149   161 wsgsqqvEQPTGSILWMAPEVIRMQdnnpfSFQSDVYSYGIVLYELMTG 209
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
 492-672 1.62e-06

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: 50.51  E-value: 1.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 492 YGKLYKGKLENGiPVVIRCIPLSKKysiRNFKLRLDLLAK--LRHTHLISLlghcidgILGERNDS----KVFLIYECVS 565
Cdd:cd13998     8 FGEVWKASLKNE-PVAVKIFSSRDK---QSWFREKEIYRTpmLKHENILQF-------IAADERDTalrtELWLVTAFHP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 566 NGNFQTYLSGDscgkIFNWSERLSVLISVAKAIHFLHTGmIPGFFRNR-------LKTNNILFNENWMAKLSDYGLSIVS 638
Cdd:cd13998    77 NGSL*DYLSLH----TIDWVSLCRLALSVARGLAHLHSE-IPGCTQGKpaiahrdLKSKNILVKNDGTCCIADFGLAVRL 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1379623326 639 EETDASGVIGESP--------------NSWQMKKLED----DIYSFGFIILE 672
Cdd:cd13998   152 SPSTGEEDNANNGqvgtkrymapevleGAINLRDFESfkrvDIYAMGLVLWE 203
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
 487-676 1.69e-06

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: 50.44  E-value: 1.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLENGIPVVIRCIPLSKKYSIRNFKLRLDLLAKLRHTHLISLLGHCidgilgerNDSKVFLIYECVSN 566
Cdd:cd14151    16 IGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYS--------TKPQLAIVTQWCEG 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 567 GNFQTYLSGDSCGkiFNWSERLSVLISVAKAIHFLHTGMIpgfFRNRLKTNNILFNENWMAKLSDYGLSIVSE------- 639
Cdd:cd14151    88 SSLYHHLHIIETK--FEMIKLIDIARQTAQGMDYLHAKSI---IHRDLKSNNIFLHEDLTVKIGDFGLATVKSrwsgshq 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1379623326 640 -ETDASGVIGESPNSWQMK-----KLEDDIYSFGFIILEALVG 676
Cdd:cd14151   163 fEQLSGSILWMAPEVIRMQdknpySFQSDVYAFGIVLYELMTG 205
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
 487-633 1.69e-06

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: 49.99  E-value: 1.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLEN-GIPVVIRCIplSKK-----YSIRNFKLRLDLLAKLRHTHLISLLgHCIDgilgerNDSKVFLI 560
Cdd:cd14162     8 LGHGSYAVVKKAYSTKhKCKVAIKIV--SKKkapedYLQKFLPREIEVIKGLKHPNLICFY-EAIE------TTSRVYII 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1379623326 561 YECVSNGNF------QTYLSGDSCGKIFnwserlSVLISvakAIHFLHTgmiPGFFRNRLKTNNILFNENWMAKLSDYG 633
Cdd:cd14162    79 MELAENGDLldyirkNGALPEPQARRWF------RQLVA---GVEYCHS---KGVVHRDLKCENLLLDKNNNLKITDFG 145
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
 506-741 1.75e-06

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


Pssm-ID: 270945 [Multi-domain]  Cd Length: 267  Bit Score: 50.10  E-value: 1.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 506 VVIRCIPLSKKYSIR-NFKLRLDLLAKLRHTHLISLLGHCID-GILGerndskvfLIYECVSNGNFQTYLSGDSCGkiFN 583
Cdd:cd14043    26 VWLKKFPGGSHTELRpSTKNVFSKLRELRHENVNLFLGLFVDcGILA--------IVSEHCSRGSLEDLLRNDDMK--LD 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 584 WSERLSVLISVAKAIHFLHTgmiPGFFRNRLKTNNILFNENWMAKLSDYGLS-------IVSEETDASGVIGESPNSWQM 656
Cdd:cd14043    96 WMFKSSLLLDLIKGMRYLHH---RGIVHGRLKSRNCVVDGRFVLKITDYGYNeileaqnLPLPEPAPEELLWTAPELLRD 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 657 KKLE------DDIYSFGFIILEALVgpsmfakREAAVlnAMASFSSQdewkQIVDPVVQ-ATCCKESLSI------VISI 723
Cdd:cd14043   173 PRLErrgtfpGDVFSFAIIMQEVIV-------RGAPY--CMLGLSPE----EIIEKVRSpPPLCRPSVSMdqapleCIQL 239

                         250
                  ....*....|....*...
gi 1379623326 724 TNKCISTESWSRPSIEDV 741
Cdd:cd14043   240 MKQCWSEAPERRPTFDQI 257
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
 476-726 1.80e-06

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: 50.65  E-value: 1.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 476 EATNNFDNSTFLGENIYGKLYKGKLE-NGIPVVIRCI--PLSKKYSIRNFKLRLDLLAKLRHTHLISLlghcidgilger 552
Cdd:cd07856     7 EITTRYSDLQPVGMGAFGLVCSARDQlTGQNVAVKKImkPFSTPVLAKRTYRELKLLKHLRHENIISL------------ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 553 ndSKVFL-----IYecvsngnFQTYLSGDSCGKIFNwSERLS------VLISVAKAIHFLHTGmipGFFRNRLKTNNILF 621
Cdd:cd07856    75 --SDIFIspledIY-------FVTELLGTDLHRLLT-SRPLEkqfiqyFLYQILRGLKYVHSA---GVIHRDLKPSNILV 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 622 NENWMAKLSDYGLSIVsEETDASGVIG----ESPN---SWQMKKLEDDIYSFGFIILEALVGPSMFAKReaavlNAMASF 694
Cdd:cd07856   142 NENCDLKICDFGLARI-QDPQMTGYVStryyRAPEimlTWQKYDVEVDIWSAGCIFAEMLEGKPLFPGK-----DHVNQF 215

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1379623326 695 SS-QDEWKQIVDPVVQATCCKESLSIVISITNK 726
Cdd:cd07856   216 SIiTELLGTPPDDVINTICSENTLRFVQSLPKR 248
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
 487-672 2.11e-06

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: 50.38  E-value: 2.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLENGIPVVIRCIPLSKKYSI----RNFKLRLDLLAKL-RHTHLISLLGHCidgilgeRNDSKVFLIY 561
Cdd:cd05089    10 IGEGNFGQVIKAMIKKDGLKMNAAIKMLKEFASendhRDFAGELEVLCKLgHHPNIINLLGAC-------ENRGYLYIAI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 562 ECVSNGNFQTYLSGD-------------SCGKIFNWSERLSVLISVAKAIHFLHTGMipgFFRNRLKTNNILFNENWMAK 628
Cdd:cd05089    83 EYAPYGNLLDFLRKSrvletdpafakehGTASTLTSQQLLQFASDVAKGMQYLSEKQ---FIHRDLAARNVLVGENLVSK 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1379623326 629 LSDYGLSiVSEETDASGVIGESPNSW--------QMKKLEDDIYSFGFIILE 672
Cdd:cd05089   160 IADFGLS-RGEEVYVKKTMGRLPVRWmaieslnySVYTTKSDVWSFGVLLWE 210
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
 487-674 2.53e-06

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: 49.68  E-value: 2.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKL----ENGIPVVIRCipLSKKYSIrnfKLRLDLLA------KLRHTHLISLLGHCIDGilgerndSK 556
Cdd:cd05033    12 IGGGEFGEVCSGSLklpgKKEIDVAIKT--LKSGYSD---KQRLDFLTeasimgQFDHPNVIRLEGVVTKS-------RP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 557 VFLIYECVSNGNFQTYLSGDScGKiFNWSERLSVLISVAKAIHFLhTGMipGFFRNRLKTNNILFNENWMAKLSDYGLSI 636
Cdd:cd05033    80 VMIVTEYMENGSLDKFLREND-GK-FTVTQLVGMLRGIASGMKYL-SEM--NYVHRDLAARNILVNSDLVCKVSDFGLSR 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1379623326 637 VSEETDA----SGviGESPNSW------QMKKLE--DDIYSFGFIILEAL 674
Cdd:cd05033   155 RLEDSEAtyttKG--GKIPIRWtapeaiAYRKFTsaSDVWSFGIVMWEVM 202
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
 487-742 2.78e-06

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK1 is widely expressed and is most abundant in the testis. In hyperosmotic or hypotonic low-chloride stress conditions, WNK1 is activated and it phosphorylates its substrates including SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. Mutations in WNK1 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK1 negates WNK4-mediated inhibition of the sodium-chloride cotransporter NCC and activates the epithelial sodium channel ENaC by activating SGK1. WNK1 also decreases the surface expression of renal outer medullary potassium channel (ROMK) by stimulating their endocytosis. Hypertension and hyperkalemia in PHAII patients with WNK1 mutations may be due partly to increased activity of NCC and ENaC, and impaired renal potassium secretion by ROMK, respectively. In addition, WNK1 interacts with MEKK2/3 and acts as an activator of extracellular signal-regulated kinase (ERK) 5. It also negatively regulates TGFbeta signaling. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 49.66  E-value: 2.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLENGIPVVIRCIPLSKKYSI---RNFKLRLDLLAKLRHTHLISLLGHCIDGILGERNdskVFLIYEC 563
Cdd:cd14030    33 IGRGSFKTVYKGLDTETTVEVAWCELQDRKLSKserQRFKEEAGMLKGLQHPNIVRFYDSWESTVKGKKC---IVLVTEL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 564 VSNGNFQTYLSGDSCGKI---FNWSERlsvlisVAKAIHFLHTGMIPGFFRNrLKTNNILFN-ENWMAKLSDYGLSIVSE 639
Cdd:cd14030   110 MTSGTLKTYLKRFKVMKIkvlRSWCRQ------ILKGLQFLHTRTPPIIHRD-LKCDNIFITgPTGSVKIGDLGLATLKR 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 640 ETDASGVIGE----SPNSWQMKKLED-DIYSFGFIILEALVGPSMFAKREAAVlnamasfssqDEWKQIVDPVVQATCCK 714
Cdd:cd14030   183 ASFAKSVIGTpefmAPEMYEEKYDESvDVYAFGMCMLEMATSEYPYSECQNAA----------QIYRRVTSGVKPASFDK 252

                         250       260
                  ....*....|....*....|....*...
gi 1379623326 715 ESLSIVISITNKCISTESWSRPSIEDVL 742
Cdd:cd14030   253 VAIPEVKEIIEGCIRQNKDERYAIKDLL 280
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
 520-676 2.88e-06

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: 49.53  E-value: 2.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 520 RNFKLRLDLLAKLRHTHLISLLGHCIDGILgerndskvfLIYECVSNGNFQTYLSGDSCGKI-FNWSERLSVLISVAKAI 598
Cdd:cd14000    55 RLLRQELTVLSHLHHPSIVYLLGIGIHPLM---------LVLELAPLGSLDHLLQQDSRSFAsLGRTLQQRIALQVADGL 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 599 HFLHTGMIpgFFRNrLKTNNILF-----NENWMAKLSDYGLSIVSEETDASGVIG----ESPNSWQMKKLED---DIYSF 666
Cdd:cd14000   126 RYLHSAMI--IYRD-LKSHNVLVwtlypNSAIIIKIADYGISRQCCRMGAKGSEGtpgfRAPEIARGNVIYNekvDVFSF 202

                         170
                  ....*....|
gi 1379623326 667 GFIILEALVG 676
Cdd:cd14000   203 GMLLYEILSG 212
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
 487-672 3.00e-06

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: 49.69  E-value: 3.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLEN-----GIPVVIRCI-PLSKKYSIRNFKLRLDLLAKLRHTHLISLLGHCIDgiLGERNdskVFLI 560
Cdd:cd05038    12 LGEGHFGSVELCRYDPlgdntGEQVAVKSLqPSGEEQHMSDFKREIEILRTLDHEYIVKYKGVCES--PGRRS---LRLI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 561 YECVSNGNFQTYLSGDScGKIfNWSERLSVLISVAKAIHFLHTgmiPGFFRNRLKTNNILFNENWMAKLSDYGLS-IVSE 639
Cdd:cd05038    87 MEYLPSGSLRDYLQRHR-DQI-DLKRLLLFASQICKGMEYLGS---QRYIHRDLAARNILVESEDLVKISDFGLAkVLPE 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1379623326 640 ETDASGV--IGESPNSWQMKK--------LEDDIYSFGFIILE 672
Cdd:cd05038   162 DKEYYYVkePGESPIFWYAPEclresrfsSASDVWSFGVTLYE 204
PLN03150 PLN03150
hypothetical protein; Provisional
 262-349 3.08e-06

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 50.58  E-value: 3.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 262 LFLNRNSFSGQIPKSYGQLNSLQHLDISFNTLTGATPSELFSLPNIIYLNLGSNMLSGTLQNSLRCGRNLSFVDISNNRL 341
Cdd:PLN03150  423 LGLDNQGLRGFIPNDISKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNGNSL 502


                  ....*...
gi 1379623326 342 IGALPYSL 349
Cdd:PLN03150  503 SGRVPAAL 510
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
 487-672 3.43e-06

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: 49.00  E-value: 3.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGK-LENGIPVVIRCIPLS------KKYSIRNFKLrldlLAKLRHTHLISLLGHCIDgilgernDSKVFL 559
Cdd:cd08215     8 IGKGSFGSAYLVRrKSDGKLYVLKEIDLSnmsekeREEALNEVKL----LSKLKHPNIVKYYESFEE-------NGKLCI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 560 IYECVSNGNFQTYLS-GDSCGKIFNWSERLSVLISVAKAIHFLHTgmipgffRN---R-LKTNNILFNENWMAKLSDYGL 634
Cdd:cd08215    77 VMEYADGGDLAQKIKkQKKKGQPFPEEQILDWFVQICLALKYLHS-------RKilhRdLKTQNIFLTKDGVVKLGDFGI 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1379623326 635 SIVSEETD--ASGVIGE----SPNSWQMKKLED--DIYSFGFIILE 672
Cdd:cd08215   150 SKVLESTTdlAKTVVGTpyylSPELCENKPYNYksDIWALGCVLYE 195
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
 487-746 3.63e-06

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: 49.21  E-value: 3.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGkLENGIPVVIRCIPLSKKYSI----RNFKLRLDLLAKLRHTHLISLLGHCIdgilgerNDSKVFLIYE 562
Cdd:cd14148     2 IGVGGFGKVYKG-LWRGEEVAVKAARQDPDEDIavtaENVRQEARLFWMLQHPNIIALRGVCL-------NPPHLCLVME 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 563 CVSNGNFQTYLSGDSCGK--IFNWSerlsvlISVAKAIHFLHTGMIPGFFRNRLKTNNILFNE--------NWMAKLSDY 632
Cdd:cd14148    74 YARGGALNRALAGKKVPPhvLVNWA------VQIARGMNYLHNEAIVPIIHRDLKSSNILILEpienddlsGKTLKITDF 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 633 GLSIVSEETDASGVIGESpnSWQMKKL--------EDDIYSFGFIILEALVGPSMFAKREA-AVLNAMAsfssqdeWKQI 703
Cdd:cd14148   148 GLAREWHKTTKMSAAGTY--AWMAPEVirlslfskSSDVWSFGVLLWELLTGEVPYREIDAlAVAYGVA-------MNKL 218

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1379623326 704 VDPVvqATCCKESLSiviSITNKCISTESWSRPSIEDVLWNLQ 746
Cdd:cd14148   219 TLPI--PSTCPEPFA---RLLEECWDPDPHGRPDFGSILKRLE 256
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
 487-672 3.95e-06

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: 49.30  E-value: 3.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLENGIPVVIRCIPlSKKYSIRNFKLRLDLLAKLRHTHLISLLGHCidgilgerNDSKVFLIYECVSN 566
Cdd:cd05071    17 LGQGCFGEVWMGTWNGTTRVAIKTLK-PGTMSPEAFLQEAQVMKKLRHEKLVQLYAVV--------SEEPIYIVTEYMSK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 567 GNFQTYLSGDScGKIFNWSERLSVLISVAKAIHFLHTgmiPGFFRNRLKTNNILFNENWMAKLSDYGLSIVSEETDASGV 646
Cdd:cd05071    88 GSLLDFLKGEM-GKYLRLPQLVDMAAQIASGMAYVER---MNYVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTAR 163

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1379623326 647 IGES-PNSWQMKK--------LEDDIYSFGFIILE 672
Cdd:cd05071   164 QGAKfPIKWTAPEaalygrftIKSDVWSFGILLTE 198
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
111-325 4.32e-06

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 49.93  E-value: 4.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 111 ATLARLTSLRVLHLVSLGIwGPFPDRIHRLFSLEQLDLSSNYLygSIPPKISTMVSLQILMLGDNFFNgTIPNLFDSSsN 190
Cdd:COG4886   199 EPLGNLTNLEELDLSGNQL-TDLPEPLANLTNLETLDLSNNQL--TDLPELGNLTNLEELDLSNNQLT-DLPPLANLT-N 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 191 LTVFSLKNNKLKGPFPFSILSITTLTNIDMSRNQISGSLQDFTGLSSLEHLDLRENELDSDLPALPKGLISLFLNRNSFS 270
Cdd:COG4886   274 LKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLL 353

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1379623326 271 GQIPKSYGQLNSLQHLDISFNTLTGATPSELFSLPNIIYLNLGSNMLSGTLQNSL 325
Cdd:COG4886   354 LLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLLLTLALL 408
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
 487-742 5.11e-06

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: 48.76  E-value: 5.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKG-KLENGIPV---VIRCIPLSKKYSIRnFKLRLDLLAKLRHTHLISLLGHCIDgilgERNDSKVFlIYE 562
Cdd:cd13983     9 LGRGSFKTVYRAfDTEEGIEVawnEIKLRKLPKAERQR-FKQEIEILKSLKHPNIIKFYDSWES----KSKKEVIF-ITE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 563 CVSNGNFQTYLS--GDSCGKIF-NWSerlsvlISVAKAIHFLHTGMIPGFFRNrLKTNNILFNENW-MAKLSDYGLSIVS 638
Cdd:cd13983    83 LMTSGTLKQYLKrfKRLKLKVIkSWC------RQILEGLNYLHTRDPPIIHRD-LKCDNIFINGNTgEVKIGDLGLATLL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 639 EETDASGVIGeSPNSWQMKKLED------DIYSFGFIILEALVG--PSMFAKREAAVLNAMASFSSQDEWKQIVDPVVQA 710
Cdd:cd13983   156 RQSFAKSVIG-TPEFMAPEMYEEhydekvDIYAFGMCLLEMATGeyPYSECTNAAQIYKKVTSGIKPESLSKVKDPELKD 234

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1379623326 711 tcckeslsivisITNKCISTEsWSRPSIEDVL 742
Cdd:cd13983   235 ------------FIEKCLKPP-DERPSARELL 253
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
164-351 5.23e-06

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 49.55  E-value: 5.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 164 MVSLQILMLGDNFFNGTIPNLFDSSSNLTVFSLKNNKLKGPFPFSILSITTLTNIDMSRNQISGSLQDFTGLSSLEHLDL 243
Cdd:COG4886     3 LLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 244 RENELDSDLPALPKGLISLFLNRNSFSGQipksygqLNSLQHLDISFNTLTgATPSELFSLPNIIYLNLGSNMLSgTLQN 323
Cdd:COG4886    83 SLLLLGLTDLGDLTNLTELDLSGNEELSN-------LTNLESLDLSGNQLT-DLPEELANLTNLKELDLSNNQLT-DLPE 153

                         170       180
                  ....*....|....*....|....*...
gi 1379623326 324 SLRCGRNLSFVDISNNRLIGaLPYSLSN 351
Cdd:COG4886   154 PLGNLTNLKSLDLSNNQLTD-LPEELGN 180
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
 480-672 5.99e-06

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: 48.33  E-value: 5.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 480 NFDNSTF---LGENIYGKLYKGKLeNGIPVVIRCIPLSkkYSIRNFKLRLDLLAKLRHTHLISLLGHCIDGILgerndsk 556
Cdd:cd05083     4 NLQKLTLgeiIGEGEFGAVLQGEY-MGQKVAVKNIKCD--VTAQAFLEETAVMTKLQHKNLVRLLGVILHNGL------- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 557 vFLIYECVSNGNFQTYLSgdSCGK-IFNWSERLSVLISVAKAIHFLHTGMIpgfFRNRLKTNNILFNENWMAKLSDYGLS 635
Cdd:cd05083    74 -YIVMELMSKGNLVNFLR--SRGRaLVPVIQLLQFSLDVAEGMEYLESKKL---VHRDLAARNILVSEDGVAKISDFGLA 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1379623326 636 IVSEETDASG---VIGESPNSWQMKKL--EDDIYSFGFIILE 672
Cdd:cd05083   148 KVGSMGVDNSrlpVKWTAPEALKNKKFssKSDVWSYGVLLWE 189
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
 506-672 6.12e-06

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: 48.58  E-value: 6.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 506 VVIRCIPLS-----KKYSIRNfklRLDLLAKLRHTHLISLlghcIDGILgerNDSKVFLIYECVSNGNFQTYLSgDSCGK 580
Cdd:cd08220    28 VIIKQIPVEqmtkeERQAALN---EVKVLSMLHHPNIIEY----YESFL---EDKALMIVMEYAPGGTLFEYIQ-QRKGS 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 581 IFNWSERLSVLISVAKAIHFLHTGMIpgfFRNRLKTNNILFNENWM-AKLSDYGLS-IVSEETDASGVIGE----SPNSW 654
Cdd:cd08220    97 LLSEEEILHFFVQILLALHHVHSKQI---LHRDLKTQNILLNKKRTvVKIGDFGISkILSSKSKAYTVVGTpcyiSPELC 173

                         170       180
                  ....*....|....*....|
gi 1379623326 655 QMK--KLEDDIYSFGFIILE 672
Cdd:cd08220   174 EGKpyNQKSDIWALGCVLYE 193
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 113-250 6.29e-06

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 47.86  E-value: 6.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 113 LARLTSLRVLHLvslgiwgpFPDRIHR------LFSLEQLDLSSNYLYgSIPPkISTMVSLQILMLGDNFFNgTIPNLfD 186
Cdd:cd21340    20 LSLCKNLKVLYL--------YDNKITKienlefLTNLTHLYLQNNQIE-KIEN-LENLVNLKKLYLGGNRIS-VVEGL-E 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 187 SSSNLTVFSLKNNKLKGPF-----PFSILSI-TTLTNIDMSRNQISgSLQDFTGLSSLEHLDLRENELDS 250
Cdd:cd21340    88 NLTNLEELHIENQRLPPGEkltfdPRSLAALsNSLRVLNISGNNID-SLEPLAPLRNLEQLDASNNQISD 156
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
 487-672 7.03e-06

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: 48.47  E-value: 7.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLE-----NGIPVVIRCIPLSKKYSIRNFKLRLDLLAKLRHTHLISLLGHCIDGilGERNdskVFLIY 561
Cdd:cd14205    12 LGKGNFGSVEMCRYDplqdnTGEVVAVKKLQHSTEEHLRDFEREIEILKSLQHDNIVKYKGVCYSA--GRRN---LRLIM 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 562 ECVSNGNFQTYLSGDScgKIFNWSERLSVLISVAKAIHFLHTGMipgFFRNRLKTNNILFNENWMAKLSDYGLSIVSEET 641
Cdd:cd14205    87 EYLPYGSLRDYLQKHK--ERIDHIKLLQYTSQICKGMEYLGTKR---YIHRDLATRNILVENENRVKIGDFGLTKVLPQD 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1379623326 642 DASGVI---GESPNSWQMKK--------LEDDIYSFGFIILE 672
Cdd:cd14205   162 KEYYKVkepGESPIFWYAPEslteskfsVASDVWSFGVVLYE 203
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
 487-672 8.32e-06

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: 47.95  E-value: 8.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLENGIPVVIRCIPlSKKYSIRNFKLRLDLLAKLRHTHLISLLGHCidgilgeRNDSKVFLIYECVSN 566
Cdd:cd05113    12 LGTGQFGVVKYGKWRGQYDVAIKMIK-EGSMSEDEFIEEAKVMMNLSHEKLVQLYGVC-------TKQRPIFIITEYMAN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 567 GNFQTYLSgdSCGKIFNWSERLSVLISVAKAIHFLHTGMipgFFRNRLKTNNILFNENWMAKLSDYGLS-IVSEETDASG 645
Cdd:cd05113    84 GCLLNYLR--EMRKRFQTQQLLEMCKDVCEAMEYLESKQ---FLHRDLAARNCLVNDQGVVKVSDFGLSrYVLDDEYTSS 158

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1379623326 646 VIGESPNSWQMKKL--------EDDIYSFGFIILE 672
Cdd:cd05113   159 VGSKFPVRWSPPEVlmyskfssKSDVWAFGVLMWE 193
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
 518-745 8.74e-06

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: 48.11  E-value: 8.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 518 SIRNFKLRLDLLAKLRHTHLISLLGHCidgiLGERNdskVFLIYECVSNGNFQTYLSGDSCGK--IFNWSerlsvlISVA 595
Cdd:cd14145    48 TIENVRQEAKLFAMLKHPNIIALRGVC----LKEPN---LCLVMEFARGGPLNRVLSGKRIPPdiLVNWA------VQIA 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 596 KAIHFLHTGMIPGFFRNRLKTNNILFNE--------NWMAKLSDYGLSIVSEETDASGVIGESpnSW--------QMKKL 659
Cdd:cd14145   115 RGMNYLHCEAIVPVIHRDLKSSNILILEkvengdlsNKILKITDFGLAREWHRTTKMSAAGTY--AWmapevirsSMFSK 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 660 EDDIYSFGFIILEALVGPSMFAKREA-AVLNAMAsfssqdeWKQIVDPVvqATCCKESLSiviSITNKCISTESWSRPSI 738
Cdd:cd14145   193 GSDVWSYGVLLWELLTGEVPFRGIDGlAVAYGVA-------MNKLSLPI--PSTCPEPFA---RLMEDCWNPDPHSRPPF 260


                  ....*..
gi 1379623326 739 EDVLWNL 745
Cdd:cd14145   261 TNILDQL 267
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
 492-676 9.29e-06

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: 48.10  E-value: 9.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 492 YGKLYKGKLEnGIPVVIRCIPLSKKYSI----RNFKLRLDLLAKLRHTHLISLLGHCIDgilgernDSKVFLIYECVSNG 567
Cdd:cd14147    16 FGKVYRGSWR-GELVAVKAARQDPDEDIsvtaESVRQEARLFAMLAHPNIIALKAVCLE-------EPNLCLVMEYAAGG 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 568 NFQTYLSGDSCGK--IFNWSerlsvlISVAKAIHFLHT-GMIPGFFRNrLKTNNIL--FN------ENWMAKLSDYGLSI 636
Cdd:cd14147    88 PLSRALAGRRVPPhvLVNWA------VQIARGMHYLHCeALVPVIHRD-LKSNNILllQPienddmEHKTLKITDFGLAR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1379623326 637 VSEETDASGVIGESpnSWQMKK--------LEDDIYSFGFIILEALVG 676
Cdd:cd14147   161 EWHKTTQMSAAGTY--AWMAPEvikastfsKGSDVWSFGVLLWELLTG 206
PHA02988 PHA02988
hypothetical protein; Provisional
 482-745 9.92e-06

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 48.20  E-value: 9.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 482 DNSTFLGENIYGKLYKGKLeNGIPVVIR---CIPLSKKYSIRNFKLRLDLLAKLRHTHLISLLGHCIDGIlgernDS--K 556
Cdd:PHA02988   23 YTSVLIKENDQNSIYKGIF-NNKEVIIRtfkKFHKGHKVLIDITENEIKNLRRIDSNNILKIYGFIIDIV-----DDlpR 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 557 VFLIYECVSNGNFQTYLSGDscgKIFNWSERLSVLISVAKAIHFLHTgmipgfFRNR----LKTNNILFNENWMAKLSDY 632
Cdd:PHA02988   97 LSLILEYCTRGYLREVLDKE---KDLSFKTKLDMAIDCCKGLYNLYK------YTNKpyknLTSVSFLVTENYKLKIICH 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 633 GLSIVSEETDASGVIGESPNSWQMKK-------LEDDIYSFGFIILEALVGPSMFAkreaavlnamaSFSSQDEWKQIVD 705
Cdd:PHA02988  168 GLEKILSSPPFKNVNFMVYFSYKMLNdifseytIKDDIYSLGVVLWEIFTGKIPFE-----------NLTTKEIYDLIIN 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1379623326 706 PVVQATCCKESLSIVISITNKCISTESWSRPSIEDVLWNL 745
Cdd:PHA02988  237 KNNSLKLPLDCPLEIKCIVEACTSHDSIKRPNIKEILYNL 276
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
 487-672 1.04e-05

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: 47.65  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKG-KLENGIPVVIRCIPLskKYSIRNFKLRLDLLAKLRHTHLISLLGHCIdgilgerNDSKVFLIYECVS 565
Cdd:cd06612    11 LGEGSYGSVYKAiHKETGQVVAIKVVPV--EEDLQEIIKEISILKQCDSPYIVKYYGSYF-------KNTDLWIVMEYCG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 566 NGNFQTYLsgDSCGKIFNWSERLSVLISVAKAIHFLHT-GMIpgffrNR-LKTNNILFNENWMAKLSDYGLS--IVSEET 641
Cdd:cd06612    82 AGSVSDIM--KITNKTLTEEEIAAILYQTLKGLEYLHSnKKI-----HRdIKAGNILLNEEGQAKLADFGVSgqLTDTMA 154

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1379623326 642 DASGVIGE----SPNSWQMKKLED--DIYSFGFIILE 672
Cdd:cd06612   155 KRNTVIGTpfwmAPEVIQEIGYNNkaDIWSLGITAIE 191
LRR_8 pfam13855
Leucine rich repeat;
282-341 1.14e-05

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 43.28  E-value: 1.14e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 282 SLQHLDISFNTLTGATPSELFSLPNIIYLNLGSNMLSGTLQNSLRCGRNLSFVDISNNRL 341
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
 487-672 2.07e-05

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: 46.99  E-value: 2.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLENGIPVVIRCIPlSKKYSIRNFKLRLDLLAKLRHTHLISLLGHCidgilgerNDSKVFLIYECVSN 566
Cdd:cd05069    20 LGQGCFGEVWMGTWNGTTKVAIKTLK-PGTMMPEAFLQEAQIMKKLRHDKLVPLYAVV--------SEEPIYIVTEFMGK 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 567 GNFQTYL-SGDscGKIFNWSERLSVLISVAKAIHFLHTgmiPGFFRNRLKTNNILFNENWMAKLSDYGLSIVSEETDASG 645
Cdd:cd05069    91 GSLLDFLkEGD--GKYLKLPQLVDMAAQIADGMAYIER---MNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTA 165

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1379623326 646 VIGES-PNSWQMKK--------LEDDIYSFGFIILE 672
Cdd:cd05069   166 RQGAKfPIKWTAPEaalygrftIKSDVWSFGILLTE 201
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
 487-672 2.16e-05

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: 46.93  E-value: 2.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKL-----ENGIPVVIRCIP-LSKKYSIRNFKLRLDLLAKLRHTHLISLLGHCIdgilgerNDSKVFLI 560
Cdd:cd05090    13 LGECAFGKIYKGHLylpgmDHAQLVAIKTLKdYNNPQQWNEFQQEASLMTELHHPNIVCLLGVVT-------QEQPVCML 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 561 YECVSNGNFQTYL-----------SGDSCGKI---FNWSERLSVLISVAKAIHFLHTGMipgFFRNRLKTNNILFNENWM 626
Cdd:cd05090    86 FEFMNQGDLHEFLimrsphsdvgcSSDEDGTVkssLDHGDFLHIAIQIAAGMEYLSSHF---FVHKDLAARNILVGEQLH 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1379623326 627 AKLSDYGLSIVSEETDASGVIGES--PNSWQMKKL--------EDDIYSFGFIILE 672
Cdd:cd05090   163 VKISDLGLSREIYSSDYYRVQNKSllPIRWMPPEAimygkfssDSDIWSFGVVLWE 218
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
 492-672 2.90e-05

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: 46.57  E-value: 2.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 492 YGKLYKGKLENGIpVVIRCIPLSKKYSIRNfKLRLDLLAKLRHTHLISLLGHcidGILGERNDSKVFLIYECVSNGNFQT 571
Cdd:cd14141     8 FGCVWKAQLLNEY-VAVKIFPIQDKLSWQN-EYEIYSLPGMKHENILQFIGA---EKRGTNLDVDLWLITAFHEKGSLTD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 572 YLSGDscgkIFNWSERLSVLISVAKAIHFLHT-------GMIPGFFRNRLKTNNILFNENWMAKLSDYGLSIVSEETDAS 644
Cdd:cd14141    83 YLKAN----VVSWNELCHIAQTMARGLAYLHEdipglkdGHKPAIAHRDIKSKNVLLKNNLTACIADFGLALKFEAGKSA 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1379623326 645 G---------------VIGESPNSWQMKKLEDDIYSFGFIILE 672
Cdd:cd14141   159 GdthgqvgtrrymapeVLEGAINFQRDAFLRIDMYAMGLVLWE 201
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
 492-639 3.25e-05

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: 46.55  E-value: 3.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 492 YGKLYKGKLENGIpVVIRCIPLSKKYSIRNfKLRLDLLAKLRHTHLisLLGHCIDGIlGERNDSKVFLIYECVSNGNFQT 571
Cdd:cd14053     8 FGAVWKAQYLNRL-VAVKIFPLQEKQSWLT-EREIYSLPGMKHENI--LQFIGAEKH-GESLEAEYWLITEFHERGSLCD 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1379623326 572 YLSGDscgkIFNWSERLSVLISVAKAIHFLHTGmIPGFF---------RNrLKTNNILFNENWMAKLSDYGLSIVSE 639
Cdd:cd14053    83 YLKGN----VISWNELCKIAESMARGLAYLHED-IPATNgghkpsiahRD-FKSKNVLLKSDLTACIADFGLALKFE 153
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
 519-746 3.68e-05

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: 46.23  E-value: 3.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 519 IRNFKLRLDLLAKLRHTHLISLLGHCIdgilgerNDSKVFLIYECVSNGNFQTYLSGDSC--GKIFNWSerlsvlISVAK 596
Cdd:cd14061    37 LENVRQEARLFWMLRHPNIIALRGVCL-------QPPNLCLVMEYARGGALNRVLAGRKIppHVLVDWA------IQIAR 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 597 AIHFLHTGMIPGFFRNRLKTNNILFNE--------NWMAKLSDYGLSIVSEET---DASG--------VIGESPNSwqmk 657
Cdd:cd14061   104 GMNYLHNEAPVPIIHRDLKSSNILILEaienedleNKTLKITDFGLAREWHKTtrmSAAGtyawmapeVIKSSTFS---- 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 658 kLEDDIYSFGFIILEALVGPSMFAKREA-AVLNAMASfssqdewKQIVDPVvqATCCKESLSiviSITNKCISTESWSRP 736
Cdd:cd14061   180 -KASDVWSYGVLLWELLTGEVPYKGIDGlAVAYGVAV-------NKLTLPI--PSTCPEPFA---QLMKDCWQPDPHDRP 246

                         250
                  ....*....|
gi 1379623326 737 SIEDVLWNLQ 746
Cdd:cd14061   247 SFADILKQLE 256
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
 516-748 3.91e-05

Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK2 is widely expressed and has been shown to be epigenetically silenced in gliomas. It inhibits cell growth by acting as a negative regulator of MEK1-ERK1/2 signaling. WNK2 modulates growth factor-induced cancer cell proliferation, suggesting that it may be a tumor suppressor gene. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. The WNK2-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 46.22  E-value: 3.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 516 KYSIRNFKLRLDLLAKLRHTHLISLLGHCIDGILGERNdskVFLIYECVSNGNFQTYLSGDSCGK---IFNWSERlsvli 592
Cdd:cd14032    41 KVERQRFKEEAEMLKGLQHPNIVRFYDFWESCAKGKRC---IVLVTELMTSGTLKTYLKRFKVMKpkvLRSWCRQ----- 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 593 sVAKAIHFLHTGMIPGFFRNrLKTNNILFN-ENWMAKLSDYGLSIVSEETDASGVIGE----SPNSWQMKKLED-DIYSF 666
Cdd:cd14032   113 -ILKGLLFLHTRTPPIIHRD-LKCDNIFITgPTGSVKIGDLGLATLKRASFAKSVIGTpefmAPEMYEEHYDESvDVYAF 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 667 GFIILEALVG--PSMFAKREAAVLNAMASFSSQDEWKQIVDPVVQatcckeslsiviSITNKCISTESWSRPSIEDVLWN 744
Cdd:cd14032   191 GMCMLEMATSeyPYSECQNAAQIYRKVTCGIKPASFEKVTDPEIK------------EIIGECICKNKEERYEIKDLLSH 258


                  ....
gi 1379623326 745 LQYA 748
Cdd:cd14032   259 AFFA 262
LRR_8 pfam13855
Leucine rich repeat;
213-291 4.17e-05

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 41.74  E-value: 4.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 213 TTLTNIDMSRNQISgSLQD--FTGLSSLEHLDLRENELDSdlpalpkglislfLNRNSFSGqipksygqLNSLQHLDISF 290
Cdd:pfam13855   1 PNLRSLDLSNNRLT-SLDDgaFKGLSNLKVLDLSNNLLTT-------------LSPGAFSG--------LPSLRYLDLSG 58


                  .
gi 1379623326 291 N 291
Cdd:pfam13855  59 N 59
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
 487-635 4.36e-05

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: 46.15  E-value: 4.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKG--KLENGIpVVIRCIPLSKKYSIRNFKLR-LDLLAKLRHTHLISLlgHciDGILGERNdskVFLIYEC 563
Cdd:cd07873    10 LGEGTYATVYKGrsKLTDNL-VALKEIRLEHEEGAPCTAIReVSLLKDLKHANIVTL--H--DIIHTEKS---LTLVFEY 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1379623326 564 VsNGNFQTYLsgDSCGKIFNWSERLSVLISVAKAIHFLHTGMIpgfFRNRLKTNNILFNENWMAKLSDYGLS 635
Cdd:cd07873    82 L-DKDLKQYL--DDCGNSINMHNVKLFLFQLLRGLAYCHRRKV---LHRDLKPQNLLINERGELKLADFGLA 147
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
 487-672 4.57e-05

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: 46.14  E-value: 4.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKL-ENGI---PVVIRCIPLSKKYSIRNFKLRLDLLAKL-RHTHLISLLGHCidgilgeRNDSKVFLIY 561
Cdd:cd05088    15 IGEGNFGQVLKARIkKDGLrmdAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGAC-------EHRGYLYLAI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 562 ECVSNGNFQTYLS-------------GDSCGKIFNWSERLSVLISVAKAIHFLHTGMipgFFRNRLKTNNILFNENWMAK 628
Cdd:cd05088    88 EYAPHGNLLDFLRksrvletdpafaiANSTASTLSSQQLLHFAADVARGMDYLSQKQ---FIHRDLAARNILVGENYVAK 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1379623326 629 LSDYGLSiVSEETDASGVIGESPNSW--------QMKKLEDDIYSFGFIILE 672
Cdd:cd05088   165 IADFGLS-RGQEVYVKKTMGRLPVRWmaieslnySVYTTNSDVWSYGVLLWE 215
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
 488-674 6.35e-05

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: 45.24  E-value: 6.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 488 GENIYGKL-YKGKLEngIPVVIRCipLSKKYS---IRNFKLRLDLLAKLRHTHLISLLGHCIDGilgerndSKVFLIYEC 563
Cdd:cd05066    18 GEVCSGRLkLPGKRE--IPVAIKT--LKAGYTekqRRDFLSEASIMGQFDHPNIIHLEGVVTRS-------KPVMIVTEY 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 564 VSNGNFQTYLSGDScGKiFNWSERLSVLISVAKAIHFLhTGMipGFFRNRLKTNNILFNENWMAKLSDYGLSIVSEE--- 640
Cdd:cd05066    87 MENGSLDAFLRKHD-GQ-FTVIQLVGMLRGIASGMKYL-SDM--GYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDdpe 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1379623326 641 ---TDASGVIG---ESPNSWQMKKLE--DDIYSFGFIILEAL 674
Cdd:cd05066   162 aayTTRGGKIPirwTAPEAIAYRKFTsaSDVWSYGIVMWEVM 203
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
 594-644 7.93e-05

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: 44.98  E-value: 7.93e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1379623326 594 VAKAIHFLHT-GMIpgffRNRLKTNNILFNENWMAKLSDYGLSIVSEETDAS 644
Cdd:cd14010   103 LVRGLHYIHSkGII----YCDLKPSNILLDGNGTLKLSDFGLARREGEILKE 150
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
 487-672 8.64e-05

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: 45.00  E-value: 8.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKL---ENGIPVVIRC--IPLSKKYSIRNFKLRLDLLAKLRHTHLISLLGHCIDGILGERNDSKVfLIY 561
Cdd:cd05075     8 LGEGEFGSVMEGQLnqdDSVLKVAVKTmkIAICTRSEMEDFLSEAVCMKEFDHPNVMRLIGVCLQNTESEGYPSPV-VIL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 562 ECVSNGNFQTYLS----GDScgKIFNWSERL-SVLISVAKAIHFLHTgmiPGFFRNRLKTNNILFNENWMAKLSDYGLS- 635
Cdd:cd05075    87 PFMKHGDLHSFLLysrlGDC--PVYLPTQMLvKFMTDIASGMEYLSS---KNFIHRDLAARNCMLNENMNVCVADFGLSk 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1379623326 636 -IVSEETDASGVIGESPNSW-QMKKLED-------DIYSFGFIILE 672
Cdd:cd05075   162 kIYNGDYYRQGRISKMPVKWiAIESLADrvyttksDVWSFGVTMWE 207
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
 487-635 9.64e-05

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: 45.10  E-value: 9.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGK-LENGIPVVIRCIPL-SKKYSIRNFKLR-LDLLAKLRHTHLISLLghciDGILGErndSKVFLIYEC 563
Cdd:cd07861     8 IGEGTYGVVYKGRnKKTGQIVAMKKIRLeSEEEGVPSTAIReISLLKELQHPNIVCLE----DVLMQE---NRLYLVFEF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1379623326 564 VSNgNFQTYLSGDSCGKIFNWSERLSVLISVAKAIHFLHTGMIpgfFRNRLKTNNILFNENWMAKLSDYGLS 635
Cdd:cd07861    81 LSM-DLKKYLDSLPKGKYMDAELVKSYLYQILQGILFCHSRRV---LHRDLKPQNLLIDNKGVIKLADFGLA 148
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
 492-672 9.86e-05

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: 45.02  E-value: 9.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 492 YGKLYKGKLENGIpVVIRCIPLSKKYSIRNFKLRLDLlAKLRHTHLISLlghcidgILGERNDS----KVFLIYECVSNG 567
Cdd:cd14140     8 FGCVWKAQLMNEY-VAVKIFPIQDKQSWQSEREIFST-PGMKHENLLQF-------IAAEKRGSnlemELWLITAFHDKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 568 NFQTYLSGDscgkIFNWSERLSVLISVAKAIHFLHT--------GMIPGFFRNRLKTNNILFNENWMAKLSDYGLSIVSE 639
Cdd:cd14140    79 SLTDYLKGN----IVSWNELCHIAETMARGLSYLHEdvprckgeGHKPAIAHRDFKSKNVLLKNDLTAVLADFGLAVRFE 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1379623326 640 ----ETDASGVIG----------ESPNSWQMKK-LEDDIYSFGFIILE 672
Cdd:cd14140   155 pgkpPGDTHGQVGtrrymapevlEGAINFQRDSfLRIDMYAMGLVLWE 202
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
 487-672 9.92e-05

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: 45.06  E-value: 9.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLENGIPVVIRCIPlSKKYSIRNFKLRLDLLAKLRHTHLISLLGhcidgILGERndsKVFLIYECVSN 566
Cdd:cd05070    17 LGNGQFGEVWMGTWNGNTKVAIKTLK-PGTMSPESFLEEAQIMKKLKHDKLVQLYA-----VVSEE---PIYIVTEYMSK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 567 GNFQTYLSgDSCGKIFNWSERLSVLISVAKAIHFLHTgmiPGFFRNRLKTNNILFNENWMAKLSDYGLSIVSEETDASGV 646
Cdd:cd05070    88 GSLLDFLK-DGEGRALKLPNLVDMAAQVAAGMAYIER---MNYIHRDLRSANILVGNGLICKIADFGLARLIEDNEYTAR 163

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1379623326 647 IGES-PNSWQMKK--------LEDDIYSFGFIILE 672
Cdd:cd05070   164 QGAKfPIKWTAPEaalygrftIKSDVWSFGILLTE 198
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
 487-674 1.05e-04

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: 44.58  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLE----NGIPVVIRCIPLSKKYSIRN-FKLRLDLLAKLRHTHLISLlghciDGILGERNDskVFLIY 561
Cdd:cd05063    13 IGAGEFGEVFRGILKmpgrKEVAVAIKTLKPGYTEKQRQdFLSEASIMGQFSHHNIIRL-----EGVVTKFKP--AMIIT 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 562 ECVSNGNFQTYLSgDSCGKiFNWSERLSVLISVAKAIHFLhTGMipGFFRNRLKTNNILFNENWMAKLSDYGLSIVSEE- 640
Cdd:cd05063    86 EYMENGALDKYLR-DHDGE-FSSYQLVGMLRGIAAGMKYL-SDM--NYVHRDLAARNILVNSNLECKVSDFGLSRVLEDd 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1379623326 641 -----TDASGVIG---ESPNSWQMKKL--EDDIYSFGFIILEAL 674
Cdd:cd05063   161 pegtyTTSGGKIPirwTAPEAIAYRKFtsASDVWSFGIVMWEVM 204
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
 487-672 1.09e-04

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: 45.03  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLEnGIPVVIRCIPLSKKYS-IRNFKLRLDLLakLRHThliSLLGHCIDGILGERNDSKVFLIYECVS 565
Cdd:cd14220     3 IGKGRYGEVWMGKWR-GEKVAVKVFFTTEEASwFRETEIYQTVL--MRHE---NILGFIAADIKGTGSWTQLYLITDYHE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 566 NGNFQTYLSGDScgkiFNWSERLSVLISVAKAIHFLHTGMI-----PGFFRNRLKTNNILFNENWMAKLSDYGLSIV--- 637
Cdd:cd14220    77 NGSLYDFLKCTT----LDTRALLKLAYSAACGLCHLHTEIYgtqgkPAIAHRDLKSKNILIKKNGTCCIADLGLAVKfns 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1379623326 638 -SEETD-------------ASGVIGESPNSWQMKK-LEDDIYSFGFIILE 672
Cdd:cd14220   153 dTNEVDvplntrvgtkrymAPEVLDESLNKNHFQAyIMADIYSFGLIIWE 202
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
 534-669 1.34e-04

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: 44.40  E-value: 1.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 534 HTHLISLLGHCIDGILGERNDSKVFLIYECVSNGNFQTYLSGDScgkifnWSERLSVLISVAKAIHFLHTgmiPGFFRNR 613
Cdd:cd13975    57 HERIVSLHGSVIDYSYGGGSSIAVLLIMERLHRDLYTGIKAGLS------LEERLQIALDVVEGIRFLHS---QGLVHRD 127

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1379623326 614 LKTNNILFNENWMAKLSDYGLSIvsEETDASGVIGESPnsWQMK------KLED--DIYSFGFI 669
Cdd:cd13975   128 IKLKNVLLDKKNRAKITDLGFCK--PEAMMSGSIVGTP--IHMApelfsgKYDNsvDVYAFGIL 187
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
 511-704 1.45e-04

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: 44.35  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 511 IPLSKKYSIRNFKLR-LDLLAKLRHTHLISLLGHCidgiLGERNDSKVFLIY-ECVS-------NGNFQTylsgDSCGKI 581
Cdd:cd06620    38 IHIDAKSSVRKQILReLQILHECHSPYIVSFYGAF----LNENNNIIICMEYmDCGSldkilkkKGPFPE----EVLGKI 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 582 -FNWSERLSVLISVAKAIHflhtgmipgffRNrLKTNNILFNENWMAKLSDYGLSIVSEETDASGVIGES----PNSWQM 656
Cdd:cd06620   110 aVAVLEGLTYLYNVHRIIH-----------RD-IKPSNILVNSKGQIKLCDFGVSGELINSIADTFVGTStymsPERIQG 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1379623326 657 KK--LEDDIYSFGFIILEALVGPSMFAKREAAVLNAMASFSSQDEWKQIV 704
Cdd:cd06620   178 GKysVKSDVWSLGLSIIELALGEFPFAGSNDDDDGYNGPMGILDLLQRIV 227
LRR_8 pfam13855
Leucine rich repeat;
258-317 1.70e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 40.20  E-value: 1.70e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 258 GLISLFLNRNSFSGQIPKSYGQLNSLQHLDISFNTLTGATPSELFSLPNIIYLNLGSNML 317
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
 487-679 1.82e-04

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: 44.00  E-value: 1.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKL---YKGKLenGIPVVIRCIplSKKYSIRNFKLR-----LDLLAKLRHTHLISLLGhcidgILgERNDSKVF 558
Cdd:cd14165     9 LGEGSYAKVksaYSERL--KCNVAIKII--DKKKAPDDFVEKflpreLEILARLNHKSIIKTYE-----IF-ETSDGKVY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 559 LIYECVSNGNFQTYLSgdsCGKIFNWSERLSVLISVAKAIHFLHTgmiPGFFRNRLKTNNILFNENWMAKLSDYGLSiVS 638
Cdd:cd14165    79 IVMELGVQGDLLEFIK---LRGALPEDVARKMFHQLSSAIKYCHE---LDIVHRDLKCENLLLDKDFNIKLTDFGFS-KR 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1379623326 639 EETDASGVIGES-----------PNSWQMKKLED---DIYSFGfIILEALVGPSM 679
Cdd:cd14165   152 CLRDENGRIVLSktfcgsaayaaPEVLQGIPYDPriyDIWSLG-VILYIMVCGSM 205
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
 487-748 1.89e-04

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: 43.64  E-value: 1.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLeNGIPVVIRCIPLSKKYSIRNfklrldlLAKLRHTHLISLLGHCidgilgerNDSKVF-LIYECVS 565
Cdd:cd14059     1 LGSGAQGAVFLGKF-RGEEVAVKKVRDEKETDIKH-------LRKLNHPNIIKFKGVC--------TQAPCYcILMEYCP 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 566 NGNFQTYLSGD---SCGKIFNWSERLsvlisvAKAIHFLHTGMIpgfFRNRLKTNNILFNENWMAKLSDYGLSivSEETD 642
Cdd:cd14059    65 YGQLYEVLRAGreiTPSLLVDWSKQI------ASGMNYLHLHKI---IHRDLKSPNVLVTYNDVLKISDFGTS--KELSE 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 643 ASG--------------VIGESPNSWQMkkledDIYSFGFIILEALVGPSMFAKRE-AAVLNAMASFSSQdewkqivDPV 707
Cdd:cd14059   134 KSTkmsfagtvawmapeVIRNEPCSEKV-----DIWSFGVVLWELLTGEIPYKDVDsSAIIWGVGSNSLQ-------LPV 201

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1379623326 708 vqATCCKESLSIVIsitNKCISTESWSRPSIEDVLWNLQYA 748
Cdd:cd14059   202 --PSTCPDGFKLLM---KQCWNSKPRNRPSFRQILMHLDIA 237
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
 487-741 2.03e-04

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: 43.85  E-value: 2.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLENGIP------VVIRCIPLSKKYSIR-NFKLRLDLLAKLRHTHLISLLGHCIdgilgerNDSKVFL 559
Cdd:cd05091    14 LGEDRFGKVYKGHLFGTAPgeqtqaVAIKTLKDKAEGPLReEFRHEAMLRSRLQHPNIVCLLGVVT-------KEQPMSM 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 560 IYECVSNGNFQTYL----------SGD---SCGKIFNWSERLSVLISVAKAIHFLHTGMIpgfFRNRLKTNNILFNENWM 626
Cdd:cd05091    87 IFSYCSHGDLHEFLvmrsphsdvgSTDddkTVKSTLEPADFLHIVTQIAAGMEYLSSHHV---VHKDLATRNVLVFDKLN 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 627 AKLSDYGLSIVSEETDASGVIGES--PNSWQMKK--------LEDDIYSFGFIILEALvgpsmfakreAAVLNAMASFSS 696
Cdd:cd05091   164 VKISDLGLFREVYAADYYKLMGNSllPIRWMSPEaimygkfsIDSDIWSYGVVLWEVF----------SYGLQPYCGYSN 233

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1379623326 697 QDEWKQIVDPVVqATCCKESLSIVISITNKCISTESWSRPSIEDV 741
Cdd:cd05091   234 QDVIEMIRNRQV-LPCPDDCPAWVYTLMLECWNEFPSRRPRFKDI 277
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
 487-635 2.19e-04

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: 43.80  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYK------GKL-----------ENGIPV-VIRCIPLSKKysirnfklrldlLAKLRHTHLISLLGHCidgi 548
Cdd:cd07838     7 IGEGAYGTVYKardlqdGRFvalkkvrvplsEEGIPLsTIREIALLKQ------------LESFEHPNVVRLLDVC---- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 549 LGERNDS--KVFLIYECVSNgNFQTYL-----SGDSCGKIFNWSERLsvlisvAKAIHFLHTGMIpgFFRNrLKTNNILF 621
Cdd:cd07838    71 HGPRTDRelKLTLVFEHVDQ-DLATYLdkcpkPGLPPETIKDLMRQL------LRGLDFLHSHRI--VHRD-LKPQNILV 140

                         170
                  ....*....|....
gi 1379623326 622 NENWMAKLSDYGLS 635
Cdd:cd07838   141 TSDGQVKLADFGLA 154
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
 532-672 2.56e-04

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: 43.62  E-value: 2.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 532 LRHThliSLLGHCIDGILGERNDSKVFLIYECVSNGNFQTYLSGDscgkIFNWSERLSVLISVAKAIHFLHTGMI----- 606
Cdd:cd14144    46 MRHE---NILGFIAADIKGTGSWTQLYLITDYHENGSLYDFLRGN----TLDTQSMLKLAYSAACGLAHLHTEIFgtqgk 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 607 PGFFRNRLKTNNILFNENWMAKLSDYGLSI--VSE--ETD-------------ASGVIGES--PNSWQMKKLEDdIYSFG 667
Cdd:cd14144   119 PAIAHRDIKSKNILVKKNGTCCIADLGLAVkfISEtnEVDlppntrvgtkrymAPEVLDESlnRNHFDAYKMAD-MYSFG 197


                  ....*
gi 1379623326 668 FIILE 672
Cdd:cd14144   198 LVLWE 202
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
 487-644 2.57e-04

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: 43.33  E-value: 2.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLEN-GIPVVIRCIPLSKKYSIRNFKLR-----LDLLAKLRHTHLISLLGhcidgILgERNdSKVFLI 560
Cdd:cd14080     8 IGEGSYSKVKLAEYTKsGLKEKVACKIIDKKKAPKDFLEKflpreLEILRKLRHPNIIQVYS-----IF-ERG-SKVFIF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 561 YECVSNGNFQTYLSgdSCGKIfnwSERLSVLI--SVAKAIHFLHTGMIPgffrNR-LKTNNILFNENWMAKLSDYGLSIV 637
Cdd:cd14080    81 MEYAEHGDLLEYIQ--KRGAL---SESQARIWfrQLALAVQYLHSLDIA----HRdLKCENILLDSNNNVKLSDFGFARL 151


                  ....*..
gi 1379623326 638 SEETDAS 644
Cdd:cd14080   152 CPDDDGD 158
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
 487-679 3.22e-04

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: 43.31  E-value: 3.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLENGIPVVIRCIPLSKKYSiRNFKLRLDLLAKLRHTHLISLLGHCIdgilgerNDSKVFLIYECVSN 566
Cdd:cd05114    12 LGSGLFGVVRLGKWRAQYKVAIKAIREGAMSE-EDFIEEAKVMMKLTHPKLVQLYGVCT-------QQKPIYIVTEFMEN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 567 GNFQTYLSGDScGKiFNWSERLSVLISVAKAIHFLHTGmipGFFRNRLKTNNILFNENWMAKLSDYGLS---IVSEETDA 643
Cdd:cd05114    84 GCLLNYLRQRR-GK-LSRDMLLSMCQDVCEGMEYLERN---NFIHRDLAARNCLVNDTGVVKVSDFGMTryvLDDQYTSS 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1379623326 644 SG----VIGESPNSWQMKKL--EDDIYSFGFIILEALVGPSM 679
Cdd:cd05114   159 SGakfpVKWSPPEVFNYSKFssKSDVWSFGVLMWEVFTEGKM 200
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
 487-674 3.36e-04

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: 43.32  E-value: 3.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLE----NGIPVVIRCipLSKKYS---IRNFKLRLDLLAKLRHTHLISLlghciDGILgeRNDSKVFL 559
Cdd:cd05065    12 IGAGEFGEVCRGRLKlpgkREIFVAIKT--LKSGYTekqRRDFLSEASIMGQFDHPNIIHL-----EGVV--TKSRPVMI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 560 IYECVSNGNFQTYLSGDScGKiFNWSERLSVLISVAKAIHFLhTGMipGFFRNRLKTNNILFNENWMAKLSDYGLSIVSE 639
Cdd:cd05065    83 ITEFMENGALDSFLRQND-GQ-FTVIQLVGMLRGIAAGMKYL-SEM--NYVHRDLAARNILVNSNLVCKVSDFGLSRFLE 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1379623326 640 E-----TDASGVIGESPNSW------QMKKL--EDDIYSFGFIILEAL 674
Cdd:cd05065   158 DdtsdpTYTSSLGGKIPIRWtapeaiAYRKFtsASDVWSYGIVMWEVM 205
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 78-208 3.58e-04

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 44.07  E-value: 3.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326  78 SIFGDKPNKgrgFDGFAIPNQTLSQSFSMDSFVATLARLTSLRVLHLVSLGIWGPFPDRIHRLFSLEQLDLSSNYLYGSI 157
Cdd:PLN00113  463 KFFGGLPDS---FGSKRLENLDLSRNQFSGAVPRKLGSLSELMQLKLSENKLSGEIPDELSSCKKLVSLDLSHNQLSGQI 539

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1379623326 158 PPKISTMVSLQILMLGDNFFNGTIPNLFDSSSNLTVFSLKNNKLKGPFPFS 208
Cdd:PLN00113  540 PASFSEMPVLSQLDLSQNQLSGEIPKNLGNVESLVQVNISHNHLHGSLPST 590
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 143-341 4.71e-04

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 43.11  E-value: 4.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 143 LEQLDLSSNYLYGS----IPPKISTMVSLQILMLGDNFFNGTIPNLFDSSSNLTvfslknnklkgpfpfsilSITTLTNI 218
Cdd:cd00116    25 LQVLRLEGNTLGEEaakaLASALRPQPSLKELCLSLNETGRIPRGLQSLLQGLT------------------KGCGLQEL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 219 DMSRNQIS----GSLQDFTGLSSLEHLDLRENELDSD--------LPALPKGLISLFLNRNSFSGQ----IPKSYGQLNS 282
Cdd:cd00116    87 DLSDNALGpdgcGVLESLLRSSSLQELKLNNNGLGDRglrllakgLKDLPPALEKLVLGRNRLEGAsceaLAKALRANRD 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1379623326 283 LQHLDISFNTLTGA----TPSELFSLPNIIYLNLGSNML----SGTLQNSLRCGRNLSFVDISNNRL 341
Cdd:cd00116   167 LKELNLANNGIGDAgiraLAEGLKANCNLEVLDLNNNGLtdegASALAETLASLKSLEVLNLGDNNL 233
PTK_Jak2_rpt1 cd05078
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely ...
 487-745 4.72e-04

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: 42.63  E-value: 4.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLE--------NGIPVVIRCIPLSKKYSIRNFKLRLDLLAKLRHTHLISLLGHCidgILGERNdskvF 558
Cdd:cd05078     7 LGQGTFTKIFKGIRRevgdygqlHETEVLLKVLDKAHRNYSESFFEAASMMSQLSHKHLVLNYGVC---VCGDEN----I 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 559 LIYECVSNGNFQTYLSGDScgKIFNWSERLSVLISVAKAIHFLH-TGMIPGFF--RNRL-------KTNNILFnenwmAK 628
Cdd:cd05078    80 LVQEYVKFGSLDTYLKKNK--NCINILWKLEVAKQLAWAMHFLEeKTLVHGNVcaKNILlireedrKTGNPPF-----IK 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 629 LSDYGLSIVSEETD-----ASGVIGESPNSWQMKKLEDDIYSFGFIILEALVGpsmfAKREAAVLNAMASFSSQDEWKQI 703
Cdd:cd05078   153 LSDPGISITVLPKDillerIPWVPPECIENPKNLSLATDKWSFGTTLWEICSG----GDKPLSALDSQRKLQFYEDRHQL 228

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1379623326 704 vdPVVQATcckeSLSIVIsitNKCISTESWSRPSIEDVLWNL 745
Cdd:cd05078   229 --PAPKWT----ELANLI---NNCMDYEPDHRPSFRAIIRDL 261
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
 507-672 4.97e-04

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: 42.62  E-value: 4.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 507 VIRCIPLSKKysirNFKLRLDLLAKLRHTHLISLLGhcidgILgeRNDSKVFLIYECVSNGNFQTYLSGDSCgkiFNWSE 586
Cdd:cd14222    26 LIRCDEETQK----TFLTEVKVMRSLDHPNVLKFIG-----VL--YKDKRLNLLTEFIEGGTLKDFLRADDP---FPWQQ 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 587 RLSVLISVAKAIHFLHTGMIpgfFRNRLKTNNILFNENWMAKLSDYGLS--IVSEETDAS-------------------- 644
Cdd:cd14222    92 KVSFAKGIASGMAYLHSMSI---IHRDLNSHNCLIKLDKTVVVADFGLSrlIVEEKKKPPpdkpttkkrtlrkndrkkry 168

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1379623326 645 GVIGE----SPNSWQMKKLED--DIYSFGFIILE 672
Cdd:cd14222   169 TVVGNpywmAPEMLNGKSYDEkvDIFSFGIVLCE 202
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
 528-635 5.03e-04

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: 42.53  E-value: 5.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 528 LLAKLRHTHLISLLGHCIDgilgeRNDSKVFLIYECVSNGNFQTYLS-----GDSCGKIFNWSerlsVLISVAKAIHFLH 602
Cdd:cd08217    52 ILRELKHPNIVRYYDRIVD-----RANTTLYIVMEYCEGGDLAQLIKkckkeNQYIPEEFIWK----IFTQLLLALYECH 122

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1379623326 603 TGMIPGffrNR-----LKTNNILFNENWMAKLSDYGLS 635
Cdd:cd08217   123 NRSVGG---GKilhrdLKPANIFLDSDNNVKLGDFGLA 157
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
 528-676 6.08e-04

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: 42.33  E-value: 6.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 528 LLAKLRHTHLISLLGHCIDgilgernDSKVFLIYECVSNGNFQTYLSGDSCGKIFNWSERLS--VLIS----VAKAIHFL 601
Cdd:cd14146    46 LFSMLRHPNIIKLEGVCLE-------EPNLCLVMEFARGGTLNRALAAANAAPGPRRARRIPphILVNwavqIARGMLYL 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 602 HTGMIPGFFRNRLKTNNILFNE--------NWMAKLSDYGLSIVSEETDASGVIGESpnSWQMKKL--------EDDIYS 665
Cdd:cd14146   119 HEEAVVPILHRDLKSSNILLLEkiehddicNKTLKITDFGLAREWHRTTKMSAAGTY--AWMAPEViksslfskGSDIWS 196

                         170
                  ....*....|.
gi 1379623326 666 FGFIILEALVG 676
Cdd:cd14146   197 YGVLLWELLTG 207
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
 487-674 6.41e-04

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: 42.52  E-value: 6.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKL--ENG--IPVVIRCIPL--SKKYSIRNFKLRLDLLAKLRHTHLISLLGHCIDGILGERNDSKVfLI 560
Cdd:cd05035     7 LGEGEFGSVMEAQLkqDDGsqLKVAVKTMKVdiHTYSEIEEFLSEAACMKDFDHPNVMRLIGVCFTASDLNKPPSPM-VI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 561 YECVSNGNFQTYLSGDSCG---KIFNWSERLSVLISVAKAIHFLHTgmiPGFFRNRLKTNNILFNENWMAKLSDYGLS-- 635
Cdd:cd05035    86 LPFMKHGDLHSYLLYSRLGglpEKLPLQTLLKFMVDIAKGMEYLSN---RNFIHRDLAARNCMLDENMTVCVADFGLSrk 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1379623326 636 IVSEETDASGVIGESPNSW-QMKKLED-------DIYSFGFIILEAL 674
Cdd:cd05035   163 IYSGDYYRQGRISKMPVKWiALESLADnvytsksDVWSFGVTMWEIA 209
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
 479-680 6.61e-04

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: 42.20  E-value: 6.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 479 NNFDNSTFLGENIYGKLYKGKL-ENGIPVVIRCipLSKKYSIRNFKLRL-----DLLAKLRHTHLISLLGHCIDgilger 552
Cdd:cd05581     1 NDFKFGKPLGEGSYSTVVLAKEkETGKEYAIKV--LDKRHIIKEKKVKYvtiekEVLSRLAHPGIVKLYYTFQD------ 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 553 nDSKVFLIYECVSNGNFQTYLSgdscgKIFNWSERLSVLIS--VAKAIHFLHT-GMIpgffrNR-LKTNNILFNENWMAK 628
Cdd:cd05581    73 -ESKLYFVLEYAPNGDLLEYIR-----KYGSLDEKCTRFYTaeIVLALEYLHSkGII-----HRdLKPENILLDEDMHIK 141

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1379623326 629 LSDYG----LSIVSEETDASGVIGESPNSWQMKK--------------LED-------DIYSFGFIILEALVGPSMF 680
Cdd:cd05581   142 ITDFGtakvLGPDSSPESTKGDADSQIAYNQARAasfvgtaeyvspelLNEkpagkssDLWALGCIIYQMLTGKPPF 218
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
 487-672 6.90e-04

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: 42.42  E-value: 6.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGK-LENGIPVVIRCIPLSKKYSIRNFKLRLDLLAKLRHTHLISLLGhcidgilGERNDSKVFLIYECVS 565
Cdd:cd06611    13 LGDGAFGKVYKAQhKETGLFAAAKIIQIESEEELEDFMVEIDILSECKHPNIVGLYE-------AYFYENKLWILIEFCD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 566 NGNFQTYLsgDSCGKIFNWSERLSVLISVAKAIHFLHTGMIpgfFRNRLKTNNILFNENWMAKLSDYGLSIVSEETDA-- 643
Cdd:cd06611    86 GGALDSIM--LELERGLTEPQIRYVCRQMLEALNFLHSHKV---IHRDLKAGNILLTLDGDVKLADFGVSAKNKSTLQkr 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1379623326 644 SGVIGeSPNsWQMKKL-------------EDDIYSFGFIILE 672
Cdd:cd06611   161 DTFIG-TPY-WMAPEVvacetfkdnpydyKADIWSLGITLIE 200
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
 521-741 7.72e-04

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: 42.27  E-value: 7.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 521 NFKLRLDLLAKLRHTHLISLLGHCIdgilgerNDSKVFLIYECVSNGNFQTYLSGDSCGKIFNWSERLSVlISVAKAIHF 600
Cdd:cd05097    63 DFLKEIKIMSRLKNPNIIRLLGVCV-------SDDPLCMITEYMENGDLNQFLSQREIESTFTHANNIPS-VSIANLLYM 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 601 ---LHTGM----IPGFFRNRLKTNNILFNENWMAKLSDYGLSIVSEETDASGVIGES--PNSWQ------MKKLE--DDI 663
Cdd:cd05097   135 avqIASGMkylaSLNFVHRDLATRNCLVGNHYTIKIADFGMSRNLYSGDYYRIQGRAvlPIRWMawesilLGKFTtaSDV 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 664 YSFGFIILEALV----GPSMFAKREAAVLNAMASFSSQDewKQIVdpVVQATCCKESlsiVISITNKCISTESWSRPSIE 739
Cdd:cd05097   215 WAFGVTLWEMFTlckeQPYSLLSDEQVIENTGEFFRNQG--RQIY--LSQTPLCPSP---VFKLMMRCWSRDIKDRPTFN 287


                  ..
gi 1379623326 740 DV 741
Cdd:cd05097   288 KI 289
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
 487-635 7.95e-04

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: 42.14  E-value: 7.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGK-LENGIPVVIR-----------CIPLSKKYSIRnfKLRldllaklRHTHLISLLghciDGIlgeRND 554
Cdd:cd07830     7 LGDGTFGSVYLARnKETGELVAIKkmkkkfysweeCMNLREVKSLR--KLN-------EHPNIVKLK----EVF---REN 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 555 SKVFLIYECVSNGNFQTYLSGDscGKIFNWSERLSVLISVAKAIHFLHTGmipGFFRNRLKTNNILFNENWMAKLSDYGL 634
Cdd:cd07830    71 DELYFVFEYMEGNLYQLMKDRK--GKPFSESVIRSIIYQILQGLAHIHKH---GFFHRDLKPENLLVSGPEVVKIADFGL 145


                  .
gi 1379623326 635 S 635
Cdd:cd07830   146 A 146
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
 520-651 8.03e-04

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: 41.91  E-value: 8.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 520 RNFKLRL----DLLAKLRHTHLISLLGHCIDgilgerNDSKVFLIYECVSNGNFQTYLS-GDSCGKifnwSERLSVLISV 594
Cdd:cd13994    38 KDYVKRLtseyIISSKLHHPNIVKVLDLCQD------LHGKWCLVMEYCPGGDLFTLIEkADSLSL----EEKDCFFKQI 107

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1379623326 595 AKAIHFLHTGMIPgffrNR-LKTNNILFNENWMAKLSDYGLSIV------SEETDASGVIGESP 651
Cdd:cd13994   108 LRGVAYLHSHGIA----HRdLKPENILLDEDGVLKLTDFGTAEVfgmpaeKESPMSAGLCGSEP 167
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
 534-707 8.30e-04

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: 41.88  E-value: 8.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 534 HTHLISLlghcIDGIlgeRNDSKVFLIYECVSNGNFQTYLSGDSCgkiFNWSERLSVLISVAKAIHFLHTGMIpgfFRNR 613
Cdd:cd14181    75 HPSIITL----IDSY---ESSTFIFLVFDLMRRGELFDYLTEKVT---LSEKETRSIMRSLLEAVSYLHANNI---VHRD 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 614 LKTNNILFNENWMAKLSDYGLSIVSEETDASGVIGESPNSWQMKKL-------------EDDIYSFGFIILEALVGPSMF 680
Cdd:cd14181   142 LKPENILLDDQLHIKLSDFGFSCHLEPGEKLRELCGTPGYLAPEILkcsmdethpgygkEVDLWACGVILFTLLAGSPPF 221

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1379623326 681 AKREAAVLNAMA-----SFSSQdEWKQIVDPV 707
Cdd:cd14181   222 WHRRQMLMLRMImegryQFSSP-EWDDRSSTV 252
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
 480-745 9.51e-04

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: 41.71  E-value: 9.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 480 NFDNSTFLGENIYGKLYKGK--LENGIPVVIRCiplskKYSIRNFKLRLDLLAKLRHTHLISLLgHCIDGILG-----ER 552
Cdd:cd14047     7 DFKEIELIGSGGFGQVFKAKhrIDGKTYAIKRV-----KLNNEKAEREVKALAKLDHPNIVRYN-GCWDGFDYdpetsSS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 553 NDSKV-----FLIYECVSNGNFQTYLSGDSCGKIFNWsERLSVLISVAKAIHFLHT-GMIpgffrNR-LKTNNILFNENW 625
Cdd:cd14047    81 NSSRSktkclFIQMEFCEKGTLESWIEKRNGEKLDKV-LALEIFEQITKGVEYIHSkKLI-----HRdLKPSNIFLVDTG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 626 MAKLSDYGLsiVSEETDA----------SGVIGESPNSWQMKKlEDDIYSFGFIILEAL-VGPSMFAKREaavlnamasf 694
Cdd:cd14047   155 KVKIGDFGL--VTSLKNDgkrtkskgtlSYMSPEQISSQDYGK-EVDIYALGLILFELLhVCDSAFEKSK---------- 221

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1379623326 695 ssqdEWKQIVDPVVQATCCKEsLSIVISITNKCISTESWSRPSIEDVLWNL 745
Cdd:cd14047   222 ----FWTDLRNGILPDIFDKR-YKIEKTIIKKMLSKKPEDRPNASEILRTL 267
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
 487-672 1.06e-03

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: 41.80  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLENGIPVVIRCIPlSKKYSIRNFKLRLDLLAKLRHTHLISLlgHCIdgilgeRNDSKVFLIYECVSN 566
Cdd:cd05067    15 LGAGQFGEVWMGYYNGHTKVAIKSLK-QGSMSPDAFLAEANLMKQLQHQRLVRL--YAV------VTQEPIYIITEYMEN 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 567 GNFQTYLSGDScGKIFNWSERLSVLISVAKAIHFLHTgmiPGFFRNRLKTNNILFNENWMAKLSDYGLSIVSEETDASGV 646
Cdd:cd05067    86 GSLVDFLKTPS-GIKLTINKLLDMAAQIAEGMAFIEE---RNYIHRDLRAANILVSDTLSCKIADFGLARLIEDNEYTAR 161

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1379623326 647 IGES-PNSWQMKK--------LEDDIYSFGFIILE 672
Cdd:cd05067   162 EGAKfPIKWTAPEainygtftIKSDVWSFGILLTE 196
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
 515-682 1.07e-03

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: 41.75  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 515 KKYSIRNFKLRLDLLAKLRHTHLISLLGHCIDGilgerNDSKVFLIYecVSNGNFQTYLsgDSCGKiFNWSERLSVLISV 594
Cdd:cd06628    46 KKSMLDALQREIALLRELQHENIVQYLGSSSDA-----NHLNIFLEY--VPGGSVATLL--NNYGA-FEESLVRNFVRQI 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 595 AKAIHFLHTgmiPGFFRNRLKTNNILFNENWMAKLSDYGLSIVSEETDASGVIGESPNSWQ--------------MKKLE 660
Cdd:cd06628   116 LKGLNYLHN---RGIIHRDIKGANILVDNKGGIKISDFGISKKLEANSLSTKNNGARPSLQgsvfwmapevvkqtSYTRK 192

                         170       180
                  ....*....|....*....|..
gi 1379623326 661 DDIYSFGFIILEALVGPSMFAK 682
Cdd:cd06628   193 ADIWSLGCLVVEMLTGTHPFPD 214
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
 487-672 1.14e-03

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: 41.44  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGKLENGIPVVIRCIPlSKKYSIRNFKLRLDLLAKLRHTHLISLLGhcidgILGERndsKVFLIYECVSN 566
Cdd:cd14203     3 LGQGCFGEVWMGTWNGTTKVAIKTLK-PGTMSPEAFLEEAQIMKKLRHDKLVQLYA-----VVSEE---PIYIVTEFMSK 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 567 GNFQTYLSgDSCGKIFNWSERLSVLISVAKAIHFLHTgmiPGFFRNRLKTNNILFNENWMAKLSDYGLSIVSEETDASGV 646
Cdd:cd14203    74 GSLLDFLK-DGEGKYLKLPQLVDMAAQIASGMAYIER---MNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTAR 149

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1379623326 647 IGES-PNSWQMKK--------LEDDIYSFGFIILE 672
Cdd:cd14203   150 QGAKfPIKWTAPEaalygrftIKSDVWSFGILLTE 184
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
 487-643 1.57e-03

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: 41.00  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGK-LENGIPVVIRCI--------------PLSKKYSIRNFKLRLDLLAKLRHTHLISLLGhCIDGilgE 551
Cdd:cd14008     1 LGRGSFGKVKLALdTETGQLYAIKIFnksrlrkrregkndRGKIKNALDDVRREIAIMKKLDHPNIVRLYE-VIDD---P 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 552 RNDsKVFLIYECVSNGNFQTYLSGDSCGKIfnwSERLSVLI--SVAKAIHFLHtgmipgffRNR-----LKTNNILFNEN 624
Cdd:cd14008    77 ESD-KLYLVLEYCEGGPVMELDSGDRVPPL---PEETARKYfrDLVLGLEYLH--------ENGivhrdIKPENLLLTAD 144

                         170
                  ....*....|....*....
gi 1379623326 625 WMAKLSDYGLSIVSEETDA 643
Cdd:cd14008   145 GTVKISDFGVSEMFEDGND 163
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
 487-635 1.75e-03

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: 40.88  E-value: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGK-LENGIPVVIRCIPL-SKKYSIRNFKLR-LDLLAKLRHTHLISLlghcIDGILGERndsKVFLIYE- 562
Cdd:cd07839     8 IGEGTYGTVFKAKnRETHEIVALKRVRLdDDDEGVPSSALReICLLKELKHKNIVRL----YDVLHSDK---KLTLVFEy 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1379623326 563 CvsNGNFQTYLsgDSCGKIFNWSERLSVLISVAKAIHFLHTGMIpgfFRNRLKTNNILFNENWMAKLSDYGLS 635
Cdd:cd07839    81 C--DQDLKKYF--DSCNGDIDPEIVKSFMFQLLKGLAFCHSHNV---LHRDLKPQNLLINKNGELKLADFGLA 146
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
 485-742 1.88e-03

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: 40.60  E-value: 1.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 485 TFLGENIYGKLYKG-KLENGIPVVIRCIPlskkysiRNfklRLDLLAKLRHTHLISL---LGHCIDGILGERNDSKVFLI 560
Cdd:cd14101     6 NLLGKGGFGTVYAGhRISDGLQVAIKQIS-------RN---RVQQWSKLPGVNPVPNevaLLQSVGGGPGHRGVIRLLDW 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 561 YEcVSNGNFQTYLSGDSCGKIFNW-------SERLS--VLISVAKAIHFLHTgmiPGFFRNRLKTNNILFN-ENWMAKLS 630
Cdd:cd14101    76 FE-IPEGFLLVLERPQHCQDLFDYitergalDESLArrFFKQVVEAVQHCHS---KGVVHRDIKDENILVDlRTGDIKLI 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 631 DYGLSIV---SEETDASGVIGESPNSW----QMKKLEDDIYSFGFIILEALVGPSMFaKREAAVLNAMASFSSQdewkqi 703
Cdd:cd14101   152 DFGSGATlkdSMYTDFDGTRVYSPPEWilyhQYHALPATVWSLGILLYDMVCGDIPF-ERDTDILKAKPSFNKR------ 224

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1379623326 704 vdpvVQATCCkeslsiviSITNKCISTESWSRPSIEDVL 742
Cdd:cd14101   225 ----VSNDCR--------SLIRSCLAYNPSDRPSLEQIL 251
LRR_8 pfam13855
Leucine rich repeat;
166-225 1.99e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 37.12  E-value: 1.99e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 166 SLQILMLGDNFFNGTIPNLFDSSSNLTVFSLKNNKLKGPFPFSILSITTLTNIDMSRNQI 225
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PK_GC-C cd14044
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain ...
 554-680 2.43e-03

Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-C binds and is activated by the intestinal hormones, guanylin (GN) and uroguanylin (UGN), which are secreted after salty meals to inhibit sodium absorption and induce the secretion of chloride, bicarbonate, and water. GN and UGN are also present in the kidney, where they induce increased salt and water secretion. This prevents the development of hypernatremia and hypervolemia after ingestion of high amounts of salt. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-C subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270946 [Multi-domain]  Cd Length: 271  Bit Score: 40.64  E-value: 2.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 554 DSKVFLIYECVSNGNFQTYLSGDSC---GKIFNWSERLSVLISVAKAIHFLHTGMIPgfFRNRLKTNNILFNENWMAKLS 630
Cdd:cd14044    75 DTMIFGVIEYCERGSLRDVLNDKISypdGTFMDWEFKISVMYDIAKGMSYLHSSKTE--VHGRLKSTNCVVDSRMVVKIT 152

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1379623326 631 DYGL-SIVSEETDasgvIGESPNSWQMKKLED--DIYSFGFIILEALVGPSMF 680
Cdd:cd14044   153 DFGCnSILPPSKD----LWTAPEHLRQAGTSQkgDVYSYGIIAQEIILRKETF 201
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 213-257 2.44e-03

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 36.45  E-value: 2.44e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1379623326 213 TTLTNIDMSRNQISgSLQDFTGLSSLEHLDLRENELDSDLPALPK 257
Cdd:pfam12799   1 PNLEVLDLSNNQIT-DIPPLAKLPNLETLDLSGNNKITDLSDLAN 44
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
 485-674 2.61e-03

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: 40.48  E-value: 2.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 485 TFLGENIYGKLYKGKLEN-------GIPVVIRCipLSKKYSIRNFKLRLD---LLAKLRHTHLISLLGHCIDgilgerND 554
Cdd:cd05044     1 KFLGSGAFGEVFEGTAKDilgdgsgETKVAVKT--LRKGATDQEKAEFLKeahLMSNFKHPNILKLLGVCLD------ND 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 555 SkVFLIYECVSNGNFQTYL------SGDSCGkiFNWSERLSVLISVAKAIHFL---HtgmipgFFRNRLKTNNILFNENW 625
Cdd:cd05044    73 P-QYIILELMEGGDLLSYLraarptAFTPPL--LTLKDLLSICVDVAKGCVYLedmH------FVHRDLAARNCLVSSKD 143

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1379623326 626 MA----KLSDYGLSIVSEETDASGVIGES--PNSWQMKK--------LEDDIYSFGFIILEAL 674
Cdd:cd05044   144 YRervvKIGDFGLARDIYKNDYYRKEGEGllPVRWMAPEslvdgvftTQSDVWAFGVLMWEIL 206
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
 533-680 2.73e-03

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: 40.77  E-value: 2.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 533 RHTHLISLLGHCIdgilgerNDSKVFLIYECVSNGNFQTYL----------SGDSC---GKIFNWSERLSVLISVAKAIH 599
Cdd:cd05100    76 KHKNIINLLGACT-------QDGPLYVLVEYASKGNLREYLrarrppgmdySFDTCklpEEQLTFKDLVSCAYQVARGME 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 600 FLHTGMIpgfFRNRLKTNNILFNENWMAKLSDYGLSIVSEETD--ASGVIGESPNSWQMKKL--------EDDIYSFGFI 669
Cdd:cd05100   149 YLASQKC---IHRDLAARNVLVTEDNVMKIADFGLARDVHNIDyyKKTTNGRLPVKWMAPEAlfdrvythQSDVWSFGVL 225

                         170
                  ....*....|..
gi 1379623326 670 ILEAL-VGPSMF 680
Cdd:cd05100   226 LWEIFtLGGSPY 237
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
 523-635 3.16e-03

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: 40.46  E-value: 3.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 523 KLRLDLLAKLRHTHLISLlgHcidgiLGERNDSKVFLIYECVSNGNFQTYLSGDScgkIFNWSERLSVLISVAKAIHFLH 602
Cdd:cd05582    45 KMERDILADVNHPFIVKL--H-----YAFQTEGKLYLILDFLRGGDLFTRLSKEV---MFTEEDVKFYLAELALALDHLH 114

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1379623326 603 T-GMIpgfFRNrLKTNNILFNENWMAKLSDYGLS 635
Cdd:cd05582   115 SlGII---YRD-LKPENILLDEDGHIKLTDFGLS 144
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
 531-742 3.17e-03

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: 40.36  E-value: 3.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 531 KLRHTHLISLLGHCIdgiLGERNDSK-VFLIYECVSNGNFQTYLSGDSCGKIFnWSER--LSVLISVAKAIHFLHTGMIP 607
Cdd:cd13986    53 LFNHPNILRLLDSQI---VKEAGGKKeVYLLLPYYKRGSLQDEIERRLVKGTF-FPEDriLHIFLGICRGLKAMHEPELV 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 608 GFFRNRLKTNNILFNENWMAKLSDYGlSIVSEETDASgvigespNSWQMKKLED-------------------------- 661
Cdd:cd13986   129 PYAHRDIKPGNVLLSEDDEPILMDLG-SMNPARIEIE-------GRREALALQDwaaehctmpyrapelfdvkshctide 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 662 --DIYSFGFIILEALVGPSMFAKREA-------AVLNAMASFSSqdewkqivDPVVQATCCkeslsiviSITNKCISTES 732
Cdd:cd13986   201 ktDIWSLGCTLYALMYGESPFERIFQkgdslalAVLSGNYSFPD--------NSRYSEELH--------QLVKSMLVVNP 264

                         250
                  ....*....|
gi 1379623326 733 WSRPSIEDVL 742
Cdd:cd13986   265 AERPSIDDLL 274
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
 528-672 3.45e-03

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: 39.77  E-value: 3.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 528 LLAKLRHTHLISLLGHCIdgilgerNDSKVFLIYECVSNGNFQTYLSGDscgKIFNWSERLSVLISVAKAIHFLHTgmiP 607
Cdd:cd14155    41 LMNRLSHPNILRFMGVCV-------HQGQLHALTEYINGGNLEQLLDSN---EPLSWTVRVKLALDIARGLSYLHS---K 107

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1379623326 608 GFFRNRLKTNNILF---NENWMAKLSDYGLS----IVSEETDASGVIGeSPNSWQMKKLED-------DIYSFGFIILE 672
Cdd:cd14155   108 GIFHRDLTSKNCLIkrdENGYTAVVGDFGLAekipDYSDGKEKLAVVG-SPYWMAPEVLRGepynekaDVFSYGIILCE 185
PTK_Jak3_rpt1 cd14208
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is ...
 487-745 3.56e-03

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: 39.89  E-value: 3.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKG---KLENG----IPVVIRCIPLSKKYSIRNFKLRLDLLAKLRHTHLISLLGHCIDGilgerndsKVFL 559
Cdd:cd14208     7 LGKGSFTKIYRGlrtDEEDDerceTEVLLKVMDPTHGNCQESFLEAASIMSQISHKHLVLLHGVCVGK--------DSIM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 560 IYECVSNGNFQTYLSGDSCGKIFNWSERLSVLISVAKAIHFLHTGMIPgffRNRLKTNNILFNENWMA------KLSDYG 633
Cdd:cd14208    79 VQEFVCHGALDLYLKKQQQKGPVAISWKLQVVKQLAYALNYLEDKQLV---HGNVSAKKVLLSREGDKgsppfiKLSDPG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 634 LSI--VSEETDASGVIGESP---NSWQMKKLEDDIYSFGFIILEALVGPSMfakrEAAVLNAMASFSSQDEWKQIVDPvv 708
Cdd:cd14208   156 VSIkvLDEELLAERIPWVAPeclSDPQNLALEADKWGFGATLWEIFSGGHM----PLSALDPSKKLQFYNDRKQLPAP-- 229

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1379623326 709 qatcckeSLSIVISITNKCISTESWSRPSIEDVLWNL 745
Cdd:cd14208   230 -------HWIELASLIQQCMSYNPLLRPSFRAIIRDL 259
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
 480-689 3.68e-03

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: 39.68  E-value: 3.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 480 NFDNSTFLGENIYGKLYKGKLENGipvvirciplSKKYSIRNFKLRL-------------DLLAKLRHTHLISLLGHCID 546
Cdd:cd08530     1 DFKVLKKLGKGSYGSVYKVKRLSD----------NQVYALKEVNLGSlsqkeredsvneiRLLASVNHPNIIRYKEAFLD 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 547 GilgerndSKVFLIYECVSNGNFQTYLS-GDSCGKIFNWSERLSVLISVAKAIHFLHTGMIpgFFRNrLKTNNILFNENW 625
Cdd:cd08530    71 G-------NRLCIVMEYAPFGDLSKLISkRKKKRRLFPEDDIWRIFIQMLRGLKALHDQKI--LHRD-LKSANILLSAGD 140

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 626 MAKLSDYGLSIVSEETDASGVIGE----SPNSWQMK--KLEDDIYSFGFIILEALVGPSMFAKREAAVLN 689
Cdd:cd08530   141 LVKIGDLGISKVLKKNLAKTQIGTplyaAPEVWKGRpyDYKSDIWSLGCLLYEMATFRPPFEARTMQELR 210
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
 523-634 3.86e-03

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: 39.67  E-value: 3.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 523 KLRLDLLAKLRHTHlISLLGHCIDgilgerNDSKVFLIYEcvsngnfqtYLSGdscGKIFNW---SERLS------VLIS 593
Cdd:cd14078    49 KTEIEALKNLSHQH-ICRLYHVIE------TDNKIFMVLE---------YCPG---GELFDYivaKDRLSedearvFFRQ 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1379623326 594 VAKAIHFLHTgmiPGFFRNRLKTNNILFNENWMAKLSDYGL 634
Cdd:cd14078   110 IVSAVAYVHS---QGYAHRDLKPENLLLDEDQNLKLIDFGL 147
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
 487-674 4.12e-03

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: 40.05  E-value: 4.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 487 LGENIYGKLYKGK-LENG----IPVVIRCI--PLSKKYSIRNFKLRLdLLAKLRHTHLISLLGHCIdgilgernDSKVFL 559
Cdd:cd05110    15 LGSGAFGTVYKGIwVPEGetvkIPVAIKILneTTGPKANVEFMDEAL-IMASMDHPHLVRLLGVCL--------SPTIQL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 560 IYECVSNGNFQTYL--SGDSCGK--IFNWSerlsvlISVAKAIHFLHTGMIpgfFRNRLKTNNILFNENWMAKLSDYGLS 635
Cdd:cd05110    86 VTQLMPHGCLLDYVheHKDNIGSqlLLNWC------VQIAKGMMYLEERRL---VHRDLAARNVLVKSPNHVKITDFGLA 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1379623326 636 IVSE----ETDASGviGESPNSW------QMKKL--EDDIYSFGFIILEAL 674
Cdd:cd05110   157 RLLEgdekEYNADG--GKMPIKWmaleciHYRKFthQSDVWSYGVTIWELM 205
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
 582-676 4.33e-03

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: 39.68  E-value: 4.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 582 FNWSERLSVLISVAKAIHFLHTGMIpgFFRNrLKTNNILFNENWMAKLSDYGLSIVSEETDASG---------------V 646
Cdd:cd14062    86 FEMLQLIDIARQTAQGMDYLHAKNI--IHRD-LKSNNIFLHEDLTVKIGDFGLATVKTRWSGSQqfeqptgsilwmapeV 162

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1379623326 647 I---GESPNSWQmkkleDDIYSFGFIILEALVG 676
Cdd:cd14062   163 IrmqDENPYSFQ-----SDVYAFGIVLYELLTG 190
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
 522-746 5.96e-03

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: 39.50  E-value: 5.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 522 FKLRLDLLAKLRHTHLISLLGHCIDGilgerNDSKVFLIYECVSNGNFQTYLSGDScgkiFNWSERLSVLISVAKAIHFL 601
Cdd:cd05080    53 WKQEIDILKTLYHENIVKYKGCCSEQ-----GGKSLQLIMEYVPLGSLRDYLPKHS----IGLAQLLLFAQQICEGMAYL 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 602 HTGMipgFFRNRLKTNNILFNENWMAKLSDYGLSI----------VSEEtdasgviGESPNSWQ----MKKLE----DDI 663
Cdd:cd05080   124 HSQH---YIHRDLAARNVLLDNDRLVKIGDFGLAKavpegheyyrVRED-------GDSPVFWYapecLKEYKfyyaSDV 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 664 YSFGFIILEALVGPSMFAKREAAVLNAMASFSSQDEWKQIVDPVVQAT---CCKESLSIVISITNKCISTESWSRPSIED 740
Cdd:cd05080   194 WSFGVTLYELLTHCDSSQSPPTKFLEMIGIAQGQMTVVRLIELLERGErlpCPDKCPQEVYHLMKNCWETEASFRPTFEN 273


                  ....*.
gi 1379623326 741 VLWNLQ 746
Cdd:cd05080   274 LIPILK 279
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
 480-680 9.52e-03

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: 38.69  E-value: 9.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 480 NFDNSTFLGENIYGKLYKGK-LENGIPVVIRCI---PLSKKYSIRNFKLRLDLLAKLRHTHLISLLGHCIDGilgerndS 555
Cdd:cd14186     2 DFKVLNLLGKGSFACVYRARsLHTGLEVAIKMIdkkAMQKAGMVQRVRNEVEIHCQLKHPSILELYNYFEDS-------N 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 556 KVFLIYECVSNGNFQTYLSGDScgKIFNWSERLSVLISVAKAIHFLHTGmipGFFRNRLKTNNILFNENWMAKLSDYGLS 635
Cdd:cd14186    75 YVYLVLEMCHNGEMSRYLKNRK--KPFTEDEARHFMHQIVTGMLYLHSH---GILHRDLTLSNLLLTRNMNIKIADFGLA 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1379623326 636 I-VSEETDASGVIGESPN-------SWQMKKLEDDIYSFGFIILEALVGPSMF 680
Cdd:cd14186   150 TqLKMPHEKHFTMCGTPNyispeiaTRSAHGLESDVWSLGCMFYTLLVGRPPF 202
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 103-317 9.65e-03

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 38.88  E-value: 9.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 103 SFSMDS--FVATLARLTSLRVLHLVSLGIwGPFPDRI------HRLFSLEQLDLSSNYLYG----SIPPKISTMVSLQIL 170
Cdd:cd00116    92 ALGPDGcgVLESLLRSSSLQELKLNNNGL-GDRGLRLlakglkDLPPALEKLVLGRNRLEGasceALAKALRANRDLKEL 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 171 MLGDNFFNGT-IPNL---FDSSSNLTVFSLKNNklkgpfpfsilsitTLTNIDMSrnQISGSLQDftgLSSLEHLDLREN 246
Cdd:cd00116   171 NLANNGIGDAgIRALaegLKANCNLEVLDLNNN--------------GLTDEGAS--ALAETLAS---LKSLEVLNLGDN 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379623326 247 --------ELDSDLPALPKGLISLFLNRN--------SFSGQIPKSygqlNSLQHLDISFNTLTGATPSELFSL-----P 305
Cdd:cd00116   232 nltdagaaALASALLSPNISLLTLSLSCNditddgakDLAEVLAEK----ESLLELDLRGNKFGEEGAQLLAESllepgN 307

                         250
                  ....*....|..
gi 1379623326 306 NIIYLNLGSNML 317
Cdd:cd00116   308 ELESLWVKDDSF 319
 
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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