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Conserved domains on  [gi|297822009|ref|XP_002878887|]
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probably inactive leucine-rich repeat receptor-like protein kinase At2g25790 [Arabidopsis lyrata subsp. lyrata]

Protein Classification

leucine-rich repeat domain-containing protein; leucine-rich repeat protein kinase family protein( domain architecture ID 11476383)

leucine-rich repeat (LRR) domain-containing protein may participate in protein-protein interactions; 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
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
12-960 0e+00

leucine-rich repeat receptor-like protein kinase; Provisional


:

Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 1620.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009  12 YLITTLFFLFLNFSCLHANELELLLSFKSSIQDPLKHLSSWSysSTNDVCLWTGVVCNNFSRVVSLDLSGKNISGQIlTS 91
Cdd:PLN00113  11 YLIFMLFFLFLNFSMLHAEELELLLSFKSSINDPLKYLSNWN--SSADVCLWQGITCNNSSRVVSIDLSGKNISGKI-SS 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009  92 ATFRLPFLRTINLSNNNLSGPIPQDIFTTSSpSLRYLNLSNNNFSGSISRGFLPNLYTLDLSNNMFTGEIYNDIGFFSNL 171
Cdd:PLN00113  88 AIFRLPYIQTINLSNNQLSGPIPDDIFTTSS-SLRYLNLSNNNFTGSIPRGSIPNLETLDLSNNMLSGEIPNDIGSFSSL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 172 RVLDLGGNVLTGHVPAYLGNLSKLEFLTLASNQFTGGVPAELGKMKNLKWIYLGYNNLSGEIPYQIGGLSSLNHLDLVYN 251
Cdd:PLN00113 167 KVLDLGGNVLVGKIPNSLTNLTSLEFLTLASNQLVGQIPRELGQMKSLKWIYLGYNNLSGEIPYEIGGLTSLNHLDLVYN 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 252 NLSGPIPPSLGDLKNLEYMFLYQNKLSGQIPPSIFSLQNLISLDFSDNSLSGEIPELLAQMQTLEILHLFSNNLTGTIPV 331
Cdd:PLN00113 247 NLTGPIPSSLGNLKNLQYLFLYQNKLSGPIPPSIFSLQKLISLDLSDNSLSGEIPELVIQLQNLEILHLFSNNFTGKIPV 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 332 GVTSLPRLQVLQLWSNRFSGGIPANLGKHNNLTVLDLSTNNLTGKLPDTLCDSGHLTKLILFSNSLDGQIPPSLGACSSL 411
Cdd:PLN00113 327 ALTSLPRLQVLQLWSNKFSGEIPKNLGKHNNLTVLDLSTNNLTGEIPEGLCSSGNLFKLILFSNSLEGEIPKSLGACRSL 406
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 412 ERVRLQKNAFSGDLPRGFTKLQLVNFLDLSNNNLQGNINT--WDMPQLEMLDLSRNNFSGELPDLSRSKRLKKLDLSRNR 489
Cdd:PLN00113 407 RRVRLQDNSFSGELPSEFTKLPLVYFLDISNNNLQGRINSrkWDMPSLQMLSLARNKFFGGLPDSFGSKRLENLDLSRNQ 486
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 490 ISEMVPLRLMAFPELMDMDLSENEITGVIPSELSSCKNLVNLDLSHNNLTGEIPLSFSEFPVLSDLDLSCNRLSGEIPKN 569
Cdd:PLN00113 487 FSGAVPRKLGSLSELMQLKLSENKLSGEIPDELSSCKKLVSLDLSHNQLSGQIPASFSEMPVLSQLDLSQNQLSGEIPKN 566
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 570 LGNIESLVQVNISHNLLHGSLPPTGAFLAINATAVAGNIDLCSSNSASGLRPCKVVRKrsTKSWWFIITSTVVAFLAVLV 649
Cdd:PLN00113 567 LGNVESLVQVNISHNHLHGSLPSTGAFLAINASAVAGNIDLCGGDTTSGLPPCKRVRK--TPSWWFYITCTLGAFLVLAL 644
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 650 SGFfiALVFQKTRNVLEVKKVEQEDGTkWETQFFDSRFMKSFTVNAILSSLNEQNVLVD------------KTGIKFVVK 717
Cdd:PLN00113 645 VAF--GFVFIRGRNNLELKRVENEDGT-WELQFFDSKVSKSITINDILSSLKEENVISRgkkgasykgksiKNGMQFVVK 721
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 718 EVKKYDSLPEM-ISDMRKLsEHKNILKIVATCRSEKEAYLIHEDVEGKRLSQILNGLSWERRRKIMKGIVEALRFLHCRC 796
Cdd:PLN00113 722 EINDVNSIPSSeIADMGKL-QHPNIVKLIGLCRSEKGAYLIHEYIEGKNLSEVLRNLSWERRRKIAIGIAKALRFLHCRC 800
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 797 SPAVVAGNLSPENIVIDVKDQPRLCLGLPGLLCMD------SAYMAPETRERKEMTSKSDIYGFGILLLNLLTGKNSSgd 870
Cdd:PLN00113 801 SPAVVVGNLSPEKIIIDGKDEPHLRLSLPGLLCTDtkcfisSAYVAPETRETKDITEKSDIYGFGLILIELLTGKSPA-- 878
                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 871 eDIASEVNGSLVNWARYSYSNCHIDTWIDSSI--DMSVHKREIVHVMNLALNCTAIDPQERPCTKNVLQALESTSSSSSS 948
Cdd:PLN00113 879 -DAEFGVHGSIVEWARYCYSDCHLDMWIDPSIrgDVSVNQNEIVEVMNLALHCTATDPTARPCANDVLKTLESASRSSSS 957
                        970
                 ....*....|..
gi 297822009 949 CTTYFsKIPSLA 960
Cdd:PLN00113 958 CVTGL-KFSSLF 968
 
Name Accession Description Interval E-value
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
12-960 0e+00

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 1620.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009  12 YLITTLFFLFLNFSCLHANELELLLSFKSSIQDPLKHLSSWSysSTNDVCLWTGVVCNNFSRVVSLDLSGKNISGQIlTS 91
Cdd:PLN00113  11 YLIFMLFFLFLNFSMLHAEELELLLSFKSSINDPLKYLSNWN--SSADVCLWQGITCNNSSRVVSIDLSGKNISGKI-SS 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009  92 ATFRLPFLRTINLSNNNLSGPIPQDIFTTSSpSLRYLNLSNNNFSGSISRGFLPNLYTLDLSNNMFTGEIYNDIGFFSNL 171
Cdd:PLN00113  88 AIFRLPYIQTINLSNNQLSGPIPDDIFTTSS-SLRYLNLSNNNFTGSIPRGSIPNLETLDLSNNMLSGEIPNDIGSFSSL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 172 RVLDLGGNVLTGHVPAYLGNLSKLEFLTLASNQFTGGVPAELGKMKNLKWIYLGYNNLSGEIPYQIGGLSSLNHLDLVYN 251
Cdd:PLN00113 167 KVLDLGGNVLVGKIPNSLTNLTSLEFLTLASNQLVGQIPRELGQMKSLKWIYLGYNNLSGEIPYEIGGLTSLNHLDLVYN 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 252 NLSGPIPPSLGDLKNLEYMFLYQNKLSGQIPPSIFSLQNLISLDFSDNSLSGEIPELLAQMQTLEILHLFSNNLTGTIPV 331
Cdd:PLN00113 247 NLTGPIPSSLGNLKNLQYLFLYQNKLSGPIPPSIFSLQKLISLDLSDNSLSGEIPELVIQLQNLEILHLFSNNFTGKIPV 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 332 GVTSLPRLQVLQLWSNRFSGGIPANLGKHNNLTVLDLSTNNLTGKLPDTLCDSGHLTKLILFSNSLDGQIPPSLGACSSL 411
Cdd:PLN00113 327 ALTSLPRLQVLQLWSNKFSGEIPKNLGKHNNLTVLDLSTNNLTGEIPEGLCSSGNLFKLILFSNSLEGEIPKSLGACRSL 406
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 412 ERVRLQKNAFSGDLPRGFTKLQLVNFLDLSNNNLQGNINT--WDMPQLEMLDLSRNNFSGELPDLSRSKRLKKLDLSRNR 489
Cdd:PLN00113 407 RRVRLQDNSFSGELPSEFTKLPLVYFLDISNNNLQGRINSrkWDMPSLQMLSLARNKFFGGLPDSFGSKRLENLDLSRNQ 486
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 490 ISEMVPLRLMAFPELMDMDLSENEITGVIPSELSSCKNLVNLDLSHNNLTGEIPLSFSEFPVLSDLDLSCNRLSGEIPKN 569
Cdd:PLN00113 487 FSGAVPRKLGSLSELMQLKLSENKLSGEIPDELSSCKKLVSLDLSHNQLSGQIPASFSEMPVLSQLDLSQNQLSGEIPKN 566
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 570 LGNIESLVQVNISHNLLHGSLPPTGAFLAINATAVAGNIDLCSSNSASGLRPCKVVRKrsTKSWWFIITSTVVAFLAVLV 649
Cdd:PLN00113 567 LGNVESLVQVNISHNHLHGSLPSTGAFLAINASAVAGNIDLCGGDTTSGLPPCKRVRK--TPSWWFYITCTLGAFLVLAL 644
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 650 SGFfiALVFQKTRNVLEVKKVEQEDGTkWETQFFDSRFMKSFTVNAILSSLNEQNVLVD------------KTGIKFVVK 717
Cdd:PLN00113 645 VAF--GFVFIRGRNNLELKRVENEDGT-WELQFFDSKVSKSITINDILSSLKEENVISRgkkgasykgksiKNGMQFVVK 721
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 718 EVKKYDSLPEM-ISDMRKLsEHKNILKIVATCRSEKEAYLIHEDVEGKRLSQILNGLSWERRRKIMKGIVEALRFLHCRC 796
Cdd:PLN00113 722 EINDVNSIPSSeIADMGKL-QHPNIVKLIGLCRSEKGAYLIHEYIEGKNLSEVLRNLSWERRRKIAIGIAKALRFLHCRC 800
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 797 SPAVVAGNLSPENIVIDVKDQPRLCLGLPGLLCMD------SAYMAPETRERKEMTSKSDIYGFGILLLNLLTGKNSSgd 870
Cdd:PLN00113 801 SPAVVVGNLSPEKIIIDGKDEPHLRLSLPGLLCTDtkcfisSAYVAPETRETKDITEKSDIYGFGLILIELLTGKSPA-- 878
                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 871 eDIASEVNGSLVNWARYSYSNCHIDTWIDSSI--DMSVHKREIVHVMNLALNCTAIDPQERPCTKNVLQALESTSSSSSS 948
Cdd:PLN00113 879 -DAEFGVHGSIVEWARYCYSDCHLDMWIDPSIrgDVSVNQNEIVEVMNLALHCTATDPTARPCANDVLKTLESASRSSSS 957
                        970
                 ....*....|..
gi 297822009 949 CTTYFsKIPSLA 960
Cdd:PLN00113 958 CVTGL-KFSSLF 968
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
30-401 1.99e-33

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 133.91  E-value: 1.99e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009  30 NELELLLSFKSSIQDPLKHLSSWSYSSTNDVCLWTGVVCNNFSRVVSLDLSGKNISGQILTSATFRLPFLRTINLSNNNL 109
Cdd:COG4886    3 LLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 110 SGPIPQDIFTTSSPSLRYLNLSNNNFSGSisrgfLPNLYTLDLSNNMFTgEIYNDIGFFSNLRVLDLGGNVLTgHVPAYL 189
Cdd:COG4886   83 SLLLLGLTDLGDLTNLTELDLSGNEELSN-----LTNLESLDLSGNQLT-DLPEELANLTNLKELDLSNNQLT-DLPEPL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 190 GNLSKLEFLTLASNQFTGgVPAELGKMKNLKWIYLGYNNLSgEIPYQIGGLSSLNHLDLVYNNLSgPIPPSLGDLKNLEY 269
Cdd:COG4886  156 GNLTNLKSLDLSNNQLTD-LPEELGNLTNLKELDLSNNQIT-DLPEPLGNLTNLEELDLSGNQLT-DLPEPLANLTNLET 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 270 MFLYQNKLSGqiPPSIFSLQNLISLDFSDNSLSgEIPElLAQMQTLEILHLFSNNLTGTIPVGVTSLPRLQVLQLWSNRF 349
Cdd:COG4886  233 LDLSNNQLTD--LPELGNLTNLEELDLSNNQLT-DLPP-LANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLL 308
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 297822009 350 SGGIPANLGKHNNLTVLDLSTNNLTGKLPDTLCDSGHLTKLILFSNSLDGQI 401
Cdd:COG4886  309 NLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLS 360
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
727-940 7.14e-33

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: 128.54  E-value: 7.14e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 727 EMISDMRklseHKNILKIVATCRSEKEAYLIHEDVEGKRLSQILNG------LSWERRRKIMKGIVEALRFLHCRCSPAV 800
Cdd:cd14066   42 EMLGRLR----HPNLVRLLGYCLESDEKLLVYEYMPNGSLEDRLHChkgsppLPWPQRLKIAKGIARGLEYLHEECPPPI 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 801 VAGNLSPENIVID------VKD-------QPRLCLGLPGLLCMDSAYMAPETRERKEMTSKSDIYGFGILLLNLLTGKNS 867
Cdd:cd14066  118 IHGDIKSSNILLDedfepkLTDfglarliPPSESVSKTSAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPA 197
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 297822009 868 SGDEDIASEVNgSLVNWARYSYSNC---HIDTWIDSsiDMSVHKREIVHVMNLALNCTAIDPQERPCTKNVLQALE 940
Cdd:cd14066  198 VDENRENASRK-DLVEWVESKGKEEledILDKRLVD--DDGVEEEEVEALLRLALLCTRSDPSLRPSMKEVVQMLE 270
Pkinase pfam00069
Protein kinase domain;
709-937 1.02e-15

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 77.28  E-value: 1.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009  709 KTGIKFVVKEVKKYDSLPEM-------ISDMRKLSeHKNILKIVATCRSEKEAYLIHEDVEGKRLSQILN---GLSWERR 778
Cdd:pfam00069  22 DTGKIVAIKKIKKEKIKKKKdknilreIKILKKLN-HPNIVRLYDAFEDKDNLYLVLEYVEGGSLFDLLSekgAFSEREA 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009  779 RKIMKGIVEALRFLHCRCSPAVvagnlspenividvkdqprlclglpgllcmDSAYMAPETRERKEMTSKSDIYGFGILL 858
Cdd:pfam00069 101 KFIMKQILEGLESGSSLTTFVG------------------------------TPWYMAPEVLGGNPYGPKVDVWSLGCIL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009  859 LNLLTGK----NSSGDEDIASEVNGSLvnwarysYSNCHIDTWIDSSIDmsvhkreivhvmnLALNCTAIDPQERPCTKN 934
Cdd:pfam00069 151 YELLTGKppfpGINGNEIYELIIDQPY-------AFPELPSNLSEEAKD-------------LLKKLLKKDPSKRLTATQ 210

                  ...
gi 297822009  935 VLQ 937
Cdd:pfam00069 211 ALQ 213
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
709-937 6.19e-14

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 72.56  E-value: 6.19e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009   709 KTGIKFVVKEVKK--YDSLPEM----ISDMRKLSeHKNILKIVATCRSEKEAYLIHEDVEGKRLSQIL---NGLSWERRR 779
Cdd:smart00220  22 KTGKLVAIKVIKKkkIKKDRERilreIKILKKLK-HPNIVRLYDVFEDEDKLYLVMEYCEGGDLFDLLkkrGRLSEDEAR 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009   780 KIMKGIVEALRFLHCRCspaVVAGNLSPENIVIDVKDQPR-----LCLGLPGLLCMDS-----AYMAPETRERKEMTSKS 849
Cdd:smart00220 101 FYLRQILSALEYLHSKG---IVHRDLKPENILLDEDGHVKladfgLARQLDPGEKLTTfvgtpEYMAPEVLLGKGYGKAV 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009   850 DIYGFGILLLNLLTGKNS-SGDEDIAsevngSLVNWARYSYSNCHIDTWIDSSidmsvhkreivHVMNLALNCTAIDPQE 928
Cdd:smart00220 178 DIWSLGVILYELLTGKPPfPGDDQLL-----ELFKKIGKPKPPFPPPEWDISP-----------EAKDLIRKLLVKDPEK 241

                   ....*....
gi 297822009   929 RPCTKNVLQ 937
Cdd:smart00220 242 RLTAEEALQ 250
 
Name Accession Description Interval E-value
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
12-960 0e+00

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 1620.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009  12 YLITTLFFLFLNFSCLHANELELLLSFKSSIQDPLKHLSSWSysSTNDVCLWTGVVCNNFSRVVSLDLSGKNISGQIlTS 91
Cdd:PLN00113  11 YLIFMLFFLFLNFSMLHAEELELLLSFKSSINDPLKYLSNWN--SSADVCLWQGITCNNSSRVVSIDLSGKNISGKI-SS 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009  92 ATFRLPFLRTINLSNNNLSGPIPQDIFTTSSpSLRYLNLSNNNFSGSISRGFLPNLYTLDLSNNMFTGEIYNDIGFFSNL 171
Cdd:PLN00113  88 AIFRLPYIQTINLSNNQLSGPIPDDIFTTSS-SLRYLNLSNNNFTGSIPRGSIPNLETLDLSNNMLSGEIPNDIGSFSSL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 172 RVLDLGGNVLTGHVPAYLGNLSKLEFLTLASNQFTGGVPAELGKMKNLKWIYLGYNNLSGEIPYQIGGLSSLNHLDLVYN 251
Cdd:PLN00113 167 KVLDLGGNVLVGKIPNSLTNLTSLEFLTLASNQLVGQIPRELGQMKSLKWIYLGYNNLSGEIPYEIGGLTSLNHLDLVYN 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 252 NLSGPIPPSLGDLKNLEYMFLYQNKLSGQIPPSIFSLQNLISLDFSDNSLSGEIPELLAQMQTLEILHLFSNNLTGTIPV 331
Cdd:PLN00113 247 NLTGPIPSSLGNLKNLQYLFLYQNKLSGPIPPSIFSLQKLISLDLSDNSLSGEIPELVIQLQNLEILHLFSNNFTGKIPV 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 332 GVTSLPRLQVLQLWSNRFSGGIPANLGKHNNLTVLDLSTNNLTGKLPDTLCDSGHLTKLILFSNSLDGQIPPSLGACSSL 411
Cdd:PLN00113 327 ALTSLPRLQVLQLWSNKFSGEIPKNLGKHNNLTVLDLSTNNLTGEIPEGLCSSGNLFKLILFSNSLEGEIPKSLGACRSL 406
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 412 ERVRLQKNAFSGDLPRGFTKLQLVNFLDLSNNNLQGNINT--WDMPQLEMLDLSRNNFSGELPDLSRSKRLKKLDLSRNR 489
Cdd:PLN00113 407 RRVRLQDNSFSGELPSEFTKLPLVYFLDISNNNLQGRINSrkWDMPSLQMLSLARNKFFGGLPDSFGSKRLENLDLSRNQ 486
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 490 ISEMVPLRLMAFPELMDMDLSENEITGVIPSELSSCKNLVNLDLSHNNLTGEIPLSFSEFPVLSDLDLSCNRLSGEIPKN 569
Cdd:PLN00113 487 FSGAVPRKLGSLSELMQLKLSENKLSGEIPDELSSCKKLVSLDLSHNQLSGQIPASFSEMPVLSQLDLSQNQLSGEIPKN 566
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 570 LGNIESLVQVNISHNLLHGSLPPTGAFLAINATAVAGNIDLCSSNSASGLRPCKVVRKrsTKSWWFIITSTVVAFLAVLV 649
Cdd:PLN00113 567 LGNVESLVQVNISHNHLHGSLPSTGAFLAINASAVAGNIDLCGGDTTSGLPPCKRVRK--TPSWWFYITCTLGAFLVLAL 644
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 650 SGFfiALVFQKTRNVLEVKKVEQEDGTkWETQFFDSRFMKSFTVNAILSSLNEQNVLVD------------KTGIKFVVK 717
Cdd:PLN00113 645 VAF--GFVFIRGRNNLELKRVENEDGT-WELQFFDSKVSKSITINDILSSLKEENVISRgkkgasykgksiKNGMQFVVK 721
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 718 EVKKYDSLPEM-ISDMRKLsEHKNILKIVATCRSEKEAYLIHEDVEGKRLSQILNGLSWERRRKIMKGIVEALRFLHCRC 796
Cdd:PLN00113 722 EINDVNSIPSSeIADMGKL-QHPNIVKLIGLCRSEKGAYLIHEYIEGKNLSEVLRNLSWERRRKIAIGIAKALRFLHCRC 800
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 797 SPAVVAGNLSPENIVIDVKDQPRLCLGLPGLLCMD------SAYMAPETRERKEMTSKSDIYGFGILLLNLLTGKNSSgd 870
Cdd:PLN00113 801 SPAVVVGNLSPEKIIIDGKDEPHLRLSLPGLLCTDtkcfisSAYVAPETRETKDITEKSDIYGFGLILIELLTGKSPA-- 878
                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 871 eDIASEVNGSLVNWARYSYSNCHIDTWIDSSI--DMSVHKREIVHVMNLALNCTAIDPQERPCTKNVLQALESTSSSSSS 948
Cdd:PLN00113 879 -DAEFGVHGSIVEWARYCYSDCHLDMWIDPSIrgDVSVNQNEIVEVMNLALHCTATDPTARPCANDVLKTLESASRSSSS 957
                        970
                 ....*....|..
gi 297822009 949 CTTYFsKIPSLA 960
Cdd:PLN00113 958 CVTGL-KFSSLF 968
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
30-401 1.99e-33

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 133.91  E-value: 1.99e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009  30 NELELLLSFKSSIQDPLKHLSSWSYSSTNDVCLWTGVVCNNFSRVVSLDLSGKNISGQILTSATFRLPFLRTINLSNNNL 109
Cdd:COG4886    3 LLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 110 SGPIPQDIFTTSSPSLRYLNLSNNNFSGSisrgfLPNLYTLDLSNNMFTgEIYNDIGFFSNLRVLDLGGNVLTgHVPAYL 189
Cdd:COG4886   83 SLLLLGLTDLGDLTNLTELDLSGNEELSN-----LTNLESLDLSGNQLT-DLPEELANLTNLKELDLSNNQLT-DLPEPL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 190 GNLSKLEFLTLASNQFTGgVPAELGKMKNLKWIYLGYNNLSgEIPYQIGGLSSLNHLDLVYNNLSgPIPPSLGDLKNLEY 269
Cdd:COG4886  156 GNLTNLKSLDLSNNQLTD-LPEELGNLTNLKELDLSNNQIT-DLPEPLGNLTNLEELDLSGNQLT-DLPEPLANLTNLET 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 270 MFLYQNKLSGqiPPSIFSLQNLISLDFSDNSLSgEIPElLAQMQTLEILHLFSNNLTGTIPVGVTSLPRLQVLQLWSNRF 349
Cdd:COG4886  233 LDLSNNQLTD--LPELGNLTNLEELDLSNNQLT-DLPP-LANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLL 308
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 297822009 350 SGGIPANLGKHNNLTVLDLSTNNLTGKLPDTLCDSGHLTKLILFSNSLDGQI 401
Cdd:COG4886  309 NLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLS 360
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
727-940 7.14e-33

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: 128.54  E-value: 7.14e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 727 EMISDMRklseHKNILKIVATCRSEKEAYLIHEDVEGKRLSQILNG------LSWERRRKIMKGIVEALRFLHCRCSPAV 800
Cdd:cd14066   42 EMLGRLR----HPNLVRLLGYCLESDEKLLVYEYMPNGSLEDRLHChkgsppLPWPQRLKIAKGIARGLEYLHEECPPPI 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 801 VAGNLSPENIVID------VKD-------QPRLCLGLPGLLCMDSAYMAPETRERKEMTSKSDIYGFGILLLNLLTGKNS 867
Cdd:cd14066  118 IHGDIKSSNILLDedfepkLTDfglarliPPSESVSKTSAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPA 197
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 297822009 868 SGDEDIASEVNgSLVNWARYSYSNC---HIDTWIDSsiDMSVHKREIVHVMNLALNCTAIDPQERPCTKNVLQALE 940
Cdd:cd14066  198 VDENRENASRK-DLVEWVESKGKEEledILDKRLVD--DDGVEEEEVEALLRLALLCTRSDPSLRPSMKEVVQMLE 270
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
68-460 1.26e-31

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 128.51  E-value: 1.26e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009  68 CNNFSRVVSLDLSGKNISGQILTSATFRLPFLRTINLSNNNLSGPIPQDIFTTSSPSLRYLNLSNNNFSGSISRGFLPNL 147
Cdd:COG4886   19 ELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNL 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 148 YTLDLSNNmftgeiyNDIGFFSNLRVLDLGGNVLTgHVPAYLGNLSKLEFLTLASNQFTGgVPAELGKMKNLKWIYLGYN 227
Cdd:COG4886   99 TELDLSGN-------EELSNLTNLESLDLSGNQLT-DLPEELANLTNLKELDLSNNQLTD-LPEPLGNLTNLKSLDLSNN 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 228 NLSgEIPYQIGGLSSLNHLDLVYNNLSgPIPPSLGDLKNLEYMFLYQNKLSgQIPPSIFSLQNLISLDFSDNSLSgEIPE 307
Cdd:COG4886  170 QLT-DLPEELGNLTNLKELDLSNNQIT-DLPEPLGNLTNLEELDLSGNQLT-DLPEPLANLTNLETLDLSNNQLT-DLPE 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 308 LlAQMQTLEILHLFSNNLTgTIPVGvTSLPRLQVLQLWSNRFSGGIPANLGKHNNLTVLDLSTNNLTGKLP-------DT 380
Cdd:COG4886  246 L-GNLTNLEELDLSNNQLT-DLPPL-ANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELlilllllTT 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 381 LCDSGHLTKLILFSNSLDGQIPPSLGACSSLERVRLQKNAFSGDLPRGFTKLQLVNFLDLSNNNLQGNINTWDMPQLEML 460
Cdd:COG4886  323 LLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLL 402
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
195-612 5.59e-26

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 111.95  E-value: 5.59e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 195 LEFLTLASNQFTGGVPAELGKMKNLKWIYLGYNNLSGEIPYQIGGLSSLNHLDLVYNNLSGPIPPSLGDLKNLEYMFLYQ 274
Cdd:COG4886    2 LLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 275 NKLSGQIPPSIFSLQNLISLDFSDNslsgeipELLAQMQTLEILHLFSNNLTgTIPVGVTSLPRLQVLQLWSNRFSGgIP 354
Cdd:COG4886   82 LSLLLLGLTDLGDLTNLTELDLSGN-------EELSNLTNLESLDLSGNQLT-DLPEELANLTNLKELDLSNNQLTD-LP 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 355 ANLGKHNNLTVLDLSTNNLTGkLPDTLCDSGHLTKLILFSNSLDgQIPPSLGACSSLERVRLQKNAFSgDLPRGFTKLql 434
Cdd:COG4886  153 EPLGNLTNLKSLDLSNNQLTD-LPEELGNLTNLKELDLSNNQIT-DLPEPLGNLTNLEELDLSGNQLT-DLPEPLANL-- 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 435 vnfldlsnnnlqgnintwdmPQLEMLDLSRNNFSgELPDLSRSKRLKKLDLSRNRISEMVPlrLMAFPELMDMDLSENEI 514
Cdd:COG4886  228 --------------------TNLETLDLSNNQLT-DLPELGNLTNLEELDLSNNQLTDLPP--LANLTNLKTLDLSNNQL 284
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 515 TGVIPSELSSCKNLVNLDLSHNNLTGEIPLSFSEFPVLSDLDLSCNRLSGEIPKNLGNIESLVQVNISHNLLHGSLPPTG 594
Cdd:COG4886  285 TDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLT 364
                        410
                 ....*....|....*...
gi 297822009 595 AFLAINATAVAGNIDLCS 612
Cdd:COG4886  365 LLLTLGLLGLLEATLLTL 382
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
727-940 9.21e-24

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: 102.19  E-value: 9.21e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 727 EMISDMRklseHKNILKIVATCRSEKEAYLIHEDVEGKRLSQILNG-------LSWERRRKIMKGIVEALRFLHCRCSPA 799
Cdd:cd14664   42 QTLGMIR----HRNIVRLRGYCSNPTTNLLVYEYMPNGSLGELLHSrpesqppLDWETRQRIALGSARGLAYLHHDCSPL 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 800 VVAGNLSPENIVIDVKDQPRLCLGLPGLLCMDSA------------YMAPETRERKEMTSKSDIYGFGILLLNLLTGKNS 867
Cdd:cd14664  118 IIHRDVKSNNILLDEEFEAHVADFGLAKLMDDKDshvmssvagsygYIAPEYAYTGKVSEKSDVYSYGVVLLELITGKRP 197
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 297822009 868 SGDEDIASEVNgsLVNWARYSYSNCHIDTWIDSSIDMSVHKREIVHVMNLALNCTAIDPQERPCTKNVLQALE 940
Cdd:cd14664  198 FDEAFLDDGVD--IVDWVRGLLEEKKVEALVDPDLQGVYKLEEVEQVFQVALLCTQSSPMERPTMREVVRMLE 268
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
711-939 8.99e-18

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: 83.74  E-value: 8.99e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 711 GIKFVVKEVKKYDSLPEMISD-------MRKLSeHKNILKIVATCRSEKEAYLIHEDVEGKRLSQILNG----LSWERRR 779
Cdd:cd13999   16 GTDVAIKKLKVEDDNDELLKEfrrevsiLSKLR-HPNIVQFIGACLSPPPLCIVTEYMPGGSLYDLLHKkkipLSWSLRL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 780 KIMKGIVEALRFLHcrcSPAVVAGNLSPENIVIDVKDQPR------LCLGLPGLLCMDS-----AYMAPETRERKEMTSK 848
Cdd:cd13999   95 KIALDIARGMNYLH---SPPIIHRDLKSLNILLDENFTVKiadfglSRIKNSTTEKMTGvvgtpRWMAPEVLRGEPYTEK 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 849 SDIYGFGILLLNLLTGK----NSSGDEDIASEVNGSLVnwaRYSYSNCHidtwidssIDMSvhkreivhvmNLALNCTAI 924
Cdd:cd13999  172 ADVYSFGIVLWELLTGEvpfkELSPIQIAAAVVQKGLR---PPIPPDCP--------PELS----------KLIKRCWNE 230
                        250
                 ....*....|....*
gi 297822009 925 DPQERPCTKNVLQAL 939
Cdd:cd13999  231 DPEKRPSFSEIVKRL 245
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
732-940 1.52e-17

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: 83.40  E-value: 1.52e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 732 MRKLSeHKNILKIVATCRSEKEAYLIHEDVEGKRLSQILNG---LSWERRRKIMKGIVEALRFLHcrcSPAVVAGNLSPE 808
Cdd:cd14014   54 LARLS-HPNIVRVYDVGEDDGRPYIVMEYVEGGSLADLLRErgpLPPREALRILAQIADALAAAH---RAGIVHRDIKPA 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 809 NIVIDVKDQPR-----------LCLGLPGLLCMDS-AYMAPETRERKEMTSKSDIYGFGILLLNLLTGK----NSSGDED 872
Cdd:cd14014  130 NILLTEDGRVKltdfgiaralgDSGLTQTGSVLGTpAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRppfdGDSPAAV 209
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 297822009 873 IASEVNGSLVNWARYsysNCHIDTWIDssidmsvhkreivhvmNLALNCTAIDPQERPCTKN-VLQALE 940
Cdd:cd14014  210 LAKHLQEAPPPPSPL---NPDVPPALD----------------AIILRALAKDPEERPQSAAeLLAALR 259
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
737-865 4.14e-16

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 82.37  E-value: 4.14e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 737 EHKNILKIVATCRSEKEAYLIHEDVEGKRLSQILNG---LSWERRRKIMKGIVEALRFLHCRCspaVVAGNLSPENI--- 810
Cdd:COG0515   65 NHPNIVRVYDVGEEDGRPYLVMEYVEGESLADLLRRrgpLPPAEALRILAQLAEALAAAHAAG---IVHRDIKPANIllt 141
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 297822009 811 ------VID---VKDQPRLCLGLPGLLCMDSAYMAPETRERKEMTSKSDIYGFGILLLNLLTGK 865
Cdd:COG0515  142 pdgrvkLIDfgiARALGGATLTQTGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGR 205
Pkinase pfam00069
Protein kinase domain;
709-937 1.02e-15

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 77.28  E-value: 1.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009  709 KTGIKFVVKEVKKYDSLPEM-------ISDMRKLSeHKNILKIVATCRSEKEAYLIHEDVEGKRLSQILN---GLSWERR 778
Cdd:pfam00069  22 DTGKIVAIKKIKKEKIKKKKdknilreIKILKKLN-HPNIVRLYDAFEDKDNLYLVLEYVEGGSLFDLLSekgAFSEREA 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009  779 RKIMKGIVEALRFLHCRCSPAVvagnlspenividvkdqprlclglpgllcmDSAYMAPETRERKEMTSKSDIYGFGILL 858
Cdd:pfam00069 101 KFIMKQILEGLESGSSLTTFVG------------------------------TPWYMAPEVLGGNPYGPKVDVWSLGCIL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009  859 LNLLTGK----NSSGDEDIASEVNGSLvnwarysYSNCHIDTWIDSSIDmsvhkreivhvmnLALNCTAIDPQERPCTKN 934
Cdd:pfam00069 151 YELLTGKppfpGINGNEIYELIIDQPY-------AFPELPSNLSEEAKD-------------LLKKLLKKDPSKRLTATQ 210

                  ...
gi 297822009  935 VLQ 937
Cdd:pfam00069 211 ALQ 213
PLN03150 PLN03150
hypothetical protein; Provisional
507-682 2.88e-15

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 80.24  E-value: 2.88e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 507 MDLSENEITGVIPSELSSCKNLVNLDLSHNNLTGEIPLSFSEFPVLSDLDLSCNRLSGEIPKNLGNIESLVQVNISHNLL 586
Cdd:PLN03150 423 LGLDNQGLRGFIPNDISKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNGNSL 502
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 587 HGSLPPTGAFLAINATA--VAGNIDLCssnSASGLRPCKVVRKRSTKSWwfIITSTVVAFLAVLVSGFFialVFQKTRNV 664
Cdd:PLN03150 503 SGRVPAALGGRLLHRASfnFTDNAGLC---GIPGLRACGPHLSVGAKIG--IAFGVSVAFLFLVICAMC---WWKRRQNI 574
                        170       180
                 ....*....|....*....|
gi 297822009 665 LEVKKVEQEDG--TKWETQF 682
Cdd:PLN03150 575 LRAQRIAAREApyAKARTHF 594
PLN03150 PLN03150
hypothetical protein; Provisional
150-240 3.87e-14

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 76.39  E-value: 3.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 150 LDLSNNMFTGEIYNDIGFFSNLRVLDLGGNVLTGHVPAYLGNLSKLEFLTLASNQFTGGVPAELGKMKNLKWIYLGYNNL 229
Cdd:PLN03150 423 LGLDNQGLRGFIPNDISKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNGNSL 502
                         90
                 ....*....|.
gi 297822009 230 SGEIPYQIGGL 240
Cdd:PLN03150 503 SGRVPAALGGR 513
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
709-937 6.19e-14

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 72.56  E-value: 6.19e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009   709 KTGIKFVVKEVKK--YDSLPEM----ISDMRKLSeHKNILKIVATCRSEKEAYLIHEDVEGKRLSQIL---NGLSWERRR 779
Cdd:smart00220  22 KTGKLVAIKVIKKkkIKKDRERilreIKILKKLK-HPNIVRLYDVFEDEDKLYLVMEYCEGGDLFDLLkkrGRLSEDEAR 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009   780 KIMKGIVEALRFLHCRCspaVVAGNLSPENIVIDVKDQPR-----LCLGLPGLLCMDS-----AYMAPETRERKEMTSKS 849
Cdd:smart00220 101 FYLRQILSALEYLHSKG---IVHRDLKPENILLDEDGHVKladfgLARQLDPGEKLTTfvgtpEYMAPEVLLGKGYGKAV 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009   850 DIYGFGILLLNLLTGKNS-SGDEDIAsevngSLVNWARYSYSNCHIDTWIDSSidmsvhkreivHVMNLALNCTAIDPQE 928
Cdd:smart00220 178 DIWSLGVILYELLTGKPPfPGDDQLL-----ELFKKIGKPKPPFPPPEWDISP-----------EAKDLIRKLLVKDPEK 241

                   ....*....
gi 297822009   929 RPCTKNVLQ 937
Cdd:smart00220 242 RLTAEEALQ 250
PLN03150 PLN03150
hypothetical protein; Provisional
198-308 1.36e-13

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 74.85  E-value: 1.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 198 LTLASNQFTGGVPAELGKMKNLKWIYLGYNNLSGEIPYQIGGLSSLNHLDLVYNNLSGPIPPSLGDLKNLEYMFLYQNKL 277
Cdd:PLN03150 423 LGLDNQGLRGFIPNDISKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNGNSL 502
                         90       100       110
                 ....*....|....*....|....*....|...
gi 297822009 278 SGQIPPSIFS-LQNLISLDFSDNS-LSGeIPEL 308
Cdd:PLN03150 503 SGRVPAALGGrLLHRASFNFTDNAgLCG-IPGL 534
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
285-515 3.23e-13

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: 71.62  E-value: 3.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 285 IFSLQNLISLDFSDNSLSGE----IPELLAQMQTLEILHLfSNNLTGTIPVGV-------TSLPRLQVLQLWSNRFSGGI 353
Cdd:cd00116   19 LPKLLCLQVLRLEGNTLGEEaakaLASALRPQPSLKELCL-SLNETGRIPRGLqsllqglTKGCGLQELDLSDNALGPDG 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 354 PA---NLGKHNNLTVLDLSTNNLTG----KLPDTLCDSGH-LTKLILFSNSLDGQIPPSLG----ACSSLERVRLQKNAF 421
Cdd:cd00116   98 CGvleSLLRSSSLQELKLNNNGLGDrglrLLAKGLKDLPPaLEKLVLGRNRLEGASCEALAkalrANRDLKELNLANNGI 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 422 SGD----LPRGFTKLQLVNFLDLSNNN--------LQGNINTWdmPQLEMLDLSRNNFSG----ELPD--LSRSKRLKKL 483
Cdd:cd00116  178 GDAgiraLAEGLKANCNLEVLDLNNNGltdegasaLAETLASL--KSLEVLNLGDNNLTDagaaALASalLSPNISLLTL 255
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 297822009 484 DLSRNRI----SEMVPLRLMAFPELMDMDLSENEIT 515
Cdd:cd00116  256 SLSCNDItddgAKDLAEVLAEKESLLELDLRGNKFG 291
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
737-865 7.50e-13

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: 69.72  E-value: 7.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 737 EHKNILKIVAT---CRSEKEAYLIHEDVEGKRLSQILNG----LSWERRRKIMKGIVEALRFLHCRcspAVVAGNLSPEN 809
Cdd:cd13979   57 RHENIVRVLAAetgTDFASLGLIIMEYCGNGTLQQLIYEgsepLPLAHRILISLDIARALRFCHSH---GIVHLDVKPAN 133
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 810 IVIDVKDQPR--------------LCLGLPGLLCMDSAYMAPETRERKEMTSKSDIYGFGILLLNLLTGK 865
Cdd:cd13979  134 ILISEQGVCKlcdfgcsvklgegnEVGTPRSHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRE 203
PLN03150 PLN03150
hypothetical protein; Provisional
277-358 9.70e-13

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 72.16  E-value: 9.70e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 277 LSGQIPPSIFSLQNLISLDFSDNSLSGEIPELLAQMQTLEILHLFSNNLTGTIPVGVTSLPRLQVLQLWSNRFSGGIPAN 356
Cdd:PLN03150 430 LRGFIPNDISKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNGNSLSGRVPAA 509

                 ..
gi 297822009 357 LG 358
Cdd:PLN03150 510 LG 511
PLN03150 PLN03150
hypothetical protein; Provisional
294-381 1.00e-12

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 72.16  E-value: 1.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 294 LDFSDNSLSGEIPELLAQMQTLEILHLFSNNLTGTIPVGVTSLPRLQVLQLWSNRFSGGIPANLGKHNNLTVLDLSTNNL 373
Cdd:PLN03150 423 LGLDNQGLRGFIPNDISKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNGNSL 502

                 ....*...
gi 297822009 374 TGKLPDTL 381
Cdd:PLN03150 503 SGRVPAAL 510
PLN03150 PLN03150
hypothetical protein; Provisional
246-337 1.15e-12

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 71.77  E-value: 1.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 246 LDLVYNNLSGPIPPSLGDLKNLEYMFLYQNKLSGQIPPSIFSLQNLISLDFSDNSLSGEIPELLAQMQTLEILHLFSNNL 325
Cdd:PLN03150 423 LGLDNQGLRGFIPNDISKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNGNSL 502
                         90
                 ....*....|..
gi 297822009 326 TGTIPVGVTSLP 337
Cdd:PLN03150 503 SGRVPAALGGRL 514
PLN03150 PLN03150
hypothetical protein; Provisional
318-407 1.67e-12

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 71.39  E-value: 1.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 318 LHLFSNNLTGTIPVGVTSLPRLQVLQLWSNRFSGGIPANLGKHNNLTVLDLSTNNLTGKLPDTLCDSGHLTKLILFSNSL 397
Cdd:PLN03150 423 LGLDNQGLRGFIPNDISKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNGNSL 502
                         90
                 ....*....|
gi 297822009 398 DGQIPPSLGA 407
Cdd:PLN03150 503 SGRVPAALGG 512
PLN03150 PLN03150
hypothetical protein; Provisional
30-190 1.80e-12

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 71.39  E-value: 1.80e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009  30 NELELLLSFKSSIQDPLKHlsSWSysstNDVCL-----WTGVVCNnFSRVVS------LDLSGKNISGQILTSATfRLPF 98
Cdd:PLN03150 372 EEVSALQTLKSSLGLPLRF--GWN----GDPCVpqqhpWSGADCQ-FDSTKGkwfidgLGLDNQGLRGFIPNDIS-KLRH 443
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009  99 LRTINLSNNNLSGPIPqdifttsspslrylnlsnnnfsgsISRGFLPNLYTLDLSNNMFTGEIYNDIGFFSNLRVLDLGG 178
Cdd:PLN03150 444 LQSINLSGNSIRGNIP------------------------PSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNG 499
                        170
                 ....*....|..
gi 297822009 179 NVLTGHVPAYLG 190
Cdd:PLN03150 500 NSLSGRVPAALG 511
PLN03150 PLN03150
hypothetical protein; Provisional
128-214 3.00e-11

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 67.15  E-value: 3.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 128 LNLSNNNFsgsisRGFLPN-------LYTLDLSNNMFTGEIYNDIGFFSNLRVLDLGGNVLTGHVPAYLGNLSKLEFLTL 200
Cdd:PLN03150 423 LGLDNQGL-----RGFIPNdisklrhLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNL 497
                         90
                 ....*....|....
gi 297822009 201 ASNQFTGGVPAELG 214
Cdd:PLN03150 498 NGNSLSGRVPAALG 511
PLN03150 PLN03150
hypothetical protein; Provisional
174-262 3.50e-11

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 67.15  E-value: 3.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 174 LDLGGNVLTGHVPAYLGNLSKLEFLTLASNQFTGGVPAELGKMKNLKWIYLGYNNLSGEIPYQIGGLSSLNHLDLVYNNL 253
Cdd:PLN03150 423 LGLDNQGLRGFIPNDISKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNGNSL 502

                 ....*....
gi 297822009 254 SGPIPPSLG 262
Cdd:PLN03150 503 SGRVPAALG 511
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
709-937 1.34e-10

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


Pssm-ID: 270687 [Multi-domain]  Cd Length: 258  Bit Score: 62.88  E-value: 1.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 709 KTGIKFVVKEVKKYDSLPEMISD-------MRKLSeHKNILKIVATCRSEKEAYLIHEDVEGKRL-SQILNGLSW-ERR- 778
Cdd:cd05117   23 KTGEEYAVKIIDKKKLKSEDEEMlrreieiLKRLD-HPNIVKLYEVFEDDKNLYLVMELCTGGELfDRIVKKGSFsEREa 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 779 RKIMKGIVEALRFLHCRCspaVVAGNLSPENIVIDVKDQPRLC--------LGLPGLLCMDSA-----YMAPETRERKEM 845
Cdd:cd05117  102 AKIMKQILSAVAYLHSQG---IVHRDLKPENILLASKDPDSPIkiidfglaKIFEEGEKLKTVcgtpyYVAPEVLKGKGY 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 846 TSKSDIYGFGILLLNLLTGK---NSSGDEDIASEV-NGslvnwaRYSYSNchiDTWIDSSidmsvhkreiVHVMNLALNC 921
Cdd:cd05117  179 GKKCDIWSLGVILYILLCGYppfYGETEQELFEKIlKG------KYSFDS---PEWKNVS----------EEAKDLIKRL 239
                        250
                 ....*....|....*.
gi 297822009 922 TAIDPQERPCTKNVLQ 937
Cdd:cd05117  240 LVVDPKKRLTAAEALN 255
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
708-939 1.37e-10

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: 62.95  E-value: 1.37e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009   708 DKTGIKFVVKEVKKyDSLPEMISD-------MRKLSeHKNILKIVATCRSEKEAYLIHEDVEGKRLSQIL-----NGLSW 775
Cdd:smart00221  25 DGKEVEVAVKTLKE-DASEQQIEEflreariMRKLD-HPNIVKLLGVCTEEEPLMIVMEYMPGGDLLDYLrknrpKELSL 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009   776 ERRRKIMKGIVEALRFLHCRCspaVVAGNLSPENIVID----VK--------DQPRLCLGLPGLLCMDSAYMAPETRERK 843
Cdd:smart00221 103 SDLLSFALQIARGMEYLESKN---FIHRDLAARNCLVGenlvVKisdfglsrDLYDDDYYKVKGGKLPIRWMAPESLKEG 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009   844 EMTSKSDIYGFGILLLNLLTGknssGDEDIASEVNGSLVNWARYSY-----SNCHidtwidssidmsvhkREIVHVMnla 918
Cdd:smart00221 180 KFTSKSDVWSFGVLLWEIFTL----GEEPYPGMSNAEVLEYLKKGYrlpkpPNCP---------------PELYKLM--- 237
                          250       260
                   ....*....|....*....|.
gi 297822009   919 LNCTAIDPQERPCTKNVLQAL 939
Cdd:smart00221 238 LQCWAEDPEDRPTFSELVEIL 258
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
708-939 2.93e-10

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 61.78  E-value: 2.93e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009   708 DKTGIKFVVKEVKKyDSLPEMISD-------MRKLSeHKNILKIVATCRSEKEAYLIHEDVEGKRLSQIL----NGLSWE 776
Cdd:smart00219  25 GKKKVEVAVKTLKE-DASEQQIEEflreariMRKLD-HPNVVKLLGVCTEEEPLYIVMEYMEGGDLLSYLrknrPKLSLS 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009   777 RRRKIMKGIVEALRFLH-CRCspavVAGNLSPENIVID----VK--------DQPRLCLGLPGLLCMDSAYMAPETRERK 843
Cdd:smart00219 103 DLLSFALQIARGMEYLEsKNF----IHRDLAARNCLVGenlvVKisdfglsrDLYDDDYYRKRGGKLPIRWMAPESLKEG 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009   844 EMTSKSDIYGFGILLLNLLTGknssGDEDIASEVNGSLVNWARYSY-----SNCHidtwidssidmsvhkREIVHVMnla 918
Cdd:smart00219 179 KFTSKSDVWSFGVLLWEIFTL----GEQPYPGMSNEEVLEYLKNGYrlpqpPNCP---------------PELYDLM--- 236
                          250       260
                   ....*....|....*....|.
gi 297822009   919 LNCTAIDPQERPCTKNVLQAL 939
Cdd:smart00219 237 LQCWAEDPEDRPTFSELVEIL 257
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
716-865 4.16e-10

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: 61.70  E-value: 4.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 716 VKEVKKYDSLPEMISD-------MRKLSeHKNILKIVATCRSEKEAYLIHEDVEGKRLSQILNGLS----WERRRKIMKG 784
Cdd:cd13978   23 IKCLHSSPNCIEERKAllkeaekMERAR-HSYVLPLLGVCVERRSLGLVMEYMENGSLKSLLEREIqdvpWSLRFRIIHE 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 785 IVEALRFLHCrCSPAVVAGNLSPENIVID----VKDQP-------RLCLGLPGLLCMDS-----AYMAPETRE--RKEMT 846
Cdd:cd13978  102 IALGMNFLHN-MDPPLLHHDLKPENILLDnhfhVKISDfglsklgMKSISANRRRGTENlggtpIYMAPEAFDdfNKKPT 180
                        170
                 ....*....|....*....
gi 297822009 847 SKSDIYGFGILLLNLLTGK 865
Cdd:cd13978  181 SKSDVYSFAIVIWAVLTRK 199
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
359-562 9.01e-10

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: 61.22  E-value: 9.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 359 KHNNLTVLDLSTNNLTGK----LPDTLCDSGHLTKLILFSNSLdGQIPPSLGAC-------SSLERVRLQKNAFSGDLPR 427
Cdd:cd00116   21 KLLCLQVLRLEGNTLGEEaakaLASALRPQPSLKELCLSLNET-GRIPRGLQSLlqgltkgCGLQELDLSDNALGPDGCG 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 428 GFTKLQLVNFL---DLSNNNLQGNIN-------TWDMPQLEMLDLSRNNFSGELPD-----LSRSKRLKKLDLSRNRISE 492
Cdd:cd00116  100 VLESLLRSSSLqelKLNNNGLGDRGLrllakglKDLPPALEKLVLGRNRLEGASCEalakaLRANRDLKELNLANNGIGD 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 493 ----MVPLRLMAFPELMDMDLSENEIT---GVIPSE-LSSCKNLVNLDLSHNNLTGEIPLSF-----SEFPVLSDLDLSC 559
Cdd:cd00116  180 agirALAEGLKANCNLEVLDLNNNGLTdegASALAEtLASLKSLEVLNLGDNNLTDAGAAALasallSPNISLLTLSLSC 259

                 ...
gi 297822009 560 NRL 562
Cdd:cd00116  260 NDI 262
PLN03150 PLN03150
hypothetical protein; Provisional
366-449 9.98e-10

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 62.53  E-value: 9.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 366 LDLSTNNLTGKLPDTLCDSGHLTKLILFSNSLDGQIPPSLGACSSLERVRLQKNAFSGDLPRGFTKLQLVNFLDLSNNNL 445
Cdd:PLN03150 423 LGLDNQGLRGFIPNDISKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNGNSL 502

                 ....
gi 297822009 446 QGNI 449
Cdd:PLN03150 503 SGRV 506
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
709-865 1.76e-09

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


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 59.46  E-value: 1.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 709 KTGIKFVVKEV-------KKYDSLPEMISDMRKLSeHKNILKIVATCRSEKEAYLIHEDVEGKRLSQILN---GLSWERR 778
Cdd:cd06606   23 DTGELMAVKEVelsgdseEELEALEREIRILSSLK-HPNIVRYLGTERTENTLNIFLEYVPGGSLASLLKkfgKLPEPVV 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 779 RKIMKGIVEALRFLHCRCspaVVAGNLSPENIVIDVKDQ--------PRLCLGLPGLLCMDS-----AYMAPETRERKEM 845
Cdd:cd06606  102 RKYTRQILEGLEYLHSNG---IVHRDIKGANILVDSDGVvkladfgcAKRLAEIATGEGTKSlrgtpYWMAPEVIRGEGY 178
                        170       180
                 ....*....|....*....|
gi 297822009 846 TSKSDIYGFGILLLNLLTGK 865
Cdd:cd06606  179 GRAADIWSLGCTVIEMATGK 198
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
710-939 2.23e-09

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: 59.04  E-value: 2.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 710 TGIKFVVKEVKKYD---SLPEMISDMRKLSeHKNILKIVATCRSEKEAYLIHEDVEGKRLSQILNG----LSWERRRKIM 782
Cdd:cd14065   17 TGKVMVMKELKRFDeqrSFLKEVKLMRRLS-HPNILRFIGVCVKDNKLNFITEYVNGGTLEELLKSmdeqLPWSQRVSLA 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 783 KGIVEALRFLHcrcSPAVVAGNLSPENIVIDVKDQPRLCLGL-------------------PGLLCMDSAY-MAPETRER 842
Cdd:cd14065   96 KDIASGMAYLH---SKNIIHRDLNSKNCLVREANRGRNAVVAdfglarempdektkkpdrkKRLTVVGSPYwMAPEMLRG 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 843 KEMTSKSDIYGFGILLLNLLTGKNSSGDEDIASEVNGSLVNWARYSY-SNCHIDtwidssidmsvhkreivhVMNLALNC 921
Cdd:cd14065  173 ESYDEKVDVFSFGIVLCEIIGRVPADPDYLPRTMDFGLDVRAFRTLYvPDCPPS------------------FLPLAIRC 234
                        250
                 ....*....|....*...
gi 297822009 922 TAIDPQERPCTKNVLQAL 939
Cdd:cd14065  235 CQLDPEKRPSFVELEHHL 252
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
729-940 2.58e-09

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: 59.44  E-value: 2.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 729 ISDMRKLSeHKNILKIVATCRSEKEAYLIHE-DVEGKRLSQI--LNG---LSWERRRKIMKGIVEALRFLHcrcSPAVVA 802
Cdd:cd14158   65 IQVMAKCQ-HENLVELLGYSCDGPQLCLVYTyMPNGSLLDRLacLNDtppLSWHMRCKIAQGTANGINYLH---ENNHIH 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 803 GNLSPENIVID------VKDQPRLCLGLPGLLCM-------DSAYMAPETReRKEMTSKSDIYGFGILLLNLLTG----- 864
Cdd:cd14158  141 RDIKSANILLDetfvpkISDFGLARASEKFSQTImterivgTTAYMAPEAL-RGEITPKSDIFSFGVVLLEIITGlppvd 219
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 297822009 865 --KNSSGDEDIASEVNGSLVNwarysysnchIDTWIDSSidMSVHKREIVHVM-NLALNCTAIDPQERPCTKNVLQALE 940
Cdd:cd14158  220 enRDPQLLLDIKEEIEDEEKT----------IEDYVDKK--MGDWDSTSIEAMySVASQCLNDKKNRRPDIAKVQQLLQ 286
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
735-940 2.62e-09

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: 59.13  E-value: 2.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 735 LSEHKNILKIVATCRSEKEAYLIHEDVEGKRLSQILNG------LSWERRRKIMKGIVEALRFLHCRCSPAVVAGNLSPE 808
Cdd:cd14160   48 LFQHPNILELAAYFTETEKFCLVYPYMQNGTLFDRLQChgvtkpLSWHERINILIGIAKAIHYLHNSQPCTVICGNISSA 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 809 NIVIDVKDQPRL-----------CLGLPGLLCMDSA------YMAPETRERKEMTSKSDIYGFGILLLNLLTGKNSSGDE 871
Cdd:cd14160  128 NILLDDQMQPKLtdfalahfrphLEDQSCTINMTTAlhkhlwYMPEEYIRQGKLSVKTDVYSFGIVIMEVLTGCKVVLDD 207
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 297822009 872 DIASEVNGSLVNWARysysnchiDTWIDSSidMSVHKREIVH--------VMNLALNCTAIDPQERPCTKNVLQALE 940
Cdd:cd14160  208 PKHLQLRDLLHELME--------KRGLDSC--LSFLDLKFPPcprnfsakLFRLAGRCTATKAKLRPDMDEVLQRLE 274
LRRNT_2 pfam08263
Leucine rich repeat N-terminal domain; Leucine Rich Repeats pfam00560 are short sequence ...
28-69 2.69e-09

Leucine rich repeat N-terminal domain; Leucine Rich Repeats pfam00560 are short sequence motifs present in a number of proteins with diverse functions and cellular locations. Leucine Rich Repeats are often flanked by cysteine rich domains. This domain is often found at the N-terminus of tandem leucine rich repeats.


Pssm-ID: 462411 [Multi-domain]  Cd Length: 41  Bit Score: 53.45  E-value: 2.69e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 297822009   28 HANELELLLSFKSSIQDPLKHLSSWSYSSTnDVCLWTGVVCN 69
Cdd:pfam08263   1 LNDDGQALLAFKSSLNDPPGALSSWNSSSS-DPCSWTGVTCD 41
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
708-875 4.61e-09

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


Pssm-ID: 270983 [Multi-domain]  Cd Length: 255  Bit Score: 58.42  E-value: 4.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 708 DKTGIKFVVKEVKKYDSLP---EM-ISDMrKLSEHKNILKIVATCRSEKEAYLIHEDVEGKRLSQILN---GLSWERRRK 780
Cdd:cd14081   27 QKVAIKIVNKEKLSKESVLmkvEReIAIM-KLIEHPNVLKLYDVYENKKYLYLVLEYVSGGELFDYLVkkgRLTEKEARK 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 781 IMKGIVEALRFLHCRCspaVVAGNLSPENIVIDVKDQPRLCLGLPGLLCMDSA----------YMAPET-RERKEMTSKS 849
Cdd:cd14081  106 FFRQIISALDYCHSHS---ICHRDLKPENLLLDEKNNIKIADFGMASLQPEGSlletscgsphYACPEViKGEKYDGRKA 182
                        170       180
                 ....*....|....*....|....*.
gi 297822009 850 DIYGFGILLLNLLTGKNSSGDEDIAS 875
Cdd:cd14081  183 DIWSCGVILYALLVGALPFDDDNLRQ 208
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
710-937 5.80e-09

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called Ribosomal protein S6 kinase alpha-1 or 90kDa ribosomal protein S6 kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK1 is also called S6K-alpha-1, RPS6KA1, p90RSK1 or MAPK-activated protein kinase 1a (MAPKAPK-1a). It is a component of the insulin transduction pathway, regulating the function of IRS1. It also interacts with PKA and promotes its inactivation. RSK1 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271077 [Multi-domain]  Cd Length: 291  Bit Score: 58.50  E-value: 5.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 710 TGIKFVVKEVKKYDSLP-EMISDMRKLSEHKNILKIVATCRSEKEAYLIHEDVEG-KRLSQILNGLSWERRRK--IMKGI 785
Cdd:cd14175   25 TNMEYAVKVIDKSKRDPsEEIEILLRYGQHPNIITLKDVYDDGKHVYLVTELMRGgELLDKILRQKFFSEREAssVLHTI 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 786 VEALRFLHcrcSPAVVAGNLSPENIV-IDVKDQP--------------RLCLGLPGLLCMDSAYMAPETRERKEMTSKSD 850
Cdd:cd14175  105 CKTVEYLH---SQGVVHRDLKPSNILyVDESGNPeslricdfgfakqlRAENGLLMTPCYTANFVAPEVLKRQGYDEGCD 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 851 IYGFGILLLNLLTGKN--SSGDEDIASEVNgSLVNWARYSYSNCHIDTWIDSSIDMsVHKreIVHVmnlalnctaiDPQE 928
Cdd:cd14175  182 IWSLGILLYTMLAGYTpfANGPSDTPEEIL-TRIGSGKFTLSGGNWNTVSDAAKDL-VSK--MLHV----------DPHQ 247

                 ....*....
gi 297822009 929 RPCTKNVLQ 937
Cdd:cd14175  248 RLTAKQVLQ 256
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
714-865 2.21e-08

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: 56.76  E-value: 2.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 714 FVVKEVKKYDSLP------EMISDMRKLSE--HKNILKIVATCRSEKEAYLIHEDVEGKRLSQILN------GLSWERRR 779
Cdd:cd14159   19 YAVKRLKEDSELDwsvvknSFLTEVEKLSRfrHPNIVDLAGYSAQQGNYCLIYVYLPNGSLEDRLHcqvscpCLSWSQRL 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 780 KIMKGIVEALRFLHcRCSPAVVAGNLSPENIVIDVKDQPRLC-------LGLPGLLCMDS------------AYMAPETR 840
Cdd:cd14159   99 HVLLGTARAIQYLH-SDSPSLIHGDVKSSNILLDAALNPKLGdfglarfSRRPKQPGMSStlartqtvrgtlAYLPEEYV 177
                        170       180
                 ....*....|....*....|....*
gi 297822009 841 ERKEMTSKSDIYGFGILLLNLLTGK 865
Cdd:cd14159  178 KTGTLSVEIDVYSFGVVLLELLTGR 202
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
246-497 3.07e-08

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: 56.59  E-value: 3.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 246 LDLVYNNLSGP----IPPSLGDLKNLEYMFLYQNKLsGQIPPSIFSL-QNLIS------LDFSDNSLSGEIP---ELLAQ 311
Cdd:cd00116   28 LRLEGNTLGEEaakaLASALRPQPSLKELCLSLNET-GRIPRGLQSLlQGLTKgcglqeLDLSDNALGPDGCgvlESLLR 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 312 MQTLEILHLFSNNLTGTI-PVGVTSL----PRLQVLQLWSNRFSGGIPANLGK----HNNLTVLDLSTNNLTGKLPDTLC 382
Cdd:cd00116  107 SSSLQELKLNNNGLGDRGlRLLAKGLkdlpPALEKLVLGRNRLEGASCEALAKalraNRDLKELNLANNGIGDAGIRALA 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 383 ----DSGHLTKLILFSNSL----DGQIPPSLGACSSLERVRLQKN--------AFSGDLPRGFTKLQLvnfLDLSNNNLQ 446
Cdd:cd00116  187 eglkANCNLEVLDLNNNGLtdegASALAETLASLKSLEVLNLGDNnltdagaaALASALLSPNISLLT---LSLSCNDIT 263
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 297822009 447 GN--------INtwDMPQLEMLDLSRNNFSGELPDLSRSKRLKKldlsRNRISEMVPLR 497
Cdd:cd00116  264 DDgakdlaevLA--EKESLLELDLRGNKFGEEGAQLLAESLLEP----GNELESLWVKD 316
PLN03150 PLN03150
hypothetical protein; Provisional
460-551 3.25e-08

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 57.52  E-value: 3.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 460 LDLSRNNFSGELP-DLSRSKRLKKLDLSRNRISEMVPLRLMAFPELMDMDLSENEITGVIPSELSSCKNLVNLDLSHNNL 538
Cdd:PLN03150 423 LGLDNQGLRGFIPnDISKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNGNSL 502
                         90
                 ....*....|...
gi 297822009 539 TGEIPLSFSEFPV 551
Cdd:PLN03150 503 SGRVPAALGGRLL 515
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
727-930 4.98e-08

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: 55.47  E-value: 4.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 727 EMISDMRKLSeHKNILKIVATCRSEKEAYLIHEDVEGKRLSQILN----GLSWERRRKIMKGIVEALRFLHCrcSPAVVA 802
Cdd:cd13992   45 QELNQLKELV-HDNLNKFIGICINPPNIAVVTEYCTRGSLQDVLLnreiKMDWMFKSSFIKDIVKGMNYLHS--SSIGYH 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 803 GNLSPENIVID----VK------DQPRLCLGLPGLLCMDSA----YMAPE-TRER---KEMTSKSDIYGFGILLLNLLTG 864
Cdd:cd13992  122 GRLKSSNCLVDsrwvVKltdfglRNLLEEQTNHQLDEDAQHkkllWTAPElLRGSlleVRGTQKGDVYSFAIILYEILFR 201
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 297822009 865 KNSSGDEDIASEVngslvnwarYSYSNCHIDTWIdssIDMSVHKREI-VHVMNLALNCTAIDPQERP 930
Cdd:cd13992  202 SDPFALEREVAIV---------EKVISGGNKPFR---PELAVLLDEFpPRLVLLVKQCWAENPEKRP 256
PLN03150 PLN03150
hypothetical protein; Provisional
414-502 5.11e-08

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 56.75  E-value: 5.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 414 VRLQKNAFSGDLPRGFTKLQLVNFLDLSNNNLQGNI--NTWDMPQLEMLDLSRNNFSGELPD-LSRSKRLKKLDLSRNRI 490
Cdd:PLN03150 423 LGLDNQGLRGFIPNDISKLRHLQSINLSGNSIRGNIppSLGSITSLEVLDLSYNSFNGSIPEsLGQLTSLRILNLNGNSL 502
                         90
                 ....*....|..
gi 297822009 491 SEMVPLRLMAFP 502
Cdd:PLN03150 503 SGRVPAALGGRL 514
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
710-937 6.81e-08

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called Ribosomal protein S6 kinase alpha-6 or 90kDa ribosomal protein S6 kinase 6); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK4 is also called S6K-alpha-6, RPS6KA6, p90RSK6 or pp90RSK4. RSK4 is a substrate of ERK and is a modulator of p53-dependent proliferation arrest in human cells. Deletion of the RSK4 gene, RPS6KA6, frequently occurs in patients of X-linked deafness type 3, mental retardation and choroideremia. Studies of RSK4 in cancer cells and tissues suggest that it may be oncogenic or tumor suppressive depending on many factors. RSK4 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 55.41  E-value: 6.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 710 TGIKFVVKEVKKYDSLP-EMISDMRKLSEHKNILKIVATCRSEKEAYLIHEDVEG-KRLSQILNGLSWERRRK--IMKGI 785
Cdd:cd14177   28 TNMEFAVKIIDKSKRDPsEEIEILMRYGQHPNIITLKDVYDDGRYVYLVTELMKGgELLDRILRQKFFSEREAsaVLYTI 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 786 VEALRFLHCRcspAVVAGNLSPENIV----------IDVKD-----QPRLCLGLPGLLCMDSAYMAPETRERKEMTSKSD 850
Cdd:cd14177  108 TKTVDYLHCQ---GVVHRDLKPSNILymddsanadsIRICDfgfakQLRGENGLLLTPCYTANFVAPEVLMRQGYDAACD 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 851 IYGFGILLLNLLTGKN--SSGDEDIASEVNGSLVNwARYSYSNCHIDTWIDSSIDMSVHkreIVHVmnlalnctaiDPQE 928
Cdd:cd14177  185 IWSLGVLLYTMLAGYTpfANGPNDTPEEILLRIGS-GKFSLSGGNWDTVSDAAKDLLSH---MLHV----------DPHQ 250

                 ....*....
gi 297822009 929 RPCTKNVLQ 937
Cdd:cd14177  251 RYTAEQVLK 259
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
695-858 1.78e-07

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: 53.70  E-value: 1.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 695 AILSSLNEQNVLVDktgikfvVKEVKKYDSLPEM------ISDMRKLSeHKNILKIVATCRSEKEAYLIHEDVEGKRL-- 766
Cdd:cd00192   14 GKLKGGDGKTVDVA-------VKTLKEDASESERkdflkeARVMKKLG-HPNVVRLLGVCTEEEPLYLVMEYMEGGDLld 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 767 ----------SQILNGLSWERRRKIMKGIVEALRFLHcrcSPAVVAGNLSPENIVIDVKDQP--------RLCLGLPGLL 828
Cdd:cd00192   86 flrksrpvfpSPEPSTLSLKDLLSFAIQIAKGMEYLA---SKKFVHRDLAARNCLVGEDLVVkisdfglsRDIYDDDYYR 162
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 297822009 829 CMDSA-----YMAPETRERKEMTSKSDIYGFGILL 858
Cdd:cd00192  163 KKTGGklpirWMAPESLKDGIFTSKSDVWSFGVLL 197
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
710-893 2.63e-07

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


Pssm-ID: 270908 [Multi-domain]  Cd Length: 247  Bit Score: 52.66  E-value: 2.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 710 TGIKFVVKEVKKYDSLPEM----ISDMRKLSeHKNILKIVATCRSEKEAYLIHEDVEGKRLSQILNG---LSWERRRKIM 782
Cdd:cd14006   17 TGREFAAKFIPKRDKKKEAvlreISILNQLQ-HPRIIQLHEAYESPTELVLILELCSGGELLDRLAErgsLSEEEVRTYM 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 783 KGIVEALRFLH-CRcspaVVAGNLSPENIVIDVKDQP-----------RLCLGLPGLLCMDSA-YMAPETRERKEMTSKS 849
Cdd:cd14006   96 RQLLEGLQYLHnHH----ILHLDLKPENILLADRPSPqikiidfglarKLNPGEELKEIFGTPeFVAPEIVNGEPVSLAT 171
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 297822009 850 DIYGFGILLLNLLTGKNS-SGDEDIASEVNgslVNWARYSYSNCH 893
Cdd:cd14006  172 DMWSIGVLTYVLLSGLSPfLGEDDQETLAN---ISACRVDFSEEY 213
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
438-587 3.20e-07

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: 52.10  E-value: 3.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 438 LDLSNNNLQ--GNINTwdMPQLEMLDLSRNNFSgELPDLSRSKRLKKLDLSRNRISEmvplrlmafpelmdmdlseneIT 515
Cdd:cd21340   29 LYLYDNKITkiENLEF--LTNLTHLYLQNNQIE-KIENLENLVNLKKLYLGGNRISV---------------------VE 84
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 297822009 516 GvipseLSSCKNLVNLDLSHNNLTGEIPLSFSEF------PVLSDLDLSCNRLSgeIPKNLGNIESLVQVNISHNLLH 587
Cdd:cd21340   85 G-----LENLTNLEELHIENQRLPPGEKLTFDPRslaalsNSLRVLNISGNNID--SLEPLAPLRNLEQLDASNNQIS 155
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
710-937 4.17e-07

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called Ribosomal protein S6 kinase alpha-2 or 90kDa ribosomal protein S6 kinase 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK3 is also called S6K-alpha-2, RPS6KA2, p90RSK2 or MAPK-activated protein kinase 1c (MAPKAPK-1c). RSK3 binds muscle A-kinase anchoring protein (mAKAP)-b directly and regulates concentric cardiac myocyte growth. The RSK3 gene, RPS6KA2, is a putative tumor suppressor gene in sporadic epithelial ovarian cancer and variations to the gene may be associated with rectal cancer risk. RSK3 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 52.71  E-value: 4.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 710 TGIKFVVKEVKKYDSLP-EMISDMRKLSEHKNILKIVATCRSEKEAYLIHEDVEG-KRLSQILNGLSWERRR--KIMKGI 785
Cdd:cd14178   27 TSTEYAVKIIDKSKRDPsEEIEILLRYGQHPNIITLKDVYDDGKFVYLVMELMRGgELLDRILRQKCFSEREasAVLCTI 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 786 VEALRFLHcrcSPAVVAGNLSPENIV----------IDVKD-----QPRLCLGLPGLLCMDSAYMAPETRERKEMTSKSD 850
Cdd:cd14178  107 TKTVEYLH---SQGVVHRDLKPSNILymdesgnpesIRICDfgfakQLRAENGLLMTPCYTANFVAPEVLKRQGYDAACD 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 851 IYGFGILLLNLLTGKN--SSGDEDIASEVNGSlVNWARYSYSNCHIDTWIDSSIDMSVhkrEIVHVmnlalnctaiDPQE 928
Cdd:cd14178  184 IWSLGILLYTMLAGFTpfANGPDDTPEEILAR-IGSGKYALSGGNWDSISDAAKDIVS---KMLHV----------DPHQ 249

                 ....*....
gi 297822009 929 RPCTKNVLQ 937
Cdd:cd14178  250 RLTAPQVLR 258
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
710-937 5.25e-07

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called 90kDa ribosomal protein S6 kinase 3 or Ribosomal protein S6 kinase alpha-3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK2 is also called p90RSK3, RPS6KA3, S6K-alpha-3, or MAPK-activated protein kinase 1b (MAPKAPK-1b). RSK2 is expressed highly in the regions of the brain with high synaptic activity. It plays a role in the maintenance and consolidation of excitatory synapses. It is a specific modulator of phospholipase D in calcium-regulated exocytosis. Mutations in the RSK2 gene, RPS6KA3, cause Coffin-Lowry syndrome (CLS), a rare syndromic form of X-linked mental retardation characterized by growth and psychomotor retardation and skeletal abnormalities. RSK2 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 52.72  E-value: 5.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 710 TGIKFVVKEVKKYDSLP-EMISDMRKLSEHKNILKIVATCRSEKEAYLIHEDVEG-KRLSQILNGLSWERRRK--IMKGI 785
Cdd:cd14176   43 TNMEFAVKIIDKSKRDPtEEIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGgELLDKILRQKFFSEREAsaVLFTI 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 786 VEALRFLHcrcSPAVVAGNLSPENIV-IDVKDQP--------------RLCLGLPGLLCMDSAYMAPETRERKEMTSKSD 850
Cdd:cd14176  123 TKTVEYLH---AQGVVHRDLKPSNILyVDESGNPesiricdfgfakqlRAENGLLMTPCYTANFVAPEVLERQGYDAACD 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 851 IYGFGILLLNLLTGKN--SSGDEDIASEVNGSlVNWARYSYSNCHIDTWIDSSIDMSvhkREIVHVmnlalnctaiDPQE 928
Cdd:cd14176  200 IWSLGVLLYTMLTGYTpfANGPDDTPEEILAR-IGSGKFSLSGGYWNSVSDTAKDLV---SKMLHV----------DPHQ 265

                 ....*....
gi 297822009 929 RPCTKNVLQ 937
Cdd:cd14176  266 RLTAALVLR 274
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
709-865 5.33e-07

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


Pssm-ID: 270896 [Multi-domain]  Cd Length: 265  Bit Score: 52.31  E-value: 5.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 709 KTGIKFVVKEVKKyDSLPEMISDMRK--LSE--------HKNILKIVATCRSEKEAY-LIHEDVEGKRLSQIL---NGLS 774
Cdd:cd13994   18 RSGVLYAVKEYRR-RDDESKRKDYVKrlTSEyiissklhHPNIVKVLDLCQDLHGKWcLVMEYCPGGDLFTLIekaDSLS 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 775 WERRRKIMKGIVEALRFLHcrcSPAVVAGNLSPENIVID---------------VKDQPRLCLGLPGLLCMDSAYMAPET 839
Cdd:cd13994   97 LEEKDCFFKQILRGVAYLH---SHGIAHRDLKPENILLDedgvlkltdfgtaevFGMPAEKESPMSAGLCGSEPYMAPEV 173
                        170       180
                 ....*....|....*....|....*..
gi 297822009 840 RERKEMTSKS-DIYGFGILLLNLLTGK 865
Cdd:cd13994  174 FTSGSYDGRAvDVWSCGIVLFALFTGR 200
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
710-858 6.39e-07

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


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 52.12  E-value: 6.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 710 TGIKFVVKEVKKYDS------LPEmISDMRKLsEHKNILKIVATCRSEKEAYLIHEDVEGKRLSQILNG----LSWERRR 779
Cdd:cd14154   17 TGEVMVMKELIRFDEeaqrnfLKE-VKVMRSL-DHPNVLKFIGVLYKDKKLNLITEYIPGGTLKDVLKDmarpLPWAQRV 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 780 KIMKGIVEALRFLH-------------C--RCSPAVVAGNLSPENIVIDVKDQPRLCLGLPGLLCMDSA----------- 833
Cdd:cd14154   95 RFAKDIASGMAYLHsmniihrdlnshnClvREDKTVVVADFGLARLIVEERLPSGNMSPSETLRHLKSPdrkkrytvvgn 174
                        170       180
                 ....*....|....*....|....*..
gi 297822009 834 --YMAPETRERKEMTSKSDIYGFGILL 858
Cdd:cd14154  175 pyWMAPEMLNGRSYDEKVDIFSFGIVL 201
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
738-865 6.56e-07

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


Pssm-ID: 270909 [Multi-domain]  Cd Length: 253  Bit Score: 51.71  E-value: 6.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 738 HKNILKIVATCRSEKEAYLIHEDVEGKRLSQILNG---LSWERRRKIMKGIVEALRFLHcrcSPAVVAGNLSPENIVIDV 814
Cdd:cd14007   59 HPNILRLYGYFEDKKRIYLILEYAPNGELYKELKKqkrFDEKEAAKYIYQLALALDYLH---SKNIIHRDIKPENILLGS 135
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 297822009 815 K---------------DQPRLCLGLPgllcMDsaYMAPETRERKEMTSKSDIYGFGILLLNLLTGK 865
Cdd:cd14007  136 NgelkladfgwsvhapSNRRKTFCGT----LD--YLPPEMVEGKEYDYKVDIWSLGVLCYELLVGK 195
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
710-940 7.58e-07

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


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 51.88  E-value: 7.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 710 TGIKFVVKEVKKYD-----SLPEMISDMRKLsEHKNILKIVATCRSEKEAYLIHEDVEGKRLSQILNGLS----WERRRK 780
Cdd:cd14221   17 TGEVMVMKELIRFDeetqrTFLKEVKVMRCL-EHPNVLKFIGVLYKDKRLNFITEYIKGGTLRGIIKSMDshypWSQRVS 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 781 IMKGIVEALRFLH---------------CRCSPAVVAGNLSPENIVIDVKDQPRLCLGLPGLLCM-------DSAYMAPE 838
Cdd:cd14221   96 FAKDIASGMAYLHsmniihrdlnshnclVRENKSVVVADFGLARLMVDEKTQPEGLRSLKKPDRKkrytvvgNPYWMAPE 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 839 TRERKEMTSKSDIYGFGILLLNLLTGKNSSGD-----EDIASEVNGSLvnwARYSYSNCHidtwidssidmsvhkreiVH 913
Cdd:cd14221  176 MINGRSYDEKVDVFSFGIVLCEIIGRVNADPDylprtMDFGLNVRGFL---DRYCPPNCP------------------PS 234
                        250       260
                 ....*....|....*....|....*..
gi 297822009 914 VMNLALNCTAIDPQERPCTKNVLQALE 940
Cdd:cd14221  235 FFPIAVLCCDLDPEKRPSFSKLEHWLE 261
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
732-940 8.84e-07

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: 51.32  E-value: 8.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 732 MRKLSeHKNILKIVATCRSEKEAYLIHEDVEGKRLSQILNG---LSWERRRKIMKGIVEALRFLHcrcSPAVVAGNLSPE 808
Cdd:cd14155   42 MNRLS-HPNILRFMGVCVHQGQLHALTEYINGGNLEQLLDSnepLSWTVRVKLALDIARGLSYLH---SKGIFHRDLTSK 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 809 NIVIDVKDQ---------------PRLCLGLPGLLCMDSAY-MAPETRERKEMTSKSDIYGFGILLLNLLTGKNSSGDED 872
Cdd:cd14155  118 NCLIKRDENgytavvgdfglaekiPDYSDGKEKLAVVGSPYwMAPEVLRGEPYNEKADVFSYGIILCEIIARIQADPDYL 197
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 297822009 873 IASEVNGSLVNWARYSYSNCHIDtwidssidmsvhkreivhVMNLALNCTAIDPQERPCTKNVLQALE 940
Cdd:cd14155  198 PRTEDFGLDYDAFQHMVGDCPPD------------------FLQLAFNCCNMDPKSRPSFHDIVKTLE 247
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
706-813 9.94e-07

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). Each subunit has tissue-specific isoforms or splice variants. Vertebrates contain two isoforms of the gamma subunit (gamma 1 and gamma 2). The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270995 [Multi-domain]  Cd Length: 272  Bit Score: 51.20  E-value: 9.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 706 LVDKTGIKFVVKEVKK-YDSLPEMISDMRKLSEHKNILKIVATCRSEKEAYLIHEDVEGKRLSQILNG---LSWERRRKI 781
Cdd:cd14093   35 IIDITGEKSSENEAEElREATRREIEILRQVSGHPNIIELHDVFESPTFIFLVFELCRKGELFDYLTEvvtLSEKKTRRI 114
                         90       100       110
                 ....*....|....*....|....*....|..
gi 297822009 782 MKGIVEALRFLHCRCspaVVAGNLSPENIVID 813
Cdd:cd14093  115 MRQLFEAVEFLHSLN---IVHRDLKPENILLD 143
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
294-532 1.11e-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: 50.55  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 294 LDFSDNSLSgEIPELlAQMQTLEILHLFSNNLTgTIPvGVTSLPRLQVLQLwsnrfsggipanlgKHNNLTVLDlstnNL 373
Cdd:cd21340    7 LYLNDKNIT-KIDNL-SLCKNLKVLYLYDNKIT-KIE-NLEFLTNLTHLYL--------------QNNQIEKIE----NL 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 374 TGkLPdtlcdsgHLTKLILFSNS---LDGqippsLGACSSLERVRLQKNafsgDLPRGFTKLqlvnFLDLSNNNLQGNin 450
Cdd:cd21340   65 EN-LV-------NLKKLYLGGNRisvVEG-----LENLTNLEELHIENQ----RLPPGEKLT----FDPRSLAALSNS-- 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 451 twdmpqLEMLDLSRNNFSgELPDLSRSKRLKKLDLSRNRISEMVPLR--LMAFPELMDMDLSENEITG-------VIpse 521
Cdd:cd21340  122 ------LRVLNISGNNID-SLEPLAPLRNLEQLDASNNQISDLEELLdlLSSWPSLRELDLTGNPVCKkpkyrdkII--- 191
                        250
                 ....*....|.
gi 297822009 522 lSSCKNLVNLD 532
Cdd:cd21340  192 -LASKSLEVLD 201
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
709-865 1.22e-06

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


Pssm-ID: 270911 [Multi-domain]  Cd Length: 251  Bit Score: 50.68  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 709 KTGIKFVVKEV-------KKYDSLPEMISDMRKLSeHKNILKIVATCRSEKEAYLIHEDVEGKRLSQILN---GLSWERR 778
Cdd:cd14009   16 QTGEVVAIKEIsrkklnkKLQENLESEIAILKSIK-HPNIVRLYDVQKTEDFIYLVLEYCAGGDLSQYIRkrgRLPEAVA 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 779 RKIMKGIVEALRFLHCRcspAVVAGNLSPENIVIDVKD----------------QPRLCLGLPGLLCMdsaYMAPETRER 842
Cdd:cd14009   95 RHFMQQLASGLKFLRSK---NIIHRDLKPQNLLLSTSGddpvlkiadfgfarslQPASMAETLCGSPL---YMAPEILQF 168
                        170       180
                 ....*....|....*....|...
gi 297822009 843 KEMTSKSDIYGFGILLLNLLTGK 865
Cdd:cd14009  169 QKYDAKADLWSVGAILFEMLVGK 191
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
712-865 1.38e-06

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


Pssm-ID: 270904 [Multi-domain]  Cd Length: 253  Bit Score: 50.71  E-value: 1.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 712 IKFVVK---EVKKYDSLPEMISDMRKLSeHKNILKIVATCRSEKEAYLIHEDVEGKrLSQIL--NG-LSWERRRKIMKGI 785
Cdd:cd14002   31 LKFIPKrgkSEKELRNLRQEIEILRKLN-HPNIIEMLDSFETKKEFVVVTEYAQGE-LFQILedDGtLPEEEVRSIAKQL 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 786 VEALRFLHcrcSPAVVAGNLSPENIVID----VK--DQPRLCLGLPGLLCMDSA-----YMAPETRERKEMTSKSDIYGF 854
Cdd:cd14002  109 VSALHYLH---SNRIIHRDMKPQNILIGkggvVKlcDFGFARAMSCNTLVLTSIkgtplYMAPELVQEQPYDHTADLWSL 185
                        170
                 ....*....|.
gi 297822009 855 GILLLNLLTGK 865
Cdd:cd14002  186 GCILYELFVGQ 196
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
362-536 1.65e-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: 50.17  E-value: 1.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 362 NLTVLDLSTNNLTgKLPDtLCDSGHLTKLILFSNSLDgQIPpSLGACSSLERVRLQKNAFS--GDLpRGFTKLQLvnfLD 439
Cdd:cd21340    3 RITHLYLNDKNIT-KIDN-LSLCKNLKVLYLYDNKIT-KIE-NLEFLTNLTHLYLQNNQIEkiENL-ENLVNLKK---LY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 440 LSNN------NLQGnintwdMPQLEMLDLSRNN-FSGE--LPD----LSRSKRLKKLDLSRNRISEMVPLRlmAFPELMD 506
Cdd:cd21340   75 LGGNrisvveGLEN------LTNLEELHIENQRlPPGEklTFDprslAALSNSLRVLNISGNNIDSLEPLA--PLRNLEQ 146
                        170       180       190
                 ....*....|....*....|....*....|..
gi 297822009 507 MDLSENEITGV--IPSELSSCKNLVNLDLSHN 536
Cdd:cd21340  147 LDASNNQISDLeeLLDLLSSWPSLRELDLTGN 178
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
734-865 1.72e-06

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


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 50.44  E-value: 1.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 734 KLSeHKNILKIVATCRSEKEA------YLIHEDVEGKRLSQILN---GLSWERRRKIMKGIVEALRFLHCRcspAVVAGN 804
Cdd:cd14012   54 KLR-HPNLVSYLAFSIERRGRsdgwkvYLLTEYAPGGSLSELLDsvgSVPLDTARRWTLQLLEALEYLHRN---GVVHKS 129
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 297822009 805 LSPENIVIDVKDQ--------------PRLCLGLPGLLCMDSAY-MAPE-TRERKEMTSKSDIYGFGILLLNLLTGK 865
Cdd:cd14012  130 LHAGNVLLDRDAGtgivkltdyslgktLLDMCSRGSLDEFKQTYwLPPElAQGSKSPTRKTDVWDLGLLFLQMLFGL 206
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
708-858 1.76e-06

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: 50.57  E-value: 1.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009  708 DKTGIKFVVKEVKKYDSLPEM------ISDMRKLSeHKNILKIVATCRSEKEAYLIHEDVEG----KRLSQILNGLSWER 777
Cdd:pfam07714  25 ENTKIKVAVKTLKEGADEEERedfleeASIMKKLD-HPNIVKLLGVCTQGEPLYIVTEYMPGgdllDFLRKHKRKLTLKD 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009  778 RRKIMKGIVEALRFLHCRCspaVVAGNLSPENIVIDVKDQ--------PRLCLGLPGLLCMDSA-----YMAPETRERKE 844
Cdd:pfam07714 104 LLSMALQIAKGMEYLESKN---FVHRDLAARNCLVSENLVvkisdfglSRDIYDDDYYRKRGGGklpikWMAPESLKDGK 180
                         170
                  ....*....|....
gi 297822009  845 MTSKSDIYGFGILL 858
Cdd:pfam07714 181 FTSKSDVWSFGVLL 194
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
704-865 2.08e-06

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


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 50.28  E-value: 2.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 704 NVLVDKTGIKFVVKEVK-----KYDSLPEMISDMRKLSeHKNILKIVATCRSEKEAYLIHEDVEGKRLSQILNG----LS 774
Cdd:cd05122   18 KARHKKTGQIVAIKKINleskeKKESILNEIAILKKCK-HPNIVKYYGSYLKKDELWIVMEFCSGGSLKDLLKNtnktLT 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 775 WERRRKIMKGIVEALRFLHcrcSPAVVAGNLSPENI---------VIDVKDQPRLCLGLPGLLCMDSA-YMAPETRERKE 844
Cdd:cd05122   97 EQQIAYVCKEVLKGLEYLH---SHGIIHRDIKAANIlltsdgevkLIDFGLSAQLSDGKTRNTFVGTPyWMAPEVIQGKP 173
                        170       180
                 ....*....|....*....|.
gi 297822009 845 MTSKSDIYGFGILLLNLLTGK 865
Cdd:cd05122  174 YGFKADIWSLGITAIEMAEGK 194
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
76-386 2.49e-06

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: 50.43  E-value: 2.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009  76 SLDLSGKNISGQILTSATFRLPFLRTINLSNNNLSGPIPQDIFT--TSSPSLRYLNLSNNnFSGSISRGF---------L 144
Cdd:cd00116    2 QLSLKGELLKTERATELLPKLLCLQVLRLEGNTLGEEAAKALASalRPQPSLKELCLSLN-ETGRIPRGLqsllqgltkG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 145 PNLYTLDLSNNMFTGE---IYNDIGFFSNLRVLDLGGNVLTGhvpaylgnlSKLEFL--TLASNQftggvpaelgkmKNL 219
Cdd:cd00116   81 CGLQELDLSDNALGPDgcgVLESLLRSSSLQELKLNNNGLGD---------RGLRLLakGLKDLP------------PAL 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 220 KWIYLGYNNLSGEIPYQIGGLSslnhldlvynnlsgpipPSLGDLKNLEymfLYQNKLSGQIPPSIF----SLQNLISLD 295
Cdd:cd00116  140 EKLVLGRNRLEGASCEALAKAL-----------------RANRDLKELN---LANNGIGDAGIRALAeglkANCNLEVLD 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 296 FSDNSL----SGEIPELLAQMQTLEILHLFSNNLTGTIPVGVTS-----LPRLQVLQLWSNR--------FSGGIPANLg 358
Cdd:cd00116  200 LNNNGLtdegASALAETLASLKSLEVLNLGDNNLTDAGAAALASallspNISLLTLSLSCNDitddgakdLAEVLAEKE- 278
                        330       340
                 ....*....|....*....|....*...
gi 297822009 359 khnNLTVLDLSTNNLTGKLPDTLCDSGH 386
Cdd:cd00116  279 ---SLLELDLRGNKFGEEGAQLLAESLL 303
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
727-940 2.62e-06

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: 50.19  E-value: 2.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 727 EMISDMRKLSEHK--NILKIVATCRseKEAYLIHEDVEGKRLSQIL--NGLSWERRRKIMKGIVEALRFLHCrCSPAVVA 802
Cdd:cd14025   41 ELLEEAKKMEMAKfrHILPVYGICS--EPVGLVMEYMETGSLEKLLasEPLPWELRFRIIHETAVGMNFLHC-MKPPLLH 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 803 GNLSPENIVID----VK----------DQPRLCLGLPGLLCMDSAYMAPETRERKEMTS--KSDIYGFGILLLNLLTGKN 866
Cdd:cd14025  118 LDLKPANILLDahyhVKisdfglakwnGLSHSHDLSRDGLRGTIAYLPPERFKEKNRCPdtKHDVYSFAIVIWGILTQKK 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 867 SSGDEDIASEVNGSLVNWARYSYsnchidtwidsSIDMSVHKREIVHVMNLALNCTAIDPQERPC-------TKNVLQAL 939
Cdd:cd14025  198 PFAGENNILHIMVKVVKGHRPSL-----------SPIPRQRPSECQQMICLMKRCWDQDPRKRPTfqditseTENLLSLL 266

                 .
gi 297822009 940 E 940
Cdd:cd14025  267 E 267
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
444-592 3.56e-06

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 50.85  E-value: 3.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 444 NLQGNINTwdmpqlemLDLSRNNFS---GELPDlsrskRLKKLDLSRNRISEMvPLRLMAfpELMDMDLSENEITgVIPS 520
Cdd:PRK15370 217 NLQGNIKT--------LYANSNQLTsipATLPD-----TIQEMELSINRITEL-PERLPS--ALQSLDLFHNKIS-CLPE 279
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 297822009 521 ELSscKNLVNLDLSHNNLTG---EIPLSFSEFPVLSDldlSCNRLSGEIPKNLgniESLVQVNISHNLLHGSLPP 592
Cdd:PRK15370 280 NLP--EELRYLSVYDNSIRTlpaHLPSGITHLNVQSN---SLTALPETLPPGL---KTLEAGENALTSLPASLPP 346
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
711-937 3.98e-06

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


Pssm-ID: 271069 [Multi-domain]  Cd Length: 263  Bit Score: 49.64  E-value: 3.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 711 GIKFVVKEV--KKYDSLPEMISDMRKLsEHKNILKIVATCRSEKEAYLIHEDVEGKRLSQ--ILNGLSWER-RRKIMKGI 785
Cdd:cd14167   32 AIKCIAKKAleGKETSIENEIAVLHKI-KHPNIVALDDIYESGGHLYLIMQLVSGGELFDriVEKGFYTERdASKLIFQI 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 786 VEALRFLHcrcSPAVVAGNLSPENIVIDVKDQPRL--------CLGLPGLLCMDSA-----YMAPETRERKEMTSKSDIY 852
Cdd:cd14167  111 LDAVKYLH---DMGIVHRDLKPENLLYYSLDEDSKimisdfglSKIEGSGSVMSTAcgtpgYVAPEVLAQKPYSKAVDCW 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 853 GFGILLLNLLTGKNSSGDEDIASEVNGSLVnwARYSYSNCHIDTWIDSSIDMsvhkreIVHVMNLalnctaiDPQERPCT 932
Cdd:cd14167  188 SIGVIAYILLCGYPPFYDENDAKLFEQILK--AEYEFDSPYWDDISDSAKDF------IQHLMEK-------DPEKRFTC 252

                 ....*
gi 297822009 933 KNVLQ 937
Cdd:cd14167  253 EQALQ 257
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
702-873 4.09e-06

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Triple functional domain protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Triple functional domain protein (Trio), also called PTPRF-interacting protein, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. Trio plays important roles in neuronal cell migration and axon guidance. It was originally identified as an interacting partner of the of the receptor-like tyrosine phosphatase (RPTP) LAR (leukocyte-antigen-related protein), a family of receptors that function in the signaling to the actin cytoskeleton during development. Trio functions as a GEF for Rac1, RhoG, and RhoA, and is involved in the regulation of lamellipodia formation, mediating Rac1-dependent cell spreading and migration. The Trio subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 49.59  E-value: 4.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 702 EQNVLVDKTGIKFVVKEVKKYDSLPEMISDMRKLsEHKNILKIVATCRSEKEAYLIHEDVEGKRLSQIL---NGLSWERR 778
Cdd:cd14113   27 DQRGTKRAVATKFVNKKLMKRDQVTHELGVLQSL-QHPQLVGLLDTFETPTSYILVLEMADQGRLLDYVvrwGNLTEEKI 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 779 RKIMKGIVEALRFLH-CRcspaVVAGNLSPENIVID-------VK-----DQPRLCLGLPGLLCMDSA-YMAPETRERKE 844
Cdd:cd14113  106 RFYLREILEALQYLHnCR----IAHLDLKPENILVDqslskptIKladfgDAVQLNTTYYIHQLLGSPeFAAPEIILGNP 181
                        170       180
                 ....*....|....*....|....*....
gi 297822009 845 MTSKSDIYGFGILLLNLLTGKNSSGDEDI 873
Cdd:cd14113  182 VSLTSDLWSIGVLTYVLLSGVSPFLDESV 210
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
708-884 4.77e-06

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


Pssm-ID: 270971 [Multi-domain]  Cd Length: 261  Bit Score: 49.25  E-value: 4.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 708 DKTGIKFVVKEVKKYDSLPEMISDMRK------LSEHKNILKIVAtCRSEKE-AYLIHEDVEGKRLSQIL---NGLSWER 777
Cdd:cd14069   23 RNTEEAVAVKFVDMKRAPGDCPENIKKevciqkMLSHKNVVRFYG-HRREGEfQYLFLEYASGGELFDKIepdVGMPEDV 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 778 RRKIMKGIVEALRFLHcrcSPAVVAGNLSPENIVID-----------------VKDQPRLCLGLPGLLcmdsAYMAPE-T 839
Cdd:cd14069  102 AQFYFQQLMAGLKYLH---SCGITHRDIKPENLLLDendnlkisdfglatvfrYKGKERLLNKMCGTL----PYVAPElL 174
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 297822009 840 RERKEMTSKSDIYGFGILLLNLLTGkNSSGDEdiASEVNGSLVNW 884
Cdd:cd14069  175 AKKKYRAEPVDVWSCGIVLFAMLAG-ELPWDQ--PSDSCQEYSDW 216
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
710-862 5.69e-06

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: 49.17  E-value: 5.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 710 TGIKFVVKEVKKYDS------LPEmISDMRKLsEHKNILKIVATCRSEKEAYLIHEDVEGKRLSQIL---NGLSWERRRK 780
Cdd:cd14222   17 TGKVMVMKELIRCDEetqktfLTE-VKVMRSL-DHPNVLKFIGVLYKDKRLNLLTEFIEGGTLKDFLradDPFPWQQKVS 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 781 IMKGIVEALRFLHCRC---------------SPAVVAGNLSPENIVIDVKDQP-------------RLCLGLPGLLCMDS 832
Cdd:cd14222   95 FAKGIASGMAYLHSMSiihrdlnshncliklDKTVVVADFGLSRLIVEEKKKPppdkpttkkrtlrKNDRKKRYTVVGNP 174
                        170       180       190
                 ....*....|....*....|....*....|
gi 297822009 833 AYMAPETRERKEMTSKSDIYGFGILLLNLL 862
Cdd:cd14222  175 YWMAPEMLNGKSYDEKVDIFSFGIVLCEII 204
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
705-865 6.20e-06

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


Pssm-ID: 270724 [Multi-domain]  Cd Length: 262  Bit Score: 48.76  E-value: 6.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 705 VLVDKTGIKFVVKEVKKY----DSLPEMISDMRKLSE---HKNILKIVATCRSEKEAYLIHEDVEGKRLSQIL---NGLS 774
Cdd:cd05572   12 VQLKSKGRTFALKCVKKRhivqTRQQEHIFSEKEILEecnSPFIVKLYRTFKDKKYLYMLMEYCLGGELWTILrdrGLFD 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 775 WERRRKIMKGIVEALRFLHCRcspAVVAGNLSPENIVID----VK--DqprlclglpgllcMDSA--------------- 833
Cdd:cd05572   92 EYTARFYTACVVLAFEYLHSR---GIIYRDLKPENLLLDsngyVKlvD-------------FGFAkklgsgrktwtfcgt 155
                        170       180       190
                 ....*....|....*....|....*....|....
gi 297822009 834 --YMAPETRERKEMTSKSDIYGFGILLLNLLTGK 865
Cdd:cd05572  156 peYVAPEIILNKGYDFSVDYWSLGILLYELLTGR 189
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
180-414 8.85e-06

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 49.40  E-value: 8.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 180 VLTGHVPAYLGNLSKLEFLTLASNQFTGGVPAELGKM----KNLKWIYLGYNNLSGEIPYQIG----GLSSLNHLDLVYN 251
Cdd:COG5238  167 LLAAISMAKALQNNSVETVYLGCNQIGDEGIEELAEAltqnTTVTTLWLKRNPIGDEGAEILAealkGNKSLTTLDLSNN 246
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 252 NLSGPIPPSLGDL----KNLEYMFLYQNKLSGQIPPSIFSL----QNLISLDFSDNSLSGE----IPELLAQMQTLEILH 319
Cdd:COG5238  247 QIGDEGVIALAEAlknnTTVETLYLSGNQIGAEGAIALAKAlqgnTTLTSLDLSVNRIGDEgaiaLAEGLQGNKTLHTLN 326
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 320 LFSNNLT--GTIPVG--VTSLPRLQVLQLWSNRFSG----GIPANLGKHNNLTVLDLSTNNLTGKLPDTLCDS---GHLT 388
Cdd:COG5238  327 LAYNGIGaqGAIALAkaLQENTTLHSLDLSDNQIGDegaiALAKYLEGNTTLRELNLGKNNIGKQGAEALIDAlqtNRLH 406
                        250       260
                 ....*....|....*....|....*..
gi 297822009 389 KLILFSNSLDGQIPPSL-GACSSLERV 414
Cdd:COG5238  407 TLILDGNLIGAEAQQRLeQLLERIKSV 433
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
99-326 1.03e-05

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 49.02  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009  99 LRTINLSNNNLSGPIPQDIFT--TSSPSLRYLNLSNNNFSGSISRGF------LPNLYTLDLSNNMFTGE----IYNDIG 166
Cdd:COG5238  182 VETVYLGCNQIGDEGIEELAEalTQNTTVTTLWLKRNPIGDEGAEILaealkgNKSLTTLDLSNNQIGDEgviaLAEALK 261
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 167 FFSNLRVLDLGGNVLTGHVPAYLGNLsklefltlasnqftggvpaeLGKMKNLKWIYLGYNNLSGE----IPYQIGGLSS 242
Cdd:COG5238  262 NNTTVETLYLSGNQIGAEGAIALAKA--------------------LQGNTTLTSLDLSVNRIGDEgaiaLAEGLQGNKT 321
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 243 LNHLDLVYNNLSG----PIPPSLGDLKNLEYMFLYQNKLSGQ----IPPSIFSLQNLISLDFSDNSLSGE-IPELLAQMQ 313
Cdd:COG5238  322 LHTLNLAYNGIGAqgaiALAKALQENTTLHSLDLSDNQIGDEgaiaLAKYLEGNTTLRELNLGKNNIGKQgAEALIDALQ 401
                        250
                 ....*....|....*
gi 297822009 314 T--LEILHLFSNNLT 326
Cdd:COG5238  402 TnrLHTLILDGNLIG 416
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
709-866 1.04e-05

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


Pssm-ID: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 48.12  E-value: 1.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 709 KTGIKFVVKEVKK--YDSLP----------EMISDMRKLSEHKNILKIVATCRSEKEAYLIHEDVEGKRL------SQIL 770
Cdd:cd13993   23 RTGRKYAIKCLYKsgPNSKDgndfqklpqlREIDLHRRVSRHPNIITLHDVFETEVAIYIVLEYCPNGDLfeaiteNRIY 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 771 NGlSWERRRKIMKGIVEALRFLHcrcSPAVVAGNLSPENIVID-----VK--------DQPRLclglpgllcMD-----S 832
Cdd:cd13993  103 VG-KTELIKNVFLQLIDAVKHCH---SLGIYHRDIKPENILLSqdegtVKlcdfglatTEKIS---------MDfgvgsE 169
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 297822009 833 AYMAPET-----RERKEM-TSKSDIYGFGILLLNLLTGKN 866
Cdd:cd13993  170 FYMAPECfdevgRSLKGYpCAAGDIWSLGIILLNLTFGRN 209
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
709-940 1.06e-05

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


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 47.90  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 709 KTGIKFVVKEVKKYD----SLPEMISDMRKLSeHKNILKIVATCRSEKEAYLIHEDVEGKRLSQILN----GLSWERRRK 780
Cdd:cd14156   15 GATGKVMVVKIYKNDvdqhKIVREISLLQKLS-HPNIVRYLGICVKDEKLHPILEYVSGGCLEELLAreelPLSWREKVE 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 781 IMKGIVEALRFLH-------------C--RCSPAVVAGNLSPENIVIDVKDQPRLCLGLPGLLCMDSAYMAPETRERKEM 845
Cdd:cd14156   94 LACDISRGMVYLHskniyhrdlnsknCliRVTPRGREAVVTDFGLAREVGEMPANDPERKLSLVGSAFWMAPEMLRGEPY 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 846 TSKSDIYGFGILLLNLLtGKNSSGDEDIASEVngslvnwarysysnchidtwiDSSIDMSVHKrEIV-----HVMNLALN 920
Cdd:cd14156  174 DRKVDVFSFGIVLCEIL-ARIPADPEVLPRTG---------------------DFGLDVQAFK-EMVpgcpePFLDLAAS 230
                        250       260
                 ....*....|....*....|
gi 297822009 921 CTAIDPQERPCTKNVLQALE 940
Cdd:cd14156  231 CCRMDAFKRPSFAELLDELE 250
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
712-865 1.20e-05

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


Pssm-ID: 270889 [Multi-domain]  Cd Length: 259  Bit Score: 48.09  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 712 IKFVVKEVKKYDSLPEMISDMRKLSEHKNILKIVATCRSEKEAYLI-HEDVEGKRLSQIL---NGLSWERRRKIMKGIVE 787
Cdd:cd13987   23 LKFVPKPSTKLKDFLREYNISLELSVHPHIIKTYDVAFETEDYYVFaQEYAPYGDLFSIIppqVGLPEERVKRCAAQLAS 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 788 ALRFLHcrcSPAVVAGNLSPENIVIDVKD----------QPRLCLGLPGLLCMDSAYMAPETRERKEMTS-----KSDIY 852
Cdd:cd13987  103 ALDFMH---SKNLVHRDIKPENVLLFDKDcrrvklcdfgLTRRVGSTVKRVSGTIPYTAPEVCEAKKNEGfvvdpSIDVW 179
                        170
                 ....*....|...
gi 297822009 853 GFGILLLNLLTGK 865
Cdd:cd13987  180 AFGVLLFCCLTGN 192
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
710-880 1.26e-05

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


Pssm-ID: 270887 [Multi-domain]  Cd Length: 272  Bit Score: 48.10  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 710 TGIKFVVK-----EVKKYDSLPEMISDMRKLSEHKNIlkiVATCRSE-------KEAYLIHEDVEGKrLSQIL-----NG 772
Cdd:cd13985   24 TGRRYALKrmyfnDEEQLRVAIKEIEIMKRLCGHPNI---VQYYDSAilssegrKEVLLLMEYCPGS-LVDILeksppSP 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 773 LSWERRRKIMKGIVEALRFLHCrCSPAVVAGNLSPENI--------------------VIDVKDQPRLCLGLPGLLCMDS 832
Cdd:cd13985  100 LSEEEVLRIFYQICQAVGHLHS-QSPPIIHRDIKIENIlfsntgrfklcdfgsattehYPLERAEEVNIIEEEIQKNTTP 178
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 297822009 833 AYMAPET---RERKEMTSKSDIYGFGILLLNLLTGKNSSGDEDIASEVNGS 880
Cdd:cd13985  179 MYRAPEMidlYSKKPIGEKADIWALGCLLYKLCFFKLPFDESSKLAIVAGK 229
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
785-930 2.01e-05

Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This subfamily is composed of the catalytically inactive kinases with similarity to yeast Scy1. It includes four mammalian proteins called SCY1-like protein 1 (SCYL1), SCYL2, SCYL3, as well as Testis-EXpressed protein 14 (TEX14). SCYL1 binds to and co-localizes with the membrane trafficking coatomer I (COPI) complex, and regulates COPI-mediated vesicle trafficking. Null mutations in the SCYL1 gene are responsible for the pathology in mdf (muscle-deficient) mice which display progressive motor neuropathy. SCYL2, also called coated vesicle-associated kinase of 104 kDa (CVAK104), is involved in the trafficking of clathrin-coated vesicles. It also binds the HIV-1 accessory protein Vpu and acts as a regulatory factor that promotes the dephosphorylation of Vpu, facilitating the restriction of HIV-1 release. SCYL3, also called ezrin-binding protein PACE-1, may be involved in regulating cell adhesion and migration. TEX14 is required for spermatogenesis and male fertility. It localizes to kinetochores (KT) during mitosis and is a target of the mitotic kinase PLK1. It regulates the maturation of the outer KT and the KT-microtubule attachment. The SCY1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 47.32  E-value: 2.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 785 IVEALRFLHCRCSpaVVAGNLSPENIVIDVKD--------------QPRLCLGLPGLLCMDSA--------YMAPETRER 842
Cdd:cd14011  123 ISEALSFLHNDVK--LVHGNICPESVVINSNGewklagfdfcisseQATDQFPYFREYDPNLPplaqpnlnYLAPEYILS 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 843 KEMTSKSDIYGFGILLLNLL-TGKnssgdedIASEVNGSLVNWARYSYSNCHIDTWIDSSIDMSVhkREIVHvMNLALnc 921
Cdd:cd14011  201 KTCDPASDMFSLGVLIYAIYnKGK-------PLFDCVNNLLSYKKNSNQLRQLSLSLLEKVPEEL--RDHVK-TLLNV-- 268

                 ....*....
gi 297822009 922 taiDPQERP 930
Cdd:cd14011  269 ---TPEVRP 274
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
732-813 2.11e-05

Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ChoK, ethanolamine kinase (ETNK), macrolide 2'-phosphotransferase (MPH2'), an unusual homoserine kinase, and uncharacterized proteins with similarity to the N-terminal domain of acyl-CoA dehydrogenase 10 (ACAD10). The members of this family catalyze the transfer of the gamma-phosphoryl group from ATP (or CTP) to small molecule substrates such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine. Phosphorylation of the antibiotics, aminoglycosides and macrolides, leads to their inactivation and to bacterial antibiotic resistance. Phosphorylation of choline, ethanolamine, and homoserine serves as precursors to the synthesis of important biological compounds, such as the major phospholipids, phosphatidylcholine and phosphatidylethanolamine and the amino acids, threonine, methionine, and isoleucine. The APH/ChoK family is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270690 [Multi-domain]  Cd Length: 158  Bit Score: 45.76  E-value: 2.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 732 MRKLSEHKNIL--KIVATCRSEKEAYLIHEDVEGKRLSQILNGLSWERRRKIMKGIVEALRFLHCRCSPAVVAGNLSPEN 809
Cdd:cd05120   43 LQLLAGKLSLPvpKVYGFGESDGWEYLLMERIEGETLSEVWPRLSEEEKEKIADQLAEILAALHRIDSSVLTHGDLHPGN 122

                 ....
gi 297822009 810 IVID 813
Cdd:cd05120  123 ILVK 126
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
121-302 2.26e-05

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: 46.70  E-value: 2.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 121 SSPSLRYLNLSNNNFSgSISR-GFLPNLYTLDLSNNMFTgEIYNdIGFFSNLRVLDLGGN---VLTGhvpayLGNLSKLE 196
Cdd:cd21340   22 LCKNLKVLYLYDNKIT-KIENlEFLTNLTHLYLQNNQIE-KIEN-LENLVNLKKLYLGGNrisVVEG-----LENLTNLE 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 197 FLTLASNQFTGGVPAELGkmknlkwiylgynnlsgeiPYQIGGLS-SLNHLDLVYNNLSGPIPpsLGDLKNLEYMFLYQN 275
Cdd:cd21340   94 ELHIENQRLPPGEKLTFD-------------------PRSLAALSnSLRVLNISGNNIDSLEP--LAPLRNLEQLDASNN 152
                        170       180
                 ....*....|....*....|....*....
gi 297822009 276 KLS--GQIPPSIFSLQNLISLDFSDNSLS 302
Cdd:cd21340  153 QISdlEELLDLLSSWPSLRELDLTGNPVC 181
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
95-179 4.98e-05

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: 45.55  E-value: 4.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009  95 RLPFLRTINLSNNNLSGPIP----QDIFTTSSPSLRYLNLSNNNFSGSISRGFLPNLYTLDLSNNMFT--GEIYNDIGFF 168
Cdd:cd21340   88 NLTNLEELHIENQRLPPGEKltfdPRSLAALSNSLRVLNISGNNIDSLEPLAPLRNLEQLDASNNQISdlEELLDLLSSW 167
                         90
                 ....*....|.
gi 297822009 169 SNLRVLDLGGN 179
Cdd:cd21340  168 PSLRELDLTGN 178
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
709-811 5.34e-05

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 46.14  E-value: 5.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 709 KTGIKFVVKEV-KKYDSLPEmISDMRKLSEHKNILKIVATCRSEKEAYLIHEDVEGKRLsqilnglsWERRRK------- 780
Cdd:cd14092   29 KTGQEFAVKIVsRRLDTSRE-VQLLRLCQGHPNIVKLHEVFQDELHTYLVMELLRGGEL--------LERIRKkkrftes 99
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 297822009 781 ----IMKGIVEALRFLHCRcspAVVAGNLSPENIV 811
Cdd:cd14092  100 easrIMRQLVSAVSFMHSK---GVVHRDLKPENLL 131
LRR_8 pfam13855
Leucine rich repeat;
502-562 5.53e-05

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 41.74  E-value: 5.53e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 297822009  502 PELMDMDLSENEITGVIPSELSSCKNLVNLDLSHNNLTGEIPLSFSEFPVLSDLDLSCNRL 562
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
709-864 5.81e-05

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


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 46.18  E-value: 5.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 709 KTGIKFVVKEVKKY--DSLPEMISDMRKLSE---HKNILKIVATCRSEKEAYLIHEDVEGKR-LSQILNGLSWERRR--K 780
Cdd:cd14174   25 QNGKEYAVKIIEKNagHSRSRVFREVETLYQcqgNKNILELIEFFEDDTRFYLVFEKLRGGSiLAHIQKRKHFNEREasR 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 781 IMKGIVEALRFLHCRcspAVVAGNLSPENIVIDVKDQPRLCLG----LPGLLCMDSA-----------------YMAPE- 838
Cdd:cd14174  105 VVRDIASALDFLHTK---GIAHRDLKPENILCESPDKVSPVKIcdfdLGSGVKLNSActpittpelttpcgsaeYMAPEv 181
                        170       180       190
                 ....*....|....*....|....*....|
gi 297822009 839 ----TRERKEMTSKSDIYGFGILLLNLLTG 864
Cdd:cd14174  182 vevfTDEATFYDKRCDLWSLGVILYIMLSG 211
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
732-865 7.59e-05

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


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 45.56  E-value: 7.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 732 MRKLSEHKNILKIVATC-------RSEKEAYLIHEDVEGKRLSQILNGLSWERRRKIMKGIVEALRFLHcrcSPAVVAGN 804
Cdd:cd13975   51 TRSLPKHERIVSLHGSVidysyggGSSIAVLLIMERLHRDLYTGIKAGLSLEERLQIALDVVEGIRFLH---SQGLVHRD 127
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 297822009 805 LSPENIVIDVKDQPRLCLGLP-GLLCMDSA-------YMAPETRERKEMTSkSDIYGFGILLLNLLTGK 865
Cdd:cd13975  128 IKLKNVLLDKKNRAKITDLGFcKPEAMMSGsivgtpiHMAPELFSGKYDNS-VDVYAFGILFWYLCAGH 195
LRR_8 pfam13855
Leucine rich repeat;
337-397 7.65e-05

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 41.36  E-value: 7.65e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 297822009  337 PRLQVLQLWSNRFSGGIPANLGKHNNLTVLDLSTNNLTGKLPDTLCDSGHLTKLILFSNSL 397
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
738-940 9.63e-05

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: 45.41  E-value: 9.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 738 HKNILKIVATCRSEKEAYLIHEDVEGKRLSQILNG--------LSWERRrkimkgIVEALRFLHCRCSPAVVAGNLSPEN 809
Cdd:cd14147   61 HPNIIALKAVCLEEPNLCLVMEYAAGGPLSRALAGrrvpphvlVNWAVQ------IARGMHYLHCEALVPVIHRDLKSNN 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 810 IVI-------DVKDQ---------PRLCLGLPGLLCMDS-AYMAPETRERKEMTSKSDIYGFGILLLNLLTGKNSSGDED 872
Cdd:cd14147  135 ILLlqpiendDMEHKtlkitdfglAREWHKTTQMSAAGTyAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPYRGID 214
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 297822009 873 IASEVNGSLVNwarysysnchidtwidsSIDMSVHKREIVHVMNLALNCTAIDPQERPCTKNVLQALE 940
Cdd:cd14147  215 CLAVAYGVAVN-----------------KLTLPIPSTCPEPFAQLMADCWAQDPHRRPDFASILQQLE 265
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
702-871 1.01e-04

Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to Calcium/calmodulin-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized STKs with similarity to CaMKs, which are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. This uncharacterized subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 45.02  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 702 EQNVLVDKTGIKFVVKEVKKYDSLPEMISDMRKLSEHKNILKIVATCRSEKEAYLIHEDVEGKRL-SQILN-GLSWER-R 778
Cdd:cd14088   22 DKTTGKLYTCKKFLKRDGRKVRKAAKNEINILKMVKHPNILQLVDVFETRKEYFIFLELATGREVfDWILDqGYYSERdT 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 779 RKIMKGIVEALRFLHCRCspaVVAGNLSPEN-----------IVIDVKDQPRLCLGLPGLLCMDSAYMAPETRERKEMTS 847
Cdd:cd14088  102 SNVIRQVLEAVAYLHSLK---IVHRNLKLENlvyynrlknskIVISDFHLAKLENGLIKEPCGTPEYLAPEVVGRQRYGR 178
                        170       180
                 ....*....|....*....|....
gi 297822009 848 KSDIYGFGILLLNLLTGKNSSGDE 871
Cdd:cd14088  179 PVDCWAIGVIMYILLSGNPPFYDE 202
LRR_8 pfam13855
Leucine rich repeat;
218-277 1.03e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 40.97  E-value: 1.03e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009  218 NLKWIYLGYNNLSGEIPYQIGGLSSLNHLDLVYNNLSGPIPPSLGDLKNLEYMFLYQNKL 277
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
697-865 1.22e-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: 44.79  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 697 LSSLNEQNVLVDKtgikfvVKEVKKYDslpemISDMRKLsEHKNILKIVATCRSEKEAYLIHEDVEGKRLSQILnglswE 776
Cdd:cd14059   11 LGKFRGEEVAVKK------VRDEKETD-----IKHLRKL-NHPNIIKFKGVCTQAPCYCILMEYCPYGQLYEVL-----R 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 777 RRRKIM--------KGIVEALRFLHcrcSPAVVAGNLSPENIVIDVKDQPRLCLGLPGLLCMDS----------AYMAPE 838
Cdd:cd14059   74 AGREITpsllvdwsKQIASGMNYLH---LHKIIHRDLKSPNVLVTYNDVLKISDFGTSKELSEKstkmsfagtvAWMAPE 150
                        170       180
                 ....*....|....*....|....*..
gi 297822009 839 TRERKEMTSKSDIYGFGILLLNLLTGK 865
Cdd:cd14059  151 VIRNEPCSEKVDIWSFGVVLWELLTGE 177
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
429-565 1.43e-04

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 45.55  E-value: 1.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 429 FTKLQLVNFLDLSNNNL--QGNINTWDM----PQLEMLDLSRNNFSGELPD-----LSRSKRLKKLDLSRNRISEMvplR 497
Cdd:COG5238  176 ALQNNSVETVYLGCNQIgdEGIEELAEAltqnTTVTTLWLKRNPIGDEGAEilaeaLKGNKSLTTLDLSNNQIGDE---G 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 498 LMAFPELMD-------MDLSENEIT--GVI--PSELSSCKNLVNLDLSHNNLTGEIPLSFSE----FPVLSDLDLSCNRL 562
Cdd:COG5238  253 VIALAEALKnnttvetLYLSGNQIGaeGAIalAKALQGNTTLTSLDLSVNRIGDEGAIALAEglqgNKTLHTLNLAYNGI 332

                 ...
gi 297822009 563 SGE 565
Cdd:COG5238  333 GAQ 335
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
683-882 1.73e-04

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


Pssm-ID: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 44.61  E-value: 1.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 683 FDSRFMKSFTVNAILSSLNEQNVlvDKTGIkFVVKEVKKYDSLpemisdmrklsEHKNILKIVATCRSEKEAYLIHEDVE 762
Cdd:cd14201   23 FKGRHRKKTDWEVAIKSINKKNL--SKSQI-LLGKEIKILKEL-----------QHENIVALYDVQEMPNSVFLVMEYCN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 763 GKRLSQILNG---LSWERRRKIMKGIVEALRFLHcrcSPAVVAGNLSPENIVIDVKDQPRLCLGLPGLLCMD-------- 831
Cdd:cd14201   89 GGDLADYLQAkgtLSEDTIRVFLQQIAAAMRILH---SKGIIHRDLKPQNILLSYASRKKSSVSGIRIKIADfgfarylq 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 297822009 832 -----------SAYMAPETRERKEMTSKSDIYGFGILLLNLLTGK-----NSSGDEDIASEVNGSLV 882
Cdd:cd14201  166 snmmaatlcgsPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKppfqaNSPQDLRMFYEKNKNLQ 232
LRR_8 pfam13855
Leucine rich repeat;
527-586 1.99e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 40.20  E-value: 1.99e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009  527 NLVNLDLSHNNLTGEIPLSFSEFPVLSDLDLSCNRLSGEIPKNLGNIESLVQVNISHNLL 586
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
780-865 2.15e-04

Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase Kinases 3 and 6; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK3 and MKK6 are dual-specificity PKs that phosphorylate and activate their downstream target, p38 MAPK, on specific threonine and tyrosine residues. MKK3/6 play roles in the regulation of cell cycle progression, cytokine- and stress-induced apoptosis, oncogenic transformation, and adult tissue regeneration. In addition, MKK6 plays a critical role in osteoclast survival in inflammatory disease while MKK3 is associated with tumor invasion, progression, and poor patient survival in glioma. The MKK3/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 44.34  E-value: 2.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 780 KIMKGIVEALRFLHCRCSpaVVAGNLSPENIVIDVKDQPRLCLGLPGLLCMDS----------AYMAPE----TRERKEM 845
Cdd:cd06617  107 KIAVSIVKALEYLHSKLS--VIHRDVKPSNVLINRNGQVKLCDFGISGYLVDSvaktidagckPYMAPErinpELNQKGY 184
                         90       100
                 ....*....|....*....|
gi 297822009 846 TSKSDIYGFGILLLNLLTGK 865
Cdd:cd06617  185 DVKSDVWSLGITMIELATGR 204
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
710-865 2.46e-04

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


Pssm-ID: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 43.66  E-value: 2.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 710 TGIKFVVKEVKKydslpEMISDmRKLSEH----KNILK------IV---ATCRSEKEAYLIHEDVEGKRLSQILN---GL 773
Cdd:cd05123   17 TGKLYAMKVLRK-----KEIIK-RKEVEHtlneRNILErvnhpfIVklhYAFQTEEKLYLVLDYVPGGELFSHLSkegRF 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 774 SWERRRKIMKGIVEALRFLHcrcSPAVVAGNLSPENIVID----VK--DQPRLCLGLPGLLCMDSA-----YMAPETRER 842
Cdd:cd05123   91 PEERARFYAAEIVLALEYLH---SLGIIYRDLKPENILLDsdghIKltDFGLAKELSSDGDRTYTFcgtpeYLAPEVLLG 167
                        170       180
                 ....*....|....*....|...
gi 297822009 843 KEMTSKSDIYGFGILLLNLLTGK 865
Cdd:cd05123  168 KGYGKAVDWWSLGVLLYEMLTGK 190
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
707-864 2.89e-04

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


Pssm-ID: 270985 [Multi-domain]  Cd Length: 259  Bit Score: 43.51  E-value: 2.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 707 VDKTGIKfvvkevKKYDSLPEMISDMRKLSeHKNILKIVATCRSEKEAYLIHEDVEGKRL-SQILNGLSWERR--RKIMK 783
Cdd:cd14083   36 IDKKALK------GKEDSLENEIAVLRKIK-HPNIVQLLDIYESKSHLYLVMELVTGGELfDRIVEKGSYTEKdaSHLIR 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 784 GIVEALRFLHcrcSPAVVAGNLSPENIV---------IDVKDqpRLCLGLPGLLCMDSA-----YMAPETRERKEMTSKS 849
Cdd:cd14083  109 QVLEAVDYLH---SLGIVHRDLKPENLLyyspdedskIMISD--FGLSKMEDSGVMSTAcgtpgYVAPEVLAQKPYGKAV 183
                        170
                 ....*....|....*
gi 297822009 850 DIYGFGILLLNLLTG 864
Cdd:cd14083  184 DCWSIGVISYILLCG 198
LRR_8 pfam13855
Leucine rich repeat;
193-253 3.18e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 39.43  E-value: 3.18e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 297822009  193 SKLEFLTLASNQFTGGVPAELGKMKNLKWIYLGYNNLSGEIPYQIGGLSSLNHLDLVYNNL 253
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
710-865 3.29e-04

Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CASK belongs to the MAGUK (membrane-associated guanylate kinase) protein family, which functions as multiple domain adaptor proteins and is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The enzymatically inactive GuK domain in MAGUK proteins mediates protein-protein interactions and associates intramolecularly with the SH3 domain. In addition, CASK contains a catalytic kinase and two L27 domains. It is highly expressed in the nervous system and plays roles in synaptic protein targeting, neural development, and regulation of gene expression. Binding partners include parkin (a Parkinson's disease molecule), neurexin (adhesion molecule), syndecans, calcium channel proteins, CINAP (nucleosome assembly protein), transcription factor Tbr-1, and the cytoplasmic adaptor proteins Mint1, Veli/mLIN-7/MALS, SAP97, caskin, and CIP98. Deletion or mutations in the CASK gene have been implicated in X-linked mental retardation. The CASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 43.68  E-value: 3.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 710 TGIKFVVK--EVKKYDSLPEM-ISDMRK------LSEHKNILKIVATCRSEKEAYLIHEDVEGKRL-----SQILNGLSW 775
Cdd:cd14094   27 TGQQFAVKivDVAKFTSSPGLsTEDLKReasichMLKHPHIVELLETYSSDGMLYMVFEFMDGADLcfeivKRADAGFVY 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 776 ERR--RKIMKGIVEALRFLHCRcspAVVAGNLSPENIVIDVKDQPRLCLGLPGLLCMD--------------SAYMAPET 839
Cdd:cd14094  107 SEAvaSHYMRQILEALRYCHDN---NIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQlgesglvaggrvgtPHFMAPEV 183
                        170       180
                 ....*....|....*....|....*.
gi 297822009 840 RERKEMTSKSDIYGFGILLLNLLTGK 865
Cdd:cd14094  184 VKREPYGKPVDVWGCGVILFILLSGC 209
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
710-864 3.73e-04

Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include Saccharomyces cerevisiae Rim15, Schizosaccharomyces pombe cek1, and similar fungal proteins. They contain a central catalytic domain, which contains an insert relative to MAST kinases. In addition, Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. Rim15 (or Rim15p) functions as a regulator of meiosis. It acts as a downstream effector of PKA and regulates entry into stationary phase (G0). Thus, it plays a crucial role in regulating yeast proliferation, differentiation, and aging. Cek1 may facilitate progression of mitotic anaphase. The Rim15-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270762 [Multi-domain]  Cd Length: 263  Bit Score: 43.24  E-value: 3.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 710 TGIKFVVKEVKKYDslpeMISD------------MRKLSEHKNILKIVATCRSEKEAYLIHEDVEG---KRLSQILNGLS 774
Cdd:cd05611   20 TGDYFAIKVLKKSD----MIAKnqvtnvkaeraiMMIQGESPYVAKLYYSFQSKDYLYLVMEYLNGgdcASLIKTLGGLP 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 775 WERRRKIMKGIVEALRFLHCRcspAVVAGNLSPENIVID-----------------VKDQPRLCLGLPGllcmdsaYMAP 837
Cdd:cd05611   96 EDWAKQYIAEVVLGVEDLHQR---GIIHRDIKPENLLIDqtghlkltdfglsrnglEKRHNKKFVGTPD-------YLAP 165
                        170       180
                 ....*....|....*....|....*..
gi 297822009 838 ETRERKEMTSKSDIYGFGILLLNLLTG 864
Cdd:cd05611  166 ETILGVGDDKMSDWWSLGCVIFEFLFG 192
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
708-812 3.88e-04

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


Pssm-ID: 270836 [Multi-domain]  Cd Length: 286  Bit Score: 43.57  E-value: 3.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 708 DKTGIKFVVKEVKkydslpemisdMRKLSEHKNILKIVATCRSEKEAYLIHEDVEG---KRLSQILNGLSWERRRKIMKG 784
Cdd:cd07846   40 DKMVKKIAMREIK-----------MLKQLRHENLVNLIEVFRRKKRWYLVFEFVDHtvlDDLEKYPNGLDESRVRKYLFQ 108
                         90       100
                 ....*....|....*....|....*...
gi 297822009 785 IVEALRFLHcrcSPAVVAGNLSPENIVI 812
Cdd:cd07846  109 ILRGIDFCH---SHNIIHRDIKPENILV 133
LRR_8 pfam13855
Leucine rich repeat;
123-181 5.26e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 39.04  E-value: 5.26e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 297822009  123 PSLRYLNLSNNNFSgSISRGF---LPNLYTLDLSNNMFTGEIYNDIGFFSNLRVLDLGGNVL 181
Cdd:pfam13855   1 PNLRSLDLSNNRLT-SLDDGAfkgLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
708-864 5.73e-04

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


Pssm-ID: 270972 [Multi-domain]  Cd Length: 262  Bit Score: 42.88  E-value: 5.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 708 DKTGIKFVVKEVKKYDSLpeMISDMRK------LSEHKNILKIVATCRSEKEAYLIHEDVEGKRL-SQILNGLSWERR-- 778
Cdd:cd14070   28 EKVAIKVIDKKKAKKDSY--VTKNLRRegriqqMIRHPNITQLLDILETENSYYLVMELCPGGNLmHRIYDKKRLEERea 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 779 RKIMKGIVEALRFLHCRcspAVVAGNLSPENIVIDVKDQPRL-------------CLGLPGLLCMDSAYMAPETRERKEM 845
Cdd:cd14070  106 RRYIRQLVSAVEHLHRA---GVVHRDLKIENLLLDENDNIKLidfglsncagilgYSDPFSTQCGSPAYAAPELLARKKY 182
                        170
                 ....*....|....*....
gi 297822009 846 TSKSDIYGFGILLLNLLTG 864
Cdd:cd14070  183 GPKVDVWSIGVNMYAMLTG 201
STKc_IRAK2 cd14157
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; ...
738-864 5.85e-04

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: 42.90  E-value: 5.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 738 HKNILKIVATCRSEKEAYLIHEDVEGKRLSQILNG------LSWERRRKIMKGIVEALRFLHcrcSPAVVAGNLSPENIV 811
Cdd:cd14157   51 HPNILPLLGFCVESDCHCLIYPYMPNGSLQDRLQQqggshpLPWEQRLSISLGLLKAVQHLH---NFGILHGNIKSSNVL 127
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 297822009 812 IDVKDQPRLCLGLPGLLCMD---------------SAYMAPETRERK-EMTSKSDIYGFGILLLNLLTG 864
Cdd:cd14157  128 LDGNLLPKLGHSGLRLCPVDkksvytmmktkvlqiSLAYLPEDFVRHgQLTEKVDIFSCGVVLAEILTG 196
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
712-937 6.03e-04

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Kalirin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kalirin, also called Duo or Duet, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. As a GEF, it activates Rac1, RhoA, and RhoG. It is highly expressed in neurons and is required for spine formation. The kalirin gene produces at least 10 isoforms from alternative promoter use and splicing. Of the major isoforms (Kalirin-7, -9, and -12), only kalirin-12 contains the C-terminal kinase domain. Kalirin-12 is highly expressed during embryonic development and it plays an important role in axon outgrowth. The Kalirin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 42.64  E-value: 6.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 712 IKFVVKEVKKYDSLPEMISDMRKLsEHKNILKIVATCRSEKEAYLIHEDVEGKRLSQIL---NGLSWERRRKIMKGIVEA 788
Cdd:cd14115   23 VKFVSKKMKKKEQAAHEAALLQHL-QHPQYITLHDTYESPTSYILVLELMDDGRLLDYLmnhDELMEEKVAFYIRDIMEA 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 789 LRFLH-CRcspaVVAGNLSPENIVIDV-KDQPRLCLGLPGLLCMDSA------------YMAPETRERKEMTSKSDIYGF 854
Cdd:cd14115  102 LQYLHnCR----VAHLDIKPENLLIDLrIPVPRVKLIDLEDAVQISGhrhvhhllgnpeFAAPEVIQGTPVSLATDIWSI 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 855 GILLLNLLTGKNSSGDEDIASevngSLVNWARYSYSNCHidtwiDSSIDMSVHKREIVHVMnlalncTAIDPQERPCTKN 934
Cdd:cd14115  178 GVLTYVMLSGVSPFLDESKEE----TCINVCRVDFSFPD-----EYFGDVSQAARDFINVI------LQEDPRRRPTAAT 242

                 ...
gi 297822009 935 VLQ 937
Cdd:cd14115  243 CLQ 245
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
701-863 6.46e-04

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. No function has yet been ascribed to Nek10. The gene encoding Nek10 is a putative causative gene for breast cancer; it is located within a breast cancer susceptibility loci on chromosome 3p24. Nek10 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270867 [Multi-domain]  Cd Length: 270  Bit Score: 42.87  E-value: 6.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 701 NEQNVL----VDKTGIKFVVKEVKKYDSLPEMISDMRKLSE---HKNILKIVATCRSEKEAYLIHEDVEGKRLSQILNGL 773
Cdd:cd08528   24 NGQTLLalkeINMTNPAFGRTEQERDKSVGDIISEVNIIKEqlrHPNIVRYYKTFLENDRLYIVMELIEGAPLGEHFSSL 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 774 -------SWERRRKIMKGIVEALRFLHCRcsPAVVAGNLSPENIVIDVKD-----------QPRLCLGLPGLLCMDSAYM 835
Cdd:cd08528  104 keknehfTEDRIWNIFVQMVLALRYLHKE--KQIVHRDLKPNNIMLGEDDkvtitdfglakQKGPESSKMTSVVGTILYS 181
                        170       180
                 ....*....|....*....|....*...
gi 297822009 836 APETRERKEMTSKSDIYGFGILLLNLLT 863
Cdd:cd08528  182 CPEIVQNEPYGEKADIWALGCILYQMCT 209
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
834-936 6.73e-04

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 43.32  E-value: 6.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 834 YMAPETRERKEMTSKSDIYGFGILLLNLLTGKNSSGDEDIASEVNGSLVnwARYsysnchiDTWIDSsidMSVHKREIVH 913
Cdd:PTZ00283 211 YVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPFDGENMEEVMHKTLA--GRY-------DPLPPS---ISPEMQEIVT 278
                         90       100
                 ....*....|....*....|...
gi 297822009 914 vmnlALNCTaiDPQERPCTKNVL 936
Cdd:PTZ00283 279 ----ALLSS--DPKRRPSSSKLL 295
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
706-937 7.00e-04

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called Doublecortin-like and CAM kinase-like 3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL3 (or DCAMKL3) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. DCKL3 contains a single DCX domain (instead of a tandem) and a C-terminal kinase domain with similarity to CAMKs. It has been shown to interact with tubulin and JIP1/2. The DCKL3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271087 [Multi-domain]  Cd Length: 258  Bit Score: 42.63  E-value: 7.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 706 LVDKTGIKfvvkevKKYDSLPEMISDMRKLSeHKNILKIVATCRSEKEAYLIHEDVEGKRL-SQILNGLSW-ERRRKIM- 782
Cdd:cd14185   32 IIDKSKLK------GKEDMIESEILIIKSLS-HPNIVKLFEVYETEKEIYLILEYVRGGDLfDAIIESVKFtEHDAALMi 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 783 KGIVEALRFLHcrcSPAVVAGNLSPENIVIDVKDQPRLCLGLPGLLCMDSA------------YMAPETRERKEMTSKSD 850
Cdd:cd14185  105 IDLCEALVYIH---SKHIVHRDLKPENLLVQHNPDKSTTLKLADFGLAKYVtgpiftvcgtptYVAPEILSEKGYGLEVD 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 851 IYGFGILLLNLLTGKNSSGDEDIASEVNGSLVNWARYSYSNCHIDTWIDSSIDmsvhkreivhvmnLALNCTAIDPQERP 930
Cdd:cd14185  182 MWAAGVILYILLCGFPPFRSPERDQEELFQIIQLGHYEFLPPYWDNISEAAKD-------------LISRLLVVDPEKRY 248

                 ....*..
gi 297822009 931 CTKNVLQ 937
Cdd:cd14185  249 TAKQVLQ 255
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
709-872 8.01e-04

Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK33 is highly expressed in the testis and is present in low levels in most tissues. It may be involved in spermatogenesis and organ ontogenesis. It interacts with and phosphorylates vimentin and may be involved in regulating intermediate filament cytoskeletal dynamics. Its role in promoting the cell viability of KRAS-dependent cancer cells is under debate; some studies have found STK33 to promote cancer cell viability, while other studies have found it to be non-essential. KRAS is the most commonly mutated human oncogene, thus, studies on the role of STK33 in KRAS mutant cancer cells are important. The STK33 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 42.54  E-value: 8.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 709 KTGIKFVVKEVKKydslPEMISDMRKLSEHK-NILKIV---------ATCRSEKEAYLIHEDVEGKRLSQILNG---LSW 775
Cdd:cd14097   24 ETQTKWAIKKINR----EKAGSSAVKLLEREvDILKHVnhahiihleEVFETPKRMYLVMELCEDGELKELLLRkgfFSE 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 776 ERRRKIMKGIVEALRFLHCRcspAVVAGNLSPENIV-------------IDVKDQPRLCLGLPGLLCMDSA------YMA 836
Cdd:cd14097  100 NETRHIIQSLASAVAYLHKN---DIVHRDLKLENILvkssiidnndklnIKVTDFGLSVQKYGLGEDMLQEtcgtpiYMA 176
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 297822009 837 PETRERKEMTSKSDIYGFGILLLNLLTGKN--SSGDED 872
Cdd:cd14097  177 PEVISAHGYSQQCDIWSIGVIMYMLLCGEPpfVAKSEE 214
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
683-891 8.69e-04

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 42.13  E-value: 8.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 683 FDSRFmkSFTVNAILSSlneqnvlvDKTGIKFVVKEVKKYDSLPEMIS--DMRKLSEHKNILKIVATCRSEKEAYLIHED 760
Cdd:cd14112   12 FRGRF--SVIVKAVDST--------TETDAHCAVKIFEVSDEASEAVRefESLRTLQHENVQRLIAAFKPSNFAYLVMEK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 761 VEGKRLSQIL--NGLSWERRRKIMKGIVEALRFLHCRcspAVVAGNLSPENIV-----------IDVKDQPRLCLGLPGL 827
Cdd:cd14112   82 LQEDVFTRFSsnDYYSEEQVATTVRQILDALHYLHFK---GIAHLDVQPDNIMfqsvrswqvklVDFGRAQKVSKLGKVP 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 297822009 828 LCMDSAYMAPET-RERKEMTSKSDIYGFGILLLNLLTGKNS-SGDEDIASEVNGSLVNwARYSYSN 891
Cdd:cd14112  159 VDGDTDWASPEFhNPETPITVQSDIWGLGVLTFCLLSGFHPfTSEYDDEEETKENVIF-VKCRPNL 223
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
709-884 9.50e-04

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK2 (or MYLK2) phosphorylates myosin regulatory light chain and controls the contraction of skeletal muscles. MLCK2 contains a single kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site. The MLCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271092 [Multi-domain]  Cd Length: 261  Bit Score: 42.21  E-value: 9.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 709 KTGIKFVVKEVKKYDSLP-EM----ISDMRKLSeHKNILKIVATCRSEKEAYLIHEDVEGKRL-SQILNGLSWERRRKIM 782
Cdd:cd14190   27 RTGLKLAAKVINKQNSKDkEMvlleIQVMNQLN-HRNLIQLYEAIETPNEIVLFMEYVEGGELfERIVDEDYHLTEVDAM 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 783 ---KGIVEALRFLHcrcSPAVVAGNLSPENI-----------VIDVKDQPRLCLGLPGLLCMDSA-YMAPETRERKEMTS 847
Cdd:cd14190  106 vfvRQICEGIQFMH---QMRVLHLDLKPENIlcvnrtghqvkIIDFGLARRYNPREKLKVNFGTPeFLSPEVVNYDQVSF 182
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 297822009 848 KSDIYGFGILLLNLLTGKNSS-GDEDIASEVNGSLVNW 884
Cdd:cd14190  183 PTDMWSMGVITYMLLSGLSPFlGDDDTETLNNVLMGNW 220
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
729-813 1.03e-03

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 1 subunit (PhKG1) is also referred to as the muscle gamma isoform. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 42.21  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 729 ISDMRKLSEHKNILKIVATCRSEKEAYLIHEDVEGKRLSQILN---GLSWERRRKIMKGIVEALRFLHcrcSPAVVAGNL 805
Cdd:cd14182   60 IDILRKVSGHPNIIQLKDTYETNTFFFLVFDLMKKGELFDYLTekvTLSEKETRKIMRALLEVICALH---KLNIVHRDL 136

                 ....*...
gi 297822009 806 SPENIVID 813
Cdd:cd14182  137 KPENILLD 144
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
683-865 1.09e-03

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


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 41.92  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 683 FDSRFMKSFTVNAILSSLNEQNVLVDKTgikFVVKEVKKYDSLpemisdmrklsEHKNILKIVATCRSEKEAYLIHEDVE 762
Cdd:cd14202   19 FKGRHKEKHDLEVAVKCINKKNLAKSQT---LLGKEIKILKEL-----------KHENIVALYDFQEIANSVYLVMEYCN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 763 GKRLSQILNG---LSWERRRKIMKGIVEALRFLHcrcSPAVVAGNLSPENIVIDVKDQPRLCLGLPGLLCMD-------- 831
Cdd:cd14202   85 GGDLADYLHTmrtLSEDTIRLFLQQIAGAMKMLH---SKGIIHRDLKPQNILLSYSGGRKSNPNNIRIKIADfgfarylq 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 297822009 832 -----------SAYMAPETRERKEMTSKSDIYGFGILLLNLLTGK 865
Cdd:cd14202  162 nnmmaatlcgsPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGK 206
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
717-813 1.25e-03

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


Pssm-ID: 270827 [Multi-domain]  Cd Length: 288  Bit Score: 41.92  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 717 KEVKKYdSLPEMisDMRKLSEHKNILKIVATCRSEKEAYLIHEDVEgKRLSQIL----NGLSWERRRKIMKGIVEALRFL 792
Cdd:cd07833   41 EDVKKT-ALREV--KVLRQLRHENIVNLKEAFRRKGRLYLVFEYVE-RTLLELLeaspGGLPPDAVRSYIWQLLQAIAYC 116
                         90       100
                 ....*....|....*....|.
gi 297822009 793 HcrcSPAVVAGNLSPENIVID 813
Cdd:cd07833  117 H---SHNIIHRDIKPENILVS 134
LRR_8 pfam13855
Leucine rich repeat;
145-205 1.27e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 37.89  E-value: 1.27e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 297822009  145 PNLYTLDLSNNMFTGeIynDIGFF---SNLRVLDLGGNVLTGHVPAYLGNLSKLEFLTLASNQF 205
Cdd:pfam13855   1 PNLRSLDLSNNRLTS-L--DDGAFkglSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
714-939 1.43e-03

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


Pssm-ID: 270639 [Multi-domain]  Cd Length: 279  Bit Score: 41.67  E-value: 1.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 714 FVVKEVKKYDSLPE---MISDMRKLSE--HKNILKIVATCRSEKEAYLIHEDVEGK----------RLSQILNGLSWERR 778
Cdd:cd05043   37 VLVKTVKDHASEIQvtmLLQESSLLYGlsHQNLLPILHVCIEDGEKPMVLYPYMNWgnlklflqqcRLSEANNPQALSTQ 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 779 RKIMKG--IVEALRFLHCRcspAVVAGNLSPENIVIDVKDQPRLClglpgllcmDSA----------------------Y 834
Cdd:cd05043  117 QLVHMAlqIACGMSYLHRR---GVIHKDIAARNCVIDDELQVKIT---------DNAlsrdlfpmdyhclgdnenrpikW 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 835 MAPETRERKEMTSKSDIYGFGILLLNLLT-GKNSSGDEDIaSEVNGSLVNWARYSYS-NChidtwidssidmsvhKREIV 912
Cdd:cd05043  185 MSLESLVNKEYSSASDVWSFGVLLWELMTlGQTPYVEIDP-FEMAAYLKDGYRLAQPiNC---------------PDELF 248
                        250       260
                 ....*....|....*....|....*..
gi 297822009 913 HVMNLalnCTAIDPQERPCTKNVLQAL 939
Cdd:cd05043  249 AVMAC---CWALDPEERPSFQQLVQCL 272
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
720-865 1.78e-03

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


Pssm-ID: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 41.27  E-value: 1.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 720 KKYDSLPEMIsDMRKLSEHKNILKIVATCRSEKEAYLIHEDVEGKRLSQILN---GLSWERRRKIMKGIVEALRFLHCRC 796
Cdd:cd06631   45 KEYEKLQEEV-DLLKTLKHVNIVGYLGTCLEDNVVSIFMEFVPGGSIASILArfgALEEPVFCRYTKQILEGVAYLHNNN 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 797 spaVV-----AGN--LSPENIV--IDVKDQPRLCLGLPGLLCMD--------SAYMAPETRERKEMTSKSDIYGFGILLL 859
Cdd:cd06631  124 ---VIhrdikGNNimLMPNGVIklIDFGCAKRLCINLSSGSQSQllksmrgtPYWMAPEVINETGHGRKSDIWSIGCTVF 200

                 ....*.
gi 297822009 860 NLLTGK 865
Cdd:cd06631  201 EMATGK 206
LRR_8 pfam13855
Leucine rich repeat;
409-467 1.85e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 37.50  E-value: 1.85e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 297822009  409 SSLERVRLQKNAFSGDLPRGFTKLQLVNFLDLSNNNLQGnINT---WDMPQLEMLDLSRNNF 467
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTT-LSPgafSGLPSLRYLDLSGNRL 61
LRR_8 pfam13855
Leucine rich repeat;
438-490 2.56e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 37.12  E-value: 2.56e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 297822009  438 LDLSNNNLQGNINTW--DMPQLEMLDLSRNNFSGELPD-LSRSKRLKKLDLSRNRI 490
Cdd:pfam13855   6 LDLSNNRLTSLDDGAfkGLSNLKVLDLSNNLLTTLSPGaFSGLPSLRYLDLSGNRL 61
LRR_8 pfam13855
Leucine rich repeat;
169-229 3.22e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 36.73  E-value: 3.22e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 297822009  169 SNLRVLDLGGNVLTGHVPAYLGNLSKLEFLTLASNQFTGGVPAELGKMKNLKWIYLGYNNL 229
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
727-903 3.59e-03

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 (also called STK17A) and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. Rabbit DRAK1 has been shown to induce apoptosis in osteoclasts and overexpressio of human DRAK1 induces apoptosis in cultured fibroblast cells. DRAK1 may be involved in apoptotic signaling. The DRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 40.30  E-value: 3.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 727 EMISDMRKLSEHKNILKIVATCRSEKEAYLIHEDVegkrlsqilnglswerrRKIMKGIVEALRFLHCRcspAVVAGNLS 806
Cdd:cd14197   79 ETASEMILVLEYAAGGEIFNQCVADREEAFKEKDV-----------------KRLMKQILEGVSFLHNN---NVVHLDLK 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 807 PENIVI-------DVK----DQPRLCLGLPGLLCM--DSAYMAPETRERKEMTSKSDIYGFGILLLNLLTGKNSS-GDED 872
Cdd:cd14197  139 PQNILLtsesplgDIKivdfGLSRILKNSEELREImgTPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFlGDDK 218
                        170       180       190
                 ....*....|....*....|....*....|.
gi 297822009 873 IASEVNGSLVNwarYSYSNCHIDTWIDSSID 903
Cdd:cd14197  219 QETFLNISQMN---VSYSEEEFEHLSESAID 246
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
710-872 3.85e-03

Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB1 interacts directly with the mitogen activated protein kinase (MAPK) kinase MKK4, an activator of JNK. It regulates vascular smooth muscle cell proliferation and chemotaxis through the JNK signaling pathway. It is found to be down-regulated in human acute myeloid leukaemia (AML) and may play a role in the pathogenesis of the disease. It has also been identified as a potential biomarker for antibody-mediated allograft failure. TRB1 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB1 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270925 [Multi-domain]  Cd Length: 242  Bit Score: 40.03  E-value: 3.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 710 TGIKFVVKeVKKYDSLPEMISDMRKLSEHKNILKIVATCRSEKEAYLIHEDVEGKRLSQI--LNGLSWERRRKIMKGIVE 787
Cdd:cd14023   17 SGAELQCK-VFPLKHYQDKIRPYIQLPSHRNITGIVEVILGDTKAYVFFEKDFGDMHSYVrsCKRLREEEAARLFKQIVS 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 788 ALRflHCRCSpAVVAGNLSPENIVIDVKDQPRLCLGLPGLLCM-----DS--------AYMAPETRERKEMTS--KSDIY 852
Cdd:cd14023   96 AVA--HCHQS-AIVLGDLKLRKFVFSDEERTQLRLESLEDTHImkgedDAlsdkhgcpAYVSPEILNTTGTYSgkSADVW 172
                        170       180
                 ....*....|....*....|
gi 297822009 853 GFGILLLNLLTGKNSSGDED 872
Cdd:cd14023  173 SLGVMLYTLLVGRYPFHDSD 192
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
738-866 4.31e-03

Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Titin, also called connectin, is a muscle-specific elastic protein and is the largest known protein to date. It contains multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains, and a single kinase domain near the C-terminus. It spans half of the sarcomere, the repeating contractile unit of striated muscle, and performs mechanical and catalytic functions. Titin contributes to the passive force generated when muscle is stretched during relaxation. Its kinase domain phosphorylates and regulates the muscle protein telethonin, which is required for sarcomere formation in differentiating myocytes. In addition, titin binds many sarcomere proteins and acts as a molecular scaffold for filament formation during myofibrillogenesis. The Titin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 40.23  E-value: 4.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 738 HKNILKIVATCRSEKEAYLIHEDVEGKRLSQILNGLSWE-RRRKIM---KGIVEALRFLHcrcSPAVVAGNLSPENIV-- 811
Cdd:cd14104   55 HRNILRLHESFESHEELVMIFEFISGVDIFERITTARFElNEREIVsyvRQVCEALEFLH---SKNIGHFDIRPENIIyc 131
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 297822009 812 ---------IDVKDQPRLCLGLPGLLCMDSA-YMAPETRERKEMTSKSDIYGFGILLLNLLTGKN 866
Cdd:cd14104  132 trrgsyikiIEFGQSRQLKPGDKFRLQYTSAeFYAPEVHQHESVSTATDMWSLGCLVYVLLSGIN 196
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
710-937 4.33e-03

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


Pssm-ID: 271008 [Multi-domain]  Cd Length: 268  Bit Score: 40.03  E-value: 4.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 710 TGIKFVVKEVKK----YDSLPEMISDMRKL---SEHKNILKIVATCRSEKEAYLIHEDVEGKRLSQILNG---LSWERRR 779
Cdd:cd14106   32 TGKEYAAKFLRKrrrgQDCRNEILHEIAVLelcKDCPRVVNLHEVYETRSELILILELAAGGELQTLLDEeecLTEADVR 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 780 KIMKGIVEALRFLHCRcspAVVAGNLSPENIVI-------DVK----DQPRLCLGLPGLLCMDSA--YMAPETRERKEMT 846
Cdd:cd14106  112 RLMRQILEGVQYLHER---NIVHLDLKPQNILLtsefplgDIKlcdfGISRVIGEGEEIREILGTpdYVAPEILSYEPIS 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 847 SKSDIYGFGILLLNLLTGKNS-SGDEDIASEVNGSLVNwarYSYSNCHIDTWIDSSIDMSvhKREIVhvmnlalnctaID 925
Cdd:cd14106  189 LATDMWSIGVLTYVLLTGHSPfGGDDKQETFLNISQCN---LDFPEELFKDVSPLAIDFI--KRLLV-----------KD 252
                        250
                 ....*....|..
gi 297822009 926 PQERPCTKNVLQ 937
Cdd:cd14106  253 PEKRLTAKECLE 264
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
73-160 4.33e-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: 40.42  E-value: 4.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009  73 RVVSLDLSGKNISGQILTSATFR-LPFLRTINLSNNNLSGPIPQDI---FTTSSPSLRYLNLSNNNF--SGSIS-RGFLP 145
Cdd:cd00116  196 EVLDLNNNGLTDEGASALAETLAsLKSLEVLNLGDNNLTDAGAAALasaLLSPNISLLTLSLSCNDItdDGAKDlAEVLA 275
                         90
                 ....*....|....*...
gi 297822009 146 N---LYTLDLSNNMFTGE 160
Cdd:cd00116  276 EkesLLELDLRGNKFGEE 293
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
764-864 4.65e-03

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKbeta is involved in the classical pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. It involves NEMO (NF-kB Essential MOdulator)- and IKKbeta-dependent phosphorylation and degradation of the Inhibitor of NF-kB (IkB), which liberates NF-kB dimers (typified by the p50-p65 heterodimer) from an inactive IkB/dimeric NF-kB complex, enabling them to migrate to the nucleus where they regulate gene transcription. The IKKbeta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 40.33  E-value: 4.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 764 KRLSQILN--GLSWERRRKIMKGIVEALRFLHcrcSPAVVAGNLSPENIVIDVKDQP--RLCLGLPGLLCMDSA------ 833
Cdd:cd14038   87 KYLNQFENccGLREGAILTLLSDISSALRYLH---ENRIIHRDLKPENIVLQQGEQRliHKIIDLGYAKELDQGslctsf 163
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 297822009 834 -----YMAPETRERKEMTSKSDIYGFGILLLNLLTG 864
Cdd:cd14038  164 vgtlqYLAPELLEQQKYTVTVDYWSFGTLAFECITG 199
pknD PRK13184
serine/threonine-protein kinase PknD;
834-929 5.78e-03

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 40.52  E-value: 5.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 834 YMAPETRERKEMTSKSDIYGFGILLLNLLTGKNSsgdediasevngslvnWARYSYSNCHIDTWIDSSIDMSVHkREIVH 913
Cdd:PRK13184 197 YMAPERLLGVPASESTDIYALGVILYQMLTLSFP----------------YRRKKGRKISYRDVILSPIEVAPY-REIPP 259
                         90
                 ....*....|....*..
gi 297822009 914 VMN-LALNCTAIDPQER 929
Cdd:PRK13184 260 FLSqIAMKALAVDPAER 276
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
709-858 7.62e-03

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: 39.45  E-value: 7.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 709 KTGIKFVVKEVKkYDSLPE----MISD----MRKLsEHKNILK----IVAtcRSEKEAYLIHEDVEGKRLSQILNGLSWE 776
Cdd:cd08217   23 SDGKILVWKEID-YGKMSEkekqQLVSevniLREL-KHPNIVRyydrIVD--RANTTLYIVMEYCEGGDLAQLIKKCKKE 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 777 RRR-------KIMKGIVEALRFLHCRCSP--AVVAGNLSPENIVID----VK--DqprlclgLPGLLCMDSA-------- 833
Cdd:cd08217   99 NQYipeefiwKIFTQLLLALYECHNRSVGggKILHRDLKPANIFLDsdnnVKlgD-------FGLARVLSHDssfaktyv 171
                        170       180
                 ....*....|....*....|....*....
gi 297822009 834 ----YMAPETRERKEMTSKSDIYGFGILL 858
Cdd:cd08217  172 gtpyYMSPELLNEQSYDEKSDIWSLGCLI 200
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
738-864 7.96e-03

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


Pssm-ID: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 39.24  E-value: 7.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 738 HKNILKIVATCRSEKEAYLIHEDVEGkrlSQILNGLswERRRK--------IMKGIVEALRFLHcrcSPAVVAGNLSPEN 809
Cdd:cd14173   59 HRNVLELIEFFEEEDKFYLVFEKMRG---GSILSHI--HRRRHfneleasvVVQDIASALDFLH---NKGIAHRDLKPEN 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 810 IVIDVKDQPRLCLG------LPGLLCMDSA---------------YMAPETRER-KEMTS----KSDIYGFGILLLNLLT 863
Cdd:cd14173  131 ILCEHPNQVSPVKIcdfdlgSGIKLNSDCSpistpelltpcgsaeYMAPEVVEAfNEEASiydkRCDLWSLGVILYIMLS 210

                 .
gi 297822009 864 G 864
Cdd:cd14173  211 G 211
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
780-937 8.88e-03

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


Pssm-ID: 270782 [Multi-domain]  Cd Length: 265  Bit Score: 39.25  E-value: 8.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 780 KIMKGIVEALRFLHCRCSpaVVAGNLSPENIVIDVKDQPRLCLGLPGLLCMDS---------AYMAPETRERKEMTSKSD 850
Cdd:cd06605  103 KIAVAVVKGLIYLHEKHK--IIHRDVKPSNILVNSRGQVKLCDFGVSGQLVDSlaktfvgtrSYMAPERISGGKYTVKSD 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 851 IYGFGILLLNLLTGknssgdediasevngslvnwaRYSYSNCHIDTWI------DSSIDM-------SVHKREIVHVMNL 917
Cdd:cd06605  181 IWSLGLSLVELATG---------------------RFPYPPPNAKPSMmifellSYIVDEpppllpsGKFSPDFQDFVSQ 239
                        170       180
                 ....*....|....*....|
gi 297822009 918 alnCTAIDPQERPCTKNVLQ 937
Cdd:cd06605  240 ---CLQKDPTERPSYKELME 256
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
788-865 9.17e-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: 39.31  E-value: 9.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297822009 788 ALRFLHcrcSPAVVAGNLSPENIVIDVKDQPRLCLGLPGLLCMDSA-----------YMAPETRERKEMTSKSDIYGFGI 856
Cdd:cd05582  109 ALDHLH---SLGIIYRDLKPENILLDEDGHIKLTDFGLSKESIDHEkkaysfcgtveYMAPEVVNRRGHTQSADWWSFGV 185

                 ....*....
gi 297822009 857 LLLNLLTGK 865
Cdd:cd05582  186 LMFEMLTGS 194
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
123-161 9.57e-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: 34.91  E-value: 9.57e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 297822009  123 PSLRYLNLSNNNFSGSISRGFLPNLYTLDLSNNMFTGEI 161
Cdd:pfam12799   1 PNLEVLDLSNNQITDIPPLAKLPNLETLDLSGNNKITDL 39
 
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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