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Conserved domains on  [gi|1958659070|ref|XP_038942094|]
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STE20-related kinase adapter protein alpha isoform X5 [Rattus norvegicus]

Protein Classification

STE20-related kinase adapter protein alpha( domain architecture ID 10169501)

STE20-related kinase adapter protein alpha is a pseudokinase that binds ATP but lacks activity due to non-conservative substitutions of essential catalytic residues; in complex with CAB39/MO25, it binds to and activates STK11/LKB1

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PK_STRAD_alpha cd08227
Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain ...
62-388 0e+00

Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha, stabilized through ATP and MO25, may be needed to activate LKB1. A mutation which results in a truncation of a C-terminal part of the human STRAD-alpha pseudokinase domain and disrupts its association with LKB1, leads to PMSE (polyhydramnios, megalencephaly, symptomatic epilepsy) syndrome. Several splice variants of STRAD-alpha exist which exhibit different effects on the localization and activation of LKB1. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. The STRAD alpha subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


:

Pssm-ID: 173767 [Multi-domain]  Cd Length: 327  Bit Score: 672.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  62 ELLSVIGKGFEDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTSF 141
Cdd:cd08227     1 ELLTVIGRGFEDLMTVNLARYKPTGEYVTVRRINLEACTNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 142 MAYGSAKDLIGTHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLRSNLSMISHGQRQRA 221
Cdd:cd08227    81 MAYGSAKDLICTHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMINHGQRLRV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 222 VHDFPKYSIKVLPWLSPEVLQQNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPCLLDTSTIPAEE 301
Cdd:cd08227   161 VHDFPKYSVKVLPWLSPEVLQQNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPCLLDTTTIPAEE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 302 LTMSPSRSIANPGLNDSLAAGSLRPANGDSPSHPYHRTFSPHFHNFVEQCLQRNPDARPNASTLLNHSFFKQIKRRASEA 381
Cdd:cd08227   241 LTMKPSRSGANSGLGESTTVSTPRPSNGESSSHPYNRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQIKRRASEA 320

                  ....*..
gi 1958659070 382 LPELLRP 388
Cdd:cd08227   321 LPELLRP 327
 
Name Accession Description Interval E-value
PK_STRAD_alpha cd08227
Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain ...
62-388 0e+00

Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha, stabilized through ATP and MO25, may be needed to activate LKB1. A mutation which results in a truncation of a C-terminal part of the human STRAD-alpha pseudokinase domain and disrupts its association with LKB1, leads to PMSE (polyhydramnios, megalencephaly, symptomatic epilepsy) syndrome. Several splice variants of STRAD-alpha exist which exhibit different effects on the localization and activation of LKB1. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. The STRAD alpha subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173767 [Multi-domain]  Cd Length: 327  Bit Score: 672.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  62 ELLSVIGKGFEDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTSF 141
Cdd:cd08227     1 ELLTVIGRGFEDLMTVNLARYKPTGEYVTVRRINLEACTNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 142 MAYGSAKDLIGTHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLRSNLSMISHGQRQRA 221
Cdd:cd08227    81 MAYGSAKDLICTHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMINHGQRLRV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 222 VHDFPKYSIKVLPWLSPEVLQQNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPCLLDTSTIPAEE 301
Cdd:cd08227   161 VHDFPKYSVKVLPWLSPEVLQQNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPCLLDTTTIPAEE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 302 LTMSPSRSIANPGLNDSLAAGSLRPANGDSPSHPYHRTFSPHFHNFVEQCLQRNPDARPNASTLLNHSFFKQIKRRASEA 381
Cdd:cd08227   241 LTMKPSRSGANSGLGESTTVSTPRPSNGESSSHPYNRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQIKRRASEA 320

                  ....*..
gi 1958659070 382 LPELLRP 388
Cdd:cd08227   321 LPELLRP 327
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
61-371 2.80e-50

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 170.40  E-value: 2.80e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070   61 YELLSVIGKG-FEdlmTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQgELHVSKLFSHPNIVPYRATFIADNELWAVT 139
Cdd:smart00220   1 YEILEKLGEGsFG---KVYLARDKKTGKLVAIKVIKKKKIKKDRERILR-EIKILKKLKHPNIVRLYDVFEDEDKLYLVM 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  140 SFMAYGSAKDLIgtHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRsnlsmishgq 217
Cdd:smart00220  77 EYCEGGDLFDLL--KKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLAdfGLA---------- 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  218 rqRAVHDFPKYSIKV--LPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLngtvpclldts 295
Cdd:smart00220 145 --RQLDPGEKLTTFVgtPEYMAPEVLLG--KGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKI----------- 209
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958659070  296 tipaeeltmspsrsianpglndslaagslrpANGDSPSHPYHRTFSPHFHNFVEQCLQRNPDARPNASTLLNHSFF 371
Cdd:smart00220 210 -------------------------------GKPKPPFPPPEWDISPEAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
51-360 6.15e-30

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 120.89  E-value: 6.15e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  51 MSSflPEGGCYELLSVIGKGFedlM-TVNLARYKPTGEYVTVRRINLEACSNE--MVTFLQgELHVSKLFSHPNIVPYRA 127
Cdd:COG0515     1 MSA--LLLGRYRILRLLGRGG---MgVVYLARDLRLGRPVALKVLRPELAADPeaRERFRR-EARALARLNHPNIVRVYD 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 128 TFIADNELWAVTSFMAYGSAKDLIGTHfmDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYL---- 203
Cdd:COG0515    75 VGEEDGRPYLVMEYVEGESLADLLRRR--GPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLidfg 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 204 -SGLRSNLSMISHGQRQRAVHdfpkysikvlpWLSPEVLQqnLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLE 282
Cdd:COG0515   153 iARALGGATLTQTGTVVGTPG-----------YMAPEQAR--GEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRA 219
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958659070 283 KLNGTVPclldtstiPAEELtmspsrsiaNPGLNDSLAAgslrpangdspshpyhrtfsphfhnFVEQCLQRNPDARP 360
Cdd:COG0515   220 HLREPPP--------PPSEL---------RPDLPPALDA-------------------------IVLRALAKDPEERY 255
Pkinase pfam00069
Protein kinase domain;
61-371 9.98e-24

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 98.47  E-value: 9.98e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKG-FEdlmTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVT 139
Cdd:pfam00069   1 YEVLRKLGSGsFG---TVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 140 SFMAYGSAKDLIGTHFmdGMSE-LAIAYILQgVLKALDyihhmgyvhRSVKASHILIStdgkvylsglrsnlsmishgqr 218
Cdd:pfam00069  78 EYVEGGSLFDLLSEKG--AFSErEAKFIMKQ-ILEGLE---------SGSSLTTFVGT---------------------- 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 219 qravhdfpkysikvLPWLSPEVLQQNlqGYDAKSDIYSVGITACELANGHVPFKDmpatqmlleklngtvpcllDTSTIP 298
Cdd:pfam00069 124 --------------PWYMAPEVLGGN--PYGPKVDVWSLGCILYELLTGKPPFPG-------------------INGNEI 168
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958659070 299 AEELTMSPSRSIANPglndslaagslrpangdspshpyhRTFSPHFHNFVEQCLQRNPDARPNASTLLNHSFF 371
Cdd:pfam00069 169 YELIIDQPYAFPELP------------------------SNLSEEAKDLLKKLLKKDPSKRLTATQALQHPWF 217
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
26-391 1.41e-14

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 74.47  E-value: 1.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  26 PPGDTRRKANEASSESIASFSKPEIMSSFlpeggcyELLSVIGKGFEDlmTVNLARYKPTGEYVTVRRI--NLEACSNEM 103
Cdd:PLN00034   48 PPPSSSSSSSSSSSASGSAPSAAKSLSEL-------ERVNRIGSGAGG--TVYKVIHRPTGRLYALKVIygNHEDTVRRQ 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 104 VTflqGELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGSakdLIGTHFMDgmsELAIAYILQGVLKALDYIHHMGY 183
Cdd:PLN00034  119 IC---REIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGS---LEGTHIAD---EQFLADVARQILSGIAYLHRRHI 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 184 VHRSVKASHILIStdgkvylSGLRSNLSMISHGQRQRAVHDFPKYSIKVLPWLSPEVLQQNL-QG-YDAKS-DIYSVGIT 260
Cdd:PLN00034  190 VHRDIKPSNLLIN-------SAKNVKIADFGVSRILAQTMDPCNSSVGTIAYMSPERINTDLnHGaYDGYAgDIWSLGVS 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 261 ACELANGHVPFkdmpatqmlleklngtvpclldtstipaeeltmspsrsianpGLNDSLAAGSLRPA--NGDSPSHPyhR 338
Cdd:PLN00034  263 ILEFYLGRFPF------------------------------------------GVGRQGDWASLMCAicMSQPPEAP--A 298
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958659070 339 TFSPHFHNFVEQCLQRNPDARPNASTLLNHSFFKQIKRRASEALPElLRPVTP 391
Cdd:PLN00034  299 TASREFRHFISCCLQREPAKRWSAMQLLQHPFILRAQPGQGQGGPN-LHQLLP 350
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
58-271 9.27e-13

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 69.82  E-value: 9.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  58 GGCYELLSVIGKG-------FEDL----------MTVNLARyKPTgeyvTVRRINLEACSnemvtflqgelhVSKLfSHP 120
Cdd:NF033483    6 GGRYEIGERIGRGgmaevylAKDTrldrdvavkvLRPDLAR-DPE----FVARFRREAQS------------AASL-SHP 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 121 NIV-----------PYratfIAdnelwavtsfMAY--GSA-KDLIGTHFMdgMSELAIAYILQGVLKALDYIHHMGYVHR 186
Cdd:NF033483   68 NIVsvydvgedggiPY----IV----------MEYvdGRTlKDYIREHGP--LSPEEAVEIMIQILSALEHAHRNGIVHR 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 187 SVKASHILISTDGKV---------YLSGlrSNL----SMIshGqrqrAVHdfpkYsikvlpwLSPEvlqQNLQGY-DAKS 252
Cdd:NF033483  132 DIKPQNILITKDGRVkvtdfgiarALSS--TTMtqtnSVL--G----TVH----Y-------LSPE---QARGGTvDARS 189
                         250
                  ....*....|....*....
gi 1958659070 253 DIYSVGITACELANGHVPF 271
Cdd:NF033483  190 DIYSLGIVLYEMLTGRPPF 208
 
Name Accession Description Interval E-value
PK_STRAD_alpha cd08227
Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain ...
62-388 0e+00

Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha, stabilized through ATP and MO25, may be needed to activate LKB1. A mutation which results in a truncation of a C-terminal part of the human STRAD-alpha pseudokinase domain and disrupts its association with LKB1, leads to PMSE (polyhydramnios, megalencephaly, symptomatic epilepsy) syndrome. Several splice variants of STRAD-alpha exist which exhibit different effects on the localization and activation of LKB1. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. The STRAD alpha subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173767 [Multi-domain]  Cd Length: 327  Bit Score: 672.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  62 ELLSVIGKGFEDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTSF 141
Cdd:cd08227     1 ELLTVIGRGFEDLMTVNLARYKPTGEYVTVRRINLEACTNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 142 MAYGSAKDLIGTHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLRSNLSMISHGQRQRA 221
Cdd:cd08227    81 MAYGSAKDLICTHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMINHGQRLRV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 222 VHDFPKYSIKVLPWLSPEVLQQNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPCLLDTSTIPAEE 301
Cdd:cd08227   161 VHDFPKYSVKVLPWLSPEVLQQNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPCLLDTTTIPAEE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 302 LTMSPSRSIANPGLNDSLAAGSLRPANGDSPSHPYHRTFSPHFHNFVEQCLQRNPDARPNASTLLNHSFFKQIKRRASEA 381
Cdd:cd08227   241 LTMKPSRSGANSGLGESTTVSTPRPSNGESSSHPYNRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQIKRRASEA 320

                  ....*..
gi 1958659070 382 LPELLRP 388
Cdd:cd08227   321 LPELLRP 327
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
62-388 0e+00

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


Pssm-ID: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 523.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  62 ELLSVIGKGFEDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTSF 141
Cdd:cd08216     1 ELLYEIGKCFKGGGVVHLAKHKPTNTLVAVKKINLESDSKEDLKFLQQEILTSRQLQHPNILPYVTSFVVDNDLYVVTPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 142 MAYGSAKDLIGTHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLRSNLSMISHGQRQRA 221
Cdd:cd08216    81 MAYGSCRDLLKTHFPEGLPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGLRYAYSMVKHGKRQRV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 222 VHDFPKYSIKVLPWLSPEVLQQNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPCLLDTSTIPAEE 301
Cdd:cd08216   161 VHDFPKSSEKNLPWLSPEVLQQNLLGYNEKSDIYSVGITACELANGVVPFSDMPATQMLLEKVRGTTPQLLDCSTYPLEE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 302 LTMSPSRSIANPglndslaagslRPANGDSPSHPYHRTFSPHFHNFVEQCLQRNPDARPNASTLLNHSFFKQIkRRASEA 381
Cdd:cd08216   241 DSMSQSEDSSTE-----------HPNNRDTRDIPYQRTFSEAFHQFVELCLQRDPELRPSASQLLAHSFFKQC-RRSNTS 308

                  ....*..
gi 1958659070 382 LPELLRP 388
Cdd:cd08216   309 LLDLLKP 315
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
62-388 8.44e-138

Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity.STRAD-beta is also referred to as ALS2CR2 (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 2 protein), since the human gene encoding it is located within the juvenile ALS2 critical region on chromosome 2q33-q34. It is not linked to the development of ALS2. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. The STRAD-beta subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270864 [Multi-domain]  Cd Length: 328  Bit Score: 397.32  E-value: 8.44e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  62 ELLSVIGKGFEDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTSF 141
Cdd:cd08226     1 ELQVELGKGFCNLTSVYLARHTPTGTLVTVKITNLDNCSEEHLKALQNEVVLSHFFRHPNIMTHWTVFTEGSWLWVISPF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 142 MAYGSAKDLIGTHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLRSNLSMISHGQRQRA 221
Cdd:cd08226    81 MAYGSARGLLKTYFPEGMNEALIGNILYGAIKALNYLHQNGCIHRSVKASHILISGDGLVSLSGLSHLYSMVTNGQRSKV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 222 VHDFPKYSIKVLPWLSPEVLQQNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPCLLDTSTIPAEE 301
Cdd:cd08226   161 VYDFPQFSTSVLPWLSPELLRQDLHGYNVKSDIYSVGITACELARGQVPFQDMRRTQMLLQKLKGPPYSPLDIFPFPELE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 302 LTMSPSRSIANPGLNDSLAAGSLRPANGDSPSH-PYHRTFSPHFHNFVEQCLQRNPDARPNASTLLNHSFFKQIKRRASE 380
Cdd:cd08226   241 SRMKNSQSGMDSGIGESVATSSMTRTMTSERLQtPSSKTFSPAFHNLVELCLQQDPEKRPSASSLLSHSFFKQVKEQTQA 320

                  ....*...
gi 1958659070 381 ALPELLRP 388
Cdd:cd08226   321 SLLSLLPP 328
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
61-371 4.44e-67

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


Pssm-ID: 270787 [Multi-domain]  Cd Length: 267  Bit Score: 214.53  E-value: 4.44e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGFEdlMTVNLARYKPTGEYVTVRRINLEACSNEMvTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTS 140
Cdd:cd06610     3 YELIEVIGSGAT--AVVYAAYCLPKKEKVAIKRIDLEKCQTSM-DELRKEIQAMSQCNHPNVVSYYTSFVVGDELWLVMP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 141 FMAYGSAKDLIGTHF-MDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLRSNLSMISHGQRQ 219
Cdd:cd06610    80 LLSGGSLLDIMKSSYpRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVSASLATGGDRT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 220 RAVhdfpKYSIKVLP-WLSPEVLQQnLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPCLldtstip 298
Cdd:cd06610   160 RKV----RKTFVGTPcWMAPEVMEQ-VRGYDFKADIWSFGITAIELATGAAPYSKYPPMKVLMLTLQNDPPSL------- 227
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958659070 299 aeeltmspsrsianpglndslaagslrPANGDspshpyHRTFSPHFHNFVEQCLQRNPDARPNASTLLNHSFF 371
Cdd:cd06610   228 ---------------------------ETGAD------YKKYSKSFRKMISLCLQKDPSKRPTAEELLKHKFF 267
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
60-371 1.54e-57

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: 189.34  E-value: 1.54e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  60 CYELLSVIGKG-FEdlmTVNLARYKPTGEYVTVRRINLEACSNEmvTFLQGELHVSKLFSHPNIVPYRATFIADNELWAV 138
Cdd:cd05122     1 LFEILEKIGKGgFG---VVYKARHKKTGQIVAIKKINLESKEKK--ESILNEIAILKKCKHPNIVKYYGSYLKKDELWIV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 139 TSFMAYGSAKDLIgTHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSNLSmiSHG 216
Cdd:cd05122    76 MEFCSGGSLKDLL-KNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIdfGLSAQLS--DGK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 217 QRQRAVhdfpkysiKVLPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEklngtvpclldTST 296
Cdd:cd05122   153 TRNTFV--------GTPYWMAPEVIQG--KPYGFKADIWSLGITAIEMAEGKPPYSELPPMKALFL-----------IAT 211
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958659070 297 IPAeeltmspsrsianPGLndslaagslrpangDSPShpyhrTFSPHFHNFVEQCLQRNPDARPNASTLLNHSFF 371
Cdd:cd05122   212 NGP-------------PGL--------------RNPK-----KWSKEFKDFLKKCLQKDPEKRPTAEQLLKHPFI 254
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
61-387 3.82e-51

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


Pssm-ID: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 173.20  E-value: 3.82e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKG-FEDlmtVNLARYKPTGEYVTVRRINLEAcSNEMVTFLQGELHV-SKLFShPNIVPYRATFIADNELWAV 138
Cdd:cd06609     3 FTLLERIGKGsFGE---VYKGIDKRTNQVVAIKVIDLEE-AEDEIEDIQQEIQFlSQCDS-PYITKYYGSFLKGSKLWII 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 139 TSFMAYGSAKDLIGthfMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYL-----SG-LRSNLSm 212
Cdd:cd06609    78 MEYCGGGSVLDLLK---PGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLadfgvSGqLTSTMS- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 213 ishgQRQRAVHDfpkysikvlP-WLSPEVLQQNlqGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEklngtvpcl 291
Cdd:cd06609   154 ----KRNTFVGT---------PfWMAPEVIKQS--GYDEKADIWSLGITAIELAKGEPPLSDLHPMRVLFL--------- 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 292 ldtstIPAEeltmspsrsiaNPglndslaagslrpangdsPSHPyHRTFSPHFHNFVEQCLQRNPDARPNASTLLNHSFF 371
Cdd:cd06609   210 -----IPKN-----------NP------------------PSLE-GNKFSKPFKDFVELCLNKDPKERPSAKELLKHKFI 254
                         330
                  ....*....|....*.
gi 1958659070 372 KQIKRRASeaLPELLR 387
Cdd:cd06609   255 KKAKKTSY--LTLLIE 268
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
61-371 2.80e-50

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 170.40  E-value: 2.80e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070   61 YELLSVIGKG-FEdlmTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQgELHVSKLFSHPNIVPYRATFIADNELWAVT 139
Cdd:smart00220   1 YEILEKLGEGsFG---KVYLARDKKTGKLVAIKVIKKKKIKKDRERILR-EIKILKKLKHPNIVRLYDVFEDEDKLYLVM 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  140 SFMAYGSAKDLIgtHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRsnlsmishgq 217
Cdd:smart00220  77 EYCEGGDLFDLL--KKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLAdfGLA---------- 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  218 rqRAVHDFPKYSIKV--LPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLngtvpclldts 295
Cdd:smart00220 145 --RQLDPGEKLTTFVgtPEYMAPEVLLG--KGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKI----------- 209
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958659070  296 tipaeeltmspsrsianpglndslaagslrpANGDSPSHPYHRTFSPHFHNFVEQCLQRNPDARPNASTLLNHSFF 371
Cdd:smart00220 210 -------------------------------GKPKPPFPPPEWDISPEAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
61-371 8.39e-49

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


Pssm-ID: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 166.71  E-value: 8.39e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKG-FEDlmtVNLARYKPTGEYVTVRRINLEAcsNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVT 139
Cdd:cd06613     2 YELIQRIGSGtYGD---VYKARNIATGELAAVKVIKLEP--GDDFEIIQQEISMLKECRHPNIVAYFGSYLRRDKLWIVM 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 140 SFMAYGSAKDLIgtHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRsnlSMISHGQ 217
Cdd:cd06613    77 EYCGGGSLQDIY--QVTGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLAdfGVS---AQLTATI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 218 RQRavhdfpKYSIKVLPWLSPEVLQQNLQ-GYDAKSDIYSVGITACELANGHVPFKDMPatqmlleklngtvpclldtst 296
Cdd:cd06613   152 AKR------KSFIGTPYWMAPEVAAVERKgGYDGKCDIWALGITAIELAELQPPMFDLH--------------------- 204
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958659070 297 iPAEELTMSPSRSIANPGLNDSlaagslrpangdspshpyHRtFSPHFHNFVEQCLQRNPDARPNASTLLNHSFF 371
Cdd:cd06613   205 -PMRALFLIPKSNFDPPKLKDK------------------EK-WSPDFHDFIKKCLTKNPKKRPTATKLLQHPFV 259
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
61-371 4.19e-45

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


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 157.04  E-value: 4.19e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEmvtfLQGELHVSKLFSHPNIVPYRATFIADNELWAVTS 140
Cdd:cd06612     5 FDILEKLGEG--SYGSVYKAIHKETGQVVAIKVVPVEEDLQE----IIKEISILKQCDSPYIVKYYGSYFKNTDLWIVME 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 141 FMAYGSAKDLIGThFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSNLsmiSHGQR 218
Cdd:cd06612    79 YCGAGSVSDIMKI-TNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLAdfGVSGQL---TDTMA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 219 QRavhdfpKYSIKVLPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLeklngtvpclldtsTIP 298
Cdd:cd06612   155 KR------NTVIGTPFWMAPEVIQE--IGYNNKADIWSLGITAIEMAEGKPPYSDIHPMRAIF--------------MIP 212
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958659070 299 aeelTMSPsrsianPGLNDslaagslrpangdsPSHpyhrtFSPHFHNFVEQCLQRNPDARPNASTLLNHSFF 371
Cdd:cd06612   213 ----NKPP------PTLSD--------------PEK-----WSPEFNDFVKKCLVKDPEERPSAIQLLQHPFI 256
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
61-372 9.54e-44

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


Pssm-ID: 270789 [Multi-domain]  Cd Length: 255  Bit Score: 153.14  E-value: 9.54e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGFEDlmTVNLARYKPTGEYVTVRRINLEACSNEMvtfLQGELHVSKLFSHPNIVPYRATFIADNELWAVTS 140
Cdd:cd06614     2 YKNLEKIGEGASG--EVYKATDRATGKEVAIKKMRLRKQNKEL---IINEILIMKECKHPNIVDYYDSYLVGDELWVVME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 141 FMAYGSAKDLIGTHFMDgMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSNLSMiSHGQR 218
Cdd:cd06614    77 YMDGGSLTDIITQNPVR-MNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLAdfGFAAQLTK-EKSKR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 219 QravhdfpkySIKVLP-WLSPEVLQQNLqgYDAKSDIYSVGITACELANGHVPFKDMPATQMLLeklngtvpcLLDTSTI 297
Cdd:cd06614   155 N---------SVVGTPyWMAPEVIKRKD--YGPKVDIWSLGIMCIEMAEGEPPYLEEPPLRALF---------LITTKGI 214
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958659070 298 PAeeltmspsrsianpglndslaagsLRPANGdspshpyhrtFSPHFHNFVEQCLQRNPDARPNASTLLNHSFFK 372
Cdd:cd06614   215 PP------------------------LKNPEK----------WSPEFKDFLNKCLVKDPEKRPSAEELLQHPFLK 255
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
66-371 7.78e-40

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: 143.04  E-value: 7.78e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  66 VIGKG-FEdlmTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAY 144
Cdd:cd06606     7 LLGKGsFG---SVYLALNLDTGELMAVKEVELSGDSEEELEALEREIRILSSLKHPNIVRYLGTERTENTLNIFLEYVPG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 145 GSAKDLIGThFmDGMSE-LAIAYILQgVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSNLSMISHGQRQRA 221
Cdd:cd06606    84 GSLASLLKK-F-GKLPEpVVRKYTRQ-ILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLAdfGCAKRLAEIATGEGTKS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 222 VHDFPkysikvlPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLngtvpclldtstipaee 301
Cdd:cd06606   161 LRGTP-------YWMAPEVIRG--EGYGRAADIWSLGCTVIEMATGKPPWSELGNPVAALFKI----------------- 214
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958659070 302 ltmspsrsianpglndslaagslrpanGDSPSHPY-HRTFSPHFHNFVEQCLQRNPDARPNASTLLNHSFF 371
Cdd:cd06606   215 ---------------------------GSSGEPPPiPEHLSEEAKDFLRKCLQRDPKKRPTADELLQHPFL 258
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
67-369 5.63e-38

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


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 136.63  E-value: 5.63e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  67 IGKG-FedlMTVNLARYKPTGEYVTVRRINLEaCSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYG 145
Cdd:cd00180     1 LGKGsF---GKVYKARDKETGKKVAVKVIPKE-KLKKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 146 SAKDLIGTHFmDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLRSNLSMISHGqrqravhDF 225
Cdd:cd00180    77 SLKDLLKENK-GPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDD-------SL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 226 PKYSIKVLPWLSPEVLQQNLQGYDAKSDIYSVGITACELanghvpfkdmpatqmlleklngtvpclldtstipaeeltms 305
Cdd:cd00180   149 LKTTGGTTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL----------------------------------------- 187
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958659070 306 psrsianpglndslaagslrpangdspshpyhrtfsPHFHNFVEQCLQRNPDARPNASTLLNHS 369
Cdd:cd00180   188 ------------------------------------EELKDLIRRMLQYDPKKRPSAKELLEHL 215
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
55-370 6.60e-38

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


Pssm-ID: 270785 [Multi-domain]  Cd Length: 275  Bit Score: 138.59  E-value: 6.60e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  55 LPE-GGCYELLSVIGKGFEDLmtVNLARYKPTGEYVTVRRINLEAcsnEMVTFLQGELHVSKLFS-HPNIVPYRATFI-- 130
Cdd:cd06608     1 LPDpAGIFELVEVIGEGTYGK--VYKARHKKTGQLAAIKIMDIIE---DEEEEIKLEINILRKFSnHPNIATFYGAFIkk 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 131 ----ADNELWAVTSFMAYGSAKDLI-GTHFMDG-MSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS 204
Cdd:cd06608    76 dppgGDDQLWLVMEYCGGGSVTDLVkGLRKKGKrLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 205 --GLRSNLSMiSHGQRQRavhdfpkySIKVLPWLSPEVL---QQNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQM 279
Cdd:cd06608   156 dfGVSAQLDS-TLGRRNT--------FIGTPYWMAPEVIacdQQPDASYDARCDVWSLGITAIELADGKPPLCDMHPMRA 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 280 LLEklngtvpclldtstIPAeeltmSPSrsianPGLndslaagsLRPANgdspshpyhrtFSPHFHNFVEQCLQRNPDAR 359
Cdd:cd06608   227 LFK--------------IPR-----NPP-----PTL--------KSPEK-----------WSKEFNDFISECLIKNYEQR 263
                         330
                  ....*....|.
gi 1958659070 360 PNASTLLNHSF 370
Cdd:cd06608   264 PFTEELLEHPF 274
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
60-371 3.48e-37

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


Pssm-ID: 270797 [Multi-domain]  Cd Length: 254  Bit Score: 135.82  E-value: 3.48e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  60 CYELLSVIGKG-FEdlmTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAV 138
Cdd:cd06627     1 NYQLGDLIGRGaFG---SVYKGLNLNTGEFVAIKQISLEKIPKSDLKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYII 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 139 TSFMAYGSAKDLIGTHfmDGMSE-LAIAYILQgVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSNLSMiSH 215
Cdd:cd06627    78 LEYVENGSLASIIKKF--GKFPEsLVAVYIYQ-VLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLAdfGVATKLNE-VE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 216 GQRQRAVHDfpkysikvlP-WLSPEVLQqnLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLleklngtvpclldt 294
Cdd:cd06627   154 KDENSVVGT---------PyWMAPEVIE--MSGVTTASDIWSVGCTVIELLTGNPPYYDLQPMAAL-------------- 208
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958659070 295 stipaeeltmspsrsianpglndslaagsLRPANGDSPshPYHRTFSPHFHNFVEQCLQRNPDARPNASTLLNHSFF 371
Cdd:cd06627   209 -----------------------------FRIVQDDHP--PLPENISPELRDFLLQCFQKDPTLRPSAKELLKHPWL 254
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
62-374 7.00e-36

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


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 132.72  E-value: 7.00e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  62 ELLSVIGKGFEDlmTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQgELHVSKLFSHPNIVPYRATFIADNELWAVTSF 141
Cdd:cd06623     4 ERVKVLGQGSSG--VVYKVRHKPTGKIYALKKIHVDGDEEFRKQLLR-ELKTLRSCESPYVVKCYGAFYKEGEISIVLEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 142 MAYGSAKDLIGTHfmDGMSELAIAYILQGVLKALDYIH---HMgyVHRSVKASHILISTDGKVYLS--GLRSNLSMIshg 216
Cdd:cd06623    81 MDGGSLADLLKKV--GKIPEPVLAYIARQILKGLDYLHtkrHI--IHRDIKPSNLLINSKGEVKIAdfGISKVLENT--- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 217 qrqravhDFPKYS-IKVLPWLSPEVLQQNLQGYDakSDIYSVGITACELANGHVPFKdmPATQM----LLEKLNgtvpcl 291
Cdd:cd06623   154 -------LDQCNTfVGTVTYMSPERIQGESYSYA--ADIWSLGLTLLECALGKFPFL--PPGQPsffeLMQAIC------ 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 292 ldtstipaeeltmspsrsianpglndslaagslrpaNGDSPSHPYHrTFSPHFHNFVEQCLQRNPDARPNASTLLNHSFF 371
Cdd:cd06623   217 ------------------------------------DGPPPSLPAE-EFSPEFRDFISACLQKDPKKRPSAAELLQHPFI 259

                  ...
gi 1958659070 372 KQI 374
Cdd:cd06623   260 KKA 262
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
62-373 1.59e-35

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: 131.70  E-value: 1.59e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  62 ELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQgELHVSKLFSHPNIVPYRATFIADNELWAVTSF 141
Cdd:cd06605     4 EYLGELGEG--NGGVVSKVRHRPSGQIMAVKVIRLEIDEALQKQILR-ELDVLHKCNSPYIVGFYGAFYSEGDISICMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 142 MAYGSAKDLIgtHFMDGMSELAIAYILQGVLKALDYIHH-MGYVHRSVKASHILISTDGKVYLS--GLRSNLsmishgqr 218
Cdd:cd06605    81 MDGGSLDKIL--KEVGRIPERILGKIAVAVVKGLIYLHEkHKIIHRDVKPSNILVNSRGQVKLCdfGVSGQL-------- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 219 qraVHDFPKYSIKVLPWLSPEVLQQNlqGYDAKSDIYSVGITACELANGHVPFKdmpatqmlleklngtvPCLLDTSTIP 298
Cdd:cd06605   151 ---VDSLAKTFVGTRSYMAPERISGG--KYTVKSDIWSLGLSLVELATGRFPYP----------------PPNAKPSMMI 209
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958659070 299 AEELTmspsrsianpglndslaagslRPANGDSPSHPYHRtFSPHFHNFVEQCLQRNPDARPNASTLLNHSFFKQ 373
Cdd:cd06605   210 FELLS---------------------YIVDEPPPLLPSGK-FSPDFQDFVSQCLQKDPTERPSYKELMEHPFIKR 262
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
61-373 1.24e-33

Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. They activate the MAPKs, p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating the respective MAP/ERK kinases (MEKs, also known as MKKs or MAPKKs), MEK3/MEK6 and MKK4/MKK7. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. Vertebrates contain three TAO subfamily members, named TAO1, TAO2, and TAO3. The TAO subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270784 [Multi-domain]  Cd Length: 258  Bit Score: 126.41  E-value: 1.24e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEA-CSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVt 139
Cdd:cd06607     3 FEDLREIGHG--SFGAVYYARNKRTSEVVAIKKMSYSGkQSTEKWQDIIKEVKFLRQLRHPNTIEYKGCYLREHTAWLV- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 140 sfMAY--GSAKDLIGTHfMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLRSnLSMIShgq 217
Cdd:cd06607    80 --MEYclGSASDIVEVH-KKPLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFGS-ASLVC--- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 218 rqravhdfPKYSIKVLP-WLSPEVLQQNLQG-YDAKSDIYSVGITACELANGHVPFKDMPAtqmlleklngtvpclldts 295
Cdd:cd06607   153 --------PANSFVGTPyWMAPEVILAMDEGqYDGKVDVWSLGITCIELAERKPPLFNMNA------------------- 205
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958659070 296 tipaeeltMSPSRSIANpglNDSlaagslrPANGDSPshpyhrtFSPHFHNFVEQCLQRNPDARPNASTLLNHSFFKQ 373
Cdd:cd06607   206 --------MSALYHIAQ---NDS-------PTLSSGE-------WSDDFRNFVDSCLQKIPQDRPSAEDLLKHPFVTR 258
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
76-372 1.13e-32

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


Pssm-ID: 270815 [Multi-domain]  Cd Length: 261  Bit Score: 124.09  E-value: 1.13e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  76 TVNLARYKPTGEYVTVRRINLEACSNEMVTFlqGELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGSAKDLIgTHF 155
Cdd:cd06648    22 IVCIATDKSTGRQVAVKKMDLRKQQRRELLF--NEVVIMRDYQHPNIVEMYSSYLVGDELWVVMEFLEGGALTDIV-THT 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 156 MdgMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSNLSmishgqrqravHDFPKYSIKV- 232
Cdd:cd06648    99 R--MNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSdfGFCAQVS-----------KEVPRRKSLVg 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 233 LP-WLSPEVLQQNLqgYDAKSDIYSVGITACELANGHVPFKDMPATQmlleklngtvpclldtstipaeelTMSPSRSIA 311
Cdd:cd06648   166 TPyWMAPEVISRLP--YGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQ------------------------AMKRIRDNE 219
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958659070 312 NPGLNDslaagslrpangdspshpyHRTFSPHFHNFVEQCLQRNPDARPNASTLLNHSFFK 372
Cdd:cd06648   220 PPKLKN-------------------LHKVSPRLRSFLDRMLVRDPAQRATAAELLNHPFLA 261
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
77-386 1.34e-32

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


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 124.47  E-value: 1.34e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  77 VNLARYKPTGEYVTVRRINLEAcSNEMVTFLQgELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAyGSAKDLIGTHFM 156
Cdd:cd06611    21 VYKAQHKETGLFAAAKIIQIES-EEELEDFMV-EIDILSECKHPNIVGLYEAYFYENKLWILIEFCD-GGALDSIMLELE 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 157 DGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLRSNLSMISHGQRQravHDFpkysIKVLPWL 236
Cdd:cd06611    98 RGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSAKNKSTLQKR---DTF----IGTPYWM 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 237 SPEVLQQNL---QGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPCLldtstipaeeltmspsrsianp 313
Cdd:cd06611   171 APEVVACETfkdNPYDYKADIWSLGITLIELAQMEPPHHELNPMRVLLKILKSEPPTL---------------------- 228
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958659070 314 glndslaagslrpangDSPSHpyhrtFSPHFHNFVEQCLQRNPDARPNASTLLNHSFFKQIKRRasEALPELL 386
Cdd:cd06611   229 ----------------DQPSK-----WSSSFNDFLKSCLVKDPDDRPTAAELLKHPFVSDQSDN--KAIKDLL 278
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
61-370 9.35e-32

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


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 121.67  E-value: 9.35e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKG-FEDlmtVNLARYKPTGEYVTVRRINLEACSNemVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVT 139
Cdd:cd06646    11 YELIQRVGSGtYGD---VYKARNLHTGELAAVKIIKLEPGDD--FSLIQQEIFMVKECKHCNIVAYFGSYLSREKLWICM 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 140 SFMAYGSAKDLIgtHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLRSNLSMISHGQRQ 219
Cdd:cd06646    86 EYCGGGSLQDIY--HVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVAAKITATIAKR 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 220 RAVHDFPKysikvlpWLSPEV--LQQNlQGYDAKSDIYSVGITACELANGHVPFKDMPatqmlleklngtvpclldtsti 297
Cdd:cd06646   164 KSFIGTPY-------WMAPEVaaVEKN-GGYNQLCDIWAVGITAIELAELQPPMFDLH---------------------- 213
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958659070 298 PAEELTMSPSRSIANPGLNDSLaagslrpangdspshpyhrTFSPHFHNFVEQCLQRNPDARPNASTLLNHSF 370
Cdd:cd06646   214 PMRALFLMSKSNFQPPKLKDKT-------------------KWSSTFHNFVKISLTKNPKKRPTAERLLTHLF 267
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
61-386 9.42e-32

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


Pssm-ID: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 121.81  E-value: 9.42e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEmVTFLQGELHV---SKLFSHPNIVPYRATFIADNELWA 137
Cdd:cd06917     3 YRRLELVGRG--SYGAVYRGYHVKTGRVVALKVLNLDTDDDD-VSDIQKEVALlsqLKLGQPKNIIKYYGSYLKGPSLWI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 138 VTSFMAYGSAKDLIGThfmDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSNLSmISH 215
Cdd:cd06917    80 IMDYCEGGSIRTLMRA---GPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCdfGVAASLN-QNS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 216 GQRQRAVHdfPKYsikvlpWLSPEVLQQNlQGYDAKSDIYSVGITACELANGHVPFKDMPATQ--MLLEKlngTVPclld 293
Cdd:cd06917   156 SKRSTFVG--TPY------WMAPEVITEG-KYYDTKADIWSLGITTYEMATGNPPYSDVDALRavMLIPK---SKP---- 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 294 tstipaeeltmspsrsianPGLNDslaagslrpangdspshpyhRTFSPHFHNFVEQCLQRNPDARPNASTLLNHSFFKQ 373
Cdd:cd06917   220 -------------------PRLEG--------------------NGYSPLLKEFVAACLDEEPKDRLSADELLKSKWIKQ 260
                         330
                  ....*....|...
gi 1958659070 374 IKRRASEALPELL 386
Cdd:cd06917   261 HSKTPTSVLKELI 273
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
51-360 6.15e-30

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 120.89  E-value: 6.15e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  51 MSSflPEGGCYELLSVIGKGFedlM-TVNLARYKPTGEYVTVRRINLEACSNE--MVTFLQgELHVSKLFSHPNIVPYRA 127
Cdd:COG0515     1 MSA--LLLGRYRILRLLGRGG---MgVVYLARDLRLGRPVALKVLRPELAADPeaRERFRR-EARALARLNHPNIVRVYD 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 128 TFIADNELWAVTSFMAYGSAKDLIGTHfmDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYL---- 203
Cdd:COG0515    75 VGEEDGRPYLVMEYVEGESLADLLRRR--GPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLidfg 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 204 -SGLRSNLSMISHGQRQRAVHdfpkysikvlpWLSPEVLQqnLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLE 282
Cdd:COG0515   153 iARALGGATLTQTGTVVGTPG-----------YMAPEQAR--GEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRA 219
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958659070 283 KLNGTVPclldtstiPAEELtmspsrsiaNPGLNDSLAAgslrpangdspshpyhrtfsphfhnFVEQCLQRNPDARP 360
Cdd:COG0515   220 HLREPPP--------PPSEL---------RPDLPPALDA-------------------------IVLRALAKDPEERY 255
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
85-386 8.75e-30

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


Pssm-ID: 270809 [Multi-domain]  Cd Length: 277  Bit Score: 116.71  E-value: 8.75e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  85 TGEYVTVRRINLEACSNEmVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGSAKDLIGTHFMDgmsELAI 164
Cdd:cd06641    28 TQKVVAIKIIDLEEAEDE-IEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYLGGGSALDLLEPGPLD---ETQI 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 165 AYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLrSNLSMISHGQRQRavhdfpKYSIKVLPWLSPEVLQQN 244
Cdd:cd06641   104 ATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADF-GVAGQLTDTQIKR------N*FVGTPFWMAPEVIKQS 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 245 lqGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLeklngtvpclldtsTIPAEeltmspsrsiaNPGLNDSlaagsl 324
Cdd:cd06641   177 --AYDSKADIWSLGITAIELARGEPPHSELHPMKVLF--------------LIPKN-----------NPPTLEG------ 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958659070 325 rpangdspshpyhrTFSPHFHNFVEQCLQRNPDARPNASTLLNHSFFKQIKRRASeALPELL 386
Cdd:cd06641   224 --------------NYSKPLKEFVEACLNKEPSFRPTAKELLKHKFILRNAKKTS-YLTELI 270
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
85-370 9.42e-30

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


Pssm-ID: 270802 [Multi-domain]  Cd Length: 259  Bit Score: 115.96  E-value: 9.42e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  85 TGEYVTVRRINL---EACSNEMVTFLQGELHV-SKLfSHPNIVPYRATFIADNELWAVTSFMAYGSAKDLIgtHFMDGMS 160
Cdd:cd06632    24 TGDFFAVKEVSLvddDKKSRESVKQLEQEIALlSKL-RHPNIVQYYGTEREEDNLYIFLEYVPGGSIHKLL--QRYGAFE 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 161 ELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSglrsNLSMISHGQRQRavhdFPKySIKVLP-WLSPE 239
Cdd:cd06632   101 EPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLA----DFGMAKHVEAFS----FAK-SFKGSPyWMAPE 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 240 VLQQNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEklngtvpclldtstipaeeltmspsrsIANpglndsl 319
Cdd:cd06632   172 VIMQKNSGYGLAVDIWSLGCTVLEMATGKPPWSQYEGVAAIFK---------------------------IGN------- 217
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958659070 320 aagslrpaNGDSPSHPYHrtFSPHFHNFVEQCLQRNPDARPNASTLLNHSF 370
Cdd:cd06632   218 --------SGELPPIPDH--LSPDAKDFIRLCLQRDPEDRPTASQLLEHPF 258
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
85-386 1.01e-29

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


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 116.31  E-value: 1.01e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  85 TGEYVTVRRINLEACSNEmVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGSAKDLIGTHFMDgmsELAI 164
Cdd:cd06640    28 TQQVVAIKIIDLEEAEDE-IEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIMEYLGGGSALDLLRAGPFD---EFQI 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 165 AYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLrSNLSMISHGQRQRAVHDFPKYsikvlpWLSPEVLQQN 244
Cdd:cd06640   104 ATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADF-GVAGQLTDTQIKRNTFVGTPF------WMAPEVIQQS 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 245 lqGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPCLLdtstipaeeltmspsrsianpglndslaagsl 324
Cdd:cd06640   177 --AYDSKADIWSLGITAIELAKGEPPNSDMHPMRVLFLIPKNNPPTLV-------------------------------- 222
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958659070 325 rpanGDspshpyhrtFSPHFHNFVEQCLQRNPDARPNASTLLNHSFFKQIKRRASeALPELL 386
Cdd:cd06640   223 ----GD---------FSKPFKEFIDACLNKDPSFRPTAKELLKHKFIVKNAKKTS-YLTELI 270
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
61-373 2.56e-29

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


Pssm-ID: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 115.14  E-value: 2.56e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKG-FEDlmtVNLARYKPTGEYVTVRRINLEacSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVT 139
Cdd:cd06645    13 FELIQRIGSGtYGD---VYKARNVNTGELAAIKVIKLE--PGEDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKLWICM 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 140 SFMAYGSAKDLIgtHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLRSNLSMISHGQRQ 219
Cdd:cd06645    88 EFCGGGSLQDIY--HVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQITATIAKR 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 220 RAVHDFPKysikvlpWLSPEVLQ-QNLQGYDAKSDIYSVGITACELANGHVPFKDMPatqmlleklngtvpclldtstiP 298
Cdd:cd06645   166 KSFIGTPY-------WMAPEVAAvERKGGYNQLCDIWAVGITAIELAELQPPMFDLH----------------------P 216
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958659070 299 AEELTMSPSRSIANPGLNDSLaagslrpangdspshpyhrTFSPHFHNFVEQCLQRNPDARPNASTLLNHSFFKQ 373
Cdd:cd06645   217 MRALFLMTKSNFQPPKLKDKM-------------------KWSNSFHHFVKMALTKNPKKRPTAEKLLQHPFVTQ 272
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
61-372 3.55e-29

Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group I PAKs, also called conventional PAKs, include PAK1, PAK2, and PAK3. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). They interact with the SH3 domain containing proteins Nck, Grb2 and PIX. Binding of group I PAKs to activated GTPases leads to conformational changes that destabilize the AID, allowing autophosphorylation and full activation of the kinase domain. Known group I PAK substrates include MLCK, Bad, Raf, MEK1, LIMK, Merlin, Vimentin, Myc, Stat5a, and Aurora A, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270814 [Multi-domain]  Cd Length: 261  Bit Score: 114.64  E-value: 3.55e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGFEDlmTVNLARYKPTGEYVTVRRINL-EACSNEMVTflqGELHVSKLFSHPNIVPYRATFIADNELWAVT 139
Cdd:cd06647     9 YTRFEKIGQGASG--TVYTAIDVATGQEVAIKQMNLqQQPKKELII---NEILVMRENKNPNIVNYLDSYLVGDELWVVM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 140 SFMAYGSAKDLIGTHFMDgmsELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLrSNLSMISHGQRQ 219
Cdd:cd06647    84 EYLAGGSLTDVVTETCMD---EGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDF-GFCAQITPEQSK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 220 RAVHDFPKYsikvlpWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFkdmpatqmllekLNgtvpclldtstipa 299
Cdd:cd06647   160 RSTMVGTPY------WMAPEVVTR--KAYGPKVDIWSLGIMAIEMVEGEPPY------------LN-------------- 205
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958659070 300 eeltmspsrsiANPglndsLAAGSLRPANGdSPSHPYHRTFSPHFHNFVEQCLQRNPDARPNASTLLNHSFFK 372
Cdd:cd06647   206 -----------ENP-----LRALYLIATNG-TPELQNPEKLSAIFRDFLNRCLEMDVEKRGSAKELLQHPFLK 261
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
85-379 5.36e-29

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


Pssm-ID: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 114.38  E-value: 5.36e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  85 TGEYVTVRRINLEACSNEmVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGSAKDLIGThfmDGMSELAI 164
Cdd:cd06642    28 TKEVVAIKIIDLEEAEDE-IEDIQQEITVLSQCDSPYITRYYGSYLKGTKLWIIMEYLGGGSALDLLKP---GPLEETYI 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 165 AYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLrSNLSMISHGQRQRAVHDFPKYsikvlpWLSPEVLQQN 244
Cdd:cd06642   104 ATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADF-GVAGQLTDTQIKRNTFVGTPF------WMAPEVIKQS 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 245 lqGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLeklngtvpclldtsTIPAEeltmSPsrsianPGLNDSlaagsl 324
Cdd:cd06642   177 --AYDFKADIWSLGITAIELAKGEPPNSDLHPMRVLF--------------LIPKN----SP------PTLEGQ------ 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958659070 325 rpangdspshpyhrtFSPHFHNFVEQCLQRNPDARPNASTLLNHSFFKQIKRRAS 379
Cdd:cd06642   225 ---------------HSKPFKEFVEACLNKDPRFRPTAKELLKHKFITRYTKKTS 264
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
61-368 5.73e-29

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


Pssm-ID: 270905 [Multi-domain]  Cd Length: 252  Bit Score: 113.77  E-value: 5.73e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKG-FEdlmTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVt 139
Cdd:cd14003     2 YELGKTLGEGsFG---KVKLARHKLTGEKVAIKIIDKSKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVIETENKIYLV- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 140 sfMAYGSAKDL---IGTHfmDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLrSNLSMIs 214
Cdd:cd14003    78 --MEYASGGELfdyIVNN--GRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIdfGL-SNEFRG- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 215 hgqrqravHDFPKYSIKVLPWLSPEVLQQnlQGYDA-KSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPClld 293
Cdd:cd14003   152 --------GSLLKTFCGTPAYAAPEVLLG--RKYDGpKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYPI--- 218
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958659070 294 tstipaeeltmspsrsianpglndslaagslrpangdsPSHpyhrtFSPHFHNFVEQCLQRNPDARPNASTLLNH 368
Cdd:cd14003   219 --------------------------------------PSH-----LSPDARDLIRRMLVVDPSKRITIEEILNH 250
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
61-366 4.62e-28

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: 111.52  E-value: 4.62e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfedLM-TVNLARYKPTGEYVTVRRINLEACSN-EMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAV 138
Cdd:cd14014     2 YRLVRLLGRG---GMgEVYRARDTLLGRPVAIKVLRPELAEDeEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 139 TSFMAYGSAKDLIGTHfmDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GL--RSNLSMIS 214
Cdd:cd14014    79 MEYVEGGSLADLLRER--GPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTdfGIarALGDSGLT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 215 HGQRQravhdfpKYSikvLPWLSPEVLQqnLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVpclldt 294
Cdd:cd14014   157 QTGSV-------LGT---PAYMAPEQAR--GGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAP------ 218
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958659070 295 stipaeeltmsPSRSIANPGLNDSLAAgslrpangdspshpyhrtfsphfhnFVEQCLQRNPDARP-NASTLL 366
Cdd:cd14014   219 -----------PPPSPLNPDVPPALDA-------------------------IILRALAKDPEERPqSAAELL 255
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
51-372 6.35e-28

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


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 112.01  E-value: 6.35e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  51 MSSFLPEGGCYELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINleaCSNEMVTFLQGELHVSK-LFSHPNIVP----- 124
Cdd:cd06639    14 LESLADPSDTWDIIETIGKG--TYGKVYKVTNKKDGSLAAVKILD---PISDVDEEIEAEYNILRsLPNHPNVVKfygmf 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 125 YRATFIADNELWAVTSFMAYGSAKDLIGTHFMDG--MSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVY 202
Cdd:cd06639    89 YKADQYVGGQLWLVLELCNGGSVTELVKGLLKCGqrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVK 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 203 LSGLRSNLSMISHGQRQRAvhdfpkySIKVLPWLSPEVL---QQNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQM 279
Cdd:cd06639   169 LVDFGVSAQLTSARLRRNT-------SVGTPFWMAPEVIaceQQYDYSYDARCDVWSLGITAIELADGDPPLFDMHPVKA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 280 LLEklngtvpclldtstIPaeeltMSPSRSIANPGlndslaagslrpangdspshPYHRTFSphfhNFVEQCLQRNPDAR 359
Cdd:cd06639   242 LFK--------------IP-----RNPPPTLLNPE--------------------KWCRGFS----HFISQCLIKDFEKR 278
                         330
                  ....*....|...
gi 1958659070 360 PNASTLLNHSFFK 372
Cdd:cd06639   279 PSVTHLLEHPFIK 291
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
64-387 6.75e-28

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


Pssm-ID: 270803 [Multi-domain]  Cd Length: 313  Bit Score: 112.44  E-value: 6.75e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  64 LSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEA-CSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTSFm 142
Cdd:cd06633    26 LHEIGHG--SFGAVYFATNSHTNEVVAIKKMSYSGkQTNEKWQDIIKEVKFLQQLKHPNTIEYKGCYLKDHTAWLVMEY- 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 143 AYGSAKDLIGTHfMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLRSnLSMIShgqrqrav 222
Cdd:cd06633   103 CLGSASDLLEVH-KKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGS-ASIAS-------- 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 223 hdfPKYSIKVLP-WLSPEVLQQNLQG-YDAKSDIYSVGITACELANGHVPFKDMPAtqmlleklngtvpclldtstipae 300
Cdd:cd06633   173 ---PANSFVGTPyWMAPEVILAMDEGqYDGKVDIWSLGITCIELAERKPPLFNMNA------------------------ 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 301 eltMSPSRSIanpglndslaagslrpANGDSPSHPYHRtFSPHFHNFVEQCLQRNPDARPNASTLLNHSFFKqiKRRASE 380
Cdd:cd06633   226 ---MSALYHI----------------AQNDSPTLQSNE-WTDSFRGFVDYCLQKIPQERPSSAELLRHDFVR--RERPPR 283

                  ....*..
gi 1958659070 381 ALPELLR 387
Cdd:cd06633   284 VLIDLIQ 290
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
47-370 8.46e-28

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIA myosin is highly expressed in retina and in inner ear hair cells. It is localized to the distal ends of actin-bundled structures. Mutations in human myosin IIIA are responsible for progressive nonsyndromic hearing loss. Human myosin IIIA possesses ATPase and kinase activities, and the ability to move actin filaments in a motility assay. It may function as a cellular transporter capable of moving along actin bundles in sensory cells. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. Class III myosins may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. In photoreceptor cells, they may also function as cargo carriers during light-dependent translocation of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 111.26  E-value: 8.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  47 KPEIMSSFLPEGGCYELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVtflQGELHVSKLFS-HPNIVP- 124
Cdd:cd06638     6 KTIIFDSFPDPSDTWEIIETIGKG--TYGKVFKVLNKKNGSKAAVKILDPIHDIDEEI---EAEYNILKALSdHPNVVKf 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 125 ----YRATFIADNELWAVTSFMAYGSAKDLIGTHFMDG--MSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTD 198
Cdd:cd06638    81 ygmyYKKDVKNGDQLWLVLELCNGGSVTDLVKGFLKRGerMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 199 GKVYLSGLRSNLSMISHGQRQRAvhdfpkySIKVLPWLSPEVL---QQNLQGYDAKSDIYSVGITACELANGHVPFKDMP 275
Cdd:cd06638   161 GGVKLVDFGVSAQLTSTRLRRNT-------SVGTPFWMAPEVIaceQQLDSTYDARCDVWSLGITAIELGDGDPPLADLH 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 276 ATQMLLEklngtvpclldtstIPaeeltMSPSRSIANPGLndslaagslrpangdspshpyhrtFSPHFHNFVEQCLQRN 355
Cdd:cd06638   234 PMRALFK--------------IP-----RNPPPTLHQPEL------------------------WSNEFNDFIRKCLTKD 270
                         330
                  ....*....|....*
gi 1958659070 356 PDARPNASTLLNHSF 370
Cdd:cd06638   271 YEKRPTVSDLLQHVF 285
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
61-386 3.30e-27

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


Pssm-ID: 132975 [Multi-domain]  Cd Length: 292  Bit Score: 109.74  E-value: 3.30e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRI---NLEACSNEMVtflqgELHVSKLFSHPNIVPYRATFIADNELWA 137
Cdd:cd06644    14 WEIIGELGDG--AFGKVYKAKNKETGALAAAKVIetkSEEELEDYMV-----EIEILATCNHPYIVKLLGAFYWDGKLWI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 138 VTSFMAyGSAKDLIGTHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLRSNLSMISHGQ 217
Cdd:cd06644    87 MIEFCP-GGAVDAIMLELDRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSAKNVKTLQ 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 218 RQRAVHDFPKysikvlpWLSPEVLQ-QNLQG--YDAKSDIYSVGITACELANGHVPFKDMPATQMLLeKLNGTVPclldt 294
Cdd:cd06644   166 RRDSFIGTPY-------WMAPEVVMcETMKDtpYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLL-KIAKSEP----- 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 295 stipaeeltmspsrsianPGLndslaagslrpangDSPShpyhrTFSPHFHNFVEQCLQRNPDARPNASTLLNHSFFKQI 374
Cdd:cd06644   233 ------------------PTL--------------SQPS-----KWSMEFRDFLKTALDKHPETRPSAAQLLEHPFVSSV 275
                         330
                  ....*....|..
gi 1958659070 375 KrrASEALPELL 386
Cdd:cd06644   276 T--SNRPLRELV 285
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
51-370 3.83e-27

N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinase Kinase 4 and 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K4 is also called Nck Interacting kinase (NIK). It facilitates the activation of the MAPKs, extracellular signal-regulated kinase (ERK) 1, ERK2, and c-Jun N-terminal kinase (JNK), by phosphorylating and activating MEKK1. MAP4K4 plays a role in tumor necrosis factor (TNF) alpha-induced insulin resistance. MAP4K4 silencing in skeletal muscle cells from type II diabetic patients restores insulin-mediated glucose uptake. MAP4K4, through JNK, also plays a broad role in cell motility, which impacts inflammation, homeostasis, as well as the invasion and spread of cancer. MAP4K4 is found to be highly expressed in most tumor cell lines relative to normal tissue. MAP4K6 (also called MINK for Misshapen/NIKs-related kinase) is activated after Ras induction and mediates activation of p38 MAPK. MAP4K6 plays a role in cell cycle arrest, cytoskeleton organization, cell adhesion, and cell motility. The MAP4K4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 109.33  E-value: 3.83e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  51 MSSFLPEGGCYELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVtflQGELHVSKLFSH-PNIVPYRATF 129
Cdd:cd06636     8 LSALRDPAGIFELVEVVGNG--TYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEI---KLEINMLKKYSHhRNIATYYGAF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 130 IA------DNELWAVTSFMAYGSAKDLIGTHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYL 203
Cdd:cd06636    83 IKksppghDDQLWLVMEFCGAGSVTDLVKNTKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 204 S--GLRSNLSMiSHGQRQRAvhdfpkysIKVLPWLSPEVL--QQNLQG-YDAKSDIYSVGITACELANGHVPFKDMPatq 278
Cdd:cd06636   163 VdfGVSAQLDR-TVGRRNTF--------IGTPYWMAPEVIacDENPDAtYDYRSDIWSLGITAIEMAEGAPPLCDMH--- 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 279 mlleklngtvpclldtstiPAEELTMSPSrsiaNPglndslaagslrpangdsPSHPYHRTFSPHFHNFVEQCLQRNPDA 358
Cdd:cd06636   231 -------------------PMRALFLIPR----NP------------------PPKLKSKKWSKKFIDFIEGCLVKNYLS 269
                         330
                  ....*....|..
gi 1958659070 359 RPNASTLLNHSF 370
Cdd:cd06636   270 RPSTEQLLKHPF 281
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
38-387 4.13e-27

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


Pssm-ID: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 110.14  E-value: 4.13e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  38 SSESIASFSKPEIMSSFLPEG--GCYELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEA-CSNEMVTFLQGELHVS 114
Cdd:cd06635     2 STSRAGSLKDPDIAELFFKEDpeKLFSDLREIGHG--SFGAVYFARDVRTSEVVAIKKMSYSGkQSNEKWQDIIKEVKFL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 115 KLFSHPNIVPYRATFIADNELWAVTSFmAYGSAKDLIGTHfMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHIL 194
Cdd:cd06635    80 QRIKHPNSIEYKGCYLREHTAWLVMEY-CLGSASDLLEVH-KKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNIL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 195 ISTDGKVYLSGLRSnLSMIShgqrqravhdfPKYSIKVLP-WLSPEVLQQNLQG-YDAKSDIYSVGITACELANGHVPFK 272
Cdd:cd06635   158 LTEPGQVKLADFGS-ASIAS-----------PANSFVGTPyWMAPEVILAMDEGqYDGKVDVWSLGITCIELAERKPPLF 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 273 DMPATQMLLEKLNGTVPCLLDTStipaeeltmspsrsianpglndslaagslrpangdspshpyhrtFSPHFHNFVEQCL 352
Cdd:cd06635   226 NMNAMSALYHIAQNESPTLQSNE--------------------------------------------WSDYFRNFVDSCL 261
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1958659070 353 QRNPDARPNASTLLNHSFFkqIKRRASEALPELLR 387
Cdd:cd06635   262 QKIPQDRPTSEELLKHMFV--LRERPETVLIDLIQ 294
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
85-371 5.90e-27

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


Pssm-ID: 270795 [Multi-domain]  Cd Length: 260  Bit Score: 108.21  E-value: 5.90e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  85 TGEYVTVRRINLEACSNEM---VTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGSAKDLIGTHfmDGMSE 161
Cdd:cd06625    24 TGRELAVKQVEIDPINTEAskeVKALECEIQLLKNLQHERIVQYYGCLQDEKSLSIFMEYMPGGSVKDEIKAY--GALTE 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 162 -LAIAYILQgVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSNLSMISHGQRQRAVHDFPkYsikvlpWLSP 238
Cdd:cd06625   102 nVTRKYTRQ-ILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGdfGASKRLQTICSSTGMKSVTGTP-Y------WMSP 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 239 EVLqqNLQGYDAKSDIYSVGITACElanghvpfkdmpatqMLLEKlngtvpclldtstiP--AEELTMSPSRSIAnpgln 316
Cdd:cd06625   174 EVI--NGEGYGRKADIWSVGCTVVE---------------MLTTK--------------PpwAEFEPMAAIFKIA----- 217
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958659070 317 dslaagsLRPANGDSPSHpyhrtFSPHFHNFVEQCLQRNPDARPNASTLLNHSFF 371
Cdd:cd06625   218 -------TQPTNPQLPPH-----VSEDARDFLSLIFVRNKKQRPSAEELLSHSFV 260
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
61-371 3.42e-26

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


Pssm-ID: 270855 [Multi-domain]  Cd Length: 258  Bit Score: 106.01  E-value: 3.42e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKG-FEdlmTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVt 139
Cdd:cd08215     2 YEKIRVIGKGsFG---SAYLVRRKSDGKLYVLKEIDLSNMSEKEREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIV- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 140 sfMAYGSAKDL---------IGTHFmdgmSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GL-R 207
Cdd:cd08215    78 --MEYADGGDLaqkikkqkkKGQPF----PEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGdfGIsK 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 208 snlSMISHGQRQRAVHDFPKYsikvlpwLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPF--KDMPAtqmLLEK-L 284
Cdd:cd08215   152 ---VLESTTDLAKTVVGTPYY-------LSPELCEN--KPYNYKSDIWALGCVLYELCTLKHPFeaNNLPA---LVYKiV 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 285 NGTVPclldtsTIPAeeltmspsrsianpglndslaagslrpangdspshpyhrTFSPHFHNFVEQCLQRNPDARPNAST 364
Cdd:cd08215   217 KGQYP------PIPS---------------------------------------QYSSELRDLVNSMLQKDPEKRPSANE 251

                  ....*..
gi 1958659070 365 LLNHSFF 371
Cdd:cd08215   252 ILSSPFI 258
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
61-379 3.71e-26

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine/threonine kinases (STKs), p21-activated kinase (PAK) 3, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. PAK3 belongs to group I. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAK3 is highly expressed in the brain. It is implicated in neuronal plasticity, synapse formation, dendritic spine morphogenesis, cell cycle progression, neuronal migration, and apoptosis. Inactivating mutations in the PAK3 gene cause X-linked non-syndromic mental retardation, the severity of which depends on the site of the mutation.


Pssm-ID: 132987 [Multi-domain]  Cd Length: 297  Bit Score: 107.11  E-value: 3.71e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGFEDlmTVNLARYKPTGEYVTVRRINLEACSNEmvTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTS 140
Cdd:cd06656    21 YTRFEKIGQGASG--TVYTAIDIATGQEVAIKQMNLQQQPKK--ELIINEILVMRENKNPNIVNYLDSYLVGDELWVVME 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 141 FMAYGSAKDLIGTHFMDgmsELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLrSNLSMISHGQRQR 220
Cdd:cd06656    97 YLAGGSLTDVVTETCMD---EGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDF-GFCAQITPEQSKR 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 221 AVHDFPKYsikvlpWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPF-KDMPATQMLLEKLNGTvpclldtstipa 299
Cdd:cd06656   173 STMVGTPY------WMAPEVVTR--KAYGPKVDIWSLGIMAIEMVEGEPPYlNENPLRALYLIATNGT------------ 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 300 EELtMSPSRsianpglndslaagslrpangdspshpyhrtFSPHFHNFVEQCLQRNPDARPNASTLLNHSFFKQIKRRAS 379
Cdd:cd06656   233 PEL-QNPER-------------------------------LSAVFRDFLNRCLEMDVDRRGSAKELLQHPFLKLAKPLSS 280
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
67-389 2.69e-25

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


Pssm-ID: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 104.68  E-value: 2.69e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  67 IGKGFEDLmtVNLARYKPTGEYVTVRRINLEACSNEMVTFlqGELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGS 146
Cdd:cd06659    29 IGEGSTGV--VCIAREKHSGRQVAVKMMDLRKQQRRELLF--NEVVIMRDYQHPNVVEMYKSYLVGEELWVLMEYLQGGA 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 147 AKDLIGThfmDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSNLSmishgqrqravHD 224
Cdd:cd06659   105 LTDIVSQ---TRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSdfGFCAQIS-----------KD 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 225 FPKY-SIKVLP-WLSPEVLQQNLqgYDAKSDIYSVGITACELANGHVP-FKDMPATQMlleklngtvpclldtstipaEE 301
Cdd:cd06659   171 VPKRkSLVGTPyWMAPEVISRCP--YGTEVDIWSLGIMVIEMVDGEPPyFSDSPVQAM--------------------KR 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 302 LTMSPSRSIANpglndslaagslrpangdspshpYHRTfSPHFHNFVEQCLQRNPDARPNASTLLNHSFFKQIkrraseA 381
Cdd:cd06659   229 LRDSPPPKLKN-----------------------SHKA-SPVLRDFLERMLVRDPQERATAQELLDHPFLLQT------G 278

                  ....*...
gi 1958659070 382 LPELLRPV 389
Cdd:cd06659   279 LPECLVPL 286
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
58-372 2.74e-25

Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TNIK is an effector of Rap2, a small GTP-binding protein from the Ras family. TNIK specifically activates the c-Jun N-terminal kinase (JNK) pathway and plays a role in regulating the actin cytoskeleton. The TNIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 104.80  E-value: 2.74e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  58 GGCYELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVtflQGELHVSKLFSH-PNIVPYRATFIA----- 131
Cdd:cd06637     5 AGIFELVELVGNG--TYGQVYKGRHVKTGQLAAIKVMDVTGDEEEEI---KQEINMLKKYSHhRNIATYYGAFIKknppg 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 132 -DNELWAVTSFMAYGSAKDLIGTHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLRSNL 210
Cdd:cd06637    80 mDDQLWLVMEFCGAGSVTDLIKNTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 211 SMISHGQRQRAVHDFPKysikvlpWLSPEVL--QQNLQG-YDAKSDIYSVGITACELANGHVPFKDM-PATQMLLEKLNg 286
Cdd:cd06637   160 QLDRTVGRRNTFIGTPY-------WMAPEVIacDENPDAtYDFKSDLWSLGITAIEMAEGAPPLCDMhPMRALFLIPRN- 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 287 tvpclldtstiPAEELTmspsrsianpglndslaagslrpangdspshpyHRTFSPHFHNFVEQCLQRNPDARPNASTLL 366
Cdd:cd06637   232 -----------PAPRLK---------------------------------SKKWSKKFQSFIESCLVKNHSQRPSTEQLM 267

                  ....*.
gi 1958659070 367 NHSFFK 372
Cdd:cd06637   268 KHPFIR 273
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
61-379 3.14e-25

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK1 is important in the regulation of many cellular processes including cytoskeletal dynamics, cell motility, growth, and proliferation. Although PAK1 has been regarded mainly as a cytosolic protein, recent reports indicate that PAK1 also exists in significant amounts in the nucleus, where it is involved in transcription modulation and in cell cycle regulatory events. PAK1 is also involved in transformation and tumorigenesis. Its overexpression, hyperactivation and increased nuclear accumulation is correlated to breast cancer invasiveness and progression. Nuclear accumulation is also linked to tamoxifen resistance in breast cancer cells. PAK1 belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270820 [Multi-domain]  Cd Length: 296  Bit Score: 104.42  E-value: 3.14e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGFEDlmTVNLARYKPTGEYVTVRRINLEACSNEmvTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTS 140
Cdd:cd06654    22 YTRFEKIGQGASG--TVYTAMDVATGQEVAIRQMNLQQQPKK--ELIINEILVMRENKNPNIVNYLDSYLVGDELWVVME 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 141 FMAYGSAKDLIGTHFMDgmsELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLrSNLSMISHGQRQR 220
Cdd:cd06654    98 YLAGGSLTDVVTETCMD---EGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDF-GFCAQITPEQSKR 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 221 AVHDFPKYsikvlpWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPF-KDMPATQMLLEKLNGTvpclldtstipa 299
Cdd:cd06654   174 STMVGTPY------WMAPEVVTR--KAYGPKVDIWSLGIMAIEMIEGEPPYlNENPLRALYLIATNGT------------ 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 300 eeltmspsRSIANPglndslaagslrpangdspshpyhRTFSPHFHNFVEQCLQRNPDARPNASTLLNHSFFKQIKRRAS 379
Cdd:cd06654   234 --------PELQNP------------------------EKLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLKIAKPLSS 281
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
48-373 3.46e-25

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human TAO2 is also known as prostate-derived Ste20-like kinase (PSK) and was identified in a screen for overexpressed RNAs in prostate cancer. TAO2 possesses mitogen-activated protein kinase (MAPK) kinase kinase activity and activates both p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating their respective MAP/ERK kinases, MEK3/MEK6 and MKK4/MKK7. It contains a long C-terminal extension with autoinhibitory segments, and is activated by the release of this inhibition and the phosphorylation of its activation loop serine. TAO2 functions as a regulator of actin cytoskeletal and microtubule organization. In addition, it regulates the transforming growth factor-activated kinase 1 (TAK1), which is a MAPKKK that plays an essential role in the signaling pathways of tumor necrosis factor, interleukin 1, and Toll-like receptor. The TAO2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 104.72  E-value: 3.46e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  48 PEIMSSFL---PEGgCYELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEA-CSNEMVTFLQGELHVSKLFSHPNIV 123
Cdd:cd06634     2 PEVAELFFkddPEK-LFSDLREIGHG--SFGAVYFARDVRNNEVVAIKKMSYSGkQSNEKWQDIIKEVKFLQKLRHPNTI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 124 PYRATFIADNELWAVTSFmAYGSAKDLIGTHfMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYL 203
Cdd:cd06634    79 EYRGCYLREHTAWLVMEY-CLGSASDLLEVH-KKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 204 SGLRSnLSMIShgqrqravhdfPKYSIKVLP-WLSPEVLQQNLQG-YDAKSDIYSVGITACELANGHVPFKDMPAtqmll 281
Cdd:cd06634   157 GDFGS-ASIMA-----------PANSFVGTPyWMAPEVILAMDEGqYDGKVDVWSLGITCIELAERKPPLFNMNA----- 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 282 eklngtvpclldtstipaeeltMSPSRSIANpglNDSLAAGSlrpangdspshpyhRTFSPHFHNFVEQCLQRNPDARPN 361
Cdd:cd06634   220 ----------------------MSALYHIAQ---NESPALQS--------------GHWSEYFRNFVDSCLQKIPQDRPT 260
                         330
                  ....*....|..
gi 1958659070 362 ASTLLNHSFFKQ 373
Cdd:cd06634   261 SDVLLKHRFLLR 272
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
85-370 5.04e-25

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


Pssm-ID: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 103.29  E-value: 5.04e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  85 TGEYVTVRRINLEACSNEMVTF----LQGELHVSKLFSHPNIVPYRATFIADNelwAVTSFMAY---GSAKDLIGtHFMD 157
Cdd:cd06631    24 TGQLIAVKQVELDTSDKEKAEKeyekLQEEVDLLKTLKHVNIVGYLGTCLEDN---VVSIFMEFvpgGSIASILA-RFGA 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 158 GMSELAIAY---ILQGVlkalDYIHHMGYVHRSVKASHILISTDGKVYL------SGLRSNLSMISHGQRQRAVHDFPkY 228
Cdd:cd06631   100 LEEPVFCRYtkqILEGV----AYLHNNNVIHRDIKGNNIMLMPNGVIKLidfgcaKRLCINLSSGSQSQLLKSMRGTP-Y 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 229 sikvlpWLSPEVLqqNLQGYDAKSDIYSVGITACELANGHVPFKDMPatqmlleklngtvpclldtstipaeeltmsPSR 308
Cdd:cd06631   175 ------WMAPEVI--NETGHGRKSDIWSIGCTVFEMATGKPPWADMN------------------------------PMA 216
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958659070 309 SIanpglndsLAAGSLRpanGDSPSHPYHrtFSPHFHNFVEQCLQRNPDARPNASTLLNHSF 370
Cdd:cd06631   217 AI--------FAIGSGR---KPVPRLPDK--FSPEARDFVHACLTRDQDERPSAEQLLKHPF 265
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
119-370 2.34e-24

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


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 101.64  E-value: 2.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 119 HPNIVPYRATFIADNELWAVTSFMAyGSAKDLIGTHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTD 198
Cdd:cd06643    61 HPNIVKLLDAFYYENNLWILIEFCA-GGAVDAVMLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLD 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 199 GKVYLSGLRSNLSMISHGQRQRAVHDFPKysikvlpWLSPEVLQ---QNLQGYDAKSDIYSVGITACELANGHVPFKDMP 275
Cdd:cd06643   140 GDIKLADFGVSAKNTRTLQRRDSFIGTPY-------WMAPEVVMcetSKDRPYDYKADVWSLGVTLIEMAQIEPPHHELN 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 276 ATQMLLEKLNGTVPCLldtstipaeeltMSPSRsianpglndslaagslrpangdspshpyhrtFSPHFHNFVEQCLQRN 355
Cdd:cd06643   213 PMRVLLKIAKSEPPTL------------AQPSR-------------------------------WSPEFKDFLRKCLEKN 249
                         250
                  ....*....|....*
gi 1958659070 356 PDARPNASTLLNHSF 370
Cdd:cd06643   250 VDARWTTSQLLQHPF 264
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
61-379 8.04e-24

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK2 plays a role in pro-apoptotic signaling. It is cleaved and activated by caspases leading to morphological changes during apoptosis. PAK2 is also activated in response to a variety of stresses including DNA damage, hyperosmolarity, serum starvation, and contact inhibition, and may play a role in coordinating the stress response. PAK2 also contributes to cancer cell invasion through a mechanism distinct from that of PAK1. It belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132986 [Multi-domain]  Cd Length: 296  Bit Score: 100.57  E-value: 8.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGFEDlmTVNLARYKPTGEYVTVRRINLEACSNEmvTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTS 140
Cdd:cd06655    21 YTRYEKIGQGASG--TVFTAIDVATGQEVAIKQINLQKQPKK--ELIINEILVMKELKNPNIVNFLDSFLVGDELFVVME 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 141 FMAYGSAKDLIGTHFMDgmsELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLrSNLSMISHGQRQR 220
Cdd:cd06655    97 YLAGGSLTDVVTETCMD---EAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDF-GFCAQITPEQSKR 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 221 AVHDFPKYsikvlpWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPF-KDMPATQMLLEKLNGTvpclldtstipa 299
Cdd:cd06655   173 STMVGTPY------WMAPEVVTR--KAYGPKVDIWSLGIMAIEMVEGEPPYlNENPLRALYLIATNGT------------ 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 300 eeltmspsRSIANPglndslaagslrpangdspshpyhRTFSPHFHNFVEQCLQRNPDARPNASTLLNHSFFKQIKRRAS 379
Cdd:cd06655   233 --------PELQNP------------------------EKLSPIFRDFLNRCLEMDVEKRGSAKELLQHPFLKLAKPLSS 280
Pkinase pfam00069
Protein kinase domain;
61-371 9.98e-24

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 98.47  E-value: 9.98e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKG-FEdlmTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVT 139
Cdd:pfam00069   1 YEVLRKLGSGsFG---TVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 140 SFMAYGSAKDLIGTHFmdGMSE-LAIAYILQgVLKALDyihhmgyvhRSVKASHILIStdgkvylsglrsnlsmishgqr 218
Cdd:pfam00069  78 EYVEGGSLFDLLSEKG--AFSErEAKFIMKQ-ILEGLE---------SGSSLTTFVGT---------------------- 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 219 qravhdfpkysikvLPWLSPEVLQQNlqGYDAKSDIYSVGITACELANGHVPFKDmpatqmlleklngtvpcllDTSTIP 298
Cdd:pfam00069 124 --------------PWYMAPEVLGGN--PYGPKVDVWSLGCILYELLTGKPPFPG-------------------INGNEI 168
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958659070 299 AEELTMSPSRSIANPglndslaagslrpangdspshpyhRTFSPHFHNFVEQCLQRNPDARPNASTLLNHSFF 371
Cdd:pfam00069 169 YELIIDQPYAFPELP------------------------SNLSEEAKDLLKKLLKKDPSKRLTATQALQHPWF 217
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
61-370 1.34e-23

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: 99.09  E-value: 1.34e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKG-FEdlmTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVT 139
Cdd:cd05117     2 YELGKVLGRGsFG---VVRLAVHKKTGEEYAVKIIDKKKLKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 140 SFMAYGSAKDLIGTHFMdgMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILIST---DGKVYLS--GLRsnlSMIS 214
Cdd:cd05117    79 ELCTGGELFDRIVKKGS--FSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASkdpDSPIKIIdfGLA---KIFE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 215 HGQRQRAVHDFPKYsikvlpwLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFkDMPATQMLLEK-LNGtvpclld 293
Cdd:cd05117   154 EGEKLKTVCGTPYY-------VAPEVLKG--KGYGKKCDIWSLGVILYILLCGYPPF-YGETEQELFEKiLKG------- 216
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958659070 294 tstipaeELTMSPsrsianpglndslaagslrpangdspshPYHRTFSPHFHNFVEQCLQRNPDARPNASTLLNHSF 370
Cdd:cd05117   217 -------KYSFDS----------------------------PEWKNVSEEAKDLIKRLLVVDPKKRLTAAEALNHPW 258
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
77-373 2.22e-23

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: 99.04  E-value: 2.22e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  77 VNLARYKPTGEYVTVRRINLEACSNEMVTFLQgELHVSKLFSH-PNIVPYRATFIADNELWAVTSFMA------YGSAKD 149
Cdd:cd06617    17 VDKMRHVPTGTIMAVKRIRATVNSQEQKRLLM-DLDISMRSVDcPYTVTFYGALFREGDVWICMEVMDtsldkfYKKVYD 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 150 lIGTHfmdgMSELAIAYILQGVLKALDYIH-HMGYVHRSVKASHILISTDGKVYLS--GLRSNL--SM---ISHGQRqra 221
Cdd:cd06617    96 -KGLT----IPEDILGKIAVSIVKALEYLHsKLSVIHRDVKPSNVLINRNGQVKLCdfGISGYLvdSVaktIDAGCK--- 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 222 vhdfpkysikvlPWLSPEVL--QQNLQGYDAKSDIYSVGITACELANGHVPFkdmpatqmlleklngtvpcllDTSTIPA 299
Cdd:cd06617   168 ------------PYMAPERInpELNQKGYDVKSDVWSLGITMIELATGRFPY---------------------DSWKTPF 214
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958659070 300 EELTmspsrsianpglndslaagslRPANGDSPSHPyHRTFSPHFHNFVEQCLQRNPDARPNASTLLNHSFFKQ 373
Cdd:cd06617   215 QQLK---------------------QVVEEPSPQLP-AEKFSPEFQDFVNKCLKKNYKERPNYPELLQHPFFEL 266
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
76-374 2.23e-23

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: 97.99  E-value: 2.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  76 TVNLARYKptGEYVTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGSAKDLIgtHF 155
Cdd:cd13999     8 EVYKGKWR--GTDVAIKKLKVEDDNDELLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSLYDLL--HK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 156 MDG-MSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSNLSmiSHGQRQRAVhdfpkysIKV 232
Cdd:cd13999    84 KKIpLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIAdfGLSRIKN--STTEKMTGV-------VGT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 233 LPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKlngtvpclldtstipaeeltmspsrsian 312
Cdd:cd13999   155 PRWMAPEVLRG--EPYTEKADVYSFGIVLWELLTGEVPFKELSPIQIAAAV----------------------------- 203
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958659070 313 pglndslAAGSLRPangdspshPYHRTFSPHFHNFVEQCLQRNPDARPNastllnhsfFKQI 374
Cdd:cd13999   204 -------VQKGLRP--------PIPPDCPPELSKLIKRCWNEDPEKRPS---------FSEI 241
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
62-372 1.45e-22

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


Pssm-ID: 270791 [Multi-domain]  Cd Length: 295  Bit Score: 97.06  E-value: 1.45e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  62 ELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTSF 141
Cdd:cd06618    18 ENLGEIGSG--TCGQVYKMRHKKTGHVMAVKQMRRSGNKEENKRILMDLDVVLKSHDCPYIVKCYGYFITDSDVFICMEL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 142 MAYGSAKDLIGTHfmDGMSELAIAYILQGVLKALDYI--HHmGYVHRSVKASHILISTDGKVYLSGLRSNLSMISHGQRQ 219
Cdd:cd06618    96 MSTCLDKLLKRIQ--GPIPEDILGKMTVSIVKALHYLkeKH-GVIHRDVKPSNILLDESGNVKLCDFGISGRLVDSKAKT 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 220 RavhdfpkySIKVLPWLSPEVLQ-QNLQGYDAKSDIYSVGITACELANGHVPFKDmpatqmlleklngtvpCLLDTstip 298
Cdd:cd06618   173 R--------SAGCAAYMAPERIDpPDNPKYDIRADVWSLGISLVELATGQFPYRN----------------CKTEF---- 224
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958659070 299 aEELTmspsrsianpglndslaagslRPANGDSPSHPYHRTFSPHFHNFVEQCLQRNPDARPNASTLLNHSFFK 372
Cdd:cd06618   225 -EVLT---------------------KILNEEPPSLPPNEGFSPDFCSFVDLCLTKDHRYRPKYRELLQHPFIR 276
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
67-377 1.55e-22

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 4; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK4 is a dual-specificity PK that phosphorylates and activates the downstream targets, c-Jun N-terminal kinase (JNK) and p38 MAPK, on specific threonine and tyrosine residues. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. Their activation is associated with the induction of cell death. Mice deficient in MKK4 die during embryogenesis and display anemia, severe liver hemorrhage, and abnormal hepatogenesis. MKK4 may also play roles in the immune system and in cardiac hypertrophy. It plays a major role in cancer as a tumor and metastasis suppressor. Under certain conditions, MKK4 is pro-oncogenic. The MKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 96.67  E-value: 1.55e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  67 IGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQgELHVSKLFSH-PNIVP-YRATFiADNELWAVTSFM-- 142
Cdd:cd06616    14 IGRG--AFGTVNKMLHKPSGTIMAVKRIRSTVDEKEQKRLLM-DLDVVMRSSDcPYIVKfYGALF-REGDCWICMELMdi 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 143 --------AYGSAKDLIgthfmdgmSELAIAYILQGVLKALDYI---HHMgyVHRSVKASHILISTDGKVYLSGLRsnls 211
Cdd:cd06616    90 sldkfykyVYEVLDSVI--------PEEILGKIAVATVKALNYLkeeLKI--IHRDVKPSNILLDRNGNIKLCDFG---- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 212 mIShGQRQRAV---HDfpkysIKVLPWLSPEVLQQN--LQGYDAKSDIYSVGITACELANGHVPFkdmPATQMLLEKLNG 286
Cdd:cd06616   156 -IS-GQLVDSIaktRD-----AGCRPYMAPERIDPSasRDGYDVRSDVWSLGITLYEVATGKFPY---PKWNSVFDQLTQ 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 287 TVpclldtstipaeeltmspsrsianpglndslaagslrpaNGDSP--SHPYHRTFSPHFHNFVEQCLQRNPDARPNAST 364
Cdd:cd06616   226 VV---------------------------------------KGDPPilSNSEEREFSPSFVNFVNLCLIKDESKRPKYKE 266
                         330
                  ....*....|...
gi 1958659070 365 LLNHSFFKQIKRR 377
Cdd:cd06616   267 LLKHPFIKMYEER 279
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
61-371 2.48e-22

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


Pssm-ID: 270824 [Multi-domain]  Cd Length: 283  Bit Score: 96.06  E-value: 2.48e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKG-FEdlmTVNLARYKPTGEYVTVRRI-----NLEACSN--EmVTFLQgelhvsKLFSHPNIVPYRATFIAD 132
Cdd:cd07830     1 YKVIKQLGDGtFG---SVYLARNKETGELVAIKKMkkkfySWEECMNlrE-VKSLR------KLNEHPNIVKLKEVFREN 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 133 NELWAVTSFMA---YGSAKDLIGTHFmdgmSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLr 207
Cdd:cd07830    71 DELYFVFEYMEgnlYQLMKDRKGKPF----SESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIAdfGL- 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 208 snlsmishgqrQRAVHDFPKYSIKV-LPWL-SPEVLQQNlQGYDAKSDIYSVGITACELAN------------------- 266
Cdd:cd07830   146 -----------AREIRSRPPYTDYVsTRWYrAPEILLRS-TSYSSPVDIWALGCIMAELYTlrplfpgsseidqlykics 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 267 --GHVPFKDMPATQMLLEKLNGTVPclldtSTIPaeeltMSPSRSIANPglndslaagslrpangdspshpyhrtfSPHF 344
Cdd:cd07830   214 vlGTPTKQDWPEGYKLASKLGFRFP-----QFAP-----TSLHQLIPNA---------------------------SPEA 256
                         330       340
                  ....*....|....*....|....*..
gi 1958659070 345 HNFVEQCLQRNPDARPNASTLLNHSFF 371
Cdd:cd07830   257 IDLIKDMLRWDPKKRPTASQALQHPYF 283
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
110-377 1.57e-21

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


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 94.03  E-value: 1.57e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 110 ELHVSKLFSHPNIVPYRATFIADNE--LWAVTSFMAYGSAKDLIGTHFMDGM--SELAIAYILQGVLKALDYIHHMGYVH 185
Cdd:cd06621    49 ELEINKSCASPYIVKYYGAFLDEQDssIGIAMEYCEGGSLDSIYKKVKKKGGriGEKVLGKIAESVLKGLSYLHSRKIIH 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 186 RSVKASHILISTDGKVYLSGLrsnlsmishGQRQRAVHDFPKYSIKVLPWLSPEVLQQnlQGYDAKSDIYSVGITACELA 265
Cdd:cd06621   129 RDIKPSNILLTRKGQVKLCDF---------GVSGELVNSLAGTFTGTSYYMAPERIQG--GPYSITSDVWSLGLTLLEVA 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 266 NGHVPFkdmPAtqmlleklNGTVPclldtsTIPAEELTMSPSRSiaNPGLNDSLAAGslrpangdspshpyhRTFSPHFH 345
Cdd:cd06621   198 QNRFPF---PP--------EGEPP------LGPIELLSYIVNMP--NPELKDEPENG---------------IKWSESFK 243
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1958659070 346 NFVEQCLQRNPDARPNASTLLNHSFFKQIKRR 377
Cdd:cd06621   244 DFIEKCLEKDGTRRPGPWQMLAHPWIKAQEKK 275
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
67-372 1.83e-21

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


Pssm-ID: 132989 [Multi-domain]  Cd Length: 292  Bit Score: 93.95  E-value: 1.83e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  67 IGKGFEDLmtVNLARYKPTGEYVTVRRINLEACSNEMVTFlqGELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGS 146
Cdd:cd06658    30 IGEGSTGI--VCIATEKHTGKQVAVKKMDLRKQQRRELLF--NEVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLEGGA 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 147 AKDLIgTHfmDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLRSNLSMISHGQRQRAVHDFP 226
Cdd:cd06658   106 LTDIV-TH--TRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQVSKEVPKRKSLVGTP 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 227 KysikvlpWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQMlLEKLNGTVPclldtstipaeeltmsp 306
Cdd:cd06658   183 Y-------WMAPEVISR--LPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQA-MRRIRDNLP----------------- 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958659070 307 srsianPGLNDSLAAGSLrpangdspshpyhrtfsphFHNFVEQCLQRNPDARPNASTLLNHSFFK 372
Cdd:cd06658   236 ------PRVKDSHKVSSV-------------------LRGFLDLMLVREPSQRATAQELLQHPFLK 276
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
67-370 1.91e-21

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


Pssm-ID: 270799 [Multi-domain]  Cd Length: 270  Bit Score: 93.22  E-value: 1.91e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  67 IGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNE--------MVTFLQGELHVSKLFSHPNIVPYRAtFIADNELWAV 138
Cdd:cd06629     9 IGKG--TYGRVYLAMNATTGEMLAVKQVELPKTSSDradsrqktVVDALKSEIDTLKDLDHPNIVQYLG-FEETEDYFSI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 139 tsFMAY---GSAKDLIGTHfmDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLrsnlsMISH 215
Cdd:cd06629    86 --FLEYvpgGSIGSCLRKY--GKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDF-----GISK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 216 gQRQRAVHDFPKYSIK-VLPWLSPEVLQQNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEklngtvpclldt 294
Cdd:cd06629   157 -KSDDIYGNNGATSMQgSVFWMAPEVIHSQGQGYSAKVDIWSLGCVVLEMLAGRRPWSDDEAIAAMFK------------ 223
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958659070 295 stipaeeltmspsrsianpglndslaAGSLRPAngdsPSHPYHRTFSPHFHNFVEQCLQRNPDARPNASTLLNHSF 370
Cdd:cd06629   224 --------------------------LGNKRSA----PPVPEDVNLSPEALDFLNACFAIDPRDRPTAAELLSHPF 269
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
65-370 9.46e-21

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


Pssm-ID: 270798 [Multi-domain]  Cd Length: 267  Bit Score: 91.06  E-value: 9.46e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  65 SVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNE-------MVTFLQGELHVSKLFSHPNIVPYRATFIADNELwa 137
Cdd:cd06628     6 ALIGSG--SFGSVYLGMNASSGELMAVKQVELPSVSAEnkdrkksMLDALQREIALLRELQHENIVQYLGSSSDANHL-- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 138 vTSFMAY---GSAKDLIGTHfmDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSG------LRS 208
Cdd:cd06628    82 -NIFLEYvpgGSVATLLNNY--GAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDfgiskkLEA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 209 N-LSMISHGQRqravhdfPKYSIKVLpWLSPEVLQQNLqgYDAKSDIYSVGITACELANGHVPFKDMpaTQMlleklngt 287
Cdd:cd06628   159 NsLSTKNNGAR-------PSLQGSVF-WMAPEVVKQTS--YTRKADIWSLGCLVVEMLTGTHPFPDC--TQM-------- 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 288 vpclldtstipaeeltmspsRSIanpglndslaagsLRPANGDSPSHPYHRTFSPhfHNFVEQCLQRNPDARPNASTLLN 367
Cdd:cd06628   219 --------------------QAI-------------FKIGENASPTIPSNISSEA--RDFLEKTFEIDHNKRPTADELLK 263

                  ...
gi 1958659070 368 HSF 370
Cdd:cd06628   264 HPF 266
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
62-367 1.12e-20

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: 90.69  E-value: 1.12e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070   62 ELLSVIGKGFedLMTVNLARYKPTGEY----VTVRRINLEACSNEMVTFLQgELHVSKLFSHPNIVPYRATFIADNELWA 137
Cdd:smart00221   2 TLGKKLGEGA--FGEVYKGTLKGKGDGkeveVAVKTLKEDASEQQIEEFLR-EARIMRKLDHPNIVKLLGVCTEEEPLMI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  138 VTSFMAYGSAKDLIGTH--FMDGMSELaIAYILQgVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLrsnlsmi 213
Cdd:smart00221  79 VMEYMPGGDLLDYLRKNrpKELSLSDL-LSFALQ-IARGMEYLESKNFIHRDLAARNCLVGENLVVKISdfGL------- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  214 shgqrQRAVHDFPKYSIKV--LP--WLSPEVLQQNLqgYDAKSDIYSVGITACELA-NGHVPFKDMPATQmLLEKlngtv 288
Cdd:smart00221 150 -----SRDLYDDDYYKVKGgkLPirWMAPESLKEGK--FTSKSDVWSFGVLLWEIFtLGEEPYPGMSNAE-VLEY----- 216
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958659070  289 pclldtstipaeeltmspsrsianpglndsLAAGSLRPangdSPSHPyhrtfSPHFHNFVEQCLQRNPDARPNASTLLN 367
Cdd:smart00221 217 ------------------------------LKKGYRLP----KPPNC-----PPELYKLMLQCWAEDPEDRPTFSELVE 256
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
61-372 1.36e-20

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 and MEK2 are MAPK kinases (MAPKKs or MKKs), and are dual-specificity PKs that phosphorylate and activate the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1/2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. This cascade has also been implicated in synaptic plasticity, migration, morphological determination, and stress response immunological reactions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1/2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 91.73  E-value: 1.36e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLE---ACSNEMVTflqgELHVSKLFSHPNIVPYRATFIADNElwa 137
Cdd:cd06615     3 FEKLGELGAG--NGGVVTKVLHRPSGLIMARKLIHLEikpAIRNQIIR----ELKVLHECNSPYIVGFYGAFYSDGE--- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 138 VTSFMAYgsakdligthfMDGMS------------ELAIAYILQGVLKALDYI---HHMgyVHRSVKASHILISTDGKVY 202
Cdd:cd06615    74 ISICMEH-----------MDGGSldqvlkkagripENILGKISIAVLRGLTYLrekHKI--MHRDVKPSNILVNSRGEIK 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 203 LS--GLRSNL--SMISH--GQRQravhdfpkysikvlpWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKdmPA 276
Cdd:cd06615   141 LCdfGVSGQLidSMANSfvGTRS---------------YMSPERLQG--THYTVQSDIWSLGLSLVEMAIGRYPIP--PP 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 277 TQMLLEKLNGTvpclldtstiPAEELTMSPSRSIANPGLNDSLAAGSLRP-----ANGDSPSHPyHRTFSPHFHNFVEQC 351
Cdd:cd06615   202 DAKELEAMFGR----------PVSEGEAKESHRPVSGHPPDSPRPMAIFElldyiVNEPPPKLP-SGAFSDEFQDFVDKC 270
                         330       340
                  ....*....|....*....|.
gi 1958659070 352 LQRNPDARPNASTLLNHSFFK 372
Cdd:cd06615   271 LKKNPKERADLKELTKHPFIK 291
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
61-368 1.56e-20

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


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 90.61  E-value: 1.56e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRIN-----LEACSNEMVtflQGELHVSKLFSHPNIVPYRATFIADNEL 135
Cdd:cd14098     2 YQIIDRLGSG--TFAEVKKAVEVETGKMRAIKQIVkrkvaGNDKNLQLF---QREINILKSLEHPGIVRLIDWYEDDQHI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 136 WAVTSFMAYGSAKDLIGTHfmDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLRSNLSMISH 215
Cdd:cd14098    77 YLVMEYVEGGDLMDFIMAW--GAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDPVIVKISDFGLAKVIH 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 216 GQrqravhDFPKYSIKVLPWLSPEVL---QQNLQ-GYDAKSDIYSVGITACELANGHVPFKDmpATQMLLEKLngtvpcl 291
Cdd:cd14098   155 TG------TFLVTFCGTMAYLAPEILmskEQNLQgGYSNLVDMWSVGCLVYVMLTGALPFDG--SSQLPVEKR------- 219
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958659070 292 ldtstIPAEELTMSPsrsianpgLNDSlaagslrpangdspshpyhrTFSPHFHNFVEQCLQRNPDARPNASTLLNH 368
Cdd:cd14098   220 -----IRKGRYTQPP--------LVDF--------------------NISEEAIDFILRLLDVDPEKRMTAAQALDH 263
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
67-373 3.67e-20

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK4 regulates cell morphology and cytoskeletal organization. It is essential for embryonic viability and proper neural development. Mice lacking PAK4 die due to defects in the fetal heart. In addition, their spinal cord motor neurons showed failure to differentiate and migrate. PAK4 also plays a role in cell survival and tumorigenesis. It is overexpressed in many primary tumors including colon, esophageal, and mammary tumors. PAK4 has also been implicated in viral and bacterial infection pathways. PAK4 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 90.08  E-value: 3.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  67 IGKGFEDLmtVNLARYKPTGEYVTVRRINLEACSNEMVTFlqGELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGS 146
Cdd:cd06657    28 IGEGSTGI--VCIATVKSSGKLVAVKKMDLRKQQRRELLF--NEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGA 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 147 AKDLIgTHfmDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLRSNLSMISHGQRQRAVHDFP 226
Cdd:cd06657   104 LTDIV-TH--TRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTP 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 227 KysikvlpWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPatqmlleklngtvpclldtstiPAEELTMsp 306
Cdd:cd06657   181 Y-------WMAPELISR--LPYGPEVDIWSLGIMVIEMVDGEPPYFNEP----------------------PLKAMKM-- 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958659070 307 srsianpgLNDSLaagslrpangdSPSHPYHRTFSPHFHNFVEQCLQRNPDARPNASTLLNHSFFKQ 373
Cdd:cd06657   228 --------IRDNL-----------PPKLKNLHKVSPSLKGFLDRLLVRDPAQRATAAELLKHPFLAK 275
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
61-367 4.76e-20

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


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 89.25  E-value: 4.76e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINL---------EACSNEmVTFLQGelhvsklFSHPNIVPYRATFIA 131
Cdd:cd08224     2 YEIEKKIGKG--QFSVVYRARCLLDGRLVALKKVQIfemmdakarQDCLKE-IDLLQQ-------LNHPNIIKYLASFIE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 132 DNELWAVTSFMAYGSAKDLIgTHFMD---GMSELAI-AYILQgVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGL- 206
Cdd:cd08224    72 NNELNIVLELADAGDLSRLI-KHFKKqkrLIPERTIwKYFVQ-LCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLg 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 207 --R--SNLSMISH---GQrqravhdfPKYsikvlpwLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDmpatqm 279
Cdd:cd08224   150 lgRffSSKTTAAHslvGT--------PYY-------MSPERIRE--QGYDFKSDIWSLGCLLYEMAALQSPFYG------ 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 280 llEKLNGTVPClldtstipaeeltmspsRSIanpglndslaagslrpANGDSPSHPYHRtFSPHFHNFVEQCLQRNPDAR 359
Cdd:cd08224   207 --EKMNLYSLC-----------------KKI----------------EKCEYPPLPADL-YSQELRDLVAACIQPDPEKR 250

                  ....*...
gi 1958659070 360 PNASTLLN 367
Cdd:cd08224   251 PDISYVLD 258
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
66-368 5.16e-20

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: 89.14  E-value: 5.16e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  66 VIGKG-FEDlmtVNLARYKPTGEY---VTVRRINLEACSNEMVTFLQgELHVSKLFSHPNIVPYRATFIADNELWAVTSF 141
Cdd:cd00192     2 KLGEGaFGE---VYKGKLKGGDGKtvdVAVKTLKEDASESERKDFLK-EARVMKKLGHPNVVRLLGVCTEEEPLYLVMEY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 142 MAYGSAKDLIGTHFMDGMSELA--------IAYILQgVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSNLS 211
Cdd:cd00192    78 MEGGDLLDFLRKSRPVFPSPEPstlslkdlLSFAIQ-IAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISdfGLSRDIY 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 212 MISHGQRQRAvhdfpkysiKVLP--WLSPEVLQQNLqgYDAKSDIYSVGITACEL-ANGHVPFKDMPATQMLleklngtv 288
Cdd:cd00192   157 DDDYYRKKTG---------GKLPirWMAPESLKDGI--FTSKSDVWSFGVLLWEIfTLGATPYPGLSNEEVL-------- 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 289 pclldtstipaeeltmspsrsianpglnDSLAAGSlRPANgdsPSHpyhrtFSPHFHNFVEQCLQRNPDARPNASTLLNH 368
Cdd:cd00192   218 ----------------------------EYLRKGY-RLPK---PEN-----CPDELYELMLSCWQLDPEDRPTFSELVER 260
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
62-280 5.95e-20

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: 88.71  E-value: 5.95e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  62 ELLSVIGKG-FEdlmTVNLARYKPTGEY----VTVRRINLEACSNEMVTFLQgELHVSKLFSHPNIVPYRATFIADNELW 136
Cdd:pfam07714   2 TLGEKLGEGaFG---EVYKGTLKGEGENtkikVAVKTLKEGADEEEREDFLE-EASIMKKLDHPNIVKLLGVCTQGEPLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 137 AVTSFMAYGSAKDLIGTHFMD-GMSELaIAYILQgVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLrsnlsmi 213
Cdd:pfam07714  78 IVTEYMPGGDLLDFLRKHKRKlTLKDL-LSMALQ-IAKGMEYLESKNFVHRDLAARNCLVSENLVVKISdfGL------- 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958659070 214 shgqrQRAVHDFPKY---SIKVLP--WLSPEVLQQNLqgYDAKSDIYSVGITACELA-NGHVPFKDMPATQML 280
Cdd:pfam07714 149 -----SRDIYDDDYYrkrGGGKLPikWMAPESLKDGK--FTSKSDVWSFGVLLWEIFtLGEQPYPGMSNEEVL 214
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
62-366 9.57e-20

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 87.97  E-value: 9.57e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070   62 ELLSVIGKGFedLMTVNLARYKP----TGEYVTVRRINLEACSNEMVTFLQgELHVSKLFSHPNIVPYRATFIADNELWA 137
Cdd:smart00219   2 TLGKKLGEGA--FGEVYKGKLKGkggkKKVEVAVKTLKEDASEQQIEEFLR-EARIMRKLDHPNVVKLLGVCTEEEPLYI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  138 VTSFMAYGSAKDLIGTHFMD-GMSELaIAYILQgVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLrsnlsmis 214
Cdd:smart00219  79 VMEYMEGGDLLSYLRKNRPKlSLSDL-LSFALQ-IARGMEYLESKNFIHRDLAARNCLVGENLVVKISdfGL-------- 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  215 hgqrQRAVHDFPKYSIKV--LP--WLSPEVLQQNLqgYDAKSDIYSVGITACELA-NGHVPFKDMPATQMlLEKlngtvp 289
Cdd:smart00219 149 ----SRDLYDDDYYRKRGgkLPirWMAPESLKEGK--FTSKSDVWSFGVLLWEIFtLGEQPYPGMSNEEV-LEY------ 215
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958659070  290 clldtstipaeeltmspsrsianpglndsLAAGSLRPangdSPSHPyhrtfSPHFHNFVEQCLQRNPDARPNASTLL 366
Cdd:smart00219 216 -----------------------------LKNGYRLP----QPPNC-----PPELYDLMLQCWAEDPEDRPTFSELV 254
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
61-369 2.65e-19

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


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 86.68  E-value: 2.65e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTS 140
Cdd:cd08530     2 FKVLKKLGKG--SYGSVYKVKRLSDNQVYALKEVNLGSLSQKEREDSVNEIRLLASVNHPNIIRYKEAFLDGNRLCIVME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 141 FMAYGSAKDLIGTHFMDG--MSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLrsNLSMISHGQR 218
Cdd:cd08530    80 YAPFGDLSKLISKRKKKRrlFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDL--GISKVLKKNL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 219 QRAVHDFPKYsikvlpwLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPF--KDMpatqmlleklngtvpclldtst 296
Cdd:cd08530   158 AKTQIGTPLY-------AAPEVWKG--RPYDYKSDIWSLGCLLYEMATFRPPFeaRTM---------------------- 206
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958659070 297 ipaEELtmspsrsianpglndslaagSLRPANGDSPshPYHRTFSPHFHNFVEQCLQRNPDARPNASTLLNHS 369
Cdd:cd08530   207 ---QEL--------------------RYKVCRGKFP--PIPPVYSQDLQQIIRSLLQVNPKKRPSCDKLLQSP 254
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
76-377 3.05e-19

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


Pssm-ID: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 87.11  E-value: 3.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  76 TVNLARYKPTGEYVTVRRINLEAcSNEMVTFLQGELHVSKLFSHPNIVPYRATFIAD-NELWAVTSFMAYGSakdligth 154
Cdd:cd06620    20 SVSKVLHIPTGTIMAKKVIHIDA-KSSVRKQILRELQILHECHSPYIVSFYGAFLNEnNNIIICMEYMDCGS-------- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 155 fMDGM-------SELAIAYILQGVLKALDYI---HHMgyVHRSVKASHILISTDGKVYLSGLRSNLSMIShgqrqrAVHD 224
Cdd:cd06620    91 -LDKIlkkkgpfPEEVLGKIAVAVLEGLTYLynvHRI--IHRDIKPSNILVNSKGQIKLCDFGVSGELIN------SIAD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 225 -FPKYSIkvlpWLSPEVLQQNlqGYDAKSDIYSVGITACELANGHVPFKDmpatqmlleklngtvpclldtstipAEELT 303
Cdd:cd06620   162 tFVGTST----YMSPERIQGG--KYSVKSDVWSLGLSIIELALGEFPFAG-------------------------SNDDD 210
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958659070 304 MSPSRSIanpGLNDSLAagslRPANGDSPSHPYHRTFSPHFHNFVEQCLQRNPDARPNASTLLNHSFFKQIKRR 377
Cdd:cd06620   211 DGYNGPM---GILDLLQ----RIVNEPPPRLPKDRIFPKDLRDFVDRCLLKDPRERPSPQLLLDHDPFIQAVRA 277
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
76-373 1.21e-18

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


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 85.32  E-value: 1.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  76 TVNLARYKPTGEYVTVRRINLEAcSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGSAkDLIGThf 155
Cdd:cd06619    16 TVYKAYHLLTRRILAVKVIPLDI-TVELQKQIMSELEILYKCDSPYIIGFYGAFFVENRISICTEFMDGGSL-DVYRK-- 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 156 mdgMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLrsnlsmishGQRQRAVHDFPKYSIKVLPW 235
Cdd:cd06619    92 ---IPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDF---------GVSTQLVNSIAKTYVGTNAY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 236 LSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNgTVPCLLDTstipaeeltmspsrsianpgl 315
Cdd:cd06619   160 MAPERISG--EQYGIHSDVWSLGISFMELALGRFPYPQIQKNQGSLMPLQ-LLQCIVDE--------------------- 215
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958659070 316 ndslaagslrpangDSPSHPYHRtFSPHFHNFVEQCLQRNPDARPNASTLLNHSFFKQ 373
Cdd:cd06619   216 --------------DPPVLPVGQ-FSEKFVHFITQCMRKQPKERPAPENLMDHPFIVQ 258
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
85-370 3.21e-18

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


Pssm-ID: 270796 [Multi-domain]  Cd Length: 265  Bit Score: 83.89  E-value: 3.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  85 TGEYVTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNElwaVTSFMAY---GSAKDL--IGthfmDGM 159
Cdd:cd06626    24 TGELMAMKEIRFQDNDPKTIKEIADEMKVLEGLDHPNLVRYYGVEVHREE---VYIFMEYcqeGTLEELlrHG----RIL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 160 SELAI-AYILQgVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSG------LRSNLSMISHGQRQRAVHDfPKYsikv 232
Cdd:cd06626    97 DEAVIrVYTLQ-LLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDfgsavkLKNNTTTMAPGEVNSLVGT-PAY---- 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 233 lpwLSPEV-LQQNLQGYDAKSDIYSVGITACELANGHVPFKDMpatqmlleklngtvpclldtstipaeeltmspsrsia 311
Cdd:cd06626   171 ---MAPEViTGNKGEGHGRAADIWSLGCVVLEMATGKRPWSEL------------------------------------- 210
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958659070 312 npglnDSLAAGSLRPANGDSPSHPYHRTFSPHFHNFVEQCLQRNPDARPNASTLLNHSF 370
Cdd:cd06626   211 -----DNEWAIMYHVGMGHKPPIPDSLQLSPEGKDFLSRCLESDPKKRPTASELLDHPF 264
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
77-368 7.39e-18

Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK16 is associated with many names including Myristylated and Palmitylated Serine/threonine Kinase 1 (MPSK1), Kinase related to cerevisiae and thaliana (Krct), and Protein Kinase expressed in day 12 fetal liver (PKL12). It is widely expressed in mammals with highest levels found in liver, testis, and kidney. It is localized in the Golgi but is translocated to the nucleus upon disorganization of the Golgi. STK16 is constitutively active and is capable of phosphorylating itself and other substrates. It may be involved in regulating stromal-epithelial interactions during mammary gland ductal morphogenesis. It may also function as a transcriptional co-activator of type-C natriuretic peptide and VEGF. The STK16 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270888 [Multi-domain]  Cd Length: 282  Bit Score: 83.11  E-value: 7.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  77 VNLARYKPTGEYVTVRRInleAC-SNEMVTFLQGELHVSKLFSHPNIVPYRATFI-----ADNELWAVTSFMAYGSAKDL 150
Cdd:cd13986    16 VYLVEDLSTGRLYALKKI---LChSKEDVKEAMREIENYRLFNHPNILRLLDSQIvkeagGKKEVYLLLPYYKRGSLQDE 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 151 IGTHFMDG--MSELAIAYILQGVLKALDYIHHM---GYVHRSVKASHILISTDGKVYLSGLRS-NLSMIS-HGQRQ-RAV 222
Cdd:cd13986    93 IERRLVKGtfFPEDRILHIFLGICRGLKAMHEPelvPYAHRDIKPGNVLLSEDDEPILMDLGSmNPARIEiEGRREaLAL 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 223 HDF--PKYSIkvlPWLSPEVLQ-QNLQGYDAKSDIYSVGITACELANGHVPFkdmpatQMLLEKlngtvpclldtstipa 299
Cdd:cd13986   173 QDWaaEHCTM---PYRAPELFDvKSHCTIDEKTDIWSLGCTLYALMYGESPF------ERIFQK---------------- 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958659070 300 eeltmspsrsianpglNDSLAagsLRPANGDSpSHPYHRTFSPHFHNFVEQCLQRNPDARPNASTLLNH 368
Cdd:cd13986   228 ----------------GDSLA---LAVLSGNY-SFPDNSRYSEELHQLVKSMLVVNPAERPSIDDLLSR 276
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
61-373 1.01e-17

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 1; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. MEK1 also plays a role in cell cycle control. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 83.57  E-value: 1.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLE---ACSNEMVTflqgELHVSKLFSHPNIVPYRATFIADNELWA 137
Cdd:cd06650     7 FEKISELGAG--NGGVVFKVSHKPSGLVMARKLIHLEikpAIRNQIIR----ELQVLHECNSPYIVGFYGAFYSDGEISI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 138 VTSFMAYGSAKDLIGThfMDGMSELAIAYILQGVLKALDYIHHMGYV-HRSVKASHILISTDGKVYLSGLrsnlsmishG 216
Cdd:cd06650    81 CMEHMDGGSLDQVLKK--AGRIPEQILGKVSIAVIKGLTYLREKHKImHRDVKPSNILVNSRGEIKLCDF---------G 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 217 QRQRAVHDFPKYSIKVLPWLSPEVLQQNlqGYDAKSDIYSVGITACELANGHVPFKdmPATQMLLEKLNGtvpCLLDTST 296
Cdd:cd06650   150 VSGQLIDSMANSFVGTRSYMSPERLQGT--HYSVQSDIWSMGLSLVEMAVGRYPIP--PPDAKELELMFG---CQVEGDA 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 297 IPAEELTMSPSRSIANPGLNDS--LAAGSLRP--ANGDSPSHPyHRTFSPHFHNFVEQCLQRNPDARPNASTLLNHSFFK 372
Cdd:cd06650   223 AETPPRPRTPGRPLSSYGMDSRppMAIFELLDyiVNEPPPKLP-SGVFSLEFQDFVNKCLIKNPAERADLKQLMVHAFIK 301

                  .
gi 1958659070 373 Q 373
Cdd:cd06650   302 R 302
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
67-272 1.23e-17

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: 81.89  E-value: 1.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  67 IGKG-FEdlmTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYG 145
Cdd:cd14009     1 IGRGsFA---TVWKGRHKQTGEVVAIKEISRKKLNKKLQENLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAGG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 146 SAKDLIGTHFmdGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGkvylsglrsNLSMIShgqrqraVHDF 225
Cdd:cd14009    78 DLSQYIRKRG--RLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSG---------DDPVLK-------IADF 139
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958659070 226 ------------------PKYsikvlpwLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFK 272
Cdd:cd14009   140 gfarslqpasmaetlcgsPLY-------MAPEILQF--QKYDAKADLWSVGAILFEMLVGKPPFR 195
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
62-376 2.04e-17

Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Polymyxin B resistance protein 2 (PBS2) from Saccharomyces cerevisiae, Wis1 from Schizosaccharomyces pombe, and related proteins. PBS2 and Wis1 are components of stress-activated MAPK cascades in budding and fission yeast, respectively. PBS2 is the specific activator of the MAPK Hog1, which plays a central role in the response of budding yeast to stress including exposure to arsenite and hyperosmotic environments. Wis1 phosphorylates and activates the MAPK Sty1 (also called Spc1 or Phh1), which stimulates a transcriptional response to a wide range of cellular insults through the bZip transcription factors Atf1, Pcr1, and Pap1. The PBS2 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 82.20  E-value: 2.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  62 ELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQgELHVSKLFSHPNIVPYRATFIADNELWAVTSF 141
Cdd:cd06622     4 EVLDELGKG--NYGSVYKVLHRPTGVTMAMKEIRLELDESKFNQIIM-ELDILHKAVSPYIVDFYGAFFIEGAVYMCMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 142 MAYGSAKDLI-GTHFMDGMSELAIAYILQGVLKALDYI-HHMGYVHRSVKASHILISTDGKVYLS--GLRSNLsmishgq 217
Cdd:cd06622    81 MDAGSLDKLYaGGVATEGIPEDVLRRITYAVVKGLKFLkEEHNIIHRDVKPTNVLVNGNGQVKLCdfGVSGNL------- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 218 rqraVHDFPKYSIKVLPWLSPEVLQ-----QNLQgYDAKSDIYSVGITACELANGHVPFkdmpatqmlleklngtvpcll 292
Cdd:cd06622   154 ----VASLAKTNIGCQSYMAPERIKsggpnQNPT-YTVQSDVWSLGLSILEMALGRYPY--------------------- 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 293 dtstipaeeltmsPSRSIANpgLNDSLAAgslrPANGDSPSHPyhRTFSPHFHNFVEQCLQRNPDARPNASTLLNHSFFK 372
Cdd:cd06622   208 -------------PPETYAN--IFAQLSA----IVDGDPPTLP--SGYSDDAQDFVAKCLNKIPNRRPTYAQLLEHPWLV 266

                  ....
gi 1958659070 373 QIKR 376
Cdd:cd06622   267 KYKN 270
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
61-371 2.33e-17

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: 81.98  E-value: 2.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRInLEACSNEMV--TFLQgELHVSKLFSHPNIVPYRATFIADNELWAV 138
Cdd:cd07833     3 YEVLGVVGEG--AYGVVLKCRNKATGEIVAIKKF-KESEDDEDVkkTALR-EVKVLRQLRHENIVNLKEAFRRKGRLYLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 139 TSFMAYGSAKDLigTHFMDGMSELAI-AYILQgVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSNLsmish 215
Cdd:cd07833    79 FEYVERTLLELL--EASPGGLPPDAVrSYIWQ-LLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCdfGFARAL----- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 216 gqRQRAVHDFPKYSikVLPWL-SPEVLQQNLQgYDAKSDIYSVGITACELANGHVPFkdmPAT----QM-LLEKLNGTVP 289
Cdd:cd07833   151 --TARPASPLTDYV--ATRWYrAPELLVGDTN-YGKPVDVWAIGCIMAELLDGEPLF---PGDsdidQLyLIQKCLGPLP 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 290 clldtstiPAEELTMSpsrsiANPGLndslaAGSLRPangdSPSHP------YHRTFSPHFHNFVEQCLQRNPDARPNAS 363
Cdd:cd07833   223 --------PSHQELFS-----SNPRF-----AGVAFP----EPSQPeslerrYPGKVSSPALDFLKACLRMDPKERLTCD 280

                  ....*...
gi 1958659070 364 TLLNHSFF 371
Cdd:cd07833   281 ELLQHPYF 288
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
61-290 5.19e-17

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


Pssm-ID: 271133 [Multi-domain]  Cd Length: 256  Bit Score: 80.14  E-value: 5.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLE-ACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVT 139
Cdd:cd14663     2 YELGRTLGEG--TFAKVKFARNTKTGESVAIKIIDKEqVAREGMVEQIKREIAIMKLLRHPNIVELHEVMATKTKIFFVM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 140 SFMAYGSAKDLIGTHfmDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLrSNLSmiSHGQ 217
Cdd:cd14663    80 ELVTGGELFSKIAKN--GRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISdfGL-SALS--EQFR 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958659070 218 RQRAVHDF---PKYsikvlpwLSPEVLQQNlqGYD-AKSDIYSVGITACELANGHVPFKDmPATQMLLEKL-NGTVPC 290
Cdd:cd14663   155 QDGLLHTTcgtPNY-------VAPEVLARR--GYDgAKADIWSCGVILFVLLAGYLPFDD-ENLMALYRKImKGEFEY 222
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
61-289 8.64e-17

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


Pssm-ID: 270898 [Multi-domain]  Cd Length: 273  Bit Score: 80.03  E-value: 8.64e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGFEDlmTVNLARYKPTGEYVTVRRINL-EACSNEMVTFLQGELHVSklFSHPNIVPYRATFIADNELWAVT 139
Cdd:cd13996     8 FEEIELLGSGGFG--SVYKVRNKVDGVTYAIKKIRLtEKSSASEKVLREVKALAK--LNHPNIVRYYTAWVEEPPLYIQM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 140 SFMAYGSAKDLIG--THFMDGMSELAIAYILQgVLKALDYIHHMGYVHRSVKASHILISTDGKVY------LSGLRSNLS 211
Cdd:cd13996    84 ELCEGGTLRDWIDrrNSSSKNDRKLALELFKQ-ILKGVSYIHSKGIVHRDLKPSNIFLDNDDLQVkigdfgLATSIGNQK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 212 MISHGQRQRAVHDFPKYSIKV--LPWLSPEVLQQNLqgYDAKSDIYSVGITACELangHVPFKdmpaTQM----LLEKL- 284
Cdd:cd13996   163 RELNNLNNNNNGNTSNNSVGIgtPLYASPEQLDGEN--YNEKADIYSLGIILFEM---LHPFK----TAMerstILTDLr 233

                  ....*
gi 1958659070 285 NGTVP 289
Cdd:cd13996   234 NGILP 238
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
61-373 1.27e-16

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 2; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK2 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 80.48  E-value: 1.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLE---ACSNEMVTflqgELHVSKLFSHPNIVPYRATFIADNELWA 137
Cdd:cd06649     7 FERISELGAG--NGGVVTKVQHKPSGLIMARKLIHLEikpAIRNQIIR----ELQVLHECNSPYIVGFYGAFYSDGEISI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 138 VTSFMAYGSAKDLIGThfMDGMSELAIAYILQGVLKALDYIHHMGYV-HRSVKASHILISTDGKVYLSGLrsnlsmishG 216
Cdd:cd06649    81 CMEHMDGGSLDQVLKE--AKRIPEEILGKVSIAVLRGLAYLREKHQImHRDVKPSNILVNSRGEIKLCDF---------G 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 217 QRQRAVHDFPKYSIKVLPWLSPEVLQQNlqGYDAKSDIYSVGITACELANGHVPFKdmPATQMLLEKLNGTVpcLLDTST 296
Cdd:cd06649   150 VSGQLIDSMANSFVGTRSYMSPERLQGT--HYSVQSDIWSMGLSLVELAIGRYPIP--PPDAKELEAIFGRP--VVDGEE 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 297 ipAEELTMSP-----SRSIANPGLNDSLAAGSLR----PANGDSPSHPyHRTFSPHFHNFVEQCLQRNPDARPNASTLLN 367
Cdd:cd06649   224 --GEPHSISPrprppGRPVSGHGMDSRPAMAIFElldyIVNEPPPKLP-NGVFTPDFQEFVNKCLIKNPAERADLKMLMN 300

                  ....*.
gi 1958659070 368 HSFFKQ 373
Cdd:cd06649   301 HTFIKR 306
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
61-372 2.54e-16

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: 78.29  E-value: 2.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKG-FEdlmTVNLARYKPTGEYVTVRRINLEA-CSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAV 138
Cdd:cd14007     2 FEIGKPLGKGkFG---NVYLAREKKSGFIVALKVISKSQlQKSGLEHQLRREIEIQSHLRHPNILRLYGYFEDKKRIYLI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 139 tsfMAYGSAKDLIG-----THFMDgmsELAIAYILQgVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSglrsnlsmi 213
Cdd:cd14007    79 ---LEYAPNGELYKelkkqKRFDE---KEAAKYIYQ-LALALDYLHSKNIIHRDIKPENILLGSNGELKLA--------- 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 214 shgqrqravhDFpKYSIKV-----------LPWLSPEVLqqNLQGYDAKSDIYSVGITACELANGHVPFKdMPATQMLLE 282
Cdd:cd14007   143 ----------DF-GWSVHApsnrrktfcgtLDYLPPEMV--EGKEYDYKVDIWSLGVLCYELLVGKPPFE-SKSHQETYK 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 283 KlngtvpclldtstIPAEELTMSPSrsianpglndslaagslrpangdspshpyhrtFSPHFHNFVEQCLQRNPDARPNA 362
Cdd:cd14007   209 R-------------IQNVDIKFPSS--------------------------------VSPEAKDLISKLLQKDPSKRLSL 243
                         330
                  ....*....|
gi 1958659070 363 STLLNHSFFK 372
Cdd:cd14007   244 EQVLNHPWIK 253
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
61-371 3.45e-16

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


Pssm-ID: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 77.66  E-value: 3.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGFEDlmTVNLARYKPTGEYVTVRRInleACSNEMVTFLQGEL----HVSKLFSHPNIV--PYRATFIADNE 134
Cdd:cd05118     1 YEVLRKIGEGAFG--TVWLARDKVTGEKVAIKKI---KNDFRHPKAALREIkllkHLNDVEGHPNIVklLDVFEHRGGNH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 135 LWAVTSFMAYgSAKDLIGtHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDgkvylsglRSNLSMIS 214
Cdd:cd05118    76 LCLVFELMGM-NLYELIK-DYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLE--------LGQLKLAD 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 215 HGQrQRAVHDfPKYSIKV--LPWLSPEVLQQnLQGYDAKSDIYSVGitacelanghvpfkdmpatqmlleklngtvpCLL 292
Cdd:cd05118   146 FGL-ARSFTS-PPYTPYVatRWYRAPEVLLG-AKPYGSSIDIWSLG-------------------------------CIL 191
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 293 dtstipAEELTMSPSRSIANPglNDSLAAgslrpangdspshpYHRTF-SPHFHNFVEQCLQRNPDARPNASTLLNHSFF 371
Cdd:cd05118   192 ------AELLTGRPLFPGDSE--VDQLAK--------------IVRLLgTPEALDLLSKMLKYDPAKRITASQALAHPYF 249
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
61-366 3.50e-16

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


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 77.84  E-value: 3.50e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTS 140
Cdd:cd08529     2 FEILNKLGKG--SFGVVYKVVRKVDGRVYALKQIDISRMSRKMREEAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIVME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 141 FMAYGSAKDLIGTHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLRSNLSMISHGQRQR 220
Cdd:cd08529    80 YAENGDLHSLIKSQRGRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAKILSDTTNFAQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 221 AVHDFPKYsikvlpwLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKdmpatqmlleklngtvpclldtstipae 300
Cdd:cd08529   160 TIVGTPYY-------LSPELCED--KPYNEKSDVWALGCVLYELCTGKHPFE---------------------------- 202
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958659070 301 eltmspsrsIANPGlndslaAGSLRPANGDSPshPYHRTFSPHFHNFVEQCLQRNPDARPNASTLL 366
Cdd:cd08529   203 ---------AQNQG------ALILKIVRGKYP--PISASYSQDLSQLIDSCLTKDYRQRPDTTELL 251
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
61-371 6.52e-16

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


Pssm-ID: 270832 [Multi-domain]  Cd Length: 291  Bit Score: 77.60  E-value: 6.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfedlmT---VNLARYKPTGEYVTVRRINLEACSNEM-VTFLQgELHVSKLFSHPNIVPY------RATFI 130
Cdd:cd07840     1 YEKIAQIGEG-----TygqVYKARNKKTGELVALKKIRMENEKEGFpITAIR-EIKLLQKLDHPNVVRLkeivtsKGSAK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 131 ADNELWAVTSFMAYgsakDLIGTHFMDGM--SELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GL 206
Cdd:cd07840    75 YKGSIYMVFEYMDH----DLTGLLDNPEVkfTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLAdfGL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 207 rsnlsmishgQRQRAVHDFPKYSIKV--LPWLSPEVLQQNLQgYDAKSDIYSVGITACELANGHVPFKDmpATQML-LEK 283
Cdd:cd07840   151 ----------ARPYTKENNADYTNRVitLWYRPPELLLGATR-YGPEVDMWSVGCILAELFTGKPIFQG--KTELEqLEK 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 284 LNgtvpclldtstipaeELTMSPSRSIAnPGLNDslaagsLRPANGDSPSHPYHRTF--------SPHFHNFVEQCLQRN 355
Cdd:cd07840   218 IF---------------ELCGSPTEENW-PGVSD------LPWFENLKPKKPYKRRLrevfknviDPSALDLLDKLLTLD 275
                         330
                  ....*....|....*.
gi 1958659070 356 PDARPNASTLLNHSFF 371
Cdd:cd07840   276 PKKRISADQALQHEYF 291
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
61-371 7.86e-16

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


Pssm-ID: 270823 [Multi-domain]  Cd Length: 282  Bit Score: 77.14  E-value: 7.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfedlmT---VNLARYKPTGEYVTVRRINLEACSNEM-VTFLQgELHVSKLFSHPNIVPYRATFIADNELW 136
Cdd:cd07829     1 YEKLEKLGEG-----TygvVYKAKDKKTGEIVALKKIRLDNEEEGIpSTALR-EISLLKELKHPNIVKLLDVIHTENKLY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 137 AVTSFMAYgsakDLigTHFMD----GMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLrsnl 210
Cdd:cd07829    75 LVFEYCDQ----DL--KKYLDkrpgPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLAdfGL---- 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 211 smishgqrQRAVHdFP--KYSIKVL-PW-LSPEVLQQNlQGYDAKSDIYSVG-ITAcELANGHVPFkdmPATQ---MLLE 282
Cdd:cd07829   145 --------ARAFG-IPlrTYTHEVVtLWyRAPEILLGS-KHYSTAVDIWSVGcIFA-ELITGKPLF---PGDSeidQLFK 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 283 --KLNGTvpclldtstiPAEELTmspsrsianPGLNDSLAAGSLRPANgdsPSHPYHRTFSPHFHNFVE---QCLQRNPD 357
Cdd:cd07829   211 ifQILGT----------PTEESW---------PGVTKLPDYKPTFPKW---PKNDLEKVLPRLDPEGIDllsKMLQYNPA 268
                         330
                  ....*....|....
gi 1958659070 358 ARPNASTLLNHSFF 371
Cdd:cd07829   269 KRISAKEALKHPYF 282
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
61-271 9.79e-16

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: 76.52  E-value: 9.79e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTS 140
Cdd:cd14002     3 YHVLELIGEG--SFGKVYKGRRKYTGQVVALKFIPKRGKSEKELRNLRQEIEILRKLNHPNIIEMLDSFETKKEFVVVTE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 141 FmAYGSAKDLIGThfmDG-MSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSNLSMISHGQ 217
Cdd:cd14002    81 Y-AQGELFQILED---DGtLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCdfGFARAMSCNTLVL 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958659070 218 RqravhdfpkySIKVLP-WLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPF 271
Cdd:cd14002   157 T----------SIKGTPlYMAPELVQE--QPYDHTADLWSLGCILYELFVGQPPF 199
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
61-277 1.68e-15

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: 75.83  E-value: 1.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKG-FEDlmtVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVT 139
Cdd:cd14069     3 WDLVQTLGEGaFGE---VFLAVNRNTEEAVAVKFVDMKRAPGDCPENIKKEVCIQKMLSHKNVVRFYGHRREGEFQYLFL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 140 SFMAYGSAKDLIgtHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRsnlSMISHGQ 217
Cdd:cd14069    80 EYASGGELFDKI--EPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISdfGLA---TVFRYKG 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958659070 218 RQRAVHDfpkySIKVLPWLSPEVLQQnlQGYDA-KSDIYSVGITACELANGHVPFkDMPAT 277
Cdd:cd14069   155 KERLLNK----MCGTLPYVAPELLAK--KKYRAePVDVWSCGIVLFAMLAGELPW-DQPSD 208
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
67-371 2.42e-15

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: 75.25  E-value: 2.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  67 IGKGFEDlmTVNLARYKPTGEYVTVRRINLEAC-SNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYG 145
Cdd:cd05123     1 LGKGSFG--KVLLVRKKDTGKLYAMKVLRKKEIiKRKEVEHTLNERNILERVNHPFIVKLHYAFQTEEKLYLVLDYVPGG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 146 SAKDLIGTHFMdgMSELAIA-YILQGVLkALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSnlSMISHGQRQRAV 222
Cdd:cd05123    79 ELFSHLSKEGR--FPEERARfYAAEIVL-ALEYLHSLGIIYRDLKPENILLDSDGHIKLTdfGLAK--ELSSDGDRTYTF 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 223 HDFPKYsikvlpwLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQMlleklngtvpclldTSTIPAEEL 302
Cdd:cd05123   154 CGTPEY-------LAPEVLLG--KGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEI--------------YEKILKSPL 210
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958659070 303 TMspsrsianpglndslaagslrpangdsPSHpyhrtFSPHFHNFVEQCLQRNPDAR---PNASTLLNHSFF 371
Cdd:cd05123   211 KF---------------------------PEY-----VSPEAKSLISGLLQKDPTKRlgsGGAEEIKAHPFF 250
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
61-391 3.57e-15

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


Pssm-ID: 270841 [Multi-domain]  Cd Length: 337  Bit Score: 76.06  E-value: 3.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGFEDLmtVNLARYKPTGEYVTVRRInLEACSNEM--------VTFLQgelhvsKLFSHPNIVPYRATFIAD 132
Cdd:cd07852     9 YEILKKLGKGAYGI--VWKAIDKKTGEVVALKKI-FDAFRNATdaqrtfreIMFLQ------ELNDHPNIIKLLNVIRAE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 133 NElwavtsfmaygsaKDL-IGTHFMDG----------MSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKV 201
Cdd:cd07852    80 ND-------------KDIyLVFEYMETdlhaviraniLEDIHKQYIMYQLLKALKYLHSGGVIHRDLKPSNILLNSDCRV 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 202 YLS--GLRSNLSMISHGQRQRAVHDFpkysikVLP-WL-SPEVLQQNlQGYDAKSDIYSVGitaCELAnghvpfkdmpat 277
Cdd:cd07852   147 KLAdfGLARSLSQLEEDDENPVLTDY------VATrWYrAPEILLGS-TRYTKGVDMWSVG---CILG------------ 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 278 QMLLEKlngtvPCLLDTSTIPAEELTMSpsrSIANPGLND-----SLAAGSLRPANGDSPSHPYHRTF---SPHFHNFVE 349
Cdd:cd07852   205 EMLLGK-----PLFPGTSTLNQLEKIIE---VIGRPSAEDiesiqSPFAATMLESLPPSRPKSLDELFpkaSPDALDLLK 276
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1958659070 350 QCLQRNPDARPNASTLLNHSFFKQIKRRASEalPELLRPVTP 391
Cdd:cd07852   277 KLLVFNPNKRLTAEEALRHPYVAQFHNPADE--PSLPGPIVI 316
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
61-369 3.81e-15

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


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 75.01  E-value: 3.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLfSHPNIVPYRATFIADNELWAVts 140
Cdd:cd08219     2 YNVLRVVGEG--SFGRALLVQHVNSDQKYAMKEIRLPKSSSAVEDSRKEAVLLAKM-KHPNIVAFKESFEADGHLYIV-- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 141 fMAYGSAKDLI-------GTHFMDGMselAIAYILQGVLkALDYIHHMGYVHRSVKASHILISTDGKVYLSGLRSNLSMI 213
Cdd:cd08219    77 -MEYCDGGDLMqkiklqrGKLFPEDT---ILQWFVQMCL-GVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 214 SHGQRQRAVHDFPKYsikvlpwLSPEVLqQNLQgYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEklngtvpclld 293
Cdd:cd08219   152 SPGAYACTYVGTPYY-------VPPEIW-ENMP-YNNKSDIWSLGCILYELCTLKHPFQANSWKNLILK----------- 211
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958659070 294 tstipaeeltmspsrsianpglndsLAAGSLRPAngdsPSHpyhrtFSPHFHNFVEQCLQRNPDARPNASTLLNHS 369
Cdd:cd08219   212 -------------------------VCQGSYKPL----PSH-----YSYELRSLIKQMFKRNPRSRPSATTILSRG 253
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
62-275 4.40e-15

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


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 74.63  E-value: 4.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  62 ELLSVIGKG-FEDLMtvnLARYKptGEYVTVRRINLEACSNEMVtflqGELHVSKLFSHPNIVPYRATFIADN-ELWAVT 139
Cdd:cd05082     9 KLLQTIGKGeFGDVM---LGDYR--GNKVAVKCIKNDATAQAFL----AEASVMTQLRHSNLVQLLGVIVEEKgGLYIVT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 140 SFMAYGSAKDLI---GTHFMDGMSELAIAYilqGVLKALDYIHHMGYVHRSVKASHILISTD--GKVYLSGLRSNLSmis 214
Cdd:cd05082    80 EYMAKGSLVDYLrsrGRSVLGGDCLLKFSL---DVCEAMEYLEGNNFVHRDLAARNVLVSEDnvAKVSDFGLTKEAS--- 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958659070 215 hgqrqrAVHDFPKYSIKvlpWLSPEVLQQNLqgYDAKSDIYSVGITACELAN-GHVPFKDMP 275
Cdd:cd05082   154 ------STQDTGKLPVK---WTAPEALREKK--FSTKSDVWSFGILLWEIYSfGRVPYPRIP 204
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
26-391 1.41e-14

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 74.47  E-value: 1.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  26 PPGDTRRKANEASSESIASFSKPEIMSSFlpeggcyELLSVIGKGFEDlmTVNLARYKPTGEYVTVRRI--NLEACSNEM 103
Cdd:PLN00034   48 PPPSSSSSSSSSSSASGSAPSAAKSLSEL-------ERVNRIGSGAGG--TVYKVIHRPTGRLYALKVIygNHEDTVRRQ 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 104 VTflqGELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGSakdLIGTHFMDgmsELAIAYILQGVLKALDYIHHMGY 183
Cdd:PLN00034  119 IC---REIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGS---LEGTHIAD---EQFLADVARQILSGIAYLHRRHI 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 184 VHRSVKASHILIStdgkvylSGLRSNLSMISHGQRQRAVHDFPKYSIKVLPWLSPEVLQQNL-QG-YDAKS-DIYSVGIT 260
Cdd:PLN00034  190 VHRDIKPSNLLIN-------SAKNVKIADFGVSRILAQTMDPCNSSVGTIAYMSPERINTDLnHGaYDGYAgDIWSLGVS 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 261 ACELANGHVPFkdmpatqmlleklngtvpclldtstipaeeltmspsrsianpGLNDSLAAGSLRPA--NGDSPSHPyhR 338
Cdd:PLN00034  263 ILEFYLGRFPF------------------------------------------GVGRQGDWASLMCAicMSQPPEAP--A 298
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958659070 339 TFSPHFHNFVEQCLQRNPDARPNASTLLNHSFFKQIKRRASEALPElLRPVTP 391
Cdd:PLN00034  299 TASREFRHFISCCLQREPAKRWSAMQLLQHPFILRAQPGQGQGGPN-LHQLLP 350
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
77-273 1.68e-14

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


Pssm-ID: 270731 [Multi-domain]  Cd Length: 272  Bit Score: 73.40  E-value: 1.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  77 VNLARYKPTGEYVTVRRINLEACSNE-MVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGSAKDLIgtHF 155
Cdd:cd05579     9 VYLAKKKSTGDLYAIKVIKKRDMIRKnQVDSVLAERNILSQAQNPFVVKLYYSFQGKKNLYLVMEYLPGGDLYSLL--EN 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 156 MDGMSE-LAIAYILQGVLkALDYIHHMGYVHRSVKASHILISTDGKVYLS-------GLRSNLSMISHGQRQRAVHDFPK 227
Cdd:cd05579    87 VGALDEdVARIYIAEIVL-ALEYLHSHGIIHRDLKPDNILIDANGHLKLTdfglskvGLVRRQIKLSIQKKSNGAPEKED 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1958659070 228 YSIKVLP-WLSPEVLqqNLQGYDAKSDIYSVGITACELANGHVPFKD 273
Cdd:cd05579   166 RRIVGTPdYLAPEIL--LGQGHGKTVDWWSLGVILYEFLVGIPPFHA 210
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
61-271 1.85e-14

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


Pssm-ID: 270974 [Multi-domain]  Cd Length: 253  Bit Score: 72.94  E-value: 1.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTS 140
Cdd:cd14072     2 YRLLKTIGKG--NFAKVKLARHVLTGREVAIKIIDKTQLNPSSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 141 FMAYGSAKDLIGTHfmDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLR-SNlsMISHGQRQ 219
Cdd:cd14072    80 YASGGEVFDYLVAH--GRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGfSN--EFTPGNKL 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958659070 220 RAVHDFPkysikvlPWLSPEVLQQnlQGYDA-KSDIYSVGITACELANGHVPF 271
Cdd:cd14072   156 DTFCGSP-------PYAAPELFQG--KKYDGpEVDVWSLGVILYTLVSGSLPF 199
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
84-376 2.18e-14

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: 72.81  E-value: 2.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  84 PTGEYVTVRRINLEACSNEMVTFlqgELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGSAKDLI--GTHFMDGMSE 161
Cdd:cd13992    23 YGGRTVAIKHITFSRTEKRTILQ---ELNQLKELVHDNLNKFIGICINPPNIAVVTEYCTRGSLQDVLlnREIKMDWMFK 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 162 LAIAYilqGVLKALDYIH-HMGYVHRSVKASHILISTDGKVYLSGLrsNLSMISHGQRQRAVHDFPKYSIKVlpWLSPEV 240
Cdd:cd13992   100 SSFIK---DIVKGMNYLHsSSIGYHGRLKSSNCLVDSRWVVKLTDF--GLRNLLEEQTNHQLDEDAQHKKLL--WTAPEL 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 241 LQQNLQGY--DAKSDIYSVGITACELA--NGHVPFKDMPATQMlLEKLNGTVPCLLDtstiPAEELTMSPSRSIAnpgln 316
Cdd:cd13992   173 LRGSLLEVrgTQKGDVYSFAIILYEILfrSDPFALEREVAIVE-KVISGGNKPFRPE----LAVLLDEFPPRLVL----- 242
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 317 dslaagslrpangdspshpyhrtfsphfhnFVEQCLQRNPDARPNastllnhsfFKQIKR 376
Cdd:cd13992   243 ------------------------------LVKQCWAENPEKRPS---------FKQIKK 263
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
61-371 2.98e-14

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek2 subfamily includes Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants prevented from entering mitosis. NIMA is essential for mitotic entry and progression through mitosis, and its degradation is essential for mitotic exit. NIMA is involved in nuclear membrane fission. Vertebrate Nek2 is a cell cycle-regulated STK, localized in centrosomes and kinetochores, that regulates centrosome splitting at the G2/M phase. It also interacts with other mitotic kinases such as Polo-like kinase 1 and may play a role in spindle checkpoint. An increase in the expression of the human NEK2 gene is strongly associated with the progression of non-Hodgkin lymphoma. Nek2 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. It The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270857 [Multi-domain]  Cd Length: 265  Bit Score: 72.19  E-value: 2.98e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKG-FEdlmTVNLARYKPTGEYVTVRRINLEACSN---EMvtfLQGELHVSKLFSHPNIVPYRATFIaDNELW 136
Cdd:cd08217     2 YEVLETIGKGsFG---TVRKVRRKSDGKILVWKEIDYGKMSEkekQQ---LVSEVNILRELKHPNIVRYYDRIV-DRANT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 137 AVTSFMAYGSAKDL---IGTHFMDG--MSELAIAYILQGVLKALDYIHHMGY-----VHRSVKASHILISTDGKVYLS-- 204
Cdd:cd08217    75 TLYIVMEYCEGGDLaqlIKKCKKENqyIPEEFIWKIFTQLLLALYECHNRSVgggkiLHRDLKPANIFLDSDNNVKLGdf 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 205 GLRSNLSmishgQRQRAVHDF---PKYsikvlpwLSPEVLqqNLQGYDAKSDIYSVGITACELANGHVPFKdmPATQMLL 281
Cdd:cd08217   155 GLARVLS-----HDSSFAKTYvgtPYY-------MSPELL--NEQSYDEKSDIWSLGCLIYELCALHPPFQ--AANQLEL 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 282 EKL--NGTVPCLldtstipaeeltmspsrsianpglndslaagslrpangdsPSHpyhrtFSPHFHNFVEQCLQRNPDAR 359
Cdd:cd08217   219 AKKikEGKFPRI----------------------------------------PSR-----YSSELNEVIKSMLNVDPDKR 253
                         330
                  ....*....|..
gi 1958659070 360 PNASTLLNHSFF 371
Cdd:cd08217   254 PSVEELLQLPLI 265
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
61-371 3.74e-14

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


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 71.91  E-value: 3.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVts 140
Cdd:cd08225     2 YEIIKKIGEG--SFGKIYLAKAKSDSEHCVIKEIDLTKMPVKEKEASKKEVILLAKMKHPNIVTFFASFQENGRLFIV-- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 141 fMAYGSAKDLI-------GTHFMDgmsELAIAYILQGVLkALDYIHHMGYVHRSVKASHILISTDGKVylsglrSNLSMI 213
Cdd:cd08225    78 -MEYCDGGDLMkrinrqrGVLFSE---DQILSWFVQISL-GLKHIHDRKILHRDIKSQNIFLSKNGMV------AKLGDF 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 214 SHGQRQRAVHDFPKYSIKVLPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVpclld 293
Cdd:cd08225   147 GIARQLNDSMELAYTCVGTPYYLSPEICQN--RPYNNKTDIWSLGCVLYELCTLKHPFEGNNLHQLVLKICQGYF----- 219
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958659070 294 tstipaeeltmspsrsianpglndslaagslrpangdspsHPYHRTFSPHFHNFVEQCLQRNPDARPNASTLLNHSFF 371
Cdd:cd08225   220 ----------------------------------------APISPNFSRDLRSLISQLFKVSPRDRPSITSILKRPFL 257
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
115-267 4.20e-14

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


Pssm-ID: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 71.65  E-value: 4.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 115 KLFSHPNIVPYRATFIADNELWAVTSFMAYGSAKDLIGTHFMDG-MSELAIAYILQGVLKALDYIHHMGYVHRSVKASHI 193
Cdd:cd13997    55 ALGQHPNIVRYYSSWEEGGHLYIQMELCENGSLQDALEELSPISkLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNI 134
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958659070 194 LISTDGKVYLS--GLRSNLS---MISHGQrqravhdfPKYsikvlpwLSPEVLQQNLQgYDAKSDIYSVGITACELANG 267
Cdd:cd13997   135 FISNKGTCKIGdfGLATRLEtsgDVEEGD--------SRY-------LAPELLNENYT-HLPKADIFSLGVTVYEAATG 197
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
117-274 4.84e-14

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


Pssm-ID: 133195 [Multi-domain]  Cd Length: 266  Bit Score: 71.88  E-value: 4.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 117 FSHPNIVPYRATFIADNELWAVTSFMAYGSAKDLIGTHfmDG-MSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILI 195
Cdd:cd05064    63 FDHSNIVRLEGVITRGNTMMIVTEYMSNGALDSFLRKH--EGqLVAGQLMGMLPGLASGMKYLSEMGYVHKGLAAHKVLV 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 196 STDGKVYLSGLRsnlsmisHGQRQRAVHDFPKYSIK-VLPWLSPEVLQqnLQGYDAKSDIYSVGITACE-LANGHVPFKD 273
Cdd:cd05064   141 NSDLVCKISGFR-------RLQEDKSEAIYTTMSGKsPVLWAAPEAIQ--YHHFSSASDVWSFGIVMWEvMSYGERPYWD 211

                  .
gi 1958659070 274 M 274
Cdd:cd05064   212 M 212
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
61-271 7.16e-14

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK is also referred to as Rho-associated kinase or simply as Rho kinase. It contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain. It is activated via interaction with Rho GTPases and is involved in many cellular functions including contraction, adhesion, migration, motility, proliferation, and apoptosis. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Both isoforms are ubiquitously expressed in most tissues, but ROCK2 is more prominent in brain and skeletal muscle while ROCK1 is more pronounced in the liver, testes, and kidney. Studies in knockout mice result in different phenotypes, suggesting that the two isoforms do not compensate for each other during embryonic development. The ROCK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 72.41  E-value: 7.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKG-FEDlmtVNLARYKPTGEYVTVRRIN-LEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAV 138
Cdd:cd05596    28 FDVIKVIGRGaFGE---VQLVRHKSTKKVYAMKLLSkFEMIKRSDSAFFWEERDIMAHANSEWIVQLHYAFQDDKYLYMV 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 139 TSFMAYGSAKDLIGTHfmDGMSELAIAYILQGVLkALDYIHHMGYVHRSVKASHILISTDGKVYLSGLRSNLSMISHGQ- 217
Cdd:cd05596   105 MDYMPGGDLVNLMSNY--DVPEKWARFYTAEVVL-ALDAIHSMGFVHRDVKPDNMLLDASGHLKLADFGTCMKMDKDGLv 181
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958659070 218 RQRAVHDFPKYsikvlpwLSPEVLQ-QNLQG-YDAKSDIYSVGITACELANGHVPF 271
Cdd:cd05596   182 RSDTAVGTPDY-------ISPEVLKsQGGDGvYGRECDWWSVGVFLYEMLVGDTPF 230
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
63-293 9.47e-14

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


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 71.26  E-value: 9.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  63 LLSVIGKGfeDLMTVNLARYKP----TGEYVTVRRINLEACSNEMVTFlQGELHVSKLFSHPNIVPYR--ATFIADNELW 136
Cdd:cd05038     8 FIKQLGEG--HFGSVELCRYDPlgdnTGEQVAVKSLQPSGEEQHMSDF-KREIEILRTLDHEYIVKYKgvCESPGRRSLR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 137 AVTSFMAYGSAKDLIGTHFMDGMSELAIAYILQgVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSNLSMIS 214
Cdd:cd05038    85 LIMEYLPSGSLRDYLQRHRDQIDLKRLLLFASQ-ICKGMEYLGSQRYIHRDLAARNILVESEDLVKISdfGLAKVLPEDK 163
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958659070 215 HGQRQRAVHDFPKYsikvlpWLSPEVLQQNLqgYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPCLLD 293
Cdd:cd05038   164 EYYYVKEPGESPIF------WYAPECLRESR--FSSASDVWSFGVTLYELFTYGDPSQSPPALFLRMIGIAQGQMIVTR 234
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
61-273 1.00e-13

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: 70.86  E-value: 1.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKG-FEDlmtVNLARYKPTGEYVTVRRINLEACSNEMVTfLQGELHVSKLFSHPNIVPYRATFIADNELWAVT 139
Cdd:cd14083     5 YEFKEVLGTGaFSE---VVLAEDKATGKLVAIKCIDKKALKGKEDS-LENEIAVLRKIKHPNIVQLLDIYESKSHLYLVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 140 SFMAYGSAKDLI---GTHfmdgmSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILIST---DGKVYLSGLrsNLSMI 213
Cdd:cd14083    81 ELVTGGELFDRIvekGSY-----TEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYYSpdeDSKIMISDF--GLSKM 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 214 SHGQRQRAVHDFPKYsikvlpwLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKD 273
Cdd:cd14083   154 EDSGVMSTACGTPGY-------VAPEVLAQ--KPYGKAVDCWSIGVISYILLCGYPPFYD 204
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
61-379 1.20e-13

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type II; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. In addition, CaMKII contains a C-terminal association domain that facilitates oligomerization. There are four CaMKII proteins (alpha, beta, gamma, delta) encoded by different genes; each gene undergoes alternative splicing to produce more than 30 isoforms. CaMKII-alpha and -beta are enriched in neurons while CaMKII-gamma and -delta are predominant in myocardium. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. It is a major component of the postsynaptic density and is critical in regulating synaptic plasticity including long-term potentiation. It is critical in regulating ion channels and proteins involved in myocardial excitation-contraction and excitation-transcription coupling. Excessive CaMKII activity promotes processes that contribute to heart failure and arrhythmias. The CaMKII subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 70.91  E-value: 1.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTS 140
Cdd:cd14086     3 YDLKEELGKG--AFSVVRRCVQKSTGQEFAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 141 FMAYGSA-KDLIGTHFMdgmSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGK---VYLSGLrsNLSMISHG 216
Cdd:cd14086    81 LVTGGELfEDIVAREFY---SEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSKgaaVKLADF--GLAIEVQG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 217 QrQRAVHDF---PKYsikvlpwLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVpclld 293
Cdd:cd14086   156 D-QQAWFGFagtPGY-------LSPEVLRK--DPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAY----- 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 294 tstipaeeltmspsrsianpglndslaagslrpangDSPShPYHRTFSPHFHNFVEQCLQRNPDARPNASTLLNHSFFKQ 373
Cdd:cd14086   221 ------------------------------------DYPS-PEWDTVTPEAKDLINQMLTVNPAKRITAAEALKHPWICQ 263

                  ....*.
gi 1958659070 374 IKRRAS 379
Cdd:cd14086   264 RDRVAS 269
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
62-275 1.27e-13

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


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 70.46  E-value: 1.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  62 ELLSVIGKG-FEDLMtvnLARYKptGEYVTVRRINleaCSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTS 140
Cdd:cd05039     9 KLGELIGKGeFGDVM---LGDYR--GQKVAVKCLK---DDSTAAQAFLAEASVMTTLRHPNLVQLLGVVLEGNGLYIVTE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 141 FMAYGSAKDLI---GTHFMDGMSELAIAYilqGVLKALDYIHHMGYVHRSVKASHILISTDG--KVYLSGLrsnlsmish 215
Cdd:cd05039    81 YMAKGSLVDYLrsrGRAVITRKDQLGFAL---DVCEGMEYLESKKFVHRDLAARNVLVSEDNvaKVSDFGL--------- 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958659070 216 GQRQRAVHDFPKYSIKvlpWLSPEVLQQNLqgYDAKSDIYSVGITACEL-ANGHVPFKDMP 275
Cdd:cd05039   149 AKEASSNQDGGKLPIK---WTAPEALREKK--FSTKSDVWSFGILLWEIySFGRVPYPRIP 204
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
110-375 1.61e-13

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


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 70.44  E-value: 1.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 110 ELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGSAKDLIgTHFMDG---MSELAI-AYILQgVLKALDYIHHMGYVH 185
Cdd:cd08228    52 EIDLLKQLNHPNVIKYLDSFIEDNELNIVLELADAGDLSQMI-KYFKKQkrlIPERTVwKYFVQ-LCSAVEHMHSRRVMH 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 186 RSVKASHILISTDGKVYLSGLRSNLSMISHGQRQRAVHDFPKYsikvlpwLSPEVLQQNlqGYDAKSDIYSVGITACELA 265
Cdd:cd08228   130 RDIKPANVFITATGVVKLGDLGLGRFFSSKTTAAHSLVGTPYY-------MSPERIHEN--GYNFKSDIWSLGCLLYEMA 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 266 NGHVPFKDmpatqmllEKLNGTVPClldtstipaeeltmspsrsianpglndslaagsLRPANGDSPSHPYHRtFSPHFH 345
Cdd:cd08228   201 ALQSPFYG--------DKMNLFSLC---------------------------------QKIEQCDYPPLPTEH-YSEKLR 238
                         250       260       270
                  ....*....|....*....|....*....|
gi 1958659070 346 NFVEQCLQRNPDARPNASTLlnHSFFKQIK 375
Cdd:cd08228   239 ELVSMCIYPDPDQRPDIGYV--HQIAKQMH 266
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
107-371 1.88e-13

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


Pssm-ID: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 69.89  E-value: 1.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 107 LQGELHVSKLFSHPNIV--------PYratfiaDNELWAVTSFMAYGSAKDLIGTHFMDGMSELAIAYILQGVLKALDYI 178
Cdd:cd14008    51 VRREIAIMKKLDHPNIVrlyeviddPE------SDKLYLVLEYCEGGPVMELDSGDRVPPLPEETARKYFRDLVLGLEYL 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 179 HHMGYVHRSVKASHILISTDGKVYLS--GlrsnlsmISHgqrqrAVHDFPKYSIKVL--P-WLSPEVLQQNLQGYDAK-S 252
Cdd:cd14008   125 HENGIVHRDIKPENLLLTADGTVKISdfG-------VSE-----MFEDGNDTLQKTAgtPaFLAPELCDGDSKTYSGKaA 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 253 DIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPclldtstipaeeltmspsrsianpglndslaagslrpangdsp 332
Cdd:cd14008   193 DIWALGVTLYCLVFGRLPFNGDNILELYEAIQNQNDE------------------------------------------- 229
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1958659070 333 sHPYHRTFSPHFHNFVEQCLQRNPDARPNASTLLNHSFF 371
Cdd:cd14008   230 -FPIPPELSPELKDLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
61-275 2.52e-13

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


Pssm-ID: 270993 [Multi-domain]  Cd Length: 291  Bit Score: 69.97  E-value: 2.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTG-EY-VTVRRINLEACSNEMVTFLqgelhvsKLFSHPNIVPYRATFIADNELWAV 138
Cdd:cd14091     2 YEIKEEIGKG--SYSVCKRCIHKATGkEYaVKIIDKSKRDPSEEIEILL-------RYGQHPNIITLRDVYDDGNSVYLV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 139 TSFMAYGSAKDLI--GTHFmdgmSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDgkvylSGLRSNLSMISHG 216
Cdd:cd14091    73 TELLRGGELLDRIlrQKFF----SEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADE-----SGDPESLRICDFG 143
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958659070 217 --QRQRAVHDF---PKYSIKvlpWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMP 275
Cdd:cd14091   144 faKQLRAENGLlmtPCYTAN---FVAPEVLKK--QGYDAACDIWSLGVLLYTMLAGYTPFASGP 202
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
61-286 2.98e-13

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


Pssm-ID: 270973 [Multi-domain]  Cd Length: 253  Bit Score: 69.34  E-value: 2.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTS 140
Cdd:cd14071     2 YDIERTIGKG--NFAVVKLARHRITKTEVAIKIIDKSQLDEENLKKIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVTE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 141 FMAYGSAKDLIGTHfmDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLR-SNLsmISHGQRQ 219
Cdd:cd14071    80 YASNGEIFDYLAQH--GRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGfSNF--FKPGELL 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958659070 220 RAVHDFPkysikvlPWLSPEVLQQnlQGYDA-KSDIYSVGITACELANGHVPFkDMPATQMLLEK-LNG 286
Cdd:cd14071   156 KTWCGSP-------PYAAPEVFEG--KEYEGpQLDIWSLGVVLYVLVCGALPF-DGSTLQTLRDRvLSG 214
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
61-265 3.15e-13

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


Pssm-ID: 270859 [Multi-domain]  Cd Length: 256  Bit Score: 69.38  E-value: 3.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTS 140
Cdd:cd08220     2 YEKIRVVGRG--AYGTVYLCRRKDDNKLVIIKQIPVEQMTKEERQAALNEVKVLSMLHHPNIIEYYESFLEDKALMIVME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 141 FMAYGSAKDLIGTHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLRSNLSMISHGQRQR 220
Cdd:cd08220    80 YAPGGTLFEYIQQRKGSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTVVKIGDFGISKILSSKSKAY 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1958659070 221 AVHDFPKYsikvlpwLSPEVLQQnlQGYDAKSDIYSVGITACELA 265
Cdd:cd08220   160 TVVGTPCY-------ISPELCEG--KPYNQKSDIWALGCVLYELA 195
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
61-371 3.35e-13

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: 69.76  E-value: 3.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRInLEACSNEMVTFLQ-GELHVSKLFSHPNIVPYRATFIADNELWAVT 139
Cdd:cd07846     3 YENLGLVGEG--SYGMVMKCRHKETGQIVAIKKF-LESEDDKMVKKIAmREIKMLKQLRHENLVNLIEVFRRKKRWYLVF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 140 SFMAYGSAKDLigTHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLRSNLSMISHGQrq 219
Cdd:cd07846    80 EFVDHTVLDDL--EKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGE-- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 220 ravhDFPKYsIKVLPWLSPEVLQQNLQgYDAKSDIYSVGITACELANGHVPFkdmPATQMlLEKLNGTVPCLldTSTIPA 299
Cdd:cd07846   156 ----VYTDY-VATRWYRAPELLVGDTK-YGKAVDVWAVGCLVTEMLTGEPLF---PGDSD-IDQLYHIIKCL--GNLIPR 223
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958659070 300 EELTMSPSRSIANPGLNDSLAAGSLRpangdsPSHPyhrTFSPHFHNFVEQCLQRNPDARPNASTLLNHSFF 371
Cdd:cd07846   224 HQELFQKNPLFAGVRLPEVKEVEPLE------RRYP---KLSGVVIDLAKKCLHIDPDKRPSCSELLHHEFF 286
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
61-371 4.07e-13

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


Pssm-ID: 270831 [Multi-domain]  Cd Length: 287  Bit Score: 69.23  E-value: 4.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSK---LFSHPNIVpyratfiadnELWA 137
Cdd:cd07838     1 YEEVAEIGEG--AYGTVYKARDLQDGRFVALKKVRVPLSEEGIPLSTIREIALLKqleSFEHPNVV----------RLLD 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 138 VTSFMAYGSAKD--LIGTH-------FMD-----GMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYL 203
Cdd:cd07838    69 VCHGPRTDRELKltLVFEHvdqdlatYLDkcpkpGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 204 S--GLRSnlsmishgqrqraVHDF--PKYSIKVLPWL-SPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQ 278
Cdd:cd07838   149 AdfGLAR-------------IYSFemALTSVVVTLWYrAPEVLLQ--SSYATPVDMWSVGCIFAELFNRRPLFRGSSEAD 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 279 MLLEklngtvpcLLDTSTIPAEEltMSPsrsianpgLNDSLAAGSLRPANGDSPSHPYhRTFSPHFHNFVEQCLQRNPDA 358
Cdd:cd07838   214 QLGK--------IFDVIGLPSEE--EWP--------RNSALPRSSFPSYTPRPFKSFV-PEIDEEGLDLLKKMLTFNPHK 274
                         330
                  ....*....|...
gi 1958659070 359 RPNASTLLNHSFF 371
Cdd:cd07838   275 RISAFEALQHPYF 287
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
67-264 4.56e-13

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: 69.20  E-value: 4.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  67 IGKGFedLMTVNLARYKPTGEYVTVRRinLEACSNE-MVTFLQgELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYG 145
Cdd:cd14222     1 LGKGF--FGQAIKVTHKATGKVMVMKE--LIRCDEEtQKTFLT-EVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 146 SAKDLIGThfMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLrsNLSMISHGQRQRAVHDF 225
Cdd:cd14222    76 TLKDFLRA--DDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADF--GLSRLIVEEKKKPPPDK 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958659070 226 P--------------KYSIKVLP-WLSPEVLqqNLQGYDAKSDIYSVGITACEL 264
Cdd:cd14222   152 PttkkrtlrkndrkkRYTVVGNPyWMAPEML--NGKSYDEKVDIFSFGIVLCEI 203
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
61-273 5.62e-13

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


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 68.47  E-value: 5.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVtflQGELHVSKLFSHPNIVPYRATFIADNELWAVts 140
Cdd:cd14665     2 YELVKDIGSG--NFGVARLMRDKQTKELVAVKYIERGEKIDENV---QREIINHRSLRHPNIVRFKEVILTPTHLAIV-- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 141 fMAYGSAKDLIGTHFMDG-MSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILIstDGKVylsglRSNLSMISHGQRQ 219
Cdd:cd14665    75 -MEYAAGGELFERICNAGrFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLL--DGSP-----APRLKICDFGYSK 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958659070 220 RAV-HDFPKYSIKVLPWLSPEVLQQnlQGYDAK-SDIYSVGITACELANGHVPFKD 273
Cdd:cd14665   147 SSVlHSQPKSTVGTPAYIAPEVLLK--KEYDGKiADVWSCGVTLYVMLVGAYPFED 200
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
52-293 5.76e-13

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Heme-Regulated Inhibitor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HRI (or EIF2AK1) contains an N-terminal regulatory heme-binding domain and a C-terminal catalytic kinase domain. It is suppressed under normal conditions by binding of the heme iron, and is activated during heme deficiency. It functions as a critical regulator that ensures balanced synthesis of globins and heme, in order to form stable hemoglobin during erythroid differentiation and maturation. HRI also protects cells and enhances survival under iron-deficient conditions. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The HRI subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270951 [Multi-domain]  Cd Length: 284  Bit Score: 69.07  E-value: 5.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  52 SSFLPEggcYELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIA 131
Cdd:cd14049     2 SRYLNE---FEEIARLGKG--GYGKVYKVRNKLDGQYYAIKKILIKKVTKRDCMKVLREVKVLAGLQHPNIVGYHTAWME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 132 DNEL---------------WAVTS---FMAYGSAKDLIGTHFMDgmselAIAYILQGVLKALDYIHHMGYVHRSVKASHI 193
Cdd:cd14049    77 HVQLmlyiqmqlcelslwdWIVERnkrPCEEEFKSAPYTPVDVD-----VTTKILQQLLEGVTYIHSMGIVHRDLKPRNI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 194 LIS-TDGKVYLS--GLR-SNLSMISHGQRQRAVHDFPKYSIKVLPWL--SPEVLQQNlqGYDAKSDIYSVGITACELang 267
Cdd:cd14049   152 FLHgSDIHVRIGdfGLAcPDILQDGNDSTTMSRLNGLTHTSGVGTCLyaAPEQLEGS--HYDFKSDMYSIGVILLEL--- 226
                         250       260
                  ....*....|....*....|....*..
gi 1958659070 268 HVPF-KDMPATQMLLEKLNGTVPCLLD 293
Cdd:cd14049   227 FQPFgTEMERAEVLTQLRNGQIPKSLC 253
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
61-370 6.43e-13

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


Pssm-ID: 270912 [Multi-domain]  Cd Length: 269  Bit Score: 68.47  E-value: 6.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRInlEACSNEMVTflqGELHVSKLFSHPNIVPYRATFIADNELWAVTS 140
Cdd:cd14010     2 YVLYDEIGRG--KHSVVYKGRRKGTIEFVAIKCV--DKSKRPEVL---NEVRLTHELKHPNVLKFYEWYETSNHLWLVVE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 141 FMAYGSAKDLIGTHfmDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSG----------LRSNL 210
Cdd:cd14010    75 YCTGGDLETLLRQD--GNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDfglarregeiLKELF 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 211 SMISHGQRQRAVHDfpKYSIKVLP-WLSPEVLQQNLQGYDakSDIYSVGITACELANGHVPFKDMPATQmLLEKlngtvp 289
Cdd:cd14010   153 GQFSDEGNVNKVSK--KQAKRGTPyYMAPELFQGGVHSFA--SDLWALGCVLYEMFTGKPPFVAESFTE-LVEK------ 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 290 clldtstIPAEELTMSPSRSIANPglndslaagslrpangdspshpyhrtfSPHFHNFVEQCLQRNPDARPNASTLLNHS 369
Cdd:cd14010   222 -------ILNEDPPPPPPKVSSKP---------------------------SPDFKSLLKGLLEKDPAKRLSWDELVKHP 267

                  .
gi 1958659070 370 F 370
Cdd:cd14010   268 F 268
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
119-276 7.83e-13

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


Pssm-ID: 271077 [Multi-domain]  Cd Length: 291  Bit Score: 68.52  E-value: 7.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 119 HPNIVPYRATFIADNELWAVTSFMAYGSAKDLIGTHFMdgMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTD 198
Cdd:cd14175    54 HPNIITLKDVYDDGKHVYLVTELMRGGELLDKILRQKF--FSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYVDE 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 199 gkvylSGLRSNLSMISHG--QRQRAVHDF---PKYSIKvlpWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKD 273
Cdd:cd14175   132 -----SGNPESLRICDFGfaKQLRAENGLlmtPCYTAN---FVAPEVLKR--QGYDEGCDIWSLGILLYTMLAGYTPFAN 201

                  ...
gi 1958659070 274 MPA 276
Cdd:cd14175   202 GPS 204
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
58-271 9.27e-13

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 69.82  E-value: 9.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  58 GGCYELLSVIGKG-------FEDL----------MTVNLARyKPTgeyvTVRRINLEACSnemvtflqgelhVSKLfSHP 120
Cdd:NF033483    6 GGRYEIGERIGRGgmaevylAKDTrldrdvavkvLRPDLAR-DPE----FVARFRREAQS------------AASL-SHP 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 121 NIV-----------PYratfIAdnelwavtsfMAY--GSA-KDLIGTHFMdgMSELAIAYILQGVLKALDYIHHMGYVHR 186
Cdd:NF033483   68 NIVsvydvgedggiPY----IV----------MEYvdGRTlKDYIREHGP--LSPEEAVEIMIQILSALEHAHRNGIVHR 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 187 SVKASHILISTDGKV---------YLSGlrSNL----SMIshGqrqrAVHdfpkYsikvlpwLSPEvlqQNLQGY-DAKS 252
Cdd:NF033483  132 DIKPQNILITKDGRVkvtdfgiarALSS--TTMtqtnSVL--G----TVH----Y-------LSPE---QARGGTvDARS 189
                         250
                  ....*....|....*....
gi 1958659070 253 DIYSVGITACELANGHVPF 271
Cdd:NF033483  190 DIYSLGIVLYEMLTGRPPF 208
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
61-370 1.20e-12

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


Pssm-ID: 270861 [Multi-domain]  Cd Length: 260  Bit Score: 67.45  E-value: 1.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKG-FEDLMTVNLARYKPTGEYVTVRRINL-EACSNEMVtflqGELHVSKLFS---HPNIVPYRATFIADNEL 135
Cdd:cd08222     2 YRVVRKLGSGnFGTVYLVSDLKATADEELKVLKEISVgELQPDETV----DANREAKLLSkldHPAIVKFHDSFVEKESF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 136 WAVTSFMAYGSAKDLIGTHFMDGM---SELAIAYILQgVLKALDYIHHMGYVHRSVKASHIListdgkvylsgLRSNL-- 210
Cdd:cd08222    78 CIVTEYCEGGDLDDKISEYKKSGTtidENQILDWFIQ-LLLAVQYMHERRILHRDLKAKNIF-----------LKNNVik 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 211 ------SMISHGQRQRAVhDF---PKYsikvlpwLSPEVLQQnlQGYDAKSDIYSVGITACELanghvpfkdmpatqmll 281
Cdd:cd08222   146 vgdfgiSRILMGTSDLAT-TFtgtPYY-------MSPEVLKH--EGYNSKSDIWSLGCILYEM----------------- 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 282 eklngtvpCLLDTSTIPAeeltmspsrsianpglndSLAAGSLRPANGDSPSHPYHrtFSPHFHNFVEQCLQRNPDARPN 361
Cdd:cd08222   199 --------CCLKHAFDGQ------------------NLLSVMYKIVEGETPSLPDK--YSKELNAIYSRMLNKDPALRPS 250

                  ....*....
gi 1958659070 362 ASTLLNHSF 370
Cdd:cd08222   251 AAEILKIPF 259
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
63-279 1.53e-12

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


Pssm-ID: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 67.73  E-value: 1.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  63 LLSVIGKGfeDLMTVNLARYKP----TGEYVTVRRinLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIA--DNELW 136
Cdd:cd14205     8 FLQQLGKG--NFGSVEMCRYDPlqdnTGEVVAVKK--LQHSTEEHLRDFEREIEILKSLQHDNIVKYKGVCYSagRRNLR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 137 AVTSFMAYGSAKDLIGTHfMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSNLSMIS 214
Cdd:cd14205    84 LIMEYLPYGSLRDYLQKH-KERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGdfGLTKVLPQDK 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958659070 215 HGQRQRAVHDFPKYsikvlpWLSPEVLQQNlqGYDAKSDIYSVGITACELANGHVPFKDMPATQM 279
Cdd:cd14205   163 EYYKVKEPGESPIF------WYAPESLTES--KFSVASDVWSFGVVLYELFTYIEKSKSPPAEFM 219
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
85-276 1.73e-12

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


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 67.38  E-value: 1.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  85 TGEYVTVRRINLEACSNEM---VTFLQGELHVSKLFSHPNIVPYRAtFIADNELWAVTSFMAY---GSAKDLIGTHfmDG 158
Cdd:cd06652    26 TGRELAVKQVQFDPESPETskeVNALECEIQLLKNLLHERIVQYYG-CLRDPQERTLSIFMEYmpgGSIKDQLKSY--GA 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 159 MSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSNLSMIS-HGQRQRAVHDFPKysikvlpW 235
Cdd:cd06652   103 LTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGdfGASKRLQTIClSGTGMKSVTGTPY-------W 175
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1958659070 236 LSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPA 276
Cdd:cd06652   176 MSPEVISG--EGYGRKADIWSVGCTVVEMLTEKPPWAEFEA 214
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
61-271 2.00e-12

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK1 is preferentially expressed in the liver, lung, spleen, testes, and kidney. It mediates signaling from Rho to the actin cytoskeleton. It is implicated in the development of cardiac fibrosis, cardiomyocyte apoptosis, and hyperglycemia. Mice deficient with ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 68.49  E-value: 2.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRIN-LEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVT 139
Cdd:cd05622    75 YEVVKVIGRG--AFGEVQLVRHKSTRKVYAMKLLSkFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVM 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 140 SFMAYGSAKDLIGTHfmDGMSELAIAYILQGVLkALDYIHHMGYVHRSVKASHILISTDGKVYLSGLRSNLSMISHGQ-R 218
Cdd:cd05622   153 EYMPGGDLVNLMSNY--DVPEKWARFYTAEVVL-ALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMvR 229
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958659070 219 QRAVHDFPKYsikvlpwLSPEVLQ-QNLQGYDAKS-DIYSVGITACELANGHVPF 271
Cdd:cd05622   230 CDTAVGTPDY-------ISPEVLKsQGGDGYYGREcDWWSVGVFLYEMLVGDTPF 277
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
119-275 2.47e-12

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


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 67.35  E-value: 2.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 119 HPNIVPYRATFIADNELWAVTSFMAYGSAKDLIGTHfmDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTD 198
Cdd:cd14177    57 HPNIITLKDVYDDGRYVYLVTELMKGGELLDRILRQ--KFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDD 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 199 gkvylSGLRSNLSMISHGQRQRAVHD-----FPKYSIKvlpWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKD 273
Cdd:cd14177   135 -----SANADSIRICDFGFAKQLRGEnglllTPCYTAN---FVAPEVLMR--QGYDAACDIWSLGVLLYTMLAGYTPFAN 204

                  ..
gi 1958659070 274 MP 275
Cdd:cd14177   205 GP 206
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
61-273 2.56e-12

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: 66.59  E-value: 2.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKG-FEDLMtvnLARYKPTGEYVTVRRINLEACSNEMvTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVT 139
Cdd:cd14167     5 YDFREVLGTGaFSEVV---LAEEKRTQKLVAIKCIAKKALEGKE-TSIENEIAVLHKIKHPNIVALDDIYESGGHLYLIM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 140 SFMAYGSAKDLIGTHFMdgMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHIL---ISTDGKVYLSGLrsNLSMIS-H 215
Cdd:cd14167    81 QLVSGGELFDRIVEKGF--YTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDF--GLSKIEgS 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958659070 216 GQRQRAVHDFPKYsikvlpwLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKD 273
Cdd:cd14167   157 GSVMSTACGTPGY-------VAPEVLAQ--KPYSKAVDCWSIGVIAYILLCGYPPFYD 205
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
85-276 2.92e-12

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


Pssm-ID: 270819 [Multi-domain]  Cd Length: 264  Bit Score: 66.59  E-value: 2.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  85 TGEYVTVRRINLEACSNEM---VTFLQGELHVSKLFSHPNIVPYRATfIADNE---LWAVTSFMAYGSAKDLIGTH--FM 156
Cdd:cd06653    26 TGRELAVKQVPFDPDSQETskeVNALECEIQLLKNLRHDRIVQYYGC-LRDPEekkLSIFVEYMPGGSVKDQLKAYgaLT 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 157 DGMSELAIAYILQGVlkalDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSNLSMIS-HGQRQRAVHDFPKysikvl 233
Cdd:cd06653   105 ENVTRRYTRQILQGV----SYLHSNMIVHRDIKGANILRDSAGNVKLGdfGASKRIQTICmSGTGIKSVTGTPY------ 174
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1958659070 234 pWLSPEVLqqNLQGYDAKSDIYSVGITACELANGHVPFKDMPA 276
Cdd:cd06653   175 -WMSPEVI--SGEGYGRKADVWSVACTVVEMLTEKPPWAEYEA 214
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
66-370 3.83e-12

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


Pssm-ID: 270794 [Multi-domain]  Cd Length: 268  Bit Score: 66.28  E-value: 3.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  66 VIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNemVTFLQGELHVSKLFSHPNIVPYRATFIADNelwAVTSFMAY- 144
Cdd:cd06624    15 VLGKG--TFGVVYAARDLSTQVRIAIKEIPERDSRE--VQPLHEEIALHSRLSHKNIVQYLGSVSEDG---FFKIFMEQv 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 145 --GSAKDLIGTHF---MDgmSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTdgkvYLSGLRsnLSMISHGQRQ 219
Cdd:cd06624    88 pgGSLSALLRSKWgplKD--NENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNT----YSGVVK--ISDFGTSKRL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 220 RAVHDFPKYSIKVLPWLSPEVLQQNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKlngtVPCLLDTSTIPa 299
Cdd:cd06624   160 AGINPCTETFTGTLQYMAPEVIDKGQRGYGPPADIWSLGCTIIEMATGKPPFIELGEPQAAMFK----VGMFKIHPEIP- 234
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958659070 300 eeltmspsrsianpglnDSLaagslrpangdspshpyhrtfSPHFHNFVEQCLQRNPDARPNASTLLNHSF 370
Cdd:cd06624   235 -----------------ESL---------------------SEEAKSFILRCFEPDPDKRATASDLLQDPF 267
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
82-281 4.44e-12

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: 66.14  E-value: 4.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  82 YK---PTGEYVTVRRINLEACsNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGSAKDLIGTHF--- 155
Cdd:cd14066    10 YKgvlENGTVVAVKRLNEMNC-AASKKEFLTELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPNGSLEDRLHCHKgsp 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 156 -MDGMSELAIAyilQGVLKALDYIHHMGY---VHRSVKASHILISTDG--KVYLSGLRSNLSMISHGQRQRAVHdfpkys 229
Cdd:cd14066    89 pLPWPQRLKIA---KGIARGLEYLHEECPppiIHGDIKSSNILLDEDFepKLTDFGLARLIPPSESVSKTSAVK------ 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958659070 230 iKVLPWLSPEVLQQNLqgYDAKSDIYSVGITACELANGHVPFKDMPATQMLL 281
Cdd:cd14066   160 -GTIGYLAPEYIRTGR--VSTKSDVYSFGVVLLELLTGKPAVDENRENASRK 208
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
128-271 6.01e-12

Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The DMPK-like subfamily is composed of DMPK and DMPK-related cell division control protein 42 (Cdc42) binding kinase (MRCK). DMPK is expressed in skeletal and cardiac muscles, and in central nervous tissues. The functional role of DMPK is not fully understood. It may play a role in the signal transduction and homeostasis of calcium. The DMPK gene is implicated in myotonic dystrophy 1 (DM1), an inherited multisystemic disorder with symptoms that include muscle hyperexcitability, progressive muscle weakness and wasting, cataract development, testicular atrophy, and cardiac conduction defects. The genetic basis for DM1 is the mutational expansion of a CTG repeat in the 3'-UTR of DMPK. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. The DMPK-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: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 66.22  E-value: 6.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 128 TFIADNELWAVtsfMAYGSAKDLIG--THFMDGMSE-LAIAYILQGVLkALDYIHHMGYVHRSVKASHILISTDGKVYLS 204
Cdd:cd05597    69 AFQDENYLYLV---MDYYCGGDLLTllSKFEDRLPEeMARFYLAEMVL-AIDSIHQLGYVHRDIKPDNVLLDRNGHIRLA 144
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 205 GLRSNLSMISHGQRQRAVhdfpkySIKVLPWLSPEVLQQNLQG---YDAKSDIYSVGITACELANGHVPF 271
Cdd:cd05597   145 DFGSCLKLREDGTVQSSV------AVGTPDYISPEILQAMEDGkgrYGPECDWWSLGVCMYEMLYGETPF 208
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
61-371 6.35e-12

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


Pssm-ID: 270826 [Multi-domain]  Cd Length: 287  Bit Score: 65.81  E-value: 6.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGFEDLmtVNLARYKPTGEYVTVRRI---NLEAC-SNEM---VTFLQgelhvsKLFSHPNIVPYRATFIADN 133
Cdd:cd07832     2 YKILGRIGEGAHGI--VFKAKDRETGETVALKKValrKLEGGiPNQAlreIKALQ------ACQGHPYVVKLRDVFPHGT 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 134 ELWAVTSFMAyGSAKDLIGtHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLRSNLSMI 213
Cdd:cd07832    74 GFVLVFEYML-SSLSEVLR-DEERPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLARLFS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 214 SHGQRQravhdfpkYSIKV--LPWLSPEVLQQNlQGYDAKSDIYSVGITACELANGHVPF---KDMpatqmllEKLNgtv 288
Cdd:cd07832   152 EEDPRL--------YSHQVatRWYRAPELLYGS-RKYDEGVDLWAVGCIFAELLNGSPLFpgeNDI-------EQLA--- 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 289 pCLLDTSTIPAEELTmspsrsianPGLNDSLAAGSLRPANgdSPSHPYHRTF---SPHFHNFVEQCLQRNPDARPNASTL 365
Cdd:cd07832   213 -IVLRTLGTPNEKTW---------PELTSLPDYNKITFPE--SKGIRLEEIFpdcSPEAIDLLKGLLVYNPKKRLSAEEA 280

                  ....*.
gi 1958659070 366 LNHSFF 371
Cdd:cd07832   281 LRHPYF 286
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
67-270 7.83e-12

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: 65.20  E-value: 7.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  67 IGKGFedLMTVNLARYKPTGEyVTVRRINLEacSNEMVTFLQgELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGS 146
Cdd:cd14065     1 LGKGF--FGEVYKVTHRETGK-VMVMKELKR--FDEQRSFLK-EVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 147 AKDLIGTHfMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILIStdgkvylsglrsnlsmISHGQRQRAVHDF- 225
Cdd:cd14065    75 LEELLKSM-DEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVR----------------EANRGRNAVVADFg 137
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958659070 226 ----------------PKYSIKVLP-WLSPEVLQQNLqgYDAKSDIYSVGITACELAnGHVP 270
Cdd:cd14065   138 larempdektkkpdrkKRLTVVGSPyWMAPEMLRGES--YDEKVDVFSFGIVLCEII-GRVP 196
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
119-275 8.18e-12

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


Pssm-ID: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 66.20  E-value: 8.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 119 HPNIVPYRATFIADNELWAVTSFMAYGSAKDLIGTHFMdgMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTD 198
Cdd:cd14176    72 HPNIITLKDVYDDGKYVYVVTELMKGGELLDKILRQKF--FSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDE 149
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958659070 199 gkvylSGLRSNLSMISHG--QRQRAVHDFPKYSIKVLPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMP 275
Cdd:cd14176   150 -----SGNPESIRICDFGfaKQLRAENGLLMTPCYTANFVAPEVLER--QGYDAACDIWSLGVLLYTMLTGYTPFANGP 221
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
67-305 1.03e-11

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: 65.02  E-value: 1.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  67 IGKGFEDLMTVNLARYKPTGEYVTV---RRINLEACSNEMVTFLQGELHVSKLFSHPNIVP---YRATFIAdnELWAVts 140
Cdd:cd13994     1 IGKGATSVVRIVTKKNPRSGVLYAVkeyRRRDDESKRKDYVKRLTSEYIISSKLHHPNIVKvldLCQDLHG--KWCLV-- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 141 fMAYGSAKDLIgTHFMDGMS---ELAIAYILQgVLKALDYIHHMGYVHRSVKASHILISTDGkvylsglrsNLSMISHG- 216
Cdd:cd13994    77 -MEYCPGGDLF-TLIEKADSlslEEKDCFFKQ-ILRGVAYLHSHGIAHRDLKPENILLDEDG---------VLKLTDFGt 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 217 --QRQRAVHDFPKYSIKV---LPWLSPEVLQQNlqGYDAKS-DIYSVGITACELANGHVPFKD--------MPATQMLLE 282
Cdd:cd13994   145 aeVFGMPAEKESPMSAGLcgsEPYMAPEVFTSG--SYDGRAvDVWSCGIVLFALFTGRFPWRSakksdsayKAYEKSGDF 222
                         250       260
                  ....*....|....*....|...
gi 1958659070 283 KLNGTVPCLLDTSTIpAEELTMS 305
Cdd:cd13994   223 TNGPYEPIENLLPSE-CRRLIYR 244
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
77-366 1.06e-11

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


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 64.92  E-value: 1.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  77 VNLARYKP----TGEYVTVRRINLEaCSNEMVTFLQGELHVSKLFSHPNIVPYRA--TFIADNELWAVTSFMAYGSAKDL 150
Cdd:cd05080    20 VSLYCYDPtndgTGEMVAVKALKAD-CGPQHRSGWKQEIDILKTLYHENIVKYKGccSEQGGKSLQLIMEYVPLGSLRDY 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 151 IGTHFMdGMSELAIayILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSNLSMISHGQRQRAVHDFPKY 228
Cdd:cd05080    99 LPKHSI-GLAQLLL--FAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGdfGLAKAVPEGHEYYRVREDGDSPVF 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 229 sikvlpWLSPEVLQQNLQGYdaKSDIYSVGITACELANgHVPFKDMPATQMlleklngtvpclldtstipaEELTMSPSR 308
Cdd:cd05080   176 ------WYAPECLKEYKFYY--ASDVWSFGVTLYELLT-HCDSSQSPPTKF--------------------LEMIGIAQG 226
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958659070 309 SIANPGLNDSLAAGSLRPANGDSPSHPYHrtfsphfhnFVEQCLQRNPDARPNASTLL 366
Cdd:cd05080   227 QMTVVRLIELLERGERLPCPDKCPQEVYH---------LMKNCWETEASFRPTFENLI 275
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
61-373 1.12e-11

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


Pssm-ID: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 64.94  E-value: 1.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGFEDLmtVNLARYKPTGEYVTVRRINLEAcSNEMVTFLQGELH---------VSKLFSHPNIVPYRATFIA 131
Cdd:cd14182     5 YEPKEILGRGVSSV--VRRCIHKPTRQEYAVKIIDITG-GGSFSPEEVQELReatlkeidiLRKVSGHPNIIQLKDTYET 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 132 DNELWAVTSFMAYGSAKDLIGTHFMdgMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLRSNLS 211
Cdd:cd14182    82 NTFFFLVFDLMKKGELFDYLTEKVT--LSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFSCQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 212 mISHGQRQRAVHDFPKYsikvlpwLSPEVLQ----QNLQGYDAKSDIYSVGITACELANGHVPFkdMPATQMLLEKlngt 287
Cdd:cd14182   160 -LDPGEKLREVCGTPGY-------LAPEIIEcsmdDNHPGYGKEVDMWSTGVIMYTLLAGSPPF--WHRKQMLMLR---- 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 288 vpclldtstipaeeLTMSPSRSIANPGLNDslaagslrpangdspshpyhrtFSPHFHNFVEQCLQRNPDARPNASTLLN 367
Cdd:cd14182   226 --------------MIMSGNYQFGSPEWDD----------------------RSDTVKDLISRFLVVQPQKRYTAEEALA 269

                  ....*.
gi 1958659070 368 HSFFKQ 373
Cdd:cd14182   270 HPFFQQ 275
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
60-285 1.28e-11

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


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 64.70  E-value: 1.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  60 CYELLSVIGKG-FEDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLqGELHVSKLFSHPNIVPYRATFIADNELWAV 138
Cdd:cd05033     5 YVTIEKVIGGGeFGEVCSGSLKLPGKKEIDVAIKTLKSGYSDKQRLDFL-TEASIMGQFDHPNVIRLEGVVTKSRPVMIV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 139 TSFMAYGSAKDLIGTHfmDG-MSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTD--GKVylsglrSNLSMISH 215
Cdd:cd05033    84 TEYMENGSLDKFLREN--DGkFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDlvCKV------SDFGLSRR 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958659070 216 GQRQRAVHDFPKYSIKVLpWLSPEVLQqnLQGYDAKSDIYSVGITACE-LANGHVPFKDMPaTQMLLEKLN 285
Cdd:cd05033   156 LEDSEATYTTKGGKIPIR-WTAPEAIA--YRKFTSASDVWSFGIVMWEvMSYGERPYWDMS-NQDVIKAVE 222
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
61-370 1.57e-11

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


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 64.06  E-value: 1.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKG-FEDLMtvnLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVt 139
Cdd:cd08218     2 YVRIKKIGEGsFGKAL---LVKSKEDGKQYVIKEINISKMSPKEREESRKEVAVLSKMKHPNIVQYQESFEENGNLYIV- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 140 sfMAYGSAKDLI-------GTHFMDgmsELAIAYILQGVLkALDYIHHMGYVHRSVKASHILISTDGKVYLSGLRSNLSM 212
Cdd:cd08218    78 --MDYCDGGDLYkrinaqrGVLFPE---DQILDWFVQLCL-ALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARVL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 213 ISHGQRQRAVHDFPKYsikvlpwLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPCLl 292
Cdd:cd08218   152 NSTVELARTCIGTPYY-------LSPEICEN--KPYNNKSDIWALGCVLYEMCTLKHAFEAGNMKNLVLKIIRGSYPPV- 221
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958659070 293 dtstipaeeltmspsrsianpglndslaagslrpangdsPSHpyhrtFSPHFHNFVEQCLQRNPDARPNASTLLNHSF 370
Cdd:cd08218   222 ---------------------------------------PSR-----YSYDLRSLVSQLFKRNPRDRPSINSILEKPF 255
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
118-370 2.10e-11

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: 63.92  E-value: 2.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 118 SHPNIVPYRA---TFIADNELWAV---TSFMAYGSAKDLIGTHF---MDGmselAIAYILQgVLKALDYIHHMGYVHRSV 188
Cdd:cd14012    56 RHPNLVSYLAfsiERRGRSDGWKVyllTEYAPGGSLSELLDSVGsvpLDT----ARRWTLQ-LLEALEYLHRNGVVHKSL 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 189 KASHILIS---TDGKVYLSGL---RSNLSMISHGqrqravhdfPKYSIKVLPWLSPEVLQQNLQgYDAKSDIYSVGITAC 262
Cdd:cd14012   131 HAGNVLLDrdaGTGIVKLTDYslgKTLLDMCSRG---------SLDEFKQTYWLPPELAQGSKS-PTRKTDVWDLGLLFL 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 263 ELANGHVPFKDMPATQMLLEklngtVPCLldtstipaeeltmspsrsianpglndslaagslrpangdspshpyhrtfSP 342
Cdd:cd14012   201 QMLFGLDVLEKYTSPNPVLV-----SLDL-------------------------------------------------SA 226
                         250       260
                  ....*....|....*....|....*...
gi 1958659070 343 HFHNFVEQCLQRNPDARPNASTLLNHSF 370
Cdd:cd14012   227 SLQDFLSKCLSLDPKKRPTALELLPHEF 254
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
106-360 2.57e-11

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


Pssm-ID: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 63.40  E-value: 2.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 106 FLQgELHVSKLFSHPNIVPYRATfIADNELWAVTSFMAYGSAKDLI----GTHF-MDGMSELAiAYILQGvlkaLDYIHH 180
Cdd:cd14203    37 FLE-EAQIMKKLRHDKLVQLYAV-VSEEPIYIVTEFMSKGSLLDFLkdgeGKYLkLPQLVDMA-AQIASG----MAYIER 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 181 MGYVHRSVKASHILISTD--GKVYLSGLRSNLSMISHGQRQRAvhdfpKYSIKvlpWLSPEVLqqnLQG-YDAKSDIYSV 257
Cdd:cd14203   110 MNYIHRDLRAANILVGDNlvCKIADFGLARLIEDNEYTARQGA-----KFPIK---WTAPEAA---LYGrFTIKSDVWSF 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 258 GITACEL-ANGHVPFKDMPATQMLleklngtvpclldtstipaeeltmspsrsianpglnDSLAAGSLRPANGDSPshpy 336
Cdd:cd14203   179 GILLTELvTKGRVPYPGMNNREVL------------------------------------EQVERGYRMPCPPGCP---- 218
                         250       260
                  ....*....|....*....|....
gi 1958659070 337 hrtfsPHFHNFVEQCLQRNPDARP 360
Cdd:cd14203   219 -----ESLHELMCQCWRKDPEERP 237
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
89-310 2.60e-11

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: 63.88  E-value: 2.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  89 VTVRRINLEACSNEMvTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGSAKDLIgtHFMDGMSELAIAYIL 168
Cdd:cd14202    31 VAVKCINKKNLAKSQ-TLLGKEIKILKELKHENIVALYDFQEIANSVYLVMEYCNGGDLADYL--HTMRTLSEDTIRLFL 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 169 QGVLKALDYIHHMGYVHRSVKASHILIStdgkvYLSGLRSNLSMIshgQRQRAVHDFPKY--------SIKVLP-WLSPE 239
Cdd:cd14202   108 QQIAGAMKMLHSKGIIHRDLKPQNILLS-----YSGGRKSNPNNI---RIKIADFGFARYlqnnmmaaTLCGSPmYMAPE 179
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958659070 240 VLQQnlQGYDAKSDIYSVGITACELANGHVPFK-DMPATQMLLEKLNGTVpclldTSTIPAEelTMSPSRSI 310
Cdd:cd14202   180 VIMS--QHYDAKADLWSIGTIIYQCLTGKAPFQaSSPQDLRLFYEKNKSL-----SPNIPRE--TSSHLRQL 242
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
45-282 2.67e-11

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


Pssm-ID: 270986 [Multi-domain]  Cd Length: 275  Bit Score: 63.95  E-value: 2.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  45 FSKPEIMSSFLPEGGCYEllsvigkgfedlmtVNLARYKPTGEYVTVRRIN---LEACS---NEMVTFLQGELHVSKLFS 118
Cdd:cd14084     4 LRKKYIMSRTLGSGACGE--------------VKLAYDKSTCKKVAIKIINkrkFTIGSrreINKPRNIETEIEILKKLS 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 119 HPNIVPYRATFIADNELWAVTSFMAYGSAKDLIgTHFMdGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTD 198
Cdd:cd14084    70 HPCIIKIEDFFDAEDDYYIVLELMEGGELFDRV-VSNK-RLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQ 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 199 G-----KVYLSGLRSNLSMIShgqRQRAVHDFPKYsikvlpwLSPEVLQQNLQ-GYDAKSDIYSVGITACELANGHVPF- 271
Cdd:cd14084   148 EeecliKITDFGLSKILGETS---LMKTLCGTPTY-------LAPEVLRSFGTeGYTRAVDCWSLGVILFICLSGYPPFs 217
                         250
                  ....*....|....
gi 1958659070 272 ---KDMPATQMLLE 282
Cdd:cd14084   218 eeyTQMSLKEQILS 231
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
61-272 2.78e-11

Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily contains uncharacterized STKs with similarity to the human protein designated as Yank1 or STK32A. The Yank1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270730 [Multi-domain]  Cd Length: 257  Bit Score: 63.43  E-value: 2.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKG-FEdlmTVNLARYKPTGEYVTVRRINLEAC-SNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAV 138
Cdd:cd05578     2 FQILRVIGKGsFG---KVCIVQKKDTKKMFAMKYMNKQKCiEKDSVRNVLNELEILQELEHPFLVNLWYSFQDEEDMYMV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 139 TSFMAYGsakDL---IGThfMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLrsNLSMISH 215
Cdd:cd05578    79 VDLLLGG---DLryhLQQ--KVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDF--NIATKLT 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958659070 216 GQRQravhdfpKYSIK-VLPWLSPEVLQqnLQGYDAKSDIYSVGITACELANGHVPFK 272
Cdd:cd05578   152 DGTL-------ATSTSgTKPYMAPEVFM--RAGYSFAVDWWSLGVTAYEMLRGKRPYE 200
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
91-367 3.04e-11

Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer T-cell-originated protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TOPK, also called PDZ-binding kinase (PBK), is activated at the early stage of mitosis and plays a critical role in cytokinesis. It partly functions as a mitogen-activated protein kinase (MAPK) kinase and is capable of phosphorylating p38, JNK1, and ERK2. TOPK also plays a role in DNA damage sensing and repair through its phosphorylation of histone H2AX. It contributes to cancer development and progression by downregulating the function of tumor suppressor p53 and reducing cell-cycle regulatory proteins. TOPK is found highly expressed in breast and skin cancer cells. The TOPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 63.96  E-value: 3.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  91 VRRINLEACSNEMVTF---LQGELHVSKLFSHPNIVPYRA-TFIADNELWAVtsfMAYG--SAKDLIGTHFMDGMSELAI 164
Cdd:cd14001    33 VKKINSKCDKGQRSLYqerLKEEAKILKSLNHPNIVGFRAfTKSEDGSLCLA---MEYGgkSLNDLIEERYEAGLGPFPA 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 165 AYILQ---GVLKALDYIHHMGYV-HRSVKASHILISTDGK--------VYLSgLRSNLSMISHGQRQravhdfpkYsIKV 232
Cdd:cd14001   110 ATILKvalSIARALEYLHNEKKIlHGDIKSGNVLIKGDFEsvklcdfgVSLP-LTENLEVDSDPKAQ--------Y-VGT 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 233 LPWLSPEVLQQNLQGYDaKSDIYSVGITACELANGHVPFkdmpatqmlleklngtvpclLDTSTIPAEELTMSPSRSian 312
Cdd:cd14001   180 EPWKAKEALEEGGVITD-KADIFAYGLVLWEMMTLSVPH--------------------LNLLDIEDDDEDESFDED--- 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958659070 313 pGLNDSLAAGSL--RPA-NGDSPSHPYHRTFSPHFhnfveQCLQRNPDARPNASTLLN 367
Cdd:cd14001   236 -EEDEEAYYGTLgtRPAlNLGELDDSYQKVIELFY-----ACTQEDPKDRPSAAHIVE 287
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
61-271 3.31e-11

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK2 was the first identified target of activated RhoA, and was found to play a role in stress fiber and focal adhesion formation. It is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270771 [Multi-domain]  Cd Length: 379  Bit Score: 64.64  E-value: 3.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRIN-LEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVT 139
Cdd:cd05621    54 YDVVKVIGRG--AFGEVQLVRHKASQKVYAMKLLSkFEMIKRSDSAFFWEERDIMAFANSPWVVQLFCAFQDDKYLYMVM 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 140 SFMAYGSAKDLIGTHfmDGMSELAIAYILQGVLkALDYIHHMGYVHRSVKASHILISTDGKVYLSGLRSNLSMISHGQrq 219
Cdd:cd05621   132 EYMPGGDLVNLMSNY--DVPEKWAKFYTAEVVL-ALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFGTCMKMDETGM-- 206
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958659070 220 raVHdfPKYSIKVLPWLSPEVLQ-QNLQGYDAKS-DIYSVGITACELANGHVPF 271
Cdd:cd05621   207 --VH--CDTAVGTPDYISPEVLKsQGGDGYYGREcDWWSVGVFLFEMLVGDTPF 256
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
119-275 3.39e-11

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


Pssm-ID: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 63.88  E-value: 3.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 119 HPNIVPYRATFIADNELWAVTSFMAYGSAKDLIGTHfmDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTD 198
Cdd:cd14178    56 HPNIITLKDVYDDGKFVYLVMELMRGGELLDRILRQ--KCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYMDE 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 199 gkvylSGLRSNLSMISHG--QRQRAVHDF---PKYSIKvlpWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKD 273
Cdd:cd14178   134 -----SGNPESIRICDFGfaKQLRAENGLlmtPCYTAN---FVAPEVLKR--QGYDAACDIWSLGILLYTMLAGFTPFAN 203

                  ..
gi 1958659070 274 MP 275
Cdd:cd14178   204 GP 205
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
67-264 3.47e-11

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: 63.26  E-value: 3.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  67 IGKGFedLMTVNLARYKPTGEYVTVRRINLEACSNEMVTflqgELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGS 146
Cdd:cd14155     1 IGSGF--FSEVYKVRHRTSGQVMALKMNTLSSNRANMLR----EVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGGN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 147 AKDLIGTH-FMDGMSELAIAYilqGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS-----GLRSNLSMISHGQRQR 220
Cdd:cd14155    75 LEQLLDSNePLSWTVRVKLAL---DIARGLSYLHSKGIFHRDLTSKNCLIKRDENGYTAvvgdfGLAEKIPDYSDGKEKL 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1958659070 221 AVHDFPKysikvlpWLSPEVLQQNLqgYDAKSDIYSVGITACEL 264
Cdd:cd14155   152 AVVGSPY-------WMAPEVLRGEP--YNEKADVFSYGIILCEI 186
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
110-271 3.88e-11

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


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 63.51  E-value: 3.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 110 ELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGSAKDLIgTHFMDG---MSELAIAYILQGVLKALDYIHHMGYVHR 186
Cdd:cd08229    74 EIDLLKQLNHPNVIKYYASFIEDNELNIVLELADAGDLSRMI-KHFKKQkrlIPEKTVWKYFVQLCSALEHMHSRRVMHR 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 187 SVKASHILISTDGKVYLSGLRSNLSMISHGQRQRAVHDFPKYsikvlpwLSPEVLQQNlqGYDAKSDIYSVGITACELAN 266
Cdd:cd08229   153 DIKPANVFITATGVVKLGDLGLGRFFSSKTTAAHSLVGTPYY-------MSPERIHEN--GYNFKSDIWSLGCLLYEMAA 223

                  ....*
gi 1958659070 267 GHVPF 271
Cdd:cd08229   224 LQSPF 228
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
80-372 4.19e-11

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


Pssm-ID: 270800 [Multi-domain]  Cd Length: 268  Bit Score: 63.22  E-value: 4.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  80 ARYKPTGEYVTVRRI----NLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGSAKDLIGTH- 154
Cdd:cd06630    19 ARDVKTGTLMAVKQVsfcrNSSSEQEEVVEAIREEIRMMARLNHPNIVRMLGATQHKSHFNIFVEWMAGGSVASLLSKYg 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 155 -FMDGMSelaIAYILQgVLKALDYIHHMGYVHRSVKASHILI-STDGKVYLSGLRSNLSMISHGQRqraVHDFPKYSIKV 232
Cdd:cd06630    99 aFSENVI---INYTLQ-ILRGLAYLHDNQIIHRDLKGANLLVdSTGQRLRIADFGAAARLASKGTG---AGEFQGQLLGT 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 233 LPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPF--KDMPATQMLLEKLngtvpclldtstipaeeltmspsrsi 310
Cdd:cd06630   172 IAFMAPEVLRG--EQYGRSCDVWSVGCVIIEMATAKPPWnaEKISNHLALIFKI-------------------------- 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958659070 311 anpglndslaAGSLRPangdsPSHPYHrtFSPHFHNFVEQCLQRNPDARPNASTLLNHSFFK 372
Cdd:cd06630   224 ----------ASATTP-----PPIPEH--LSPGLRDVTLRCLELQPEDRPPARELLKHPVFT 268
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
61-279 4.20e-11

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


Pssm-ID: 271071 [Multi-domain]  Cd Length: 277  Bit Score: 63.37  E-value: 4.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMvTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTS 140
Cdd:cd14169     5 YELKEKLGEG--AFSEVVLAQERGSQRLVALKCIPKKALRGKE-AMVENEIAVLRRINHENIVSLEDIYESPTHLYLAME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 141 FMAYGSAKDLI---GTHfmdgmSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILIST---DGKVYLSGLrsNLSMIS 214
Cdd:cd14169    82 LVTGGELFDRIierGSY-----TEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYATpfeDSKIMISDF--GLSKIE 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958659070 215 HGQRQRAVHDFPKYsikvlpwLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQM 279
Cdd:cd14169   155 AQGMLSTACGTPGY-------VAPELLEQ--KPYGKAVDVWAIGVISYILLCGYPPFYDENDSEL 210
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
61-273 4.72e-11

Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PSKH1 is an autophosphorylating STK that is expressed ubiquitously and exhibits multiple intracellular localizations including the centrosome, Golgi apparatus, and splice factor compartments. It contains a catalytic kinase domain and an N-terminal SH4-like motif that is acylated to facilitate membrane attachment. PSKH1 plays a rile in the maintenance of the Golgi apparatus, an important organelle within the secretory pathway. It may also function as a novel splice factor and a regulator of prostate cancer cell growth. The PSKH1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 62.94  E-value: 4.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKG-FEDLMTVnlaRYKPTGEYVTVRRINLEACSNEmvtFLQGELHVSKLFSHPNIVPYRATFIADNELWAVT 139
Cdd:cd14087     3 YDIKALIGRGsFSRVVRV---EHRVTRQPYAIKMIETKCRGRE---VCESELNVLRRVRHTNIIQLIEVFETKERVYMVM 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 140 SFMAYGSAKDLIGTHfmDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHIListdgkVYLSGLRSNLSMISHG--- 216
Cdd:cd14087    77 ELATGGELFDRIIAK--GSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLL------YYHPGPDSKIMITDFGlas 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958659070 217 QRQRAVHDFPKYSIKVLPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKD 273
Cdd:cd14087   149 TRKKGPNCLMKTTCGTPEYIAPEILLR--KPYTQSVDMWAVGVIAYILLSGTMPFDD 203
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
61-273 4.90e-11

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


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 62.86  E-value: 4.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVtflQGELHVSKLFSHPNIVPYRATFIADNELWAVTS 140
Cdd:cd14662     2 YELVKDIGSG--NFGVARLMRNKETKELVAVKYIERGLKIDENV---QREIINHRSLRHPNIIRFKEVVLTPTHLAIVME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 141 FMAYGSAKDLIGThfMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILIstDGKVylsglRSNLSMISHGQRQR 220
Cdd:cd14662    77 YAAGGELFERICN--AGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLL--DGSP-----APRLKICDFGYSKS 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958659070 221 AV-HDFPKYSIKVLPWLSPEVLQQnlQGYDAK-SDIYSVGITACELANGHVPFKD 273
Cdd:cd14662   148 SVlHSQPKSTVGTPAYIAPEVLSR--KEYDGKvADVWSCGVTLYVMLVGAYPFED 200
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
59-283 5.04e-11

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: 62.66  E-value: 5.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  59 GCYELLSVIGKGfedlMT--VNLARYKPTGEYVTVRRINLEACSNE-MVTFLQGELHVSKLFSHPNIVPYRATFIADNEL 135
Cdd:cd14081     1 GPYRLGKTLGKG----QTglVKLAKHCVTGQKVAIKIVNKEKLSKEsVLMKVEREIAIMKLIEHPNVLKLYDVYENKKYL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 136 WAVTSFMAYGSAKDLIGTHfmDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLsglrSNLSMISH 215
Cdd:cd14081    77 YLVLEYVSGGELFDYLVKK--GRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKI----ADFGMASL 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958659070 216 GQRQRAVHDF---PKYsikvlpwLSPEVLQQnlQGYD-AKSDIYSVGITACELANGHVPFKDmPATQMLLEK 283
Cdd:cd14081   151 QPEGSLLETScgsPHY-------ACPEVIKG--EKYDgRKADIWSCGVILYALLVGALPFDD-DNLRQLLEK 212
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
82-347 5.55e-11

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


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 63.14  E-value: 5.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  82 YKPTGEYVTVRRInleacSNEMVTFLQGELHVSKLF-SHPNIVPYRATFIADNELWAVTSFMAYGSAKDLI--GTHFmdg 158
Cdd:cd14179    28 HKKTNQEYAVKIV-----SKRMEANTQREIAALKLCeGHPNIVKLHEVYHDQLHTFLVMELLKGGELLERIkkKQHF--- 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 159 mSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKvylsglRSNLSMISHG-QRQRAVHDFP-KYSIKVLPWL 236
Cdd:cd14179   100 -SETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDESD------NSEIKIIDFGfARLKPPDNQPlKTPCFTLHYA 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 237 SPEVLQQNlqGYDAKSDIYSVGITACELANGHVPFKDMPATQM------LLEKL-NGTVPCLLDTSTIPAEE-------- 301
Cdd:cd14179   173 APELLNYN--GYDESCDLWSLGVILYTMLSGQVPFQCHDKSLTctsaeeIMKKIkQGDFSFEGEAWKNVSQEakdliqgl 250
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958659070 302 LTMSPSRSIANPGL--NDSLAAGS-------LRPANGDSPSHPYHRTFSPHFHNF 347
Cdd:cd14179   251 LTVDPNKRIKMSGLryNEWLQDGSqlssnplMTPDILGSSGASVHTCVKATFHAF 305
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
85-370 5.88e-11

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


Pssm-ID: 270817 [Multi-domain]  Cd Length: 271  Bit Score: 62.79  E-value: 5.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  85 TGEYVTVRRINLEACSNEM---VTFLQGELHVSKLFSHPNIVPYRATfIADNELWAVTSFMAY---GSAKDLIGTHfmDG 158
Cdd:cd06651    31 TGRELAAKQVQFDPESPETskeVSALECEIQLLKNLQHERIVQYYGC-LRDRAEKTLTIFMEYmpgGSVKDQLKAY--GA 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 159 MSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSNLSMIS-HGQRQRAVHDFPKysikvlpW 235
Cdd:cd06651   108 LTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGdfGASKRLQTICmSGTGIRSVTGTPY-------W 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 236 LSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFkdmpatqmlleklngtvpclldtstipAEELTMSPSRSIANpgl 315
Cdd:cd06651   181 MSPEVISG--EGYGRKADVWSLGCTVVEMLTEKPPW---------------------------AEYEAMAAIFKIAT--- 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958659070 316 ndslaagslRPANGDSPSHpyhrtFSPHFHNFVeQCLQRNPDARPNASTLLNHSF 370
Cdd:cd06651   229 ---------QPTNPQLPSH-----ISEHARDFL-GCIFVEARHRPSAEELLRHPF 268
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
61-271 6.87e-11

Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear Dbf2-Related (NDR)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include ROCK and ROCK-like proteins such as DMPK, MRCK, and CRIK, as well as NDR and NDR-like proteins such as LATS, CBK1 and Sid2p. ROCK and CRIK are effectors of the small GTPase Rho, while MRCK is an effector of the small GTPase Cdc42. NDR and NDR-like kinases contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Proteins in this subfamily are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. The ROCK/NDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 63.07  E-value: 6.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKG-FEDlmtVNLARYKPTGEYVTVRRIN-LEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAV 138
Cdd:cd05573     3 FEVIKVIGRGaFGE---VWLVRDKDTGQVYAMKILRkSDMLKREQIAHVRAERDILADADSPWIVRLHYAFQDEDHLYLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 139 TSFMAYGsakDLIG--THFMDGMSELAIAYILQGVLkALDYIHHMGYVHRSVKASHILISTDGKVYLS--GL-------- 206
Cdd:cd05573    80 MEYMPGG---DLMNllIKYDVFPEETARFYIAELVL-ALDSLHKLGFIHRDIKPDNILLDADGHIKLAdfGLctkmnksg 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958659070 207 ----RSNLSMISHGQRQRAVHDFPKYSIKVL-------P-WLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPF 271
Cdd:cd05573   156 dresYLNDSVNTLFQDNVLARRRPHKQRRVRaysavgtPdYIAPEVLRG--TGYGPECDWWSLGVILYEMLYGFPPF 230
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
82-323 8.43e-11

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


Pssm-ID: 270966 [Multi-domain]  Cd Length: 254  Bit Score: 62.16  E-value: 8.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  82 YKPT--GEYVTVRRINLEA-CSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWA-VTSFMAYGSAKDLIGTH--F 155
Cdd:cd14064    10 YKGRcrNKIVAIKRYRANTyCSKSDVDMFCREVSILCRLNHPCVIQFVGACLDDPSQFAiVTQYVSGGSLFSLLHEQkrV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 156 MDGMSELAIAYilqGVLKALDYIHHMGY--VHRSVKASHILISTDGKVYLSGLRSnlsmiSHGQRQRAVHDFPKYSIKvL 233
Cdd:cd14064    90 IDLQSKLIIAV---DVAKGMEYLHNLTQpiIHRDLNSHNILLYEDGHAVVADFGE-----SRFLQSLDEDNMTKQPGN-L 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 234 PWLSPEVLQQNLQgYDAKSDIYSVGITACELANGHVPFKDM----PATQMLLEKLNGTVPclldtSTIPAEELTMSPSRS 309
Cdd:cd14064   161 RWMAPEVFTQCTR-YSIKADVFSYALCLWELLTGEIPFAHLkpaaAAADMAYHHIRPPIG-----YSIPKPISSLLMRGW 234
                         250
                  ....*....|....
gi 1958659070 310 IANPGLNDSLAAGS 323
Cdd:cd14064   235 NAEPESRPSFVEIV 248
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
67-264 9.43e-11

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: 62.14  E-value: 9.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  67 IGKG-FEDLMTVNlarYKPTGEYVTVRRinLEACSNE-MVTFLQgELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAY 144
Cdd:cd14154     1 LGKGfFGQAIKVT---HRETGEVMVMKE--LIRFDEEaQRNFLK-EVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 145 GSAKDLIgtHFMDG-MSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GL--------RSNLSMI 213
Cdd:cd14154    75 GTLKDVL--KDMARpLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVAdfGLarliveerLPSGNMS 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958659070 214 SHGQRQRAVHDFPK--YSIKVLP-WLSPEVLqqNLQGYDAKSDIYSVGITACEL 264
Cdd:cd14154   153 PSETLRHLKSPDRKkrYTVVGNPyWMAPEML--NGRSYDEKVDIFSFGIVLCEI 204
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
76-271 1.08e-10

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: 62.02  E-value: 1.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  76 TVNLARYKptGEYVTVRRINLEACSNEMVTFLQGELHVSKLfSHPNIVPYRATFIADNELWAVTSFMAYGSAKDLigTHF 155
Cdd:cd13979    18 SVYKATYK--GETVAVKIVRRRRKNRASRQSFWAELNAARL-RHENIVRVLAAETGTDFASLGLIIMEYCGNGTL--QQL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 156 MDGMSELAIAY----ILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLRSNLSMishgqRQRAVHDFPKYSIK 231
Cdd:cd13979    93 IYEGSEPLPLAhrilISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCSVKL-----GEGNEVGTPRSHIG 167
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1958659070 232 VLP-WLSPEVLQQNLQGydAKSDIYSVGITACELANGHVPF 271
Cdd:cd13979   168 GTYtYRAPELLKGERVT--PKADIYSFGITLWQMLTRELPY 206
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
110-271 1.13e-10

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: 61.51  E-value: 1.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 110 ELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGSAKDLIGTHFMdgMSELAIAYILQGVLKALDYIHHMGYVHRSVK 189
Cdd:cd14006    39 EISILNQLQHPRIIQLHEAYESPTELVLILELCSGGELLDRLAERGS--LSEEEVRTYMRQLLEGLQYLHNHHILHLDLK 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 190 ASHILISTDGKvylsglrSNLSMISHGQRQRAVHDFPKYSIKVLP-WLSPEVLQQNLQGYdaKSDIYSVGITACELANGH 268
Cdd:cd14006   117 PENILLADRPS-------PQIKIIDFGLARKLNPGEELKEIFGTPeFVAPEIVNGEPVSL--ATDMWSIGVLTYVLLSGL 187

                  ...
gi 1958659070 269 VPF 271
Cdd:cd14006   188 SPF 190
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
60-368 1.56e-10

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


Pssm-ID: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 61.19  E-value: 1.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  60 CYELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNE--MVtflQGELHVSKLFSHPNIVPYRATFIADNELWA 137
Cdd:cd14095     1 KYDIGRVIGDG--NFAVVKECRDKATDKEYALKIIDKAKCKGKehMI---ENEVAILRRVKHPNIVQLIEEYDTDTELYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 138 VtsfMAYGSAKDL-----IGTHFmdgmSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILIstdgkvylsglrsnlSM 212
Cdd:cd14095    76 V---MELVKGGDLfdaitSSTKF----TERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLV---------------VE 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 213 ISHGQRQRAVHDF--------PKYSIKVLP-WLSPEVLQQNlqGYDAKSDIYSVGITACELANGHVPFKdmpatqmllek 283
Cdd:cd14095   134 HEDGSKSLKLADFglatevkePLFTVCGTPtYVAPEILAET--GYGLKVDIWAAGVITYILLCGFPPFR----------- 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 284 lngtvpclldtstipaeeltmSPSRSiaNPGLNDSLAAGSLrpangDSPShPYHRTFSPHFHNFVEQCLQRNPDARPNAS 363
Cdd:cd14095   201 ---------------------SPDRD--QEELFDLILAGEF-----EFLS-PYWDNISDSAKDLISRMLVVDPEKRYSAG 251

                  ....*
gi 1958659070 364 TLLNH 368
Cdd:cd14095   252 QVLDH 256
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
61-396 1.64e-10

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


Pssm-ID: 270828 [Multi-domain]  Cd Length: 329  Bit Score: 61.77  E-value: 1.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINleacsNEMVTFLQG-----ELHVSKLFSHPNIV--------PYRA 127
Cdd:cd07834     2 YELLKPIGSG--AYGVVCSAYDKRTGRKVAIKKIS-----NVFDDLIDAkrilrEIKILRHLKHENIIglldilrpPSPE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 128 TFiadNELWAVTSFMAygsaKDL---IgtHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS 204
Cdd:cd07834    75 EF---NDVYIVTELME----TDLhkvI--KSPQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKIC 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 205 --GLrSNLSMISHGQRQ----------RAvhdfpkysikvlpwlsPEVLqQNLQGYDAKSDIYSVGITACELANGHVPFK 272
Cdd:cd07834   146 dfGL-ARGVDPDEDKGFlteyvvtrwyRA----------------PELL-LSSKKYTKAIDIWSVGCIFAELLTRKPLFP 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 273 DMPATQMlLEKLNGTVPclldtsTIPAEELtmspsRSIANPGLNDSLAAGSLRPANGDSPSHPyhrTFSPHFHNFVEQCL 352
Cdd:cd07834   208 GRDYIDQ-LNLIVEVLG------TPSEEDL-----KFISSEKARNYLKSLPKKPKKPLSEVFP---GASPEAIDLLEKML 272
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1958659070 353 QRNPDARPNASTLLNHSFFKQIKRRASEALPEllrPVTPITSFE 396
Cdd:cd07834   273 VFNPKKRITADEALAHPYLAQLHDPEDEPVAK---PPFDFPFFD 313
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
76-279 1.81e-10

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


Pssm-ID: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 60.74  E-value: 1.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  76 TVNLARYKPTGEYVTVRRINLeacsnemvtfLQGELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGSAKDLIGTHF 155
Cdd:cd14060     8 SVYRAIWVSQDKEVAVKKLLK----------IEKEAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGSLFDYLNSNE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 156 MDGMSELAIAYILQGVLKALDYIHH---MGYVHRSVKASHILISTDGKVYLSGLRSNlSMISHGQRQRAVHDFpkysikv 232
Cdd:cd14060    78 SEEMDMDQIMTWATDIAKGMHYLHMeapVKVIHRDLKSRNVVIAADGVLKICDFGAS-RFHSHTTHMSLVGTF------- 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1958659070 233 lPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQM 279
Cdd:cd14060   150 -PWMAPEVIQS--LPVSETCDTYSYGVVLWEMLTREVPFKGLEGLQV 193
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
105-264 2.23e-10

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: 61.13  E-value: 2.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 105 TFLQgELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGSAKDLIGThfMDGM----SELAIAyilQGVLKALDYIHH 180
Cdd:cd14221    36 TFLK-EVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGTLRGIIKS--MDSHypwsQRVSFA---KDIASGMAYLHS 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 181 MGYVHRSVKASHILISTDGKVYLS--GLR----SNLSMISHGQRQRAVHDFPKYSIKVLP-WLSPEVLqqNLQGYDAKSD 253
Cdd:cd14221   110 MNIIHRDLNSHNCLVRENKSVVVAdfGLArlmvDEKTQPEGLRSLKKPDRKKRYTVVGNPyWMAPEMI--NGRSYDEKVD 187
                         170
                  ....*....|.
gi 1958659070 254 IYSVGITACEL 264
Cdd:cd14221   188 VFSFGIVLCEI 198
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
107-371 2.49e-10

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


Pssm-ID: 271001 [Multi-domain]  Cd Length: 258  Bit Score: 60.65  E-value: 2.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 107 LQGELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGSAKDLIGTHfmDGMSELAIAYILQGVLKALDYIHHMGYVHR 186
Cdd:cd14099    48 LKSEIKIHRSLKHPNIVKFHDCFEDEENVYILLELCSNGSLMELLKRR--KALTEPEVRYFMRQILSGVKYLHSNRIIHR 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 187 SVKASHILISTDGKVYLS--GLRSNLSmiSHGQRQRAVHDFPKYsikvlpwLSPEVLqQNLQGYDAKSDIYSVGITACEL 264
Cdd:cd14099   126 DLKLGNLFLDENMNVKIGdfGLAARLE--YDGERKKTLCGTPNY-------IAPEVL-EKKKGHSFEVDIWSLGVILYTL 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 265 ANGHVPF--KDMPATQMLLEKLNGTVPclldtstipaeeltmspsrsianPGLNDSLAAGSLrpangdspshpyhrtfsp 342
Cdd:cd14099   196 LVGKPPFetSDVKETYKRIKKNEYSFP-----------------------SHLSISDEAKDL------------------ 234
                         250       260
                  ....*....|....*....|....*....
gi 1958659070 343 hfhnfVEQCLQRNPDARPNASTLLNHSFF 371
Cdd:cd14099   235 -----IRSMLQPDPTKRPSLDEILSHPFF 258
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
145-287 2.50e-10

kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to the C-terminal protein kinase catalytic fold (C lobe). Its presence at the N terminus of signalling proteins and the absence of the active-site residues in the catalytic and activation loops suggest that it folds independently and is likely to be non-catalytic. The occurrence of KIND only in metazoa implies that it has evolved from the catalytic protein kinase domain into an interaction domain possibly by keeping the substrate-binding features


Pssm-ID: 214801  Cd Length: 176  Bit Score: 59.34  E-value: 2.50e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  145 GSAKDLIgTHFMDGMSELAIAYILQGVLKALDYihhmgyVHRSVKASHILISTDGKVYLSGlrsnlsmiSHGQRQRAVHD 224
Cdd:smart00750   1 VSLADIL-EVRGRPLNEEEIWAVCLQCLGALRE------LHRQAKSGNILLTWDGLLKLDG--------SVAFKTPEQSR 65
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958659070  225 FPKYsikvlpWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPA-TQMLLEKLNGT 287
Cdd:smart00750  66 PDPY------FMAPEVIQG--QSYTEKADIYSLGITLYEALDYELPYNEERElSAILEILLNGM 121
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
77-264 3.02e-10

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


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 60.71  E-value: 3.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  77 VNLARYKP----TGEYVTVRRINLEACSNEMVTfLQGELHVSKLFSHPNIVPYRA--TFIADNELWAVTSFMAYGSAKDL 150
Cdd:cd05079    20 VELCRYDPegdnTGEQVAVKSLKPESGGNHIAD-LKKEIEILRNLYHENIVKYKGicTEDGGNGIKLIMEFLPSGSLKEY 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 151 IGTHFMDGMSELAIAYILQgVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSNLSMISHGQRQRAVHDFPKY 228
Cdd:cd05079    99 LPRNKNKINLKQQLKYAVQ-ICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGdfGLTKAIETDKEYYTVKDDLDSPVF 177
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1958659070 229 sikvlpWLSPEVLQQNlQGYDAkSDIYSVGITACEL 264
Cdd:cd05079   178 ------WYAPECLIQS-KFYIA-SDVWSFGVTLYEL 205
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
76-361 3.15e-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: 60.54  E-value: 3.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  76 TVNLARYKPTGEYVTVRRIN-LEACSNEMVTFLQgELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGSAKDLIGTH 154
Cdd:cd13978     8 TVSKARHVSWFGMVAIKCLHsSPNCIEERKALLK-EAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGSLKSLLERE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 155 FMDGMSELAIAYILQGVLkALDYIHHM--GYVHRSVKASHILISTDGKVYLS--GLrSNLSMISHGQRQRAVHDFPKYSI 230
Cdd:cd13978    87 IQDVPWSLRFRIIHEIAL-GMNFLHNMdpPLLHHDLKPENILLDNHFHVKISdfGL-SKLGMKSISANRRRGTENLGGTP 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 231 KVLPwlsPEVLQQNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLL-EKLNGTVPCLldtstipaeeltmspsrs 309
Cdd:cd13978   165 IYMA---PEAFDDFNKKPTSKSDVYSFAIVIWAVLTRKEPFENAINPLLIMqIVSKGDRPSL------------------ 223
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958659070 310 ianpglndslaagslrpangDSPSHPYHRTFSPHFHNFVEQCLQRNPDARPN 361
Cdd:cd13978   224 --------------------DDIGRLKQIENVQELISLMIRCWDGNPDARPT 255
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
110-375 4.13e-10

Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase (also called MAPK12); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38gamma/MAPK12 is predominantly expressed in skeletal muscle. Unlike p38alpha and p38beta, p38gamma is insensitive to pyridinylimidazoles. It displays an antagonizing function compared to p38alpha. p38gamma inhibits, while p38alpha stimulates, c-Jun phosphorylation and AP-1 mediated transcription. p38gamma also plays a role in the signaling between Ras and the estrogen receptor and has been implicated to increase cell invasion and breast cancer progression. In Xenopus, p38gamma is critical in the meiotic maturation of oocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 60.74  E-value: 4.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 110 ELHVSKLFSHPNIVPYRATFIAD------NELWAVTSFMAygsaKDLIGTHFMDGMSELAIAYILQGVLKALDYIHHMGY 183
Cdd:cd07880    64 ELRLLKHMKHENVIGLLDVFTPDlsldrfHDFYLVMPFMG----TDLGKLMKHEKLSEDRIQFLVYQMLKGLKYIHAAGI 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 184 VHRSVKASHILISTDgkvylsglrSNLSMISHGQRQRAVHDFPKYSikVLPWL-SPEVLqQNLQGYDAKSDIYSVGITAC 262
Cdd:cd07880   140 IHRDLKPGNLAVNED---------CELKILDFGLARQTDSEMTGYV--VTRWYrAPEVI-LNWMHYTQTVDIWSVGCIMA 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 263 ELANGHVPFKDMPATQMLLE--KLNGTvpclldtstiPAEELTMSPSRSIAN------PGLNDSLAAGSLRPANgdspsh 334
Cdd:cd07880   208 EMLTGKPLFKGHDHLDQLMEimKVTGT----------PSKEFVQKLQSEDAKnyvkklPRFRKKDFRSLLPNAN------ 271
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1958659070 335 pyhrtfsPHFHNFVEQCLQRNPDARPNASTLLNHSFFKQIK 375
Cdd:cd07880   272 -------PLAVNVLEKMLVLDAESRITAAEALAHPYFEEFH 305
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
57-274 4.29e-10

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


Pssm-ID: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 60.27  E-value: 4.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  57 EGGCYELLSVIGKGfeDLMTVNLARYKPTGE---YVTVRRINLEACSNEMVTFLqGELHVSKLFSHPNIVPYRATFIADN 133
Cdd:cd05066     2 DASCIKIEKVIGAG--EFGEVCSGRLKLPGKreiPVAIKTLKAGYTEKQRRDFL-SEASIMGQFDHPNIIHLEGVVTRSK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 134 ELWAVTSFMAYGSAKDLIGTHfmDG-MSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILIStdgkvylsglrSNL-S 211
Cdd:cd05066    79 PVMIVTEYMENGSLDAFLRKH--DGqFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVN-----------SNLvC 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 212 MISHGQRQRAVHDFPKYSIKV----LP--WLSPEVLQqnLQGYDAKSDIYSVGITACE-LANGHVPFKDM 274
Cdd:cd05066   146 KVSDFGLSRVLEDDPEAAYTTrggkIPirWTAPEAIA--YRKFTSASDVWSYGIVMWEvMSYGERPYWEM 213
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
106-290 4.51e-10

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


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 60.09  E-value: 4.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 106 FLQgELHVSKLFSHPNIVPYRATfIADNELWAVTSFMAYGSAKDLI----GTHF-MDGMSELAiAYILQGvlkaLDYIHH 180
Cdd:cd05069    54 FLQ-EAQIMKKLRHDKLVPLYAV-VSEEPIYIVTEFMGKGSLLDFLkegdGKYLkLPQLVDMA-AQIADG----MAYIER 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 181 MGYVHRSVKASHILISTD--GKVYLSGLRSNLSMISHGQRQRAvhdfpKYSIKvlpWLSPEVLqqnLQG-YDAKSDIYSV 257
Cdd:cd05069   127 MNYIHRDLRAANILVGDNlvCKIADFGLARLIEDNEYTARQGA-----KFPIK---WTAPEAA---LYGrFTIKSDVWSF 195
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1958659070 258 GITACEL-ANGHVPFKDMPATQMLLEKLNG-TVPC 290
Cdd:cd05069   196 GILLTELvTKGRVPYPGMVNREVLEQVERGyRMPC 230
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
45-384 6.09e-10

Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase (also called MAPK13); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38delta/MAPK13 is found in skeletal muscle, heart, lung, testis, pancreas, and small intestine. It regulates microtubule function by phosphorylating Tau. It activates the c-jun promoter and plays a role in G2 cell cycle arrest. It also controls the degration of c-Myb, which is associated with myeloid leukemia and poor prognosis in colorectal cancer. p38delta is the main isoform involved in regulating the differentiation and apoptosis of keratinocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 60.30  E-value: 6.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  45 FSKPEIMSSF--LPEGgcYELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFSHPNI 122
Cdd:cd07879     1 FYREEVNKTVweLPER--YTSLKQVGSG--AYGSVCSAIDKRTGEKVAIKKLSRPFQSEIFAKRAYRELTLLKHMQHENV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 123 VPYRATFIAD------NELWAVTSFMAYGSAKdLIGTHFmdgmSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILIS 196
Cdd:cd07879    77 IGLLDVFTSAvsgdefQDFYLVMPYMQTDLQK-IMGHPL----SEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVN 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 197 TDgkvylsglrSNLSMISHGQRQRAVHDFPKYSikVLPWL-SPEVLqQNLQGYDAKSDIYSVGITACELANGHVPFKDMP 275
Cdd:cd07879   152 ED---------CELKILDFGLARHADAEMTGYV--VTRWYrAPEVI-LNWMHYNQTVDIWSVGCIMAEMLTGKTLFKGKD 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 276 ATQMLLEklngtvpcLLDTSTIPAEELTMSpsrsianpgLNDsLAAGSLRPANGDSPSHPYHRTF---SPHFHNFVEQCL 352
Cdd:cd07879   220 YLDQLTQ--------ILKVTGVPGPEFVQK---------LED-KAAKSYIKSLPKYPRKDFSTLFpkaSPQAVDLLEKML 281
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1958659070 353 QRNPDARPNASTLLNHSFFKQIkrRASEALPE 384
Cdd:cd07879   282 ELDVDKRLTATEALEHPYFDSF--RDADEETE 311
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
59-289 6.46e-10

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


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 59.35  E-value: 6.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  59 GCYELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAV 138
Cdd:cd14074     3 GLYDLEETLGRG--HFAVVKLARHVFTGEKVAVKVIDKTKLDDVSKAHLFQEVRCMKLVQHPNVVRLYEVIDTQTKLYLI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 139 TSFMAYGSAKDLIGTHfMDGMSE-LAIAYILQgVLKALDYIHHMGYVHRSVKASHILIS-TDGKVYLS--GLrSNLSMis 214
Cdd:cd14074    81 LELGDGGDMYDYIMKH-ENGLNEdLARKYFRQ-IVSAISYCHKLHVVHRDLKPENVVFFeKQGLVKLTdfGF-SNKFQ-- 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958659070 215 HGQRQRAvhdfpkySIKVLPWLSPEVLQQNlqGYDA-KSDIYSVGITACELANGHVPFKDMPATQMLLEKLNG--TVP 289
Cdd:cd14074   156 PGEKLET-------SCGSLAYSAPEILLGD--EYDApAVDIWSLGVILYMLVCGQPPFQEANDSETLTMIMDCkyTVP 224
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
76-271 6.48e-10

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: 59.42  E-value: 6.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  76 TVNLARYKPTGEYVTVRRI-NLEACSNEMVTFLQGE---LHVSKlfSHPNIVPYRATFIADNELWAVTSFMAYGSAKDLI 151
Cdd:cd05611    11 SVYLAKKRSTGDYFAIKVLkKSDMIAKNQVTNVKAEraiMMIQG--ESPYVAKLYYSFQSKDYLYLVMEYLNGGDCASLI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 152 GThfMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSNLSMISHGQRQRAVHDFpkys 229
Cdd:cd05611    89 KT--LGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTdfGLSRNGLEKRHNKKFVGTPDY---- 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1958659070 230 ikvlpwLSPEVLQQNlqGYDAKSDIYSVGITACELANGHVPF 271
Cdd:cd05611   163 ------LAPETILGV--GDDKMSDWWSLGCVIFEFLFGYPPF 196
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
61-280 6.80e-10

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


Pssm-ID: 270982 [Multi-domain]  Cd Length: 262  Bit Score: 59.50  E-value: 6.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYK--PTGEYVTVRRINLEACSNEMVT-FLQGELHVSKLFSHPNIVPYRATFIADNElwa 137
Cdd:cd14080     2 YRLGKTIGEG--SYSKVKLAEYTksGLKEKVACKIIDKKKAPKDFLEkFLPRELEILRKLRHPNIIQVYSIFERGSK--- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 138 VTSFMAYGSAKDL---IGTHfmDGMSE-LAIAYILQgVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSglrsnlsmi 213
Cdd:cd14080    77 VFIFMEYAEHGDLleyIQKR--GALSEsQARIWFRQ-LALAVQYLHSLDIAHRDLKCENILLDSNNNVKLS--------- 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 214 shgqrqravhDF------PKYSIKVLP--------WLSPEVlqqnLQG--YDAK-SDIYSVGITACELANGHVPFKDMPA 276
Cdd:cd14080   145 ----------DFgfarlcPDDDGDVLSktfcgsaaYAAPEI----LQGipYDPKkYDIWSLGVILYIMLCGSMPFDDSNI 210

                  ....
gi 1958659070 277 TQML 280
Cdd:cd14080   211 KKML 214
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
59-278 7.99e-10

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


Pssm-ID: 270979 [Multi-domain]  Cd Length: 267  Bit Score: 59.38  E-value: 7.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  59 GCYELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRIN---------------LEACSNEMVTFLqgELHVSKLFSHPNIV 123
Cdd:cd14077     1 GNWEFVKTIGAG--SMGKVKLAKHIRTGEKCAIKIIPrasnaglkkerekrlEKEISRDIRTIR--EAALSSLLNHPHIC 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 124 PYRATFIADNELWAVTSFMAYGSAKDLIGTHfmDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYL 203
Cdd:cd14077    77 RLRDFLRTPNHYYMLFEYVDGGQLLDYIISH--GKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 204 S--GLrSNLSmishgQRQRAVHDFpkysIKVLPWLSPEVLQQnlQGYDA-KSDIYSVGITACELANGHVPFKD--MPATQ 278
Cdd:cd14077   155 IdfGL-SNLY-----DPRRLLRTF----CGSLYFAAPELLQA--QPYTGpEVDVWSFGVVLYVLVCGKVPFDDenMPALH 222
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
83-372 8.51e-10

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: 59.25  E-value: 8.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  83 KPTGEYVTVRRINLEACSNEMVtFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGSAKDLI---GThfmdgM 159
Cdd:cd14201    29 KKTDWEVAIKSINKKNLSKSQI-LLGKEIKILKELQHENIVALYDVQEMPNSVFLVMEYCNGGDLADYLqakGT-----L 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 160 SELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDG--KVYLSGLRsnLSMISHGQRQRAVHDFPKYSIKVLP-WL 236
Cdd:cd14201   103 SEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASrkKSSVSGIR--IKIADFGFARYLQSNMMAATLCGSPmYM 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 237 SPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFK-DMPAT-QMLLEKLNGTVPclldtsTIPAEEltmspsrsianpg 314
Cdd:cd14201   181 APEVIMS--QHYDAKADLWSIGTVIYQCLVGKPPFQaNSPQDlRMFYEKNKNLQP------SIPRET------------- 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958659070 315 lndslaagslrpangdspshpyhrtfSPHFHNFVEQCLQRNPDARPNASTLLNHSFFK 372
Cdd:cd14201   240 --------------------------SPYLADLLLGLLQRNQKDRMDFEAFFSHPFLE 271
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
106-368 8.87e-10

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


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 58.87  E-value: 8.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 106 FLQGELHVSKLFSHPNIVP-YRATfiadneLWAVTS--FMAYGSAKDLIGTHFMDG-MSELAIAYILQGVLKALDYIHHM 181
Cdd:cd13995    42 FKPSDVEIQACFRHENIAElYGAL------LWEETVhlFMEAGEGGSVLEKLESCGpMREFEIIWVTKHVLKGLDFLHSK 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 182 GYVHRSVKASHILISTDGKVylsglrsnlsMISHGQRQRAVHD--FPKYSIKVLPWLSPEVLQqnLQGYDAKSDIYSVGI 259
Cdd:cd13995   116 NIIHHDIKPSNIVFMSTKAV----------LVDFGLSVQMTEDvyVPKDLRGTEIYMSPEVIL--CRGHNTKADIYSLGA 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 260 TACELANGHVPF-KDMP--ATQMLLEKLNGTVPclldtstiPAEELTMSpsrsianpglndslaagslrpangdspshpy 336
Cdd:cd13995   184 TIIHMQTGSPPWvRRYPrsAYPSYLYIIHKQAP--------PLEDIAQD------------------------------- 224
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1958659070 337 hrtFSPHFHNFVEQCLQRNPDARPNASTLLNH 368
Cdd:cd13995   225 ---CSPAMRELLEAALERNPNHRSSAAELLKH 253
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
110-314 1.11e-09

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK3, also called Prk or Fnk (FGF-inducible kinase), regulates angiogenesis and responses to DNA damage. Activated PLK3 mediates Chk2 phosphorylation by ATM and the resulting checkpoint activation. PLK3 phosphorylates DNA polymerase delta and may be involved in DNA repair. It also inhibits Cdc25c, thereby regulating the onset of mitosis. The PLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271091 [Multi-domain]  Cd Length: 255  Bit Score: 58.79  E-value: 1.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 110 ELHVSKLFSHPNIVPYRATF-IADNelwaVTSFMAYGSAKDLigTHFMDG---MSELAIAYILQGVLKALDYIHHMGYVH 185
Cdd:cd14189    51 EIELHRDLHHKHVVKFSHHFeDAEN----IYIFLELCSRKSL--AHIWKArhtLLEPEVRYYLKQIISGLKYLHLKGILH 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 186 RSVKASHILISTDGKVYLS--GLRSNLSMIShgQRQRAVHDFPKYsikvlpwLSPEVLqqNLQGYDAKSDIYSVGITACE 263
Cdd:cd14189   125 RDLKLGNFFINENMELKVGdfGLAARLEPPE--QRKKTICGTPNY-------LAPEVL--LRQGHGPESDVWSLGCVMYT 193
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958659070 264 LANGHVPFK--DMPATQMLLEKLNGTVPCLLdtsTIPAEELTMSPSRsiANPG 314
Cdd:cd14189   194 LLCGNPPFEtlDLKETYRCIKQVKYTLPASL---SLPARHLLAGILK--RNPG 241
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
61-273 1.25e-09

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


Pssm-ID: 270732 [Multi-domain]  Cd Length: 290  Bit Score: 58.74  E-value: 1.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRIN---------LEACSNEmvtflqgeLHVSKLFSHPNIVPYRATFIA 131
Cdd:cd05580     3 FEFLKTLGTG--SFGRVRLVKHKDSGKYYALKILKkakiiklkqVEHVLNE--------KRILSEVRHPFIVNLLGSFQD 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 132 DNELWAVTSFMAYGSAKDLI--GTHFMdgmSELAIAYILQgVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSglrsn 209
Cdd:cd05580    73 DRNLYMVMEYVPGGELFSLLrrSGRFP---NDVAKFYAAE-VVLALEYLHSLDIVYRDLKPENLLLDSDGHIKIT----- 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 210 lsmishgqrqravhDF----------------PKYsikvlpwLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKD 273
Cdd:cd05580   144 --------------DFgfakrvkdrtytlcgtPEY-------LAPEIILS--KGHGKAVDWWALGILIYEMLAGYPPFFD 200
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
89-282 1.32e-09

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


Pssm-ID: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 58.53  E-value: 1.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  89 VTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRAtFIADNELWAVTSFMAYGSAKDLIgtHFMDGMSEL-AIAYI 167
Cdd:cd14151    33 VAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMG-YSTKPQLAIVTQWCEGSSLYHHL--HIIETKFEMiKLIDI 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 168 LQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSglrsNLSMISHGQRQRAVHDFPKYSIKVLpWLSPEVLQ-QNLQ 246
Cdd:cd14151   110 ARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIG----DFGLATVKSRWSGSHQFEQLSGSIL-WMAPEVIRmQDKN 184
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1958659070 247 GYDAKSDIYSVGITACELANGHVPFKDMPATQMLLE 282
Cdd:cd14151   185 PYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIF 220
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
106-290 1.33e-09

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


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 58.55  E-value: 1.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 106 FLQgELHVSKLFSHPNIVPYRATfIADNELWAVTSFMAYGSAKDLIGTHFMDGMSELAIAYILQGVLKALDYIHHMGYVH 185
Cdd:cd05071    51 FLQ-EAQVMKKLRHEKLVQLYAV-VSEEPIYIVTEYMSKGSLLDFLKGEMGKYLRLPQLVDMAAQIASGMAYVERMNYVH 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 186 RSVKASHILISTD--GKVYLSGLRSNLSMISHGQRQRAvhdfpKYSIKvlpWLSPEVLqqnLQG-YDAKSDIYSVGITAC 262
Cdd:cd05071   129 RDLRAANILVGENlvCKVADFGLARLIEDNEYTARQGA-----KFPIK---WTAPEAA---LYGrFTIKSDVWSFGILLT 197
                         170       180       190
                  ....*....|....*....|....*....|
gi 1958659070 263 ELAN-GHVPFKDMPATQMLLEKLNG-TVPC 290
Cdd:cd05071   198 ELTTkGRVPYPGMVNREVLDQVERGyRMPC 227
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
110-373 1.66e-09

Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase (also called MAPK14); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38alpha/MAPK14 is expressed in most tissues and is the major isoform involved in the immune and inflammatory response. It is the central p38 MAPK involved in myogenesis. It plays a role in regulating cell cycle check-point transition and promoting cell differentiation. p38alpha also regulates cell proliferation and death through crosstalk with the JNK pathway. Its substrates include MAPK activated protein kinase 2 (MK2), MK5, and the transcription factors ATF2 and Mitf. p38 kinases MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 58.90  E-value: 1.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 110 ELHVSKLFSHPNIV-------PYRaTFIADNELWAVTSFMAygsaKDLIGTHFMDGMSELAIAYILQGVLKALDYIHHMG 182
Cdd:cd07877    66 ELRLLKHMKHENVIglldvftPAR-SLEEFNDVYLVTHLMG----ADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSAD 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 183 YVHRSVKASHILISTDgkvylsglrSNLSMISHGQRQRAVHDFPKYsIKVLPWLSPEVLqQNLQGYDAKSDIYSVGITAC 262
Cdd:cd07877   141 IIHRDLKPSNLAVNED---------CELKILDFGLARHTDDEMTGY-VATRWYRAPEIM-LNWMHYNQTVDIWSVGCIMA 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 263 ELANGHVPFkdmPATQ-----MLLEKLNGTVPCLLdTSTIPAEE-------LTMSPSRSIANPGLNdslaagslrpANgd 330
Cdd:cd07877   210 ELLTGRTLF---PGTDhidqlKLILRLVGTPGAEL-LKKISSESarnyiqsLTQMPKMNFANVFIG----------AN-- 273
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1958659070 331 spshpyhrtfsPHFHNFVEQCLQRNPDARPNASTLLNHSFFKQ 373
Cdd:cd07877   274 -----------PLAVDLLEKMLVLDSDKRITAAQALAHAYFAQ 305
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
61-282 1.72e-09

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 2 subunit (PhKG2) is also referred to as the testis/liver gamma isoform. Mutations in its gene cause autosomal-recessive glycogenosis of the liver. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271083 [Multi-domain]  Cd Length: 279  Bit Score: 58.44  E-value: 1.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGFEDlmTVNLARYKPTG-EY------VTVRRINLEACSnEMVTFLQGELHVSKLFS-HPNIVPYRATFIAD 132
Cdd:cd14181    12 YDPKEVIGRGVSS--VVRRCVHRHTGqEFavkiieVTAERLSPEQLE-EVRSSTLKEIHILRQVSgHPSIITLIDSYESS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 133 NELWAVTSFMAYGSAKDLIGTHFMdgMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSNL 210
Cdd:cd14181    89 TFIFLVFDLMRRGELFDYLTEKVT--LSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSdfGFSCHL 166
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958659070 211 smiSHGQRQRAVHDFPKYsikvlpwLSPEVLQQNL----QGYDAKSDIYSVGITACELANGHVPF---KDMPATQMLLE 282
Cdd:cd14181   167 ---EPGEKLRELCGTPGY-------LAPEILKCSMdethPGYGKEVDLWACGVILFTLLAGSPPFwhrRQMLMLRMIME 235
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
61-264 1.78e-09

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


Pssm-ID: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 58.27  E-value: 1.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLeacSNEMVtflqgELHVSKL--FSHPNIVPYratfiadNELWAV 138
Cdd:cd14047     8 FKEIELIGSG--GFGQVFKAKHRIDGKTYAIKRVKL---NNEKA-----EREVKALakLDHPNIVRY-------NGCWDG 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 139 TSFMAYGSAKD---------LIGTHFMDG--------------MSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILI 195
Cdd:cd14047    71 FDYDPETSSSNssrsktkclFIQMEFCEKgtleswiekrngekLDKVLALEIFEQITKGVEYIHSKKLIHRDLKPSNIFL 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958659070 196 STDGKVYLSGLRSNLSMISHGQRQRavhdfpkySIKVLPWLSPEvlQQNLQGYDAKSDIYSVGITACEL 264
Cdd:cd14047   151 VDTGKVKIGDFGLVTSLKNDGKRTK--------SKGTLSYMSPE--QISSQDYGKEVDIYALGLILFEL 209
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
56-374 2.01e-09

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


Pssm-ID: 271039 [Multi-domain]  Cd Length: 293  Bit Score: 58.28  E-value: 2.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  56 PEGGCYELLSVIGKG-FEdlmTVNLARYKPTGEYVTVRRInleacsnemvtfLQG------ELHVSKLFSHPNIVPYRAT 128
Cdd:cd14137     1 PVEISYTIEKVIGSGsFG---VVYQAKLLETGEVVAIKKV------------LQDkryknrELQIMRRLKHPNIVKLKYF 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 129 FIADNE------LWAVTSFMAYGSAKDLIgtHFMDGMSELAIAYI----LQgVLKALDYIHHMGYVHRSVKASHILI-ST 197
Cdd:cd14137    66 FYSSGEkkdevyLNLVMEYMPETLYRVIR--HYSKNKQTIPIIYVklysYQ-LFRGLAYLHSLGICHRDIKPQNLLVdPE 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 198 DGKVYLSglrsnlsmishgqrqravhDFPkySIKVL----PWLS---------PEVLQQNlQGYDAKSDIYSVGitaC-- 262
Cdd:cd14137   143 TGVLKLC-------------------DFG--SAKRLvpgePNVSyicsryyraPELIFGA-TDYTTAIDIWSAG---Cvl 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 263 -ELANGHVPFKDMPATQMLLE--KLNGTvpclldtstiPAEE--LTMSPSRSianpglndslaaGSLRPangDSPSHPYH 337
Cdd:cd14137   198 aELLLGQPLFPGESSVDQLVEiiKVLGT----------PTREqiKAMNPNYT------------EFKFP---QIKPHPWE 252
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1958659070 338 RTFSPH----FHNFVEQCLQRNPDARPNASTLLNHSFFKQI 374
Cdd:cd14137   253 KVFPKRtppdAIDLLSKILVYNPSKRLTALEALAHPFFDEL 293
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
61-273 2.59e-09

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


Pssm-ID: 271070 [Multi-domain]  Cd Length: 301  Bit Score: 58.14  E-value: 2.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTfLQGELHVSKLFSHPNIVPYRATFIADNELWAVTS 140
Cdd:cd14168    12 FEFKEVLGTG--AFSEVVLAEERATGKLFAVKCIPKKALKGKESS-IENEIAVLRKIKHENIVALEDIYESPNHLYLVMQ 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 141 FMAYGSAKDLIGTHFMdgMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHIListdgkvYLSGLRSNLSMISHG--QR 218
Cdd:cd14168    89 LVSGGELFDRIVEKGF--YTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLL-------YFSQDEESKIMISDFglSK 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958659070 219 QRAVHDFPKYSIKVLPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKD 273
Cdd:cd14168   160 MEGKGDVMSTACGTPGYVAPEVLAQ--KPYSKAVDCWSIGVIAYILLCGYPPFYD 212
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
110-371 2.61e-09

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK2, also called Snk (serum-inducible kinase), functions in G1 progression, S-phase arrest, and centriole duplication. Its gene is responsive to both growth factors and cellular stress, is a transcriptional target of p53, and activates a G2-M checkpoint. The PLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271090 [Multi-domain]  Cd Length: 255  Bit Score: 57.71  E-value: 2.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 110 ELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGSAKDLIGTHFMdgMSELAIAYILQGVLKALDYIHHMGYVHRSVK 189
Cdd:cd14188    51 EIELHRILHHKHVVQFYHYFEDKENIYILLEYCSRRSMAHILKARKV--LTEPEVRYYLRQIVSGLKYLHEQEILHRDLK 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 190 ASHILI--STDGKVYLSGLRSNLSMIshGQRQRAVHDFPKYsikvlpwLSPEVLqqNLQGYDAKSDIYSVGITACELANG 267
Cdd:cd14188   129 LGNFFIneNMELKVGDFGLAARLEPL--EHRRRTICGTPNY-------LSPEVL--NKQGHGCESDIWALGCVMYTMLLG 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 268 HVPFKDMpatqmlleKLNGTVPClldtstipaeeltmspsrsianpglndslaagsLRPANGDSPShpyhrTFSPHFHNF 347
Cdd:cd14188   198 RPPFETT--------NLKETYRC---------------------------------IREARYSLPS-----SLLAPAKHL 231
                         250       260
                  ....*....|....*....|....
gi 1958659070 348 VEQCLQRNPDARPNASTLLNHSFF 371
Cdd:cd14188   232 IASMLSKNPEDRPSLDEIIRHDFF 255
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
61-259 2.75e-09

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


Pssm-ID: 270948 [Multi-domain]  Cd Length: 278  Bit Score: 57.76  E-value: 2.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKG-FEDlmtVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLfSHPNIVPYRATFIADNELWAVT 139
Cdd:cd14046     8 FEELQVLGKGaFGQ---VVKVRNKLDGRYYAIKKIKLRSESKNNSRILREVMLLSRL-NHQHVVRYYQAWIERANLYIQM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 140 SFMAYGSAKDLIGTHFMDGMSElaIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSN--LSMISH 215
Cdd:cd14046    84 EYCEKSTLRDLIDSGLFQDTDR--LWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGdfGLATSnkLNVELA 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958659070 216 GQRQRAVHDFPKYS-------IKVLPWLSPEVLQQNLQGYDAKSDIYSVGI 259
Cdd:cd14046   162 TQDINKSTSAALGSsgdltgnVGTALYVAPEVQSGTKSTYNEKVDMYSLGI 212
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
166-374 2.77e-09

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


Pssm-ID: 270735 [Multi-domain]  Cd Length: 268  Bit Score: 57.79  E-value: 2.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 166 YILQGVLkALDYIHHMGYVHRSVKASHILISTDGKVYLSGLRSNLSMISHgQRQRAvHDFpkysIKVLPWLSPEVLQQNL 245
Cdd:cd05583   104 YIGEIVL-ALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLSKEFLPG-ENDRA-YSF----CGTIEYMAPEVVRGGS 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 246 QGYDAKSDIYSVGITACELANGHVPFkdmpatqmlleklngtvpclldtsTIPAEELTMSP-SRSI--ANPglndslaag 322
Cdd:cd05583   177 DGHDKAVDWWSLGVLTYELLTGASPF------------------------TVDGERNSQSEiSKRIlkSHP--------- 223
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958659070 323 slrpangdspshPYHRTFSPHFHNFVEQCLQRNPDAR-----PNASTLLNHSFFKQI 374
Cdd:cd05583   224 ------------PIPKTFSAEAKDFILKLLEKDPKKRlgagpRGAHEIKEHPFFKGL 268
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
131-279 3.07e-09

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


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 58.10  E-value: 3.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 131 ADNElWAVT---SF---------MAYGSAKDLIGTHFMDGMSE--LAIAYILQGVLkALDYIHHMGYVHRSVKASHILIS 196
Cdd:cd05598    58 ADNE-WVVKlyySFqdkenlyfvMDYIPGGDLMSLLIKKGIFEedLARFYIAELVC-AIESVHKMGFIHRDIKPDNILID 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 197 TDGKVYLS--GLRSNLsmishgqrqRAVHDFPKYSIKVL---P-WLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVP 270
Cdd:cd05598   136 RDGHIKLTdfGLCTGF---------RWTHDSKYYLAHSLvgtPnYIAPEVLLR--TGYTQLCDWWSVGVILYEMLVGQPP 204
                         170
                  ....*....|.
gi 1958659070 271 F-KDMPA-TQM 279
Cdd:cd05598   205 FlAQTPAeTQL 215
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
61-302 3.19e-09

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called Doublecortin-like and CAM kinase-like 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL2 (or DCAMKL2) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL2 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL2 has been shown to interact with tubulin, JIP1/2, JNK, neurabin 2, and actin. It is associated with the terminal segments of axons and dendrites, and may function as a phosphorylation-dependent switch to control microtubule dynamics in neuronal growth cones. The DCKL2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 57.35  E-value: 3.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMvTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTS 140
Cdd:cd14184     3 YKIGKVIGDG--NFAVVKECVERSTGKEFALKIIDKAKCCGKE-HLIENEVSILRRVKHPNIIMLIEEMDTPAELYLVME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 141 FMAYGSAKDLIGTHfmDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTdgkvYLSGLRSnLSMISHGqrQR 220
Cdd:cd14184    80 LVKGGDLFDAITSS--TKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVCE----YPDGTKS-LKLGDFG--LA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 221 AVHDFPKYSIKVLP-WLSPEVLQQNlqGYDAKSDIYSVGITACELANGHVPFK-------DMpATQMLLEKLNGTVPcLL 292
Cdd:cd14184   151 TVVEGPLYTVCGTPtYVAPEIIAET--GYGLKVDIWAAGVITYILLCGFPPFRsennlqeDL-FDQILLGKLEFPSP-YW 226
                         250
                  ....*....|
gi 1958659070 293 DTSTIPAEEL 302
Cdd:cd14184   227 DNITDSAKEL 236
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
61-272 3.39e-09

Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phototropins are blue-light receptors that control responses such as phototropism, stromatal opening, and chloroplast movement in order to optimize the photosynthetic efficiency of plants. They are light-activated STKs that contain an N-terminal photosensory domain and a C-terminal catalytic domain. The N-terminal domain contains two LOV (Light, Oxygen or Voltage) domains that binds FMN. Photoexcitation of the LOV domains results in autophosphorylation at multiple sites and activation of the catalytic domain. In addition to plant phototropins, included in this subfamily are predominantly uncharacterized fungal STKs whose catalytic domains resemble the phototropin kinase domain. One protein from Neurospora crassa is called nrc-2, which plays a role in growth and development by controlling entry into the conidiation program. The phototropin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 57.63  E-value: 3.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNE-MVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVT 139
Cdd:cd05574     3 FKKIKLLGKG--DVGRVYLVRLKGTGKLFAMKVLDKEEMIKRnKVKRVLTEREILATLDHPFLPTLYASFQTSTHLCFVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 140 SFMAYGSAKDLIGTHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLrsNLSMISH---- 215
Cdd:cd05574    81 DYCPGGELFRLLQKQPGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDF--DLSKQSSvtpp 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958659070 216 --------GQRQRAVHDFPKYSIKVLP------------WLSPEVLQQNlqGYDAKSDIYSVGITACELANGHVPFK 272
Cdd:cd05574   159 pvrkslrkGSRRSSVKSIEKETFVAEPsarsnsfvgteeYIAPEVIKGD--GHGSAVDWWTLGILLYEMLYGTTPFK 233
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
61-273 3.58e-09

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


Pssm-ID: 270980 [Multi-domain]  Cd Length: 257  Bit Score: 57.01  E-value: 3.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTfLQGELHVSKLFSHPNIVPYRATFIADNELWAVTS 140
Cdd:cd14078     5 YELHETIGSG--GFAKVKLATHILTGEKVAIKIMDKKALGDDLPR-VKTEIEALKNLSHQHICRLYHVIETDNKIFMVLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 141 FMAYGSAKDLIGTHfmDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYL----------SGLRSNL 210
Cdd:cd14078    82 YCPGGELFDYIVAK--DRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLidfglcakpkGGMDHHL 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958659070 211 sMISHGQrqravhdfPKYSikvlpwlSPEvLQQNLQGYDAKSDIYSVGITACELANGHVPFKD 273
Cdd:cd14078   160 -ETCCGS--------PAYA-------APE-LIQGKPYIGSEADVWSMGVLLYALLCGFLPFDD 205
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
65-274 3.72e-09

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


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 57.28  E-value: 3.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  65 SVIGKG-FEDlmtVNLARYKptGEYVTVRRINleacSNEMVTFL-QGELHVSKLFSHPNIVPYRATFIADN----ELWAV 138
Cdd:cd14056     1 KTIGKGrYGE---VWLGKYR--GEKVAVKIFS----SRDEDSWFrETEIYQTVMLRHENILGFIAADIKSTgswtQLWLI 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 139 TSFMAYGSAKDLIGTHFMDGMSELAIAY-ILQGvlkaLDYIHH--MGY------VHRSVKASHILISTDGKVYLSGLRSN 209
Cdd:cd14056    72 TEYHEHGSLYDYLQRNTLDTEEALRLAYsAASG----LAHLHTeiVGTqgkpaiAHRDLKSKNILVKRDGTCCIADLGLA 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 210 LSmishGQRQRAVHDfPKYSIKV--LPWLSPEVLQQNLQG--YDA--KSDIYSVGITACELA-----NGHV-----PFKD 273
Cdd:cd14056   148 VR----YDSDTNTID-IPPNPRVgtKRYMAPEVLDDSINPksFESfkMADIYSFGLVLWEIArrceiGGIAeeyqlPYFG 222

                  .
gi 1958659070 274 M 274
Cdd:cd14056   223 M 223
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
61-264 3.84e-09

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


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 57.51  E-value: 3.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEacsNEMVTF---LQGELHVSKLFSHPNIVPYRATFIADNE--- 134
Cdd:cd07864     9 FDIIGIIGEG--TYGQVYKAKDKDTGELVALKKVRLD---NEKEGFpitAIREIKILRQLNHRSVVNLKEIVTDKQDald 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 135 -------LWAVTSFMAYgsakDLIGThFMDGM---SELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS 204
Cdd:cd07864    84 fkkdkgaFYLVFEYMDH----DLMGL-LESGLvhfSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLA 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958659070 205 GLrsNLSMISHGQRQRAvhdfpkYSIKVLP-WLSPEVLQQNLQGYDAKSDIYSVGITACEL 264
Cdd:cd07864   159 DF--GLARLYNSEESRP------YTNKVITlWYRPPELLLGEERYGPAIDVWSCGCILGEL 211
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
61-271 3.97e-09

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


Pssm-ID: 271063 [Multi-domain]  Cd Length: 255  Bit Score: 56.89  E-value: 3.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARyKPTGEYVTVRRINLEACSNEM-VTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVT 139
Cdd:cd14161     5 YEFLETLGKG--TYGRVKKAR-DSSGRLVAIKSIRKDRIKDEQdLLHIRREIEIMSSLNHPHIISVYEVFENSSKIVIVM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 140 SFMAYGSAKDLIGTHfmDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLrsNLSMISHGQRQ 219
Cdd:cd14161    82 EYASRGDLYDYISER--QRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADF--GLSNLYNQDKF 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958659070 220 RAVH-DFPKYS----IKVLPWLSPEVlqqnlqgydaksDIYSVGITACELANGHVPF 271
Cdd:cd14161   158 LQTYcGSPLYAspeiVNGRPYIGPEV------------DSWSLGVLLYILVHGTMPF 202
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
61-273 4.35e-09

Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CRIK (also called citron kinase) is an effector of the small GTPase Rho. It plays an important function during cytokinesis and affects its contractile process. CRIK-deficient mice show severe ataxia and epilepsy as a result of abnormal cytokinesis and massive apoptosis in neuronal precursors. A Down syndrome critical region protein TTC3 interacts with CRIK and inhibits CRIK-dependent neuronal differentiation and neurite extension. CRIK contains a catalytic domain, a central coiled-coil domain, and a C-terminal region containing a Rho-binding domain (RBD), a zinc finger, and a pleckstrin homology (PH) domain, in addition to other motifs. The CRIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 57.71  E-value: 4.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKG-FEDlmtVNLARYKPTGEYVTVRRIN-LEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAV 138
Cdd:cd05601     3 FEVKNVIGRGhFGE---VQVVKEKATGDIYAMKVLKkSETLAQEEVSFFEEERDIMAKANSPWITKLQYAFQDSENLYLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 139 TSFMAYGsakDLIG--THFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLRSNLSMISHG 216
Cdd:cd05601    80 MEYHPGG---DLLSllSRYDDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGSAAKLSSDK 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958659070 217 qrqravHDFPKYSIKVLPWLSPEVLQ----QNLQGYDAKSDIYSVGITACELANGHVPFKD 273
Cdd:cd05601   157 ------TVTSKMPVGTPDYIAPEVLTsmngGSKGTYGVECDWWSLGIVAYEMLYGKTPFTE 211
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
61-371 4.45e-09

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


Pssm-ID: 270848 [Multi-domain]  Cd Length: 310  Bit Score: 57.38  E-value: 4.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKG-FEDlmtVNLARYKPTGEYVTVRRINLEacsNEM----VTFLQgELHVSKLFSHPNIVP----------- 124
Cdd:cd07865    14 YEKLAKIGQGtFGE---VFKARHRKTGQIVALKKVLME---NEKegfpITALR-EIKILQLLKHENVVNlieicrtkatp 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 125 ---YRATFiadnelWAVTSFMAYGSAKDLIGTHFMDGMSElaIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKV 201
Cdd:cd07865    87 ynrYKGSI------YLVFEFCEHDLAGLLSNKNVKFTLSE--IKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGVL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 202 YLS--GLRSNLSMISHGQRQRavhdfpkYSIKVLP-WLSPEVLQQNLQGYDAKSDIYSVGITACELANGHVPFK-DMPAT 277
Cdd:cd07865   159 KLAdfGLARAFSLAKNSQPNR-------YTNRVVTlWYRPPELLLGERDYGPPIDMWGAGCIMAEMWTRSPIMQgNTEQH 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 278 QM-LLEKLNGTV-----PCLLDTSTIPAEELTMSPSRSIANpglndslaagSLRPANGDspshpyhrtfsPHFHNFVEQC 351
Cdd:cd07865   232 QLtLISQLCGSItpevwPGVDKLELFKKMELPQGQKRKVKE----------RLKPYVKD-----------PYALDLIDKL 290
                         330       340
                  ....*....|....*....|
gi 1958659070 352 LQRNPDARPNASTLLNHSFF 371
Cdd:cd07865   291 LVLDPAKRIDADTALNHDFF 310
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
61-271 5.02e-09

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


Pssm-ID: 270975 [Multi-domain]  Cd Length: 254  Bit Score: 56.63  E-value: 5.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNE--MVTfLQGELHVSKLFSHPNIVPYRATFIADNELWAV 138
Cdd:cd14073     3 YELLETLGKG--TYGKVKLAIERATGREVAIKSIKKDKIEDEqdMVR-IRREIEIMSSLNHPHIIRIYEVFENKDKIVIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 139 TSFMAYGSAKDLIGTHfmDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLrSNlsmisHG 216
Cdd:cd14073    80 MEYASGGELYDYISER--RRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIAdfGL-SN-----LY 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958659070 217 QRQRAVHDF---PKYS----IKVLPWLSPEVlqqnlqgydaksDIYSVGITACELANGHVPF 271
Cdd:cd14073   152 SKDKLLQTFcgsPLYAspeiVNGTPYQGPEV------------DCWSLGVLLYTLVYGTMPF 201
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
60-274 5.05e-09

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


Pssm-ID: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 56.80  E-value: 5.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  60 CYELLSVIGKGfeDLMTVNLARYKPTGE---YVTVRRINLEACSNEMVTFLqGELHVSKLFSHPNIVPYRATFIADNELW 136
Cdd:cd05065     5 CVKIEEVIGAG--EFGEVCRGRLKLPGKreiFVAIKTLKSGYTEKQRRDFL-SEASIMGQFDHPNIIHLEGVVTKSRPVM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 137 AVTSFMAYGSAKDLIGTHfmDG-MSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTD--GKVYLSGLRSNLsmi 213
Cdd:cd05065    82 IITEFMENGALDSFLRQN--DGqFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNlvCKVSDFGLSRFL--- 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958659070 214 shgqrQRAVHDfPKYSIKV---LP--WLSPEVLQqnLQGYDAKSDIYSVGITACE-LANGHVPFKDM 274
Cdd:cd05065   157 -----EDDTSD-PTYTSSLggkIPirWTAPEAIA--YRKFTSASDVWSYGIVMWEvMSYGERPYWDM 215
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
62-271 5.22e-09

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


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 56.66  E-value: 5.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  62 ELLSVIGKGFedLMTVNLARY-KPTGEYVTVRRINLEACSNEMVT--FLQgELHVSKLFSHPNIVPYRATfIADNELWAV 138
Cdd:cd05056     9 TLGRCIGEGQ--FGDVYQGVYmSPENEKIAVAVKTCKNCTSPSVRekFLQ-EAYIMRQFDHPHIVKLIGV-ITENPVWIV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 139 TSFMAYGSAKDLIGTHFMDGMSELAIAYILQgVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLrsnlsmishg 216
Cdd:cd05056    85 MELAPLGELRSYLQVNKYSLDLASLILYAYQ-LSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGdfGL---------- 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 217 qrQRAVHD--FPKYSIKVLP--WLSPEVLqqNLQGYDAKSDIYSVGITACE-LANGHVPF 271
Cdd:cd05056   154 --SRYMEDesYYKASKGKLPikWMAPESI--NFRRFTSASDVWMFGVCMWEiLMLGVKPF 209
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
61-370 5.25e-09

Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle 1 (also called TTK); Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TTK/Mps1 is a spindle checkpoint kinase that was first discovered due to its necessity in centrosome duplication in budding yeast. It was later found to function in the spindle assembly checkpoint, which monitors the proper attachment of chromosomes to the mitotic spindle. In yeast, substrates of Mps1 include the spindle pole body components Spc98p, Spc110p, and Spc42p. The TTK/Mps1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 56.84  E-value: 5.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGFEDlmTVNLARYkPTGEYVTVRRINLEACSNEMVTFLQGEL-HVSKLFSHPNIVP---YRATFiADNELW 136
Cdd:cd14131     3 YEILKQLGKGGSS--KVYKVLN-PKKKIYALKRVDLEGADEQTLQSYKNEIeLLKKLKGSDRIIQlydYEVTD-EDDYLY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 137 AVtsfMAYGSAkDL---IGTHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILIstdgkvylsgLRSNLSMI 213
Cdd:cd14131    79 MV---MECGEI-DLatiLKKKRPKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLL----------VKGRLKLI 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 214 shgqrqravhDF------PKYSIKV--------LPWLSPEVLQQNLQGYDAK--------SDIYSVGITACELANGHVPF 271
Cdd:cd14131   145 ----------DFgiakaiQNDTTSIvrdsqvgtLNYMSPEAIKDTSASGEGKpkskigrpSDVWSLGCILYQMVYGKTPF 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 272 KDMPAtqmLLEKLNGtvpcLLDtstiPAEELTMSPsrsIANPGLNDSLaagslrpangdspshpyhrtfsphfhnfvEQC 351
Cdd:cd14131   215 QHITN---PIAKLQA----IID----PNHEIEFPD---IPNPDLIDVM-----------------------------KRC 251
                         330
                  ....*....|....*....
gi 1958659070 352 LQRNPDARPNASTLLNHSF 370
Cdd:cd14131   252 LQRDPKKRPSIPELLNHPF 270
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
164-371 5.36e-09

Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like protein kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity DYRKs and YAK1, as well as the S/T kinases (STKs), HIPKs. DYRKs and YAK1 autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. Proteins in this subfamily play important roles in cell proliferation, differentiation, survival, growth, and development. The DYRK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271035 [Multi-domain]  Cd Length: 262  Bit Score: 56.51  E-value: 5.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 164 IAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGkvylsglRSNLSMISHGQrQRAVHDFPKYSIKVLPWLSPEVLQq 243
Cdd:cd14133   104 IRKIAQQILEALVFLHSLGLIHCDLKPENILLASYS-------RCQIKIIDFGS-SCFLTQRLYSYIQSRYYRAPEVIL- 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 244 nlqG--YDAKSDIYSVGITACELANGHVPFKDMPATQMLleklngtvPCLLDTSTIPaeeltmsPSRSIANPGLNDSLaa 321
Cdd:cd14133   175 ---GlpYDEKIDMWSLGCILAELYTGEPLFPGASEVDQL--------ARIIGTIGIP-------PAHMLDQGKADDEL-- 234
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958659070 322 gslrpangdspshpyhrtfsphFHNFVEQCLQRNPDARPNASTLLNHSFF 371
Cdd:cd14133   235 ----------------------FVDFLKKLLEIDPKERPTASQALSHPWL 262
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
107-371 5.37e-09

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


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 56.46  E-value: 5.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 107 LQGELHVSKLFSHPNIVpyraTFI------ADNELWAVTSFMAYGSAKDLIGTHfmDGMSELAIAYILQGVLKALDYIHH 180
Cdd:cd13983    47 FKQEIEILKSLKHPNII----KFYdsweskSKKEVIFITELMTSGTLKQYLKRF--KRLKLKVIKSWCRQILEGLNYLHT 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 181 MGY--VHRSVKASHILI-STDGKVYLSGLrsNLSMISHGQRQRAVHDFPKYsikvlpwLSPEVLQQNlqgYDAKSDIYSV 257
Cdd:cd13983   121 RDPpiIHRDLKCDNIFInGNTGEVKIGDL--GLATLLRQSFAKSVIGTPEF-------MAPEMYEEH---YDEKVDIYAF 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 258 GITACELANGHVPFKDMPATQMLLEKLngtvpclldTSTIPAEELtmspsRSIANPGLNDslaagslrpangdspshpyh 337
Cdd:cd13983   189 GMCLLEMATGEYPYSECTNAAQIYKKV---------TSGIKPESL-----SKVKDPELKD-------------------- 234
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1958659070 338 rtfsphfhnFVEQCLqRNPDARPNASTLLNHSFF 371
Cdd:cd13983   235 ---------FIEKCL-KPPDERPSARELLEHPFF 258
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
61-284 5.82e-09

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


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 56.92  E-value: 5.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKG-FEDlmtVNLARYKPTGEYVT---VRRINLEACSNemvtfLQGELHVSKLFSHPNIVPYRATFIADNELW 136
Cdd:cd14166     5 FIFMEVLGSGaFSE---VYLVKQRSTGKLYAlkcIKKSPLSRDSS-----LENEIAVLKRIKHENIVTLEDIYESTTHYY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 137 AVTSFMAYGSAKDLI---GTHfmdgmSELAIAYILQGVLKALDYIHHMGYVHRSVKASHIListdgkvYLSGLRSNLSMI 213
Cdd:cd14166    77 LVMQLVSGGELFDRIlerGVY-----TEKDASRVINQVLSAVKYLHENGIVHRDLKPENLL-------YLTPDENSKIMI 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958659070 214 SH-GQRQRAVHDFPKYSIKVLPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQmLLEKL 284
Cdd:cd14166   145 TDfGLSKMEQNGIMSTACGTPGYVAPEVLAQ--KPYSKAVDCWSIGVITYILLCGYPPFYEETESR-LFEKI 213
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
77-302 6.00e-09

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


Pssm-ID: 270960 [Multi-domain]  Cd Length: 253  Bit Score: 56.29  E-value: 6.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  77 VNLARYKptGEYVTVRRINLEACSNEMVTFLQgelHVSKLfSHPNIVPYRATFIADNELWAVTSFMAYGSAKDLIgtHFM 156
Cdd:cd14058     9 VCKARWR--NQIVAVKIIESESEKKAFEVEVR---QLSRV-DHPNIIKLYGACSNQKPVCLVMEYAEGGSLYNVL--HGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 157 DGM----SELAIAYILQGVlKALDYIHHMG---YVHRSVKASHILISTDGKVylsglrsnLSMISHGqrqrAVHDFPKYS 229
Cdd:cd14058    81 EPKpiytAAHAMSWALQCA-KGVAYLHSMKpkaLIHRDLKPPNLLLTNGGTV--------LKICDFG----TACDISTHM 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958659070 230 IK---VLPWLSPEVLQQNLqgYDAKSDIYSVGITACELANGHVPFKDM--PATQMLLEKLNGTVPCLLDTSTIPAEEL 302
Cdd:cd14058   148 TNnkgSAAWMAPEVFEGSK--YSEKCDVFSWGIILWEVITRRKPFDHIggPAFRIMWAVHNGERPPLIKNCPKPIESL 223
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
89-371 6.62e-09

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek9, also called Nercc1, is primarily a cytoplasmic protein but can also localize in the nucleus. It is involved in modulating chromosome alignment and splitting during mitosis. It interacts with the gamma-tubulin ring complex and the Ran GTPase, and is implicated in microtubule organization. Nek9 associates with FACT (FAcilitates Chromatin Transcription) and modulates interphase progression. It also interacts with Nek6, and Nek7, during mitosis, resulting in their activation. Nek9 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 56.28  E-value: 6.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  89 VTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGSAKDLIGTHFMDGMSELAIAYIL 168
Cdd:cd08221    28 VVWKEVNLSRLSEKERRDALNEIDILSLLNHDNIITYYNHFLDGESLFIEMEYCNGGNLHDKIAQQKNQLFPEEVVLWYL 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 169 QGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSNLSmiSHGQRQRAVHDFPKYsikvlpwLSPEVLQQNlq 246
Cdd:cd08221   108 YQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGdfGISKVLD--SESSMAESIVGTPYY-------MSPELVQGV-- 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 247 GYDAKSDIYSVGitacelanghvpfkdmpatqmlleklngtvpCLLdtstipAEELTMSPSRSIANPgLNdsLAAGSLRP 326
Cdd:cd08221   177 KYNFKSDIWAVG-------------------------------CVL------YELLTLKRTFDATNP-LR--LAVKIVQG 216
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1958659070 327 ANGDSPShpyhrTFSPHFHNFVEQCLQRNPDARPNASTLLNHSFF 371
Cdd:cd08221   217 EYEDIDE-----QYSEEIIQLVHDCLHQDPEDRPTAEELLERPLL 256
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
61-373 7.03e-09

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


Pssm-ID: 173742 [Multi-domain]  Cd Length: 309  Bit Score: 56.99  E-value: 7.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGFEDLmtVNLARYKPTGEYVTVRRINLEACSNEM-VTFLQgELHVSKLFSHPNIVPYRATfIADNELWAVT 139
Cdd:cd07845     9 FEKLNRIGEGTYGI--VYRARDTTSGEIVALKKVRMDNERDGIpISSLR-EITLLLNLRHPNIVELKEV-VVGKHLDSIF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 140 SFMAYgSAKDLigTHFMDGM----SELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSNLSMI 213
Cdd:cd07845    85 LVMEY-CEQDL--ASLLDNMptpfSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIAdfGLARTYGLP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 214 SHGQRQRAVhdfpkysikVLPWLSPEVLQQNLQgYDAKSDIYSVGITACELAnGHVPFkdMPATQMlLEKLNGTVpclld 293
Cdd:cd07845   162 AKPMTPKVV---------TLWYRAPELLLGCTT-YTTAIDMWAVGCILAELL-AHKPL--LPGKSE-IEQLDLII----- 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 294 tstipaeELTMSPSRSIAnPGLNDSLAAGSLRpangdSPSHPYHrTFSPHFH-------NFVEQCLQRNPDARPNASTLL 366
Cdd:cd07845   223 -------QLLGTPNESIW-PGFSDLPLVGKFT-----LPKQPYN-NLKHKFPwlseaglRLLNFLLMYDPKKRATAEEAL 288

                  ....*..
gi 1958659070 367 NHSFFKQ 373
Cdd:cd07845   289 ESSYFKE 295
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
61-271 8.79e-09

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: 56.02  E-value: 8.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTS 140
Cdd:cd14097     3 YTFGRKLGQG--SFGVVIEATHKETQTKWAIKKINREKAGSSAVKLLEREVDILKHVNHAHIIHLEEVFETPKRMYLVME 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 141 FMAYGSAKDLIGT--HFmdgmSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDgkVYLSGLRSNLSMISHG-- 216
Cdd:cd14097    81 LCEDGELKELLLRkgFF----SENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSS--IIDNNDKLNIKVTDFGls 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958659070 217 -QRQRAVHDFPKYSIKVLPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPF 271
Cdd:cd14097   155 vQKYGLGEDMLQETCGTPIYMAPEVISA--HGYSQQCDIWSIGVIMYMLLCGEPPF 208
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
107-273 8.90e-09

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271020 [Multi-domain]  Cd Length: 275  Bit Score: 56.21  E-value: 8.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 107 LQGELHVSKLFSHPNIV--------PyratfiADNELWAVTSFMAYGSAKDLIGTHFMDgmSELAIAYiLQGVLKALDYI 178
Cdd:cd14118    61 VYREIAILKKLDHPNVVklvevlddP------NEDNLYMVFELVDKGAVMEVPTDNPLS--EETARSY-FRDIVLGIEYL 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 179 HHMGYVHRSVKASHILISTDGKVYLSGLrsNLSMISHGqrqraVHDFPKYSIKVLPWLSPEVLQQNLQGYDAKS-DIYSV 257
Cdd:cd14118   132 HYQKIIHRDIKPSNLLLGDDGHVKIADF--GVSNEFEG-----DDALLSSTAGTPAFMAPEALSESRKKFSGKAlDIWAM 204
                         170
                  ....*....|....*.
gi 1958659070 258 GITACELANGHVPFKD 273
Cdd:cd14118   205 GVTLYCFVFGRCPFED 220
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
76-271 9.60e-09

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: 56.08  E-value: 9.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  76 TVNLARYKPTGEYVTVRRINLEACSNEM-VTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGSAKDLIgtH 154
Cdd:cd05572     8 RVELVQLKSKGRTFALKCVKKRHIVQTRqQEHIFSEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLGGELWTIL--R 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 155 FMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLsglrsnlsmISHG-----QRQRAVHDF---P 226
Cdd:cd05572    86 DRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKL---------VDFGfakklGSGRKTWTFcgtP 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1958659070 227 KYsikvlpwLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPF 271
Cdd:cd05572   157 EY-------VAPEIILN--KGYDFSVDYWSLGILLYELLTGRPPF 192
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
146-371 9.62e-09

Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271009 [Multi-domain]  Cd Length: 257  Bit Score: 56.05  E-value: 9.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 146 SAKDLIGTHFMDG-MSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILIstdgkvyLSGLRSNLSMISHGQRQRAVHD 224
Cdd:cd14107    81 SSEELLDRLFLKGvVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILM-------VSPTREDIKICDFGFAQEITPS 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 225 FPKYSIKVLP-WLSPEVLQQNlqGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVpclldtstipaeelt 303
Cdd:cd14107   154 EHQFSKYGSPeFVAPEIVHQE--PVSAATDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEGVV--------------- 216
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958659070 304 mspsrsianpglndslaagslrpangdSPSHPYHRTFSPHFHNFVEQCLQRNPDARPNASTLLNHSFF 371
Cdd:cd14107   217 ---------------------------SWDTPEITHLSEDAKDFIKRVLQPDPEKRPSASECLSHEWF 257
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
118-274 1.02e-08

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


Pssm-ID: 270733 [Multi-domain]  Cd Length: 278  Bit Score: 56.07  E-value: 1.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 118 SHPNIVPYRATFIADNELWAVTSFMAYGSAKDLIgtHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILIST 197
Cdd:cd05581    59 AHPGIVKLYYTFQDESKLYFVLEYAPNGDLLEYI--RKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDE 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 198 DGKVYL---------------SGLRSNLSMISHGQRQRAvHDF---PKYsikvlpwLSPEVLQQNLQGYDakSDIYSVGI 259
Cdd:cd05581   137 DMHIKItdfgtakvlgpdsspESTKGDADSQIAYNQARA-ASFvgtAEY-------VSPELLNEKPAGKS--SDLWALGC 206
                         170
                  ....*....|....*
gi 1958659070 260 TACELANGHVPFKDM 274
Cdd:cd05581   207 IIYQMLTGKPPFRGS 221
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
109-285 1.02e-08

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


Pssm-ID: 133194 [Multi-domain]  Cd Length: 268  Bit Score: 56.14  E-value: 1.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 109 GELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGSAKDLIGTHfmDG-MSELAIAYILQGVLKALDYIHHMGYVHRS 187
Cdd:cd05063    55 SEASIMGQFSHHNIIRLEGVVTKFKPAMIITEYMENGALDKYLRDH--DGeFSSYQLVGMLRGIAAGMKYLSDMNYVHRD 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 188 VKASHILISTD--GKVYLSGLrsnlsmishgqrQRAVHDFPKYSIKV------LPWLSPEVLqqNLQGYDAKSDIYSVGI 259
Cdd:cd05063   133 LAARNILVNSNleCKVSDFGL------------SRVLEDDPEGTYTTsggkipIRWTAPEAI--AYRKFTSASDVWSFGI 198
                         170       180
                  ....*....|....*....|....*..
gi 1958659070 260 TACE-LANGHVPFKDMpATQMLLEKLN 285
Cdd:cd05063   199 VMWEvMSFGERPYWDM-SNHEVMKAIN 224
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
106-271 1.13e-08

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


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 55.60  E-value: 1.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 106 FLQGELHVSKLFSHPNIV-PYRATfiaDNELWAVTSFMAYGSAKDLI---GTHFMDGMSELAIAYILQGVLKALDYIHHM 181
Cdd:cd14109    42 FLMREVDIHNSLDHPNIVqMHDAY---DDEKLAVTVIDNLASTIELVrdnLLPGKDYYTERQVAVFVRQLLLALKHMHDL 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 182 GYVHRSVKASHILISTDgkvylsglrsNLSMISHGQRQRAVHDFPKYSIKVLP-WLSPEVLqqNLQGYDAKSDIYSVGIT 260
Cdd:cd14109   119 GIAHLDLRPEDILLQDD----------KLKLADFGQSRRLLRGKLTTLIYGSPeFVSPEIV--NSYPVTLATDMWSVGVL 186
                         170
                  ....*....|.
gi 1958659070 261 ACELANGHVPF 271
Cdd:cd14109   187 TYVLLGGISPF 197
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
60-271 1.15e-08

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: 56.01  E-value: 1.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  60 CYELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEA-CSNEMVTF--LQGELHVSKLFSHPNIVPYRATFIADNELW 136
Cdd:cd14094     4 VYELCEVIGKG--PFSVVRRCIHRETGQQFAVKIVDVAKfTSSPGLSTedLKREASICHMLKHPHIVELLETYSSDGMLY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 137 AVTSFMaygSAKDL---IGTHFMDGM--SELAIAYILQGVLKALDYIHHMGYVHRSVKASHILIS---TDGKVYLSGL-- 206
Cdd:cd14094    82 MVFEFM---DGADLcfeIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLAskeNSAPVKLGGFgv 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958659070 207 ---RSNLSMISHGQrqravhdfpkysIKVLPWLSPEVLQQNLqgYDAKSDIYSVGITACELANGHVPF 271
Cdd:cd14094   159 aiqLGESGLVAGGR------------VGTPHFMAPEVVKREP--YGKPVDVWGCGVILFILLSGCLPF 212
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
62-300 1.40e-08

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


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 55.43  E-value: 1.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  62 ELLSVIGKGfeDLMTVNLARYKptGEyVTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTSF 141
Cdd:cd14063     3 EIKEVIGKG--RFGRVHRGRWH--GD-VAIKLLNIDYLNEEQLEAFKEEVAAYKNTRHDNLVLFMGACMDPPHLAIVTSL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 142 MAYGSAKDLIGTHFMD-GMSElaIAYILQGVLKALDYIHHMGYVHRSVKASHILIStDGKVYLS--GLRSNLSMISHGQR 218
Cdd:cd14063    78 CKGRTLYSLIHERKEKfDFNK--TVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLE-NGRVVITdfGLFSLSGLLQPGRR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 219 Q---RAVHDFpkysikvLPWLSPEV---LQQNLQG-----YDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGT 287
Cdd:cd14063   155 EdtlVIPNGW-------LCYLAPEIiraLSPDLDFeeslpFTKASDVYAFGTVWYELLAGRWPFKEQPAESIIWQVGCGK 227
                         250
                  ....*....|...
gi 1958659070 288 VPCLLDTStIPAE 300
Cdd:cd14063   228 KQSLSQLD-IGRE 239
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
95-274 1.43e-08

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


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 55.28  E-value: 1.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  95 NLEACSNEMVTFLQgELHVSKLFSHPNIVPYRATfIADNELWAVTSFMAYGSAKDLIGThfmDGMSELAIAYILQ---GV 171
Cdd:cd05067    38 SLKQGSMSPDAFLA-EANLMKQLQHQRLVRLYAV-VTQEPIYIITEYMENGSLVDFLKT---PSGIKLTINKLLDmaaQI 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 172 LKALDYIHHMGYVHRSVKASHILISTD--GKVYLSGLRSNLSMISHGQRQRAvhdfpKYSIKvlpWLSPEVLqqNLQGYD 249
Cdd:cd05067   113 AEGMAFIEERNYIHRDLRAANILVSDTlsCKIADFGLARLIEDNEYTAREGA-----KFPIK---WTAPEAI--NYGTFT 182
                         170       180
                  ....*....|....*....|....*.
gi 1958659070 250 AKSDIYSVGITACELAN-GHVPFKDM 274
Cdd:cd05067   183 IKSDVWSFGILLTEIVThGRIPYPGM 208
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
61-273 1.46e-08

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


Pssm-ID: 271064 [Multi-domain]  Cd Length: 259  Bit Score: 55.38  E-value: 1.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVT-FLQGELHVSKLFSHPNIVPYRATFIADNELWAVT 139
Cdd:cd14162     2 YIVGKTLGHG--SYAVVKKAYSTKHKCKVAIKIVSKKKAPEDYLQkFLPREIEVIKGLKHPNLICFYEAIETTSRVYIIM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 140 SFMAYGSAKDLIGTHfmDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGL---RSNLsmishg 216
Cdd:cd14162    80 ELAENGDLLDYIRKN--GALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFgfaRGVM------ 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958659070 217 qrqRAVHDFPKYS---IKVLPWLSPEVLQQNLqgYDAK-SDIYSVGITACELANGHVPFKD 273
Cdd:cd14162   152 ---KTKDGKPKLSetyCGSYAYASPEILRGIP--YDPFlSDIWSMGVVLYTMVYGRLPFDD 207
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
67-295 1.76e-08

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: 55.22  E-value: 1.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  67 IGKGFedLMTVNLARYKPTGEYVTVRRINLEACSNEMVTflqgELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGS 146
Cdd:cd14156     1 IGSGF--FSKVYKVTHGATGKVMVVKIYKNDVDQHKIVR----EISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGC 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 147 AKDLIGThfmdgmSELAIAYILQGVL-----KALDYIHHMGYVHRSVKASHILISTDGKVyLSGLRSNLSMishgqrQRA 221
Cdd:cd14156    75 LEELLAR------EELPLSWREKVELacdisRGMVYLHSKNIYHRDLNSKNCLIRVTPRG-REAVVTDFGL------ARE 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 222 VHDFP------KYS-IKVLPWLSPEVLQQnlQGYDAKSDIYSVGITACELAnGHVPF--KDMPAT-------QMLLEKLN 285
Cdd:cd14156   142 VGEMPandperKLSlVGSAFWMAPEMLRG--EPYDRKVDVFSFGIVLCEIL-ARIPAdpEVLPRTgdfgldvQAFKEMVP 218
                         250
                  ....*....|
gi 1958659070 286 GTVPCLLDTS 295
Cdd:cd14156   219 GCPEPFLDLA 228
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
61-370 1.94e-08

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


Pssm-ID: 271088 [Multi-domain]  Cd Length: 256  Bit Score: 54.87  E-value: 1.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNE-MVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVT 139
Cdd:cd14186     3 FKVLNLLGKG--SFACVYRARSLHTGLEVAIKMIDKKAMQKAgMVQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 140 SFMAYGSAKDLIgTHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSNLSMIShgQ 217
Cdd:cd14186    81 EMCHNGEMSRYL-KNRKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIAdfGLATQLKMPH--E 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 218 RQRAVHDFPKYsikvlpwLSPEVLQQNLQGYDakSDIYSVGITACELANGHVPFkdmpatqmlleklngtvpcllDTSTI 297
Cdd:cd14186   158 KHFTMCGTPNY-------ISPEIATRSAHGLE--SDVWSLGCMFYTLLVGRPPF---------------------DTDTV 207
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958659070 298 PAEeltmspsrsianpgLNDSLAAGSLRPANgdspshpyhrtFSPHFHNFVEQCLQRNPDARPNASTLLNHSF 370
Cdd:cd14186   208 KNT--------------LNKVVLADYEMPAF-----------LSREAQDLIHQLLRKNPADRLSLSSVLDHPF 255
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
61-273 1.99e-08

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: 55.03  E-value: 1.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKgfEDLMTVNLARYKPTGEYVTVRRInLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAvts 140
Cdd:cd14088     3 YDLGQVIKT--EEFCEIFRAKDKTTGKLYTCKKF-LKRDGRKVRKAAKNEINILKMVKHPNILQLVDVFETRKEYFI--- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 141 FMAYGSAKDLIGTHFMDGM-SELAIAYILQGVLKALDYIHHMGYVHRSVKASHIlistdgkVYLSGLRSNLSMISHGQRQ 219
Cdd:cd14088    77 FLELATGREVFDWILDQGYySERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENL-------VYYNRLKNSKIVISDFHLA 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958659070 220 RAVHDFPKYSIKVLPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKD 273
Cdd:cd14088   150 KLENGLIKEPCGTPEYLAPEVVGR--QRYGRPVDCWAIGVIMYILLSGNPPFYD 201
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
76-370 2.00e-08

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


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 54.98  E-value: 2.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  76 TVNLARYKPTGEYVTVRRI------NLEACsnemvtflQGELHVSKLFS-HPNIVPYRATFIAD--NELWAVTSFMAYGS 146
Cdd:cd14037    18 HVYLVKTSNGGNRAALKRVyvndehDLNVC--------KREIEIMKRLSgHKNIVGYIDSSANRsgNGVYEVLLLMEYCK 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 147 AK---DLIGTHFMDGMSELAIAYILQGVLKALDYIHHMG--YVHRSVKASHILISTDGKVYL----SGLRSNLSMISHGQ 217
Cdd:cd14037    90 GGgviDLMNQRLQTGLTESEILKIFCDVCEAVAAMHYLKppLIHRDLKVENVLISDSGNYKLcdfgSATTKILPPQTKQG 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 218 RQRAVHDFPKYSikVLPWLSPEVLQQNL-QGYDAKSDIYSVGItacelanghvpfkdmpatqmLLEKLngtvpCLLdtsT 296
Cdd:cd14037   170 VTYVEEDIKKYT--TLQYRAPEMIDLYRgKPITEKSDIWALGC--------------------LLYKL-----CFY---T 219
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958659070 297 IPAEEltmspsrsianpglndslaAGSLRPANGDSPSHPYHRtFSPHFHNFVEQCLQRNPDARPNASTLLNHSF 370
Cdd:cd14037   220 TPFEE-------------------SGQLAILNGNFTFPDNSR-YSKRLHKLIRYMLEEDPEKRPNIYQVSYEAF 273
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
119-280 2.01e-08

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: 55.20  E-value: 2.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 119 HPNIVPYRATFIADNELWAVTSFMAYGSAKDLIGT------HFmdgmSELAIAYILQGVLKALDYIH-HMGYVHRSVKAS 191
Cdd:cd08528    68 HPNIVRYYKTFLENDRLYIVMELIEGAPLGEHFSSlkekneHF----TEDRIWNIFVQMVLALRYLHkEKQIVHRDLKPN 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 192 HILISTDGKVYLS--GLRSnlsmishgQRQRAVHDFpKYSIKVLPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHV 269
Cdd:cd08528   144 NIMLGEDDKVTITdfGLAK--------QKGPESSKM-TSVVGTILYSCPEIVQN--EPYGEKADIWALGCILYQMCTLQP 212
                         170
                  ....*....|.
gi 1958659070 270 PFKdmpATQML 280
Cdd:cd08528   213 PFY---STNML 220
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
114-298 2.03e-08

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


Pssm-ID: 271047 [Multi-domain]  Cd Length: 270  Bit Score: 55.05  E-value: 2.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 114 SKLFS---HPNIVPYRATFIADNELWAVTSFMAYGSAKDLIGTHFMDgmSELAIAYILQgVLKALDYIHHMGYV---HRS 187
Cdd:cd14145    56 AKLFAmlkHPNIIALRGVCLKEPNLCLVMEFARGGPLNRVLSGKRIP--PDILVNWAVQ-IARGMNYLHCEAIVpviHRD 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 188 VKASHILISTdgKVYLSGLRSNLSMISHGQRQRAVHDFPKYSIK-VLPWLSPEVLQQNLqgYDAKSDIYSVGITACELAN 266
Cdd:cd14145   133 LKSSNILILE--KVENGDLSNKILKITDFGLAREWHRTTKMSAAgTYAWMAPEVIRSSM--FSKGSDVWSYGVLLWELLT 208
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1958659070 267 GHVPFKDMP----ATQMLLEKLNGTVPclldtSTIP 298
Cdd:cd14145   209 GEVPFRGIDglavAYGVAMNKLSLPIP-----STCP 239
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
80-371 2.17e-08

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


Pssm-ID: 270844 [Multi-domain]  Cd Length: 284  Bit Score: 55.20  E-value: 2.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  80 ARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTSFMaygsAKDLigTHFMDG- 158
Cdd:cd07860    19 ARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFL----HQDL--KKFMDAs 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 159 -MSELAIAYI---LQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSnlsmiSHGQRQRAVhdfpKYSIKV 232
Cdd:cd07860    93 aLTGIPLPLIksyLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLAdfGLAR-----AFGVPVRTY----THEVVT 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 233 LPWLSPEVLqQNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEklngtvpcLLDTSTIPAEELTmspsrsian 312
Cdd:cd07860   164 LWYRAPEIL-LGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFR--------IFRTLGTPDEVVW--------- 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958659070 313 PGLNdslaagSLRPANGDSPSHPYH--RTFSPHFHN----FVEQCLQRNPDARPNASTLLNHSFF 371
Cdd:cd07860   226 PGVT------SMPDYKPSFPKWARQdfSKVVPPLDEdgrdLLSQMLHYDPNKRISAKAALAHPFF 284
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
116-369 2.24e-08

Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Wee1 is a nuclear cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. There are two distinct Wee1 proteins in vertebrates showing different expression patterns, called Wee1a and Wee1b. They are functionally dstinct and are implicated in different steps of egg maturation and embryo development. The Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270953 [Multi-domain]  Cd Length: 275  Bit Score: 55.10  E-value: 2.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 116 LFSHPNIVPYRATFIADNELWAVTSFMAYGSAKDLIGTHFMDG--MSELAIAYILQGVLKALDYIHHMGYVHRSVKASHI 193
Cdd:cd14051    56 LGKHPHVVRYYSAWAEDDHMIIQNEYCNGGSLADAISENEKAGerFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNI 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 194 LISTDGKVYLSGLRSNLSMISHGQRQRAVHDF-------------PKYSIKVLPWLSPEVLQQNlqgYD--AKSDIYSVG 258
Cdd:cd14051   136 FISRTPNPVSSEEEEEDFEGEEDNPESNEVTYkigdlghvtsisnPQVEEGDCRFLANEILQEN---YShlPKADIFALA 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 259 ITACELANGhvpfkdmpatqmlleklngtvpclldtstipaeeltmspsrsianpglndslaaGSLrPANGDSPSH---- 334
Cdd:cd14051   213 LTVYEAAGG------------------------------------------------------GPL-PKNGDEWHEirqg 237
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1958659070 335 --PYHRTFSPHFHNFVEQCLQRNPDARPNASTLLNHS 369
Cdd:cd14051   238 nlPPLPQCSPEFNELLRSMIHPDPEKRPSAAALLQHP 274
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
61-272 2.50e-08

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: 54.66  E-value: 2.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRI-----NLEACSNEMVTFLQGELHV-SKLFSHPNIVPYRATFIADNE 134
Cdd:cd13993     2 YQLISPIGEG--AYGVVYLAVDLRTGRKYAIKCLyksgpNSKDGNDFQKLPQLREIDLhRRVSRHPNIITLHDVFETEVA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 135 LWAVtsfMAYGSAKDL----IGTHFMDGMSELAIAYILQgVLKALDYIHHMGYVHRSVKASHILISTD-GKVYLS--GL- 206
Cdd:cd13993    80 IYIV---LEYCPNGDLfeaiTENRIYVGKTELIKNVFLQ-LIDAVKHCHSLGIYHRDIKPENILLSQDeGTVKLCdfGLa 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958659070 207 -RSNLSMishgqrqravhdfpKYSIKVLPWLSPEVLQQN---LQGYD-AKSDIYSVGITACELANGHVPFK 272
Cdd:cd13993   156 tTEKISM--------------DFGVGSEFYMAPECFDEVgrsLKGYPcAAGDIWSLGIILLNLTFGRNPWK 212
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
119-369 2.61e-08

Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of fungal Wee1 proteins, also called Swe1 in budding yeast and Mik1 in fission yeast. Yeast Wee1 is required to control cell size. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The fungal Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 54.74  E-value: 2.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 119 HPNIVPYRATFIADNELWAVTSFMAYGSAK---DLIGTHfmDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILI 195
Cdd:cd14052    62 HDNIVQLIDSWEYHGHLYIQTELCENGSLDvflSELGLL--GRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLI 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 196 STDGKVYLS--GLRSNLSMIS----HGQRQravhdfpkysikvlpWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHV 269
Cdd:cd14052   140 TFEGTLKIGdfGMATVWPLIRgierEGDRE---------------YIAPEILSE--HMYDKPADIFSLGLILLEAAANVV 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 270 pfkdMPATQMLLEKL-NGtvpcllDTSTIpaeeltmspsrsianPGLNDSLAAGSLRPANGDSPSHPYHRTFSPHFHNFV 348
Cdd:cd14052   203 ----LPDNGDAWQKLrSG------DLSDA---------------PRLSSTDLHSASSPSSNPPPDPPNMPILSGSLDRVV 257
                         250       260
                  ....*....|....*....|.
gi 1958659070 349 EQCLQRNPDARPNASTLLNHS 369
Cdd:cd14052   258 RWMLSPEPDRRPTADDVLATP 278
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
61-271 2.64e-08

Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR kinases regulate mitosis, cell growth, embryonic development, and neurological processes. They are also required for proper centrosome duplication. Higher eukaryotes contain two NDR isoforms, NDR1 and NDR2. This subfamily also contains fungal NDR-like kinases. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270750 [Multi-domain]  Cd Length: 324  Bit Score: 55.31  E-value: 2.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKG-FEDlmtVNLARYKPTGEYVTVRRI-NLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAV 138
Cdd:cd05599     3 FEPLKVIGRGaFGE---VRLVRKKDTGHVYAMKKLrKSEMLEKEQVAHVRAERDILAEADNPWVVKLYYSFQDEENLYLI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 139 TSFMAYGsakDLIgTHFM--DGMSELAIA-YILQGVLkALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSNLsmi 213
Cdd:cd05599    80 MEFLPGG---DMM-TLLMkkDTLTEEETRfYIAETVL-AIESIHKLGYIHRDIKPDNLLLDARGHIKLSdfGLCTGL--- 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958659070 214 shGQRQRAvhdfpkYSIKVLP-WLSPEVLQQNlqGYDAKSDIYSVGITACELANGHVPF 271
Cdd:cd05599   152 --KKSHLA------YSTVGTPdYIAPEVFLQK--GYGKECDWWSLGVIMYEMLIGYPPF 200
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
171-280 2.64e-08

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


Pssm-ID: 133178 [Multi-domain]  Cd Length: 275  Bit Score: 54.78  E-value: 2.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 171 VLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLRsnLSMISHGQrqravhDFPKYSIKVLP--WLSPEVLQQNLqgY 248
Cdd:cd05046   126 IALGMDHLSNARFVHRDLAARNCLVSSQREVKVSLLS--LSKDVYNS------EYYKLRNALIPlrWLAPEAVQEDD--F 195
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958659070 249 DAKSDIYSVGITACELAN-GHVPFKDMPATQML 280
Cdd:cd05046   196 STKSDVWSFGVLMWEVFTqGELPFYGLSDEEVL 228
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
61-304 2.96e-08

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called Doublecortin-like and CAM kinase-like 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL1 (or DCAMKL1) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL1 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL1 interacts with tubulin, glucocorticoid receptor, dynein, JIP1/2, caspases (3 and 8), and calpain, among others. It plays roles in neurogenesis, neuronal migration, retrograde transport, and neuronal apoptosis. The DCKL1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271085 [Multi-domain]  Cd Length: 268  Bit Score: 54.62  E-value: 2.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMvTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTS 140
Cdd:cd14183     8 YKVGRTIGDG--NFAVVKECVERSTGREYALKIINKSKCRGKE-HMIQNEVSILRRVKHPNIVLLIEEMDMPTELYLVME 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 141 FMAYGSAKDLIGThfMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILI--STDGKVYLSGLRSNLSMISHGqr 218
Cdd:cd14183    85 LVKGGDLFDAITS--TNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVyeHQDGSKSLKLGDFGLATVVDG-- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 219 qravhdfPKYSIKVLP-WLSPEVLQQNlqGYDAKSDIYSVGITACELANGHVPFK----DMPA--TQMLLEKLNGTVPCL 291
Cdd:cd14183   161 -------PLYTVCGTPtYVAPEIIAET--GYGLKVDIWAAGVITYILLCGFPPFRgsgdDQEVlfDQILMGQVDFPSPYW 231
                         250
                  ....*....|...
gi 1958659070 292 LDTSTIPAEELTM 304
Cdd:cd14183   232 DNVSDSAKELITM 244
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
60-270 3.03e-08

Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Myt1 is a cytoplasmic cell cycle checkpoint kinase that can keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of N-terminal thr (T14) and tyr (Y15) residues, leading to the delay of meiosis I entry. Meiotic progression is ensured by a two-step inhibition and downregulation of Myt1 by CDK1/XRINGO and p90Rsk during oocyte maturation. In addition, Myt1 targets cyclin B1/B2 and is essential for Golgi and ER assembly during telophase. In Drosophila, Myt1 may be a downstream target of Notch during eye development. The Myt1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270952 [Multi-domain]  Cd Length: 249  Bit Score: 54.24  E-value: 3.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  60 CYELLSVIGKG-F---------ED--LMTVNLARYKPTGEYVTVRRINlEACSNEmvtflqgelhvsKLFSHPNIVPYRA 127
Cdd:cd14050     2 CFTILSKLGEGsFgevfkvrsrEDgkLYAVKRSRSRFRGEKDRKRKLE-EVERHE------------KLGEHPNCVRFIK 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 128 TFIADNELWAVTSFMAYGSAKDLIGTHfmdGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--G 205
Cdd:cd14050    69 AWEEKGILYIQTELCDTSLQQYCEETH---SLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGdfG 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958659070 206 L-----RSNLSMISHGQrqravhdfPKYsikvlpwLSPEVLQQNlqgYDAKSDIYSVGITACELA-NGHVP 270
Cdd:cd14050   146 LvveldKEDIHDAQEGD--------PRY-------MAPELLQGS---FTKAADIFSLGITILELAcNLELP 198
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
61-273 3.28e-08

Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK6, also called SSTK, is expressed at the head of elongated sperm. It can phosphorylate histones and associate with heat shock protens HSP90 and HSC70. Male mice deficient in TSSK6 are infertile, showing spermatogenic impairment including reduced sperm counts, impaired DNA condensation, abnormal morphology and decreased motility rates. The TSSK6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 54.10  E-value: 3.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKG-FEDLMTVNLARYKPTgeyVTVRRINLEACSNEMVT-FLQGELHVSKLFSHPNIVpyrATFiadnELWAV 138
Cdd:cd14164     2 YTLGTTIGEGsFSKVKLATSQKYCCK---VAIKIVDRRRASPDFVQkFLPRELSILRRVNHPNIV---QMF----ECIEV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 139 TSFMAY----GSAKDLIGTHFMDGMSELAIAY-ILQGVLKALDYIHHMGYVHRSVKASHILISTDGKvylsglRSNLSMI 213
Cdd:cd14164    72 ANGRLYivmeAAATDLLQKIQEVHHIPKDLARdMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDR------KIKIADF 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958659070 214 SHGqrqRAVHDFPKYSIKVL---PWLSPEVLQQNlqGYDAKS-DIYSVGITACELANGHVPFKD 273
Cdd:cd14164   146 GFA---RFVEDYPELSTTFCgsrAYTPPEVILGT--PYDPKKyDVWSLGVVLYVMVTGTMPFDE 204
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
58-371 4.19e-08

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


Pssm-ID: 270849 [Multi-domain]  Cd Length: 311  Bit Score: 54.63  E-value: 4.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  58 GGC-----YELLSVIGKG-FEDlmtVNLARYKPTGEYVTVRRINLeacSNEM----VTFLQgELHVSKLFSHPNIVPYRA 127
Cdd:cd07866     2 YGCsklrdYEILGKLGEGtFGE---VYKARQIKTGRVVALKKILM---HNEKdgfpITALR-EIKILKKLKHPNVVPLID 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 128 TFIAD--------NELWAVTSFMAYgsakDLIG------THFmdgmSELAIAYILQGVLKALDYIHHMGYVHRSVKASHI 193
Cdd:cd07866    75 MAVERpdkskrkrGSVYMVTPYMDH----DLSGllenpsVKL----TESQIKCYMLQLLEGINYLHENHILHRDIKAANI 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 194 LISTDGKVYLS--GL-RSNLSMISHGQRQRAVHDFPKYSIKVLPWLSPEVLQQNLQGYDAKSDIYSVGITACELANGHVP 270
Cdd:cd07866   147 LIDNQGILKIAdfGLaRPYDGPPPNPKGGGGGGTRKYTNLVVTRWYRPPELLLGERRYTTAVDIWGIGCVFAEMFTRRPI 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 271 FK---DMPATQMLLeKLNGTvpclldtstiPAEElTMSPSRSIanPGLNDSLaagslrpangDSPSHPyhRTFSPHFHNF 347
Cdd:cd07866   227 LQgksDIDQLHLIF-KLCGT----------PTEE-TWPGWRSL--PGCEGVH----------SFTNYP--RTLEERFGKL 280
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1958659070 348 VEQC-------LQRNPDARPNASTLLNHSFF 371
Cdd:cd07866   281 GPEGldllsklLSLDPYKRLTASDALEHPYF 311
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
110-373 4.36e-08

Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase (also called MAPK11); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38beta/MAPK11 is widely expressed in tissues and shows more similarity with p38alpha than with the other isoforms. Both are sensitive to pyridinylimidazoles and share some common substrates such as MAPK activated protein kinase 2 (MK2) and the transcription factors ATF2, c-Fos and, ELK-1. p38beta is involved in regulating the activation of the cyclooxygenase-2 promoter and the expression of TGFbeta-induced alpha-smooth muscle cell actin. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 54.67  E-value: 4.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 110 ELHVSKLFSHPNIV-------PyrATFIAD-NELWAVTSFMAygsaKDLIGTHFMDGMSELAIAYILQGVLKALDYIHHM 181
Cdd:cd07878    64 ELRLLKHMKHENVIglldvftP--ATSIENfNEVYLVTNLMG----ADLNNIVKCQKLSDEHVQFLIYQLLRGLKYIHSA 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 182 GYVHRSVKASHILISTDgkvylsglrSNLSMISHGQRQRAVHDFPKYsIKVLPWLSPEVLqQNLQGYDAKSDIYSVGITA 261
Cdd:cd07878   138 GIIHRDLKPSNVAVNED---------CELRILDFGLARQADDEMTGY-VATRWYRAPEIM-LNWMHYNQTVDIWSVGCIM 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 262 CELANGHVPFkdmPATQMlLEKLNGtvpcLLDTSTIPAEELTMSPSRSIANPGLNdslaagSLRPANGDSPSHPYhRTFS 341
Cdd:cd07878   207 AELLKGKALF---PGNDY-IDQLKR----IMEVVGTPSPEVLKKISSEHARKYIQ------SLPHMPQQDLKKIF-RGAN 271
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1958659070 342 PHFHNFVEQCLQRNPDARPNASTLLNHSFFKQ 373
Cdd:cd07878   272 PLAIDLLEKMLVLDSDKRISASEALAHPYFSQ 303
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
141-280 4.62e-08

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


Pssm-ID: 270964 [Multi-domain]  Cd Length: 253  Bit Score: 53.94  E-value: 4.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 141 FMAYGSAKDL-IGTHFMDGMS-------------ELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS-- 204
Cdd:cd14062    54 FMGYMTKPQLaIVTQWCEGSSlykhlhvletkfeMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGdf 133
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958659070 205 GLRSNLSMISHGQRQRAvhdfPKYSIKvlpWLSPEVLQ-QNLQGYDAKSDIYSVGITACELANGHVPFKD-MPATQML 280
Cdd:cd14062   134 GLATVKTRWSGSQQFEQ----PTGSIL---WMAPEVIRmQDENPYSFQSDVYAFGIVLYELLTGQLPYSHiNNRDQIL 204
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
61-272 4.75e-08

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: 53.80  E-value: 4.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMvTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTS 140
Cdd:cd14185     2 YEIGRTIGDG--NFAVVKECRHWNENQEYAMKIIDKSKLKGKE-DMIESEILIIKSLSHPNIVKLFEVYETEKEIYLILE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 141 FMAYGSAKDLIGTHFMdgMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILI--STDGKvylsglrSNLSMISHGQR 218
Cdd:cd14185    79 YVRGGDLFDAIIESVK--FTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVqhNPDKS-------TTLKLADFGLA 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958659070 219 QRAVHdfPKYSIKVLP-WLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFK 272
Cdd:cd14185   150 KYVTG--PIFTVCGTPtYVAPEILSE--KGYGLEVDMWAAGVILYILLCGFPPFR 200
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
83-302 5.00e-08

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: 54.20  E-value: 5.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  83 KPTGEYVTVRRinleaCSNEMVTFLQG----ELHVSKLFSHPNIV-----PYRATFIADNELWAVTsfMAYGSAKDLigT 153
Cdd:cd14038    16 QETGEQVAIKQ-----CRQELSPKNRErwclEIQIMKRLNHPNVVaardvPEGLQKLAPNDLPLLA--MEYCQGGDL--R 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 154 HFMD------GMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILIStDGKVYLSGLRSNLSMISHGQRQRAVHDFpk 227
Cdd:cd14038    87 KYLNqfenccGLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQ-QGEQRLIHKIIDLGYAKELDQGSLCTSF-- 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 228 ysIKVLPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFkdMPATQ----------------MLLEKLNGTV--- 288
Cdd:cd14038   164 --VGTLQYLAPELLEQ--QKYTVTVDYWSFGTLAFECITGFRPF--LPNWQpvqwhgkvrqksnediVVYEDLTGAVkfs 237
                         250
                  ....*....|....*..
gi 1958659070 289 ---PCLLDTSTIPAEEL 302
Cdd:cd14038   238 svlPTPNNLNGILAGKL 254
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
61-371 6.63e-08

Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-like proteins show unusual expression patterns with high levels in post-mitotic tissues, suggesting that they may be involved in regulating post-mitotic cellular events. They share sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The association of PCTAIRE-like proteins with cyclins has not been widely studied, although PFTAIRE-1 has been shown to function as a CDK which is regulated by cyclin D3 as well as the membrane-associated cyclin Y. The PCTAIRE-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 53.54  E-value: 6.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQgELHVSKLFSHPNIVPYRATFIADNELWAVTS 140
Cdd:cd07844     2 YKKLDKLGEG--SYATVYKGRSKLTGQLVALKEIRLEHEEGAPFTAIR-EASLLKDLKHANIVTLHDIIHTKKTLTLVFE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 141 FMAygsaKDLigTHFMD----GMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSNLSMIS 214
Cdd:cd07844    79 YLD----TDL--KQYMDdcggGLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLAdfGLARAKSVPS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 215 HgqrqravhdfpKYSIKV--LPWLSPEVLQQNLQgYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEK---LNGTvp 289
Cdd:cd07844   153 K-----------TYSNEVvtLWYRPPDVLLGSTE-YSTSLDMWGVGCIFYEMATGRPLFPGSTDVEDQLHKifrVLGT-- 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 290 clldtstiPAEEltMSPSRSiANPGLNDSlaagslrpANGDSPSHPYHRTFS-----PHFHNFVEQCLQRNPDARPNAST 364
Cdd:cd07844   219 --------PTEE--TWPGVS-SNPEFKPY--------SFPFYPPRPLINHAPrldriPHGEELALKFLQYEPKKRISAAE 279

                  ....*..
gi 1958659070 365 LLNHSFF 371
Cdd:cd07844   280 AMKHPYF 286
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
61-271 7.58e-08

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


Pssm-ID: 270829 [Multi-domain]  Cd Length: 283  Bit Score: 53.45  E-value: 7.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGFEDLmtVNLARYKPTGEYVTVRRINLEAcSNEMV--TFLQgELHVSKLFSHPNIVPYRATFIADNELWAV 138
Cdd:cd07835     1 YQKLEKIGEGTYGV--VYKARDKLTGEIVALKKIRLET-EDEGVpsTAIR-EISLLKELNHPNIVRLLDVVHSENKLYLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 139 TSFMaygsakDLIGTHFMDGMSELAI------AYILQgVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLrsnl 210
Cdd:cd07835    77 FEFL------DLDLKKYMDSSPLTGLdpplikSYLYQ-LLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLAdfGL---- 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958659070 211 smishgqrQRAV--------HDfpkysIKVLPWLSPEVLQQNLQgYDAKSDIYSVGITACELANGHVPF 271
Cdd:cd07835   146 --------ARAFgvpvrtytHE-----VVTLWYRAPEILLGSKH-YSTPVDIWSVGCIFAEMVTRRPLF 200
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
61-197 7.73e-08

Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal STKs including Saccharomyces cerevisiae RCK1 and RCK2, Schizosaccharomyces pombe Sty1-regulated kinase 1 (Srk1), and similar proteins. RCK1, RCK2 (or Rck2p), and Srk1 are MAPK-activated protein kinases. RCK1 and RCK2 are involved in oxidative and metal stress resistance in budding yeast. RCK2 also regulates rapamycin sensitivity in both S. cerevisiae and Candida albicans. Srk1 is activated by Sty1/Spc1 and is involved in negatively regulating cell cycle progression by inhibiting Cdc25. The RCK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270998 [Multi-domain]  Cd Length: 295  Bit Score: 53.59  E-value: 7.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKG-FEDlmtVNLARYKP-TGEYVTVRRINLEACSNEMVTFLQ-----GELHVSKLFSHPNIVPYRATFIADN 133
Cdd:cd14096     3 YRLINKIGEGaFSN---VYKAVPLRnTGKPVAIKVVRKADLSSDNLKGSSranilKEVQIMKRLSHPNIVKLLDFQESDE 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958659070 134 ELWAVTSFMAYGSAKDLIG--THFMDGMSElaiaYILQGVLKALDYIHHMGYVHRSVKASHILIST 197
Cdd:cd14096    80 YYYIVLELADGGEIFHQIVrlTYFSEDLSR----HVITQVASAVKYLHEIGVVHRDIKPENLLFEP 141
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
61-271 7.86e-08

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR1 (also called STK38) plays a role in proper centrosome duplication. It is highly expressed in thymus, muscle, lung and spleen. It is not an essential protein because mice deficient of NDR1 remain viable and fertile. However, these mice develop T-cell lymphomas and appear to be hypersenstive to carcinogenic treatment. NDR1 appears to also act as a tumor suppressor. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 53.89  E-value: 7.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRI-NLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVT 139
Cdd:cd05628     3 FESLKVIGRG--AFGEVRLVQKKDTGHVYAMKILrKADMLEKEQVGHIRAERDILVEADSLWVVKMFYSFQDKLNLYLIM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 140 SFMAYGSAKDLIGTHfmDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSNLSMISHGQ 217
Cdd:cd05628    81 EFLPGGDMMTLLMKK--DTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSdfGLCTGLKKAHRTE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 218 RQRAV-HDFPK------------------------YSIKVLP-WLSPEVLQQNlqGYDAKSDIYSVGITACELANGHVPF 271
Cdd:cd05628   159 FYRNLnHSLPSdftfqnmnskrkaetwkrnrrqlaFSTVGTPdYIAPEVFMQT--GYNKLCDWWSLGVIMYEMLIGYPPF 236
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
86-276 7.95e-08

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


Pssm-ID: 271050 [Multi-domain]  Cd Length: 258  Bit Score: 53.07  E-value: 7.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  86 GEYVTVRRINLEACSNEMVTF--LQGELHVSKLFSHPNIVPYRATFIADNELWAVTSFmAYGSA--KDLIGTHFMdgmSE 161
Cdd:cd14148    17 GEEVAVKAARQDPDEDIAVTAenVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVMEY-ARGGAlnRALAGKKVP---PH 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 162 LAIAYILQgVLKALDYIHHMGYV---HRSVKASHILISTdgKVYLSGLRSNLSMISHGQRQRAVHDFPKYSIK-VLPWLS 237
Cdd:cd14148    93 VLVNWAVQ-IARGMNYLHNEAIVpiiHRDLKSSNILILE--PIENDDLSGKTLKITDFGLAREWHKTTKMSAAgTYAWMA 169
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1958659070 238 PEVLQQNLqgYDAKSDIYSVGITACELANGHVPFKDMPA 276
Cdd:cd14148   170 PEVIRLSL--FSKSSDVWSFGVLLWELLTGEVPYREIDA 206
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
115-289 8.24e-08

Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. ILK contains N-terminal ankyrin repeats, a Pleckstrin Homology (PH) domain, and a C-terminal pseudokinase domain. It is a component of the IPP (ILK/PINCH/Parvin) complex that couples beta integrins to the actin cytoskeleton, and plays important roles in cell adhesion, spreading, invasion, and migration. ILK was initially thought to be an active kinase despite the lack of key conserved residues because of in vitro studies showing that it can phosphorylate certain protein substrates. However, in vivo experiments in Caenorhabditis elegans, Drosophila melanogaster, and mice (ILK-null and knock-in) proved that ILK is not an active kinase. In addition to actin cytoskeleton regulation, ILK also influences the microtubule network and mitotic spindle orientation. The pseudokinase domain of ILK binds several adaptor proteins including the parvins and paxillin. The ILK subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270959 [Multi-domain]  Cd Length: 251  Bit Score: 52.88  E-value: 8.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 115 KLFSHPNIVPYRATFIADNELWAVTSFMAYGSAKDLI--GTHFMDGMSelaiayilQGVLKALDYIHHMGYVHR------ 186
Cdd:cd14057    47 RIFSHPNVLPVLGACNSPPNLVVISQYMPYGSLYNVLheGTGVVVDQS--------QAVKFALDIARGMAFLHTleplip 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 187 --SVKASHILISTDGKVYLSGLRSNLSMISHGQrqravhdfpkysIKVLPWLSPEVLQQNLQGYDAKS-DIYSVGITACE 263
Cdd:cd14057   119 rhHLNSKHVMIDEDMTARINMADVKFSFQEPGK------------MYNPAWMAPEALQKKPEDINRRSaDMWSFAILLWE 186
                         170       180       190
                  ....*....|....*....|....*....|
gi 1958659070 264 LANGHVPFKDMP----ATQMLLEKLNGTVP 289
Cdd:cd14057   187 LVTREVPFADLSnmeiGMKIALEGLRVTIP 216
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
61-271 8.39e-08

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


Pssm-ID: 270833 [Multi-domain]  Cd Length: 298  Bit Score: 53.34  E-value: 8.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEM----------VTFLQgELHvsklfsHPNIVPYRATFI 130
Cdd:cd07841     2 YEKGKKLGEG--TYAVVYKARDKETGRIVAIKKIKLGERKEAKdginftalreIKLLQ-ELK------HPNIIGLLDVFG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 131 ADNELWAVTSFMAYgsakDL---IGthfmDGMSELAIAYI---LQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS 204
Cdd:cd07841    73 HKSNINLVFEFMET----DLekvIK----DKSIVLTPADIksyMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLA 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958659070 205 --GL-RsnlsmiSHGQRQRavhdfpKYSIKVL-PWL-SPEVLqqnlqgYDAKS-----DIYSVGITACELANGhVPF 271
Cdd:cd07841   145 dfGLaR------SFGSPNR------KMTHQVVtRWYrAPELL------FGARHygvgvDMWSVGCIFAELLLR-VPF 202
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
163-273 8.80e-08

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


Pssm-ID: 271021 [Multi-domain]  Cd Length: 255  Bit Score: 53.03  E-value: 8.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 163 AIAYILQgVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSNLSMISHGQRQRAVHDFPKYSikvlpwlSPEV 240
Cdd:cd14119    99 AHGYFVQ-LIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISdfGVAEALDLFAEDDTCTTSQGSPAFQ-------PPEI 170
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958659070 241 L--QQNLQGYdaKSDIYSVGITACELANGHVPFKD 273
Cdd:cd14119   171 AngQDSFSGF--KVDIWSAGVTLYNMTTGKYPFEG 203
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
61-282 9.33e-08

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: 53.13  E-value: 9.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGFEDlmTVNLARYKPTGEYVTVRRINL--EACSNEMVTFLQGELH-----VSKLFSHPNIVPYRATFIADN 133
Cdd:cd14093     5 YEPKEILGRGVSS--TVRRCIEKETGQEFAVKIIDItgEKSSENEAEELREATRreieiLRQVSGHPNIIELHDVFESPT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 134 ELWAVTSFMAYGSAKDLIgTHFMDgMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSNLs 211
Cdd:cd14093    83 FIFLVFELCRKGELFDYL-TEVVT-LSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISdfGFATRL- 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958659070 212 miSHGQRQRAVHDFPKYsikvlpwLSPEVLQ----QNLQGYDAKSDIYSVGITACELANGHVPF---KDMPATQMLLE 282
Cdd:cd14093   160 --DEGEKLRELCGTPGY-------LAPEVLKcsmyDNAPGYGKEVDMWACGVIMYTLLAGCPPFwhrKQMVMLRNIME 228
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
64-264 1.07e-07

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


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 52.97  E-value: 1.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  64 LSVIGKGfeDLMTVNLARYKP----TGEYVTVRRinLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADN--ELWA 137
Cdd:cd05081     9 ISQLGKG--NFGSVELCRYDPlgdnTGALVAVKQ--LQHSGPDQQRDFQREIQILKALHSDFIVKYRGVSYGPGrrSLRL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 138 VTSFMAYGSAKDLIGTHFMDGMSELAIAYILQgVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSNLSMISH 215
Cdd:cd05081    85 VMEYLPSGCLRDFLQRHRARLDASRLLLYSSQ-ICKGMEYLGSRRCVHRDLAARNILVESEAHVKIAdfGLAKLLPLDKD 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1958659070 216 GQRQRAVHDFPKYsikvlpWLSPEVLQQNLqgYDAKSDIYSVGITACEL 264
Cdd:cd05081   164 YYVVREPGQSPIF------WYAPESLSDNI--FSRQSDVWSFGVVLYEL 204
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
61-289 1.13e-07

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mutations in the gene encoding CDKL5, previously called STK9, are associated with early onset epilepsy and severe mental retardation [X-linked infantile spasm syndrome (ISSX) or West syndrome]. In addition, CDKL5 mutations also sometimes cause a phenotype similar to Rett syndrome (RTT), a progressive neurodevelopmental disorder. These pathogenic mutations are located in the N-terminal portion of the protein within the kinase domain. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270838 [Multi-domain]  Cd Length: 287  Bit Score: 53.08  E-value: 1.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGFEDLmtVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTS 140
Cdd:cd07848     3 FEVLGVVGEGAYGV--VLKCRHKETKEIVAIKKFKDSEENEEVKETTLRELKMLRTLKQENIVELKEAFRRRGKLYLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 141 FMAyGSAKDLIGTHFMDGMSELAIAYILQgVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSNLSMISHGqr 218
Cdd:cd07848    81 YVE-KNMLELLEEMPNGVPPEKVRSYIYQ-LIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCdfGFARNLSEGSNA-- 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958659070 219 qravhDFPKYsIKVLPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQML--LEKLNGTVP 289
Cdd:cd07848   157 -----NYTEY-VATRWYRSPELLLG--APYGKAVDMWSVGCILGELSDGQPLFPGESEIDQLftIQKVLGPLP 221
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
85-274 1.17e-07

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


Pssm-ID: 270666 [Multi-domain]  Cd Length: 254  Bit Score: 52.57  E-value: 1.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  85 TGEYVTVRRINleaCSNEMVTFLQGELHVSKLfSHPNIVPYRATfIADNELWAVTSFMAYGSAKDLIGTHfmdGMSELAI 164
Cdd:cd05083    28 MGQKVAVKNIK---CDVTAQAFLEETAVMTKL-QHKNLVRLLGV-ILHNGLYIVMELMSKGNLVNFLRSR---GRALVPV 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 165 AYILQ---GVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLRsnlsmISHGQRQRAvhDFPKYSIKvlpWLSPEVL 241
Cdd:cd05083   100 IQLLQfslDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFG-----LAKVGSMGV--DNSRLPVK---WTAPEAL 169
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1958659070 242 QQNlqGYDAKSDIYSVGITACEL-ANGHVPFKDM 274
Cdd:cd05083   170 KNK--KFSSKSDVWSYGVLLWEVfSYGRAPYPKM 201
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
86-276 1.25e-07

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


Pssm-ID: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 52.40  E-value: 1.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  86 GEYVTVRRINLEACSNEMVTfLQGELHVSKLF---SHPNIVPYRATFIADNELWAVTSFMAYGS-----AKDLIGTHFMd 157
Cdd:cd14061    17 GEEVAVKAARQDPDEDISVT-LENVRQEARLFwmlRHPNIIALRGVCLQPPNLCLVMEYARGGAlnrvlAGRKIPPHVL- 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 158 gmselaIAYILQgVLKALDYIHHMGYV---HRSVKASHILIstDGKVYLSGLRSNLSMISHGQRQRAVHDFPKYSIK-VL 233
Cdd:cd14061    95 ------VDWAIQ-IARGMNYLHNEAPVpiiHRDLKSSNILI--LEAIENEDLENKTLKITDFGLAREWHKTTRMSAAgTY 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1958659070 234 PWLSPEVLQQNLqgYDAKSDIYSVGITACELANGHVPFKDMPA 276
Cdd:cd14061   166 AWMAPEVIKSST--FSKASDVWSYGVLLWELLTGEVPYKGIDG 206
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
61-373 1.26e-07

Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They function in the regulation of the cell cycle, cell development, cell differentiation, senescence, tumorigenesis, apoptosis, pain development and pain progression, and immune responses. p38 kinases are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. p38 substrates include other protein kinases and factors that regulate transcription, nuclear export, mRNA stability and translation. p38 kinases are drug targets for the inflammatory diseases psoriasis, rheumatoid arthritis, and chronic pulmonary disease. Vertebrates contain four isoforms of p38, named alpha, beta, gamma, and delta, which show varying substrate specificity and expression patterns. p38alpha and p38beta are ubiquitously expressed, p38gamma is predominantly found in skeletal muscle, and p38delta is found in the heart, lung, testis, pancreas, and small intestine. The p38 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143356 [Multi-domain]  Cd Length: 343  Bit Score: 53.07  E-value: 1.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNEL----- 135
Cdd:cd07851    17 YQNLSPVGSG--AYGQVCSAFDTKTGRKVAIKKLSRPFQSAIHAKRTYRELRLLKHMKHENVIGLLDVFTPASSLedfqd 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 136 -WAVTSFMAygsaKDLIGTHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDgkvylsglrSNLSMIS 214
Cdd:cd07851    95 vYLVTHLMG----ADLNNIVKCQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNED---------CELKILD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 215 HGQRQRAVHDFPKYSikVLPW-LSPEVLqQNLQGYDAKSDIYSVGITACELANGHVPFkdmPATQMlLEKLNgtvpCLLD 293
Cdd:cd07851   162 FGLARHTDDEMTGYV--ATRWyRAPEIM-LNWMHYNQTVDIWSVGCIMAELLTGKTLF---PGSDH-IDQLK----RIMN 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 294 TSTIPAEEL----TMSPSRSIAnpglnDSLaagslrpangdsPSHP---YHRTF---SPHFHNFVEQCLQRNPDARPNAS 363
Cdd:cd07851   231 LVGTPDEELlkkiSSESARNYI-----QSL------------PQMPkkdFKEVFsgaNPLAIDLLEKMLVLDPDKRITAA 293
                         330
                  ....*....|
gi 1958659070 364 TLLNHSFFKQ 373
Cdd:cd07851   294 EALAHPYLAE 303
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
77-259 1.30e-07

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: 52.33  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  77 VNLARYKPTGEYVTVRRINLEacSNEMVTFLQgELHVS-KLFSHPNIVPYRATFIADNELWAVTSFMA-YGSAKDLIGTH 154
Cdd:cd13987     9 VLLAVHKGSGTKMALKFVPKP--STKLKDFLR-EYNISlELSVHPHIIKTYDVAFETEDYYVFAQEYApYGDLFSIIPPQ 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 155 FmdGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILIstdgkvylsgLRSNLSMISHGQ--RQRAVHDFPKYSIKV 232
Cdd:cd13987    86 V--GLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLL----------FDKDCRRVKLCDfgLTRRVGSTVKRVSGT 153
                         170       180       190
                  ....*....|....*....|....*....|
gi 1958659070 233 LPWLSPEVLQQNL-QGY--DAKSDIYSVGI 259
Cdd:cd13987   154 IPYTAPEVCEAKKnEGFvvDPSIDVWAFGV 183
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
61-380 1.31e-07

Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ERK5 (also called Big MAPK1 (BMK1) or MAPK7) has a unique C-terminal extension, making it approximately twice as big as other MAPKs. This extension contains transcriptional activation capability which is inhibited by the N-terminal half. ERK5 is activated in response to growth factors and stress by a cascade that leads to its phosphorylation by the MAP2K MEK5, which in turn is regulated by the MAP3Ks MEKK2 and MEKK3. Activated ERK5 phosphorylates its targets including myocyte enhancer factor 2 (MEF2), Sap1a, c-Myc, and RSK. It plays a role in EGF-induced cell proliferation during the G1/S phase transition. Studies on knockout mice revealed that ERK5 is essential for cardiovascular development and plays an important role in angiogenesis. It is also critical for neural differentiation and survival. The ERK5 pathway has been implicated in the pathogenesis of many diseases including cancer, cardiac hypertrophy, and atherosclerosis. MAPKs are important mediators of cellular responses to extracellular signals. The ERK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270842 [Multi-domain]  Cd Length: 336  Bit Score: 53.14  E-value: 1.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGFEDLmtVNLARYKPTGEYVTVRRInleACSNEMVTFLQG---ELHVSKLFSHPNIVPYRatfiadnelwa 137
Cdd:cd07855     7 YEPIETIGSGAYGV--VCSAIDTKSGQKVAIKKI---PNAFDVVTTAKRtlrELKILRHFKHDNIIAIR----------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 138 vTSFMAYGSAKDLIGTHF-MDGM--------------SELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKvy 202
Cdd:cd07855    71 -DILRPKVPYADFKDVYVvLDLMesdlhhiihsdqplTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCE-- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 203 lsgLR-SNLSMishgqrQRAVHDFPK--------YsIKVLPWLSPEVLqQNLQGYDAKSDIYSVG-ITACELANGHV-PF 271
Cdd:cd07855   148 ---LKiGDFGM------ARGLCTSPEehkyfmteY-VATRWYRAPELM-LSLPEYTQAIDMWSVGcIFAEMLGRRQLfPG 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 272 KD-MPATQMLLEKLNgtvpclldtstipaeeltmSPSRSIANpglndslAAGSLRPAN-----GDSPSHPYHRTF---SP 342
Cdd:cd07855   217 KNyVHQLQLILTVLG-------------------TPSQAVIN-------AIGADRVRRyiqnlPNKQPVPWETLYpkaDQ 270
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1958659070 343 HFHNFVEQCLQRNPDARPNASTLLNHSFFKQIKRRASE 380
Cdd:cd07855   271 QALDLLSQMLRFDPSERITVAEALQHPFLAKYHDPDDE 308
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
77-272 1.57e-07

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


Pssm-ID: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 52.17  E-value: 1.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  77 VNLARYKPTGEyVTVRRINLEACSNEmvTFLQgELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGSAKDLIGTHFm 156
Cdd:cd05114    20 VRLGKWRAQYK-VAIKAIREGAMSEE--DFIE-EAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFMENGCLLNYLRQRR- 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 157 DGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLsglrSNLSMISHGQRQRAVHDF-PKYSIKvlpW 235
Cdd:cd05114    95 GKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKV----SDFGMTRYVLDDQYTSSSgAKFPVK---W 167
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1958659070 236 LSPEVLqqNLQGYDAKSDIYSVGITACEL-ANGHVPFK 272
Cdd:cd05114   168 SPPEVF--NYSKFSSKSDVWSFGVLMWEVfTEGKMPFE 203
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
66-375 1.75e-07

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


Pssm-ID: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 52.70  E-value: 1.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  66 VIGKGfeDLMTVNLARYKPTGEYVTVRRINLEAC-SNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVtsfMAY 144
Cdd:cd05595     2 LLGKG--TFGKVILVREKATGRYYAMKILRKEVIiAKDEVAHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFV---MEY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 145 GSAKDLIgTHFMDG--MSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLRSNLSMISHGQRQRAV 222
Cdd:cd05595    77 ANGGELF-FHLSRErvFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGITDGATMKTF 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 223 HDFPKYsikvlpwLSPEVLQQNlqGYDAKSDIYSVGITACELANGHVPFKDMPATQMLleklngtvpclldtstipaEEL 302
Cdd:cd05595   156 CGTPEY-------LAPEVLEDN--DYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLF-------------------ELI 207
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958659070 303 TMSPSRsianpglndslaagslrpangdspshpYHRTFSPHFHNFVEQCLQRNPDAR----PN-ASTLLNHSFFKQIK 375
Cdd:cd05595   208 LMEEIR---------------------------FPRTLSPEAKSLLAGLLKKDPKQRlgggPSdAKEVMEHRFFLSIN 258
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
59-288 1.90e-07

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


Pssm-ID: 270981 [Multi-domain]  Cd Length: 256  Bit Score: 51.89  E-value: 1.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  59 GCYELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSN-EMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWA 137
Cdd:cd14079     2 GNYILGKTLGVG--SFGKVKLAEHELTGHKVAVKILNRQKIKSlDMEEKIRREIQILKLFRHPHIIRLYEVIETPTDIFM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 138 VTSFMAYGSAKDLIGTHfmDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLrSNlsMISH 215
Cdd:cd14079    80 VMEYVSGGELFDYIVQK--GRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIAdfGL-SN--IMRD 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958659070 216 GqrqravhDFPKYSIKVLPWLSPEVLQQNL-QGYDAksDIYSVGITACELANGHVPFKDmPATQMLLEKLNGTV 288
Cdd:cd14079   155 G-------EFLKTSCGSPNYAAPEVISGKLyAGPEV--DVWSCGVILYALLCGSLPFDD-EHIPNLFKKIKSGI 218
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
89-284 2.34e-07

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


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 51.71  E-value: 2.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  89 VTVRRINLEACSNEMVT-FLQGELHVSKLFSHPNIVP-YRATFIADNELWAVTSFMAYGSAKDLIGTHfmDGMSELAIAY 166
Cdd:cd14165    29 VAIKIIDKKKAPDDFVEkFLPRELEILARLNHKSIIKtYEIFETSDGKVYIVMELGVQGDLLEFIKLR--GALPEDVARK 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 167 ILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLrsnlsmishGQRQRAVHD------FPKYSIKVLPWLSPEV 240
Cdd:cd14165   107 MFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDF---------GFSKRCLRDengrivLSKTFCGSAAYAAPEV 177
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1958659070 241 LQQnlQGYDAK-SDIYSVGITACELANGHVPFKDMPATQMLLEKL 284
Cdd:cd14165   178 LQG--IPYDPRiYDIWSLGVILYIMVCGSMPYDDSNVKKMLKIQK 220
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
61-271 2.39e-07

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-gamma is predominantly expressed in neuronal tissues. Mice deficient in PKB-gamma show a reduction in brain weight due to the decreases in cell size and cell number. PKB-gamma has also been shown to be upregulated in estrogen-deficient breast cancer cells, androgen-independent prostate cancer cells, and primary ovarian tumors. It acts as a key mediator in the genesis of ovarian cancer. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 52.39  E-value: 2.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEAC-SNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVT 139
Cdd:cd05593    17 FDYLKLLGKG--TFGKVILVREKASGKYYAMKILKKEVIiAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVM 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 140 SFMAYGSAKDLIGTHFMdgMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLRSNLSMISHGQRQ 219
Cdd:cd05593    95 EYVNGGELFFHLSRERV--FSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATM 172
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958659070 220 RAVHDFPKYsikvlpwLSPEVLQQNlqGYDAKSDIYSVGITACELANGHVPF 271
Cdd:cd05593   173 KTFCGTPEY-------LAPEVLEDN--DYGRAVDWWGLGVVMYEMMCGRLPF 215
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
118-371 2.49e-07

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


Pssm-ID: 271100 [Multi-domain]  Cd Length: 270  Bit Score: 51.85  E-value: 2.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 118 SHPNIVPYRATFIADNELWAVTSFMAYGSAKDLIGTHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILIST 197
Cdd:cd14198    66 SNPRVVNLHEVYETTSEIILILEYAAGGEIFNLCVPDLAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSS 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 198 -----DGKVYLSGLRSNlsmISHGQRQRAVHDFPKYsikvlpwLSPEVLqqNLQGYDAKSDIYSVGITACELANGHVPF- 271
Cdd:cd14198   146 iyplgDIKIVDFGMSRK---IGHACELREIMGTPEY-------LAPEIL--NYDPITTATDMWNIGVIAYMLLTHESPFv 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 272 -KDMPATQMLLEKLNgtvpclLDTStipaeELTMSpsrSIANPGLndslaagslrpangdspshpyhrtfsphfhNFVEQ 350
Cdd:cd14198   214 gEDNQETFLNISQVN------VDYS-----EETFS---SVSQLAT------------------------------DFIQK 249
                         250       260
                  ....*....|....*....|.
gi 1958659070 351 CLQRNPDARPNASTLLNHSFF 371
Cdd:cd14198   250 LLVKNPEKRPTAEICLSHSWL 270
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
105-293 2.60e-07

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


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 51.61  E-value: 2.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 105 TFLQgELHVSKLFSHPNIVPYRATfIADNELWAVTSFMAYGSAKDLIGTHFMDGMSELAIAYILQGVLKALDYIHHMGYV 184
Cdd:cd05070    50 SFLE-EAQIMKKLKHDKLVQLYAV-VSEEPIYIVTEYMSKGSLLDFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYI 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 185 HRSVKASHILISTD--GKVYLSGLRSNLSMISHGQRQRAvhdfpKYSIKvlpWLSPEVLqqnLQG-YDAKSDIYSVGITA 261
Cdd:cd05070   128 HRDLRSANILVGNGliCKIADFGLARLIEDNEYTARQGA-----KFPIK---WTAPEAA---LYGrFTIKSDVWSFGILL 196
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1958659070 262 CEL-ANGHVPFKDMPATQMLLEKLNG-TVPCLLD 293
Cdd:cd05070   197 TELvTKGRVPYPGMNNREVLEQVERGyRMPCPQD 230
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
61-265 2.70e-07

Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the mitogen-activated protein kinases (MAPKs) ERK1, ERK2, baker's yeast Fus3, and similar proteins. MAPK pathways are important mediators of cellular responses to extracellular signals. ERK1/2 activation is preferentially by mitogenic factors, differentiation stimuli, and cytokines, through a kinase cascade involving the MAPK kinases MEK1/2 and a MAPK kinase kinase from the Raf family. ERK1/2 have numerous substrates, many of which are nuclear and participate in transcriptional regulation of many cellular processes. They regulate cell growth, cell proliferation, and cell cycle progression from G1 to S phase. Although the distinct roles of ERK1 and ERK2 have not been fully determined, it is known that ERK2 can maintain most functions in the absence of ERK1, and that the deletion of ERK2 is embryonically lethal. The MAPK, Fus3, regulates yeast mating processes including mating-specific gene expression, G1 arrest, mating projection, and cell fusion. This ERK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 51.92  E-value: 2.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGFEDLmtVNLARYKPTGEYVTVRRINleacSNEMVTFLQGELHVSKL---FSHPNIVPYRATFIAD----- 132
Cdd:cd07849     7 YQNLSYIGEGAYGM--VCSAVHKPTGQKVAIKKIS----PFEHQTYCLRTLREIKIllrFKHENIIGILDIQRPPtfesf 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 133 NELWAVTSFMAYGSAKdLIGTHfmdGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILIST--DGKVYLSGL-RSN 209
Cdd:cd07849    81 KDVYIVQELMETDLYK-LIKTQ---HLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTncDLKICDFGLaRIA 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958659070 210 LSMISH-GQRQRAVhdfpkysikVLPWL-SPEVLqQNLQGYDAKSDIYSVGitaCELA 265
Cdd:cd07849   157 DPEHDHtGFLTEYV---------ATRWYrAPEIM-LNSKGYTKAIDIWSVG---CILA 201
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
81-272 2.82e-07

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 51.80  E-value: 2.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  81 RYKPTGEYVTVRRInleacSNEMVTFLQGELHVSKLF-SHPNIVPYRATFIADNELWAVTSFMAYGSAKDLIGTHFMdgM 159
Cdd:cd14180    26 RHRQSGQEYAVKII-----SRRMEANTQREVAALRLCqSHPNIVALHEVLHDQYHTYLVMELLRGGELLDRIKKKAR--F 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 160 SELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKvylsglRSNLSMISHG-QRQRAVHDFPKYS-IKVLPWLS 237
Cdd:cd14180    99 SESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESD------GAVLKVIDFGfARLRPQGSRPLQTpCFTLQYAA 172
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1958659070 238 PEVLQQnlQGYDAKSDIYSVGITACELANGHVPFK 272
Cdd:cd14180   173 PELFSN--QGYDESCDLWSLGVILYTMLSGQVPFQ 205
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
120-271 3.01e-07

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


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 51.54  E-value: 3.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 120 PNIVPYRATFIADNELWAVTSFMAYGSakdlIGTHFM--DGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILIST 197
Cdd:cd05613    65 PFLVTLHYAFQTDTKLHLILDYINGGE----LFTHLSqrERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDS 140
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958659070 198 DGKVYLSGLRSNLSMISHgQRQRAvhdfpkYSI-KVLPWLSPEVLQQNLQGYDAKSDIYSVGITACELANGHVPF 271
Cdd:cd05613   141 SGHVVLTDFGLSKEFLLD-ENERA------YSFcGTIEYMAPEIVRGGDSGHDKAVDWWSLGVLMYELLTGASPF 208
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
161-271 3.25e-07

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


Pssm-ID: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 51.64  E-value: 3.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 161 ELAIAYILQGVLkALDYIHHMGYVHRSVKASHILISTDGKVYLS-------GLRSNLSMISHGQRQRAVHDFPKYSIKVL 233
Cdd:cd05609   100 DMARMYFAETVL-ALEYLHSYGIVHRDLKPDNLLITSMGHIKLTdfglskiGLMSLTTNLYEGHIEKDTREFLDKQVCGT 178
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1958659070 234 P-WLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPF 271
Cdd:cd05609   179 PeYIAPEVILR--QGYGKPVDWWAMGIILYEFLVGCVPF 215
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
59-320 3.64e-07

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: 51.36  E-value: 3.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  59 GCYELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRIN-LEACSNEMVTF-LQGELHVSKLFSHPNIVPYRATFIADNELW 136
Cdd:cd14070     2 GSYLIGRKLGEG--SFAKVREGLHAVTGEKVAIKVIDkKKAKKDSYVTKnLRREGRIQQMIRHPNITQLLDILETENSYY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 137 AVTSFMAYGSAKDLIGTHFMDGMSElAIAYILQgVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSNLSMIS 214
Cdd:cd14070    80 LVMELCPGGNLMHRIYDKKRLEERE-ARRYIRQ-LVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIdfGLSNCAGILG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 215 HGQRQRAVHDFPKYSikvlpwlSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPAT-----QMLLEKLNGTVP 289
Cdd:cd14070   158 YSDPFSTQCGSPAYA-------APELLAR--KKYGPKVDVWSIGVNMYAMLTGTLPFTVEPFSlralhQKMVDKEMNPLP 228
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958659070 290 CLLDTSTIPAEELTMSPSrSIANPGLNDSLA 320
Cdd:cd14070   229 TDLSPGAISFLRSLLEPD-PLKRPNIKQALA 258
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
67-203 4.04e-07

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


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 48.98  E-value: 4.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  67 IGKGFEDlmTVNLARYKPTGEYVTVRRINLEAcsNEMVTFLQGELHVSKLFS--HPNIVPYRATFIADNELWAVTSFMAY 144
Cdd:cd13968     1 MGEGASA--KVFWAEGECTTIGVAVKIGDDVN--NEEGEDLESEMDILRRLKglELNIPKVLVTEDVDGPNILLMELVKG 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958659070 145 GSAKDLIGTHFMDgmsELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYL 203
Cdd:cd13968    77 GTLIAYTQEEELD---EKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKL 132
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
61-371 4.32e-07

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


Pssm-ID: 270837 [Multi-domain]  Cd Length: 286  Bit Score: 51.22  E-value: 4.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRInLEACSNEMVTFLQ-GELHVSKLFSHPNIVPYRATFIADNELWAVT 139
Cdd:cd07847     3 YEKLSKIGEG--SYGVVFKCRNRETGQIVAIKKF-VESEDDPVIKKIAlREIRMLKQLKHPNLVNLIEVFRRKRKLHLVF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 140 SFMAYGSAKDLigTHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSNLSmishgq 217
Cdd:cd07847    80 EYCDHTVLNEL--EKNPRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCdfGFARILT------ 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 218 rqRAVHDFPKYsIKVLPWLSPEVLQQNLQgYDAKSDIYSVGITACELANGHV--PFK-DMPATQMLLEKLNGTVPclldt 294
Cdd:cd07847   152 --GPGDDYTDY-VATRWYRAPELLVGDTQ-YGPPVDVWAIGCVFAELLTGQPlwPGKsDVDQLYLIRKTLGDLIP----- 222
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958659070 295 stipaeeltmspsRSIANPGLNDSLAAGSLRPANGDSPSHPYHRTFSPHFHNFVEQCLQRNPDARPNASTLLNHSFF 371
Cdd:cd07847   223 -------------RHQQIFSTNQFFKGLSIPEPETREPLESKFPNISSPALSFLKGCLQMDPTERLSCEELLEHPYF 286
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
62-291 4.95e-07

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


Pssm-ID: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 50.78  E-value: 4.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  62 ELLSVIGKGfeDLMTVNLARYKptGEyVTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTSF 141
Cdd:cd14153     3 EIGELIGKG--RFGQVYHGRWH--GE-VAIRLIDIERDNEEQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 142 MA----YGSAKDliGTHFMDGMSELAIAyilQGVLKALDYIHHMGYVHRSVKASHILIStDGKVYLS--GLRSNLSMISH 215
Cdd:cd14153    78 CKgrtlYSVVRD--AKVVLDVNKTRQIA---QEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITdfGLFTISGVLQA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 216 GQRQ---RAVHDFPKY-SIKVLPWLSPEVLQQNLQgYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPCL 291
Cdd:cd14153   152 GRREdklRIQSGWLCHlAPEIIRQLSPETEEDKLP-FSKHSDVFAFGTIWYELHAREWPFKTQPAEAIIWQVGSGMKPNL 230
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
52-307 5.37e-07

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 3 or PKR-like Endoplasmic Reticulum Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PERK (or EIF2AK3) is a type-I ER transmembrane protein containing a luminal domain bound with the chaperone BiP under unstressed conditions and a cytoplasmic catalytic kinase domain. In response to the accumulation of misfolded or unfolded proteins in the ER, PERK is activated through the release of BiP, allowing it to dimerize and autophosphorylate. It functions as the central regulator of translational control during the Unfolded Protein Response (UPR) pathway. In addition to the eIF-2 alpha subunit, PERK also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PERK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270950 [Multi-domain]  Cd Length: 281  Bit Score: 51.03  E-value: 5.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  52 SSFLPEggcYELLSVIGKG-----FEDLMTVNLARYkptgeyvTVRRI---NLEACSNEMVTflqgELHVSKLFSHPNIV 123
Cdd:cd14048     2 SRFLTD---FEPIQCLGRGgfgvvFEAKNKVDDCNY-------AVKRIrlpNNELAREKVLR----EVRALAKLDHPGIV 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 124 PYratFIADNE--------------LWAVTSFMAYGSAKDLI-GTHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSV 188
Cdd:cd14048    68 RY---FNAWLErppegwqekmdevyLYIQMQLCRKENLKDWMnRRCTMESRELFVCLNIFKQIASAVEYLHSKGLIHRDL 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 189 KASHILISTDGKVYLSGLRSNLSMISHGQRQRAVHDFPKYS-----IKVLPWLSPEvlQQNLQGYDAKSDIYSVGITACE 263
Cdd:cd14048   145 KPSNVFFSLDDVVKVGDFGLVTAMDQGEPEQTVLTPMPAYAkhtgqVGTRLYMSPE--QIHGNQYSEKVDIFALGLILFE 222
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958659070 264 LAnghVPFkdmpATQM-----LLEKLNGTVPCLLdTSTIPAEE------LTMSPS 307
Cdd:cd14048   223 LI---YSF----STQMerirtLTDVRKLKFPALF-TNKYPEERdmvqqmLSPSPS 269
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
106-280 5.51e-07

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


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 50.79  E-value: 5.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 106 FLQgELHVSKLFSHPNIVPYRATfIADNELWAVTSFMAYGSAKDLIGTHFMDGMSELAIAYILQGVLKALDYIHHMGYVH 185
Cdd:cd05073    53 FLA-EANVMKTLQHDKLVKLHAV-VTKEPIYIITEFMAKGSLLDFLKSDEGSKQPLPKLIDFSAQIAEGMAFIEQRNYIH 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 186 RSVKASHILISTD--GKVYLSGLRSNLSMISHGQRQRAvhdfpKYSIKvlpWLSPEVLqqNLQGYDAKSDIYSVGITACE 263
Cdd:cd05073   131 RDLRAANILVSASlvCKIADFGLARVIEDNEYTAREGA-----KFPIK---WTAPEAI--NFGSFTIKSDVWSFGILLME 200
                         170
                  ....*....|....*...
gi 1958659070 264 LAN-GHVPFKDMPATQML 280
Cdd:cd05073   201 IVTyGRIPYPGMSNPEVI 218
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
61-380 5.64e-07

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-1 is widely expressed except in the spleen and thymus. It is highly expressed in the brain, heart, pancreas, testis, and ovary, and is localized in the cytoplasm. It is regulated by cyclin D3 and is inhibited by the p21 cell cycle inhibitor. It has also been shown to interact with the membrane-associated cyclin Y, which recruits the protein to the plasma membrane. PFTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143374 [Multi-domain]  Cd Length: 303  Bit Score: 50.85  E-value: 5.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQgELHVSKLFSHPNIVPYRATFIADNELWAVTS 140
Cdd:cd07869     7 YEKLEKLGEG--SYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTAIR-EASLLKGLKHANIVLLHDIIHTKETLTLVFE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 141 FMAygsaKDLigTHFMD----GMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSNLSMIS 214
Cdd:cd07869    84 YVH----TDL--CQYMDkhpgGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLAdfGLARAKSVPS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 215 HGQRQRAVhdfpkysikVLPWLSPEVLQQNLQgYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKL--------NG 286
Cdd:cd07869   158 HTYSNEVV---------TLWYRPPDVLLGSTE-YSTCLDMWGVGCIFVEMIQGVAAFPGMKDIQDQLERIflvlgtpnED 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 287 TVPCLLDTSTIPAEELTMSPSRSIANpglndslAAGSLRPANgdspshpyhrtfspHFHNFVEQCLQRNPDARPNASTLL 366
Cdd:cd07869   228 TWPGVHSLPHFKPERFTLYSPKNLRQ-------AWNKLSYVN--------------HAEDLASKLLQCFPKNRLSAQAAL 286
                         330
                  ....*....|....
gi 1958659070 367 NHSFFKQIKRRASE 380
Cdd:cd07869   287 SHEYFSDLPPRLWE 300
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
110-371 5.78e-07

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. Its localization changes during mitotic progression; associating first with centrosomes in prophase, with kinetochores in prometaphase and metaphase, at the central spindle in anaphase, and in the midbody during telophase. It carries multiple functions throughout the cell cycle through interactions with differrent substrates at these specific subcellular locations. PLK1 is overexpressed in many human cancers and is associated with poor prognosis. The PLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271089 [Multi-domain]  Cd Length: 265  Bit Score: 50.70  E-value: 5.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 110 ELHVSKLFSHPNIVPYRAtFIADNELwaVTSFMAYGSAKDLIGTH-FMDGMSELAIAYILQGVLKALDYIHHMGYVHRSV 188
Cdd:cd14187    57 EIAIHRSLAHQHVVGFHG-FFEDNDF--VYVVLELCRRRSLLELHkRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDL 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 189 KASHILISTDGKVYLS--GLRSNLSMisHGQRQRAVHDFPKYsikvlpwLSPEVLQQnlQGYDAKSDIYSVGITACELAN 266
Cdd:cd14187   134 KLGNLFLNDDMEVKIGdfGLATKVEY--DGERKKTLCGTPNY-------IAPEVLSK--KGHSFEVDIWSIGCIMYTLLV 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 267 GHVPFKdmpatqmlleklngtVPCLLDTST-IPAEELTMspsrsianpglndslaagslrpangdsPSHpyhrtFSPHFH 345
Cdd:cd14187   203 GKPPFE---------------TSCLKETYLrIKKNEYSI---------------------------PKH-----INPVAA 235
                         250       260
                  ....*....|....*....|....*.
gi 1958659070 346 NFVEQCLQRNPDARPNASTLLNHSFF 371
Cdd:cd14187   236 SLIQKMLQTDPTARPTINELLNDEFF 261
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
158-391 5.87e-07

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


Pssm-ID: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 50.65  E-value: 5.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 158 GMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLRSNLSMISHGQRQRAVHDFPKYsikvlpwLS 237
Cdd:cd05608   101 GFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAVELKDGQTKTKGYAGTPGF-------MA 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 238 PEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPatqmllEKLNgtvpclldtstipaeeltmspSRSIANPGLND 317
Cdd:cd05608   174 PELLLG--EEYDYSVDYFTLGVTLYEMIAARGPFRARG------EKVE---------------------NKELKQRILND 224
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958659070 318 SLAagslrpangdspshpYHRTFSPHFHNFVEQCLQRNPDAR-----PNASTLLNHSFFKQIKRRASEALPeLLRPVTP 391
Cdd:cd05608   225 SVT---------------YSEKFSPASKSICEALLAKDPEKRlgfrdGNCDGLRTHPFFRDINWRKLEAGI-LPPPFVP 287
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
106-283 6.44e-07

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


Pssm-ID: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 50.50  E-value: 6.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 106 FLQgELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGSAKDLIGTHFMDGMSELAIAYILQGVLKALDYIHHMGYVH 185
Cdd:cd05052    49 FLK-EAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMPYGNLLDYLRECNREELNAVVLLYMATQIASAMEYLEKKNFIH 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 186 RSVKASHILISTDGKVYLSGLrsNLSMISHGQRQRAvHDFPKYSIKvlpWLSPEVLQQNLqgYDAKSDIYSVGITACELA 265
Cdd:cd05052   128 RDLAARNCLVGENHLVKVADF--GLSRLMTGDTYTA-HAGAKFPIK---WTAPESLAYNK--FSIKSDVWAFGVLLWEIA 199
                         170       180
                  ....*....|....*....|.
gi 1958659070 266 N-GHVPFKDMPATQM--LLEK 283
Cdd:cd05052   200 TyGMSPYPGIDLSQVyeLLEK 220
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
77-289 6.55e-07

Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like kinase (also called greatwall kinase); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MASTL kinases in this group carry only a catalytic domain, which contains a long insertion relative to MAST kinases. MASTL, also called greatwall kinase (Gwl), is involved in the regulation of mitotic entry, which is controlled by the coordinated activities of protein kinases and opposing protein phosphatases (PPs). The cyclin B/CDK1 complex induces entry into M-phase while PP2A-B55 shows anti-mitotic activity. MASTL/Gwl is activated downstream of cyclin B/CDK1 and indirectly inhibits PP2A-B55 by phosphorylating the small protein alpha-endosulfine (Ensa) or the cAMP-regulated phosphoprotein 19 (Arpp19), resulting in M-phase progression. Gwl kinase may also play roles in mRNA stabilization and DNA checkpoint recovery. The human MASTL gene has also been named FLJ14813; a missense mutation in FLJ14813 is associated with autosomal dominant thrombocytopenia. The MASTL kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 51.03  E-value: 6.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  77 VNLARYKPTGEYVTVRRI-NLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGSAKDLIGTH- 154
Cdd:cd05610    20 VYLGRKKNNSKLYAVKVVkKADMINKNMVHQVQAERDALALSKSPFIVHLYYSLQSANNVYLVMEYLIGGDVKSLLHIYg 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 155 FMDgmSELAIAYILQGVLkALDYIHHMGYVHRSVKASHILISTDGKVYLSG-------LRSNLSM---ISHGQRQRAVHD 224
Cdd:cd05610   100 YFD--EEMAVKYISEVAL-ALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDfglskvtLNRELNMmdiLTTPSMAKPKND 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 225 FPKYSIKVLP------------------------------------WLSPEVLQQnlQGYDAKSDIYSVGITACELANGH 268
Cdd:cd05610   177 YSRTPGQVLSlisslgfntptpyrtpksvrrgaarvegerilgtpdYLAPELLLG--KPHGPAVDWWALGVCLFEFLTGI 254
                         250       260
                  ....*....|....*....|.
gi 1958659070 269 VPFKDMPATQMLLEKLNGTVP 289
Cdd:cd05610   255 PPFNDETPQQVFQNILNRDIP 275
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
155-271 6.66e-07

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 51.00  E-value: 6.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 155 FMDGMSELA---IAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLRSNLSMISHgqrqravhdfpKYSIK 231
Cdd:PHA03207  175 YVDRSGPLPleqAITIQRRLLEALAYLHGRGIIHRDVKTENIFLDEPENAVLGDFGAACKLDAH-----------PDTPQ 243
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1958659070 232 VLPWL------SPEVLQqnLQGYDAKSDIYSVGITACELANGHVPF 271
Cdd:PHA03207  244 CYGWSgtletnSPELLA--LDPYCAKTDIWSAGLVLFEMSVKNVTL 287
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
110-273 6.80e-07

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


Pssm-ID: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 50.73  E-value: 6.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 110 ELHVSKLFSHPNIVPYRATFIADNE--LWAVTSFMAYGSAKDLIGTHfmdGMSELAIAYILQGVLKALDYIHHMGYVHRS 187
Cdd:cd14199    75 EIAILKKLDHPNVVKLVEVLDDPSEdhLYMVFELVKQGPVMEVPTLK---PLSEDQARFYFQDLIKGIEYLHYQKIIHRD 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 188 VKASHILISTDGKVYLS--GLRSNLsmishgqrqRAVHDFPKYSIKVLPWLSPEVLQQNLQGYDAKS-DIYSVGITACEL 264
Cdd:cd14199   152 VKPSNLLVGEDGHIKIAdfGVSNEF---------EGSDALLTNTVGTPAFMAPETLSETRKIFSGKAlDVWAMGVTLYCF 222

                  ....*....
gi 1958659070 265 ANGHVPFKD 273
Cdd:cd14199   223 VFGQCPFMD 231
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
61-271 7.49e-07

The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. Twitchin and Projectin are both associated with thick filaments. Twitchin is localized in the outer parts of A-bands and is involved in regulating muscle contraction. It interacts with the myofibrillar proteins myosin and actin in a phosphorylation-dependent manner, and may be involved in regulating the myosin cross-bridge cycle. The kinase activity of Twitchen is activated by Ca2+ and the Ca2+ binding protein S100A1. Projectin is associated with the end of thick filaments and is a component of flight muscle connecting filaments. The kinase domain of Projectin may play roles in autophosphorylation and transphosphorylation, which impact the formation of myosin filaments. The Twitchin-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 50.27  E-value: 7.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVtfLQGELHVSKLFSHPNIVPYRATFIADNELWAVTS 140
Cdd:cd14114     4 YDILEELGTG--AFGVVHRCTERATGNNFAAKFIMTPHESDKET--VRKEIQIMNQLHHPKLINLHDAFEDDNEMVLILE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 141 FMAYGSAKDLIGT-HFMdgMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKvylsglrSNLSMISHGqrq 219
Cdd:cd14114    80 FLSGGELFERIAAeHYK--MSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTKRS-------NEVKLIDFG--- 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958659070 220 RAVHDFPKYSIKVLP----WLSPEVLQQNLQGYdaKSDIYSVGITACELANGHVPF 271
Cdd:cd14114   148 LATHLDPKESVKVTTgtaeFAAPEIVEREPVGF--YTDMWAVGVLSYVLLSGLSPF 201
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
114-272 7.75e-07

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


Pssm-ID: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 50.42  E-value: 7.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 114 SKLFS---HPNIVPYRATFIADNELWAVTSFMAYGSA-KDLIGTHFMDGMS-------ELAIAYILQgVLKALDYIHHMG 182
Cdd:cd14146    44 AKLFSmlrHPNIIKLEGVCLEEPNLCLVMEFARGGTLnRALAAANAAPGPRrarrippHILVNWAVQ-IARGMLYLHEEA 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 183 YV---HRSVKASHILISTdgKVYLSGLRSNLSMISHGQRQRAVHDFPKYSIK-VLPWLSPEVLQQNLqgYDAKSDIYSVG 258
Cdd:cd14146   123 VVpilHRDLKSSNILLLE--KIEHDDICNKTLKITDFGLAREWHRTTKMSAAgTYAWMAPEVIKSSL--FSKGSDIWSYG 198
                         170
                  ....*....|....
gi 1958659070 259 ITACELANGHVPFK 272
Cdd:cd14146   199 VLLWELLTGEVPYR 212
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
112-280 8.47e-07

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: 49.80  E-value: 8.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 112 HVSKLfSHPNIVPYRATFIADNELWAVTSFMAYGSAKDLIgtHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKAS 191
Cdd:cd14059    34 HLRKL-NHPNIIKFKGVCTQAPCYCILMEYCPYGQLYEVL--RAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSP 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 192 HILISTDGKVYLS--GLRSNLSMIShgqrqravhdfPKYSIK-VLPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGH 268
Cdd:cd14059   111 NVLVTYNDVLKISdfGTSKELSEKS-----------TKMSFAgTVAWMAPEVIRN--EPCSEKVDIWSFGVVLWELLTGE 177
                         170
                  ....*....|..
gi 1958659070 269 VPFKDMPATQML 280
Cdd:cd14059   178 IPYKDVDSSAII 189
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
61-274 9.46e-07

Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PASK (or PASKIN) is a nutrient and energy sensor and thus, plays an important role in maintaining cellular energy homeostasis. It coordinates the utilization of glucose in response to metabolic demand. It contains an N-terminal PAS domain which directly interacts and inhibits a C-terminal catalytic kinase domain. The PAS domain serves as a sensory module for different environmental signals such as light, redox state, and various metabolites. Binding of ligands to the PAS domain causes structural changes which leads to kinase activation and the phosphorylation of substrates to trigger the appropriate cellular response. The PASK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270906 [Multi-domain]  Cd Length: 256  Bit Score: 49.69  E-value: 9.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGFEDLmtVNLARYKPTGEYVTVRRINLE-ACSNEMVT-----FLQGELHVS---KLFSHPNIVPYrATFIA 131
Cdd:cd14004     2 YTILKEMGEGAYGQ--VNLAIYKSKGKEVVIKFIFKErILVDTWVRdrklgTVPLEIHILdtlNKRSHPNIVKL-LDFFE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 132 DNELWAVTSfMAYGSAKDLIG-THFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLRSNl 210
Cdd:cd14004    79 DDEFYYLVM-EKHGSGMDLFDfIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFGSA- 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958659070 211 SMISHGqrqravhdfpKYSIKV--LPWLSPEVLQQNLqgYDAKS-DIYSVGITACELANGHVPFKDM 274
Cdd:cd14004   157 AYIKSG----------PFDTFVgtIDYAAPEVLRGNP--YGGKEqDIWALGVLLYTLVFKENPFYNI 211
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
61-380 1.13e-06

Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TDY subtype and is composed of Group D plant MAPKs including Arabidopsis thaliana MPK18 (AtMPK18), Oryza sativa Blast- and Wound-induced MAPK1 (OsBWMK1), OsWJUMK1 (Wound- and JA-Uninducible MAPK1), Zea mays MPK6, and the Medicago sativa TDY1 gene product. OsBWMK1 enhances resistance to pathogenic infections. It mediates stress-activated defense responses by activating a transcription factor that affects the expression of stress-related genes. AtMPK18 is involved in microtubule-related functions. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20 while Oryza sativa contains at least 17 MAPKs. Arabidopsis thaliana contains more TEY-type MAPKs than TDY-type, whereas the reverse is true for Oryza sativa. The TDY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 50.16  E-value: 1.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGFEDLmtVNLARYKPTGEYVTVRRIN--LEACSNemVTFLQGELHVSKLFSHPNIV--------PYRATFi 130
Cdd:cd07859     2 YKIQEVIGKGSYGV--VCSAIDTHTGEKVAIKKINdvFEHVSD--ATRILREIKLLRLLRHPDIVeikhimlpPSRREF- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 131 adNELWAVTSFM------AYGSAKDLIGTHFMdgmselaiaYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKvyls 204
Cdd:cd07859    77 --KDIYVVFELMesdlhqVIKANDDLTPEHHQ---------FFLYQLLRALKYIHTANVFHRDLKPKNILANADCK---- 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 205 glrsnLSMISHGQRQRAVHDFP------KYsIKVLPWLSPEVLQQNLQGYDAKSDIYSVGITACELANGH--VPFKDMPA 276
Cdd:cd07859   142 -----LKICDFGLARVAFNDTPtaifwtDY-VATRWYRAPELCGSFFSKYTPAIDIWSIGCIFAEVLTGKplFPGKNVVH 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 277 TQMLLEKLNGTvPCLLDTSTIPAEEltmspsrsiANPGLNdslaagSLRPangdSPSHPYHRTFS---PHFHNFVEQCLQ 353
Cdd:cd07859   216 QLDLITDLLGT-PSPETISRVRNEK---------ARRYLS------SMRK----KQPVPFSQKFPnadPLALRLLERLLA 275
                         330       340
                  ....*....|....*....|....*..
gi 1958659070 354 RNPDARPNASTLLNHSFFKQIKRRASE 380
Cdd:cd07859   276 FDPKDRPTAEEALADPYFKGLAKVERE 302
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
61-284 1.14e-06

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type IV; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKIV is found predominantly in neurons and immune cells. It is activated by the binding of calcium/CaM and phosphorylation by CaMKK (alpha or beta). The CaMKK-CaMKIV cascade participates in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors. It also is implicated in T-cell development and signaling, cytokine secretion, and signaling through Toll-like receptors, and is thus, pivotal in immune response and inflammation. The CaMKIV subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270987 [Multi-domain]  Cd Length: 294  Bit Score: 49.82  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGFEDLmtVNLARYKPTGEYVTVRRINLEACSNemvtFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTS 140
Cdd:cd14085     5 FEIESELGRGATSV--VYRCRQKGTQKPYAVKKLKKTVDKK----IVRTEIGVLLRLSHPNIIKLKEIFETPTEISLVLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 141 FMAYGSAKDLI---GTHfmdgmSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDG-----KVYLSGLRsnlSM 212
Cdd:cd14085    79 LVTGGELFDRIvekGYY-----SERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPApdaplKIADFGLS---KI 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958659070 213 ISHGQRQRAVHDFPKYSikvlpwlSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKL 284
Cdd:cd14085   151 VDQQVTMKTVCGTPGYC-------APEILRG--CAYGPEVDMWSVGVITYILLCGFEPFYDERGDQYMFKRI 213
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
70-268 1.16e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 50.38  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  70 GFEDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQ-----GELHVSKLFSHPNIVPYRATFIADNELWAV-----T 139
Cdd:PHA03212   88 GIEKAGFSILETFTPGAEGFAFACIDNKTCEHVVIKAGQrggtaTEAHILRAINHPSIIQLKGTFTYNKFTCLIlprykT 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 140 SFMAYGSAKdligthfmdgmSELAIAYIL---QGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLsglrsnlsmishG 216
Cdd:PHA03212  168 DLYCYLAAK-----------RNIAICDILaieRSVLRAIQYLHENRIIHRDIKAENIFINHPGDVCL------------G 224
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958659070 217 QRQRAVHDFPKYSIKVLPWL------SPEVLQQNlqGYDAKSDIYSVGITACELANGH 268
Cdd:PHA03212  225 DFGAACFPVDINANKYYGWAgtiatnAPELLARD--PYGPAVDIWSAGIVLFEMATCH 280
STKc_IRAK2 cd14157
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; ...
82-267 1.31e-06

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: 49.84  E-value: 1.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  82 YKPTGEYVtVRRINLEACS--NEMVTFLQGELHVSKLFSHPNIVPYRAtFIADNELWA-VTSFMAYGSAKDLI----GTH 154
Cdd:cd14157    13 YRHGKQYV-IKRLKETECEspKSTERFFQTEVQICFRCCHPNILPLLG-FCVESDCHClIYPYMPNGSLQDRLqqqgGSH 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 155 FMDGMSELAIAYilqGVLKALDYIHHMGYVHRSVKASHILISTD--GKVYLSGLRsnlsmiSHGQRQRAVHDFPKysIKV 232
Cdd:cd14157    91 PLPWEQRLSISL---GLLKAVQHLHNFGILHGNIKSSNVLLDGNllPKLGHSGLR------LCPVDKKSVYTMMK--TKV 159
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1958659070 233 L----PWLsPEVLQQNLQgYDAKSDIYSVGITACELANG 267
Cdd:cd14157   160 LqislAYL-PEDFVRHGQ-LTEKVDIFSCGVVLAEILTG 196
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
62-280 1.50e-06

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


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 49.58  E-value: 1.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  62 ELLSVIGKGFEDlmtvNLARYKPTGEyVTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTSF 141
Cdd:cd14152     3 ELGELIGQGRWG----KVHRGRWHGE-VAIRLLEIDGNNQDHLKLFKKEVMNYRQTRHENVVLFMGACMHPPHLAIITSF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 142 ----MAYGSAKDLIGTHFMDGMSELAiayilQGVLKALDYIHHMGYVHRSVKASHILIStDGKVYLS--GLRSNLSMISH 215
Cdd:cd14152    78 ckgrTLYSFVRDPKTSLDINKTRQIA-----QEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITdfGLFGISGVVQE 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958659070 216 GQRQRAVhdfpKYSIKVLPWLSPEVLQQNLQG-------YDAKSDIYSVGITACELANGHVPFKDMPATQML 280
Cdd:cd14152   152 GRRENEL----KLPHDWLCYLAPEIVREMTPGkdedclpFSKAADVYAFGTIWYELQARDWPLKNQPAEALI 219
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
67-278 1.54e-06

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


Pssm-ID: 270637 [Multi-domain]  Cd Length: 251  Bit Score: 48.98  E-value: 1.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  67 IGKG-FEDlmtVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGElHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYG 145
Cdd:cd05041     3 IGRGnFGD---VYRGVLKPDNTEVAVKTCRETLPPDLKRKFLQEA-RILKQYDHPNIVKLIGVCVQKQPIMIVMELVPGG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 146 SakdlIGTHFMDGMSELAIAYILQGVLKA---LDYIHHMGYVHRSVKASHILISTDGKVYLS--GL----RSNLSMISHG 216
Cdd:cd05041    79 S----LLTFLRKKGARLTVKQLLQMCLDAaagMEYLESKNCIHRDLAARNCLVGENNVLKISdfGMsreeEDGEYTVSDG 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958659070 217 QRQravhdFPkysIKvlpWLSPEVLqqNLQGYDAKSDIYSVGITACEL-ANGHVPFKDMPATQ 278
Cdd:cd05041   155 LKQ-----IP---IK---WTAPEAL--NYGRYTSESDVWSFGILLWEIfSLGATPYPGMSNQQ 204
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
61-271 1.72e-06

Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. The PKA subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 49.32  E-value: 1.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLE-ACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVT 139
Cdd:cd14209     3 FDRIKTLGTG--SFGRVMLVRHKETGNYYAMKILDKQkVVKLKQVEHTLNEKRILQAINFPFLVKLEYSFKDNSNLYMVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 140 SFMAYGsakDLIGTHFMDG-MSEL-AIAYILQGVLkALDYIHHMGYVHRSVKASHILISTDGkvYLsglrsnlsmishgq 217
Cdd:cd14209    81 EYVPGG---EMFSHLRRIGrFSEPhARFYAAQIVL-AFEYLHSLDLIYRDLKPENLLIDQQG--YI-------------- 140
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 218 rqrAVHDF----------------PKYsikvlpwLSPEVLQqnLQGYDAKSDIYSVGITACELANGHVPF 271
Cdd:cd14209   141 ---KVTDFgfakrvkgrtwtlcgtPEY-------LAPEIIL--SKGYNKAVDWWALGVLIYEMAAGYPPF 198
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
67-265 1.92e-06

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


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 49.01  E-value: 1.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  67 IGKGfeDLMTVNLARYKptGEYVTVRrINLEACsnEMVTFLQGELHVSKLFSHPNIVPYRATFIADN----ELWAVTSFM 142
Cdd:cd14144     3 VGKG--RYGEVWKGKWR--GEKVAVK-IFFTTE--EASWFRETEIYQTVLMRHENILGFIAADIKGTgswtQLYLITDYH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 143 AYGSAKDLIGTHFMDGMSELAIAYILQGVLKAL-DYIHHM----GYVHRSVKASHILISTDGKVYLSGLRSNLSMISHGQ 217
Cdd:cd14144    76 ENGSLYDFLRGNTLDTQSMLKLAYSAACGLAHLhTEIFGTqgkpAIAHRDIKSKNILVKKNGTCCIADLGLAVKFISETN 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958659070 218 rqrAVHDFPKYSIKVLPWLSPEVLQQNL--QGYDA--KSDIYSVGITACELA 265
Cdd:cd14144   156 ---EVDLPPNTRVGTKRYMAPEVLDESLnrNHFDAykMADMYSFGLVLWEIA 204
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
61-370 2.02e-06

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek4 is highly abundant in the testis. Its specific function is unknown. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. Nek4 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270862 [Multi-domain]  Cd Length: 257  Bit Score: 48.97  E-value: 2.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADN-ELWAVT 139
Cdd:cd08223     2 YQFLRVIGKG--SYGEVWLVRHKRDRKQYVIKKLNLKNASKRERKAAEQEAKLLSKLKHPNIVSYKESFEGEDgFLYIVM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 140 SFMAYG---------SAKDLIGTHFMDGMSELAIayilqgvlkALDYIHHMGYVHRSVKASHILISTDGKVYLSGLRSNL 210
Cdd:cd08223    80 GFCEGGdlytrlkeqKGVLLEERQVVEWFVQIAM---------ALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIAR 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 211 SMISHGQRQRAVHDFPKYsikvlpwLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPF--KDMpatqmlleklngtv 288
Cdd:cd08223   151 VLESSSDMATTLIGTPYY-------MSPELFSN--KPYNHKSDVWALGCCVYEMATLKHAFnaKDM-------------- 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 289 pclldtstipaeeltmspsrsianpglnDSLaagSLRPANGDSPSHPyhRTFSPHFHNFVEQCLQRNPDARPNASTLLNH 368
Cdd:cd08223   208 ----------------------------NSL---VYKILEGKLPPMP--KQYSPELGELIKAMLHQDPEKRPSVKRILRQ 254

                  ..
gi 1958659070 369 SF 370
Cdd:cd08223   255 PY 256
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
120-272 2.41e-06

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK2, also called beta-adrenergic receptor kinase (beta-ARK) or beta-ARK1, is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRK2 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. TheGRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271125 [Multi-domain]  Cd Length: 321  Bit Score: 49.28  E-value: 2.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 120 PNIVPYRATFIADNELWAVTSFMAYGSAKDLIGTHFMdgMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDG 199
Cdd:cd14223    63 PFIVCMSYAFHTPDKLSFILDLMNGGDLHYHLSQHGV--FSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFG 140
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958659070 200 KVYLSglrsNLSMISHGQRQRavhdfPKYSIKVLPWLSPEVLQQNLqGYDAKSDIYSVGITACELANGHVPFK 272
Cdd:cd14223   141 HVRIS----DLGLACDFSKKK-----PHASVGTHGYMAPEVLQKGV-AYDSSADWFSLGCMLFKLLRGHSPFR 203
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
158-371 2.77e-06

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: 48.86  E-value: 2.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 158 GMSELAIAYILQGVLKALDYIH---HMgyVHRSVKASHILISTDGKVYLSGL--------RSNLSMISHGQRQRaVHDFP 226
Cdd:cd14011   110 KLYDVEIKYGLLQISEALSFLHndvKL--VHGNICPESVVINSNGEWKLAGFdfcisseqATDQFPYFREYDPN-LPPLA 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 227 KYSikvLPWLSPEVLQQNlqGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLngtvPCLLDTSTIPAEELTMSP 306
Cdd:cd14011   187 QPN---LNYLAPEYILSK--TCDPASDMFSLGVLIYAIYNKGKPLFDCVNNLLSYKKN----SNQLRQLSLSLLEKVPEE 257
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958659070 307 SRSianpglndslaagslrpangdspshpyhrtfsphfhnFVEQCLQRNPDARPNASTLLNHSFF 371
Cdd:cd14011   258 LRD-------------------------------------HVKTLLNVTPEVRPDAEQLSKIPFF 285
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
59-271 2.83e-06

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


Pssm-ID: 270768 [Multi-domain]  Cd Length: 357  Bit Score: 48.86  E-value: 2.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  59 GCYELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEAC-SNEMVTFLQGELHV-SKLFSHPNIVPYRATFIADNELW 136
Cdd:cd05617    15 QDFDLIRVIGRG--SYAKVLLVRLKKNDQIYAMKVVKKELVhDDEDIDWVQTEKHVfEQASSNPFLVGLHSCFQTTSRLF 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 137 AVTSFMAYGSAkdLIGTHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLRSNLSMISHG 216
Cdd:cd05617    93 LVIEYVNGGDL--MFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPG 170
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958659070 217 QRQRAVHDFPKYsikvlpwLSPEVLQQNLQGYDAksDIYSVGITACELANGHVPF 271
Cdd:cd05617   171 DTTSTFCGTPNY-------IAPEILRGEEYGFSV--DWWALGVLMFEMMAGRSPF 216
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
171-374 3.36e-06

Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The beta-ARK group is composed of GRK2, GRK3, and similar proteins. GRK2 and GRK3 are both widely expressed in many tissues, although GRK2 is present at higher levels. They contain an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRK2 (also called beta-ARK or beta-ARK1) is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The beta-ARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270757 [Multi-domain]  Cd Length: 279  Bit Score: 48.20  E-value: 3.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 171 VLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSNLSmishgqrqravHDFPKYSIKVLPWLSPEVLQQNlQGY 248
Cdd:cd05606   107 VILGLEHMHNRFIVYRDLKPANILLDEHGHVRISdlGLACDFS-----------KKKPHASVGTHGYMAPEVLQKG-VAY 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 249 DAKSDIYSVGITACELANGHVPFKDMPATqmlleklngtvpcllDTSTIPAEELTMspsrsiaNPGLNDSlaagslrpan 328
Cdd:cd05606   175 DSSADWFSLGCMLYKLLKGHSPFRQHKTK---------------DKHEIDRMTLTM-------NVELPDS---------- 222
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958659070 329 gdspshpyhrtFSPHFHNFVEQCLQRNPDAR-----PNASTLLNHSFFKQI 374
Cdd:cd05606   223 -----------FSPELKSLLEGLLQRDVSKRlgclgRGATEVKEHPFFKGV 262
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
61-371 3.46e-06

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


Pssm-ID: 270846 [Multi-domain]  Cd Length: 290  Bit Score: 48.49  E-value: 3.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLAR-YKPTGEYVTVRRINLEACSNEMVTFLQGELHVSK---LFSHPNIVP-YRATFIADNEL 135
Cdd:cd07862     3 YECVAEIGEG--AYGKVFKARdLKNGGRFVALKRVRVQTGEEGMPLSTIREVAVLRhleTFEHPNVVRlFDVCTVSRTDR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 136 WAVTSFMAYGSAKDLigTHFMD-----GMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLrsNL 210
Cdd:cd07862    81 ETKLTLVFEHVDQDL--TTYLDkvpepGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADF--GL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 211 SMISHGQRQRAVhdfpkySIKVLPWLSPEVLQQNlqGYDAKSDIYSVGITACELanghvpFKDMPatqmlLEKLNGTVPC 290
Cdd:cd07862   157 ARIYSFQMALTS------VVVTLWYRAPEVLLQS--SYATPVDLWSVGCIFAEM------FRRKP-----LFRGSSDVDQ 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 291 L---LDTSTIPAEEltmSPSRSIANPglndslaagslRPANGDSPSHPYHRtFSPHF----HNFVEQCLQRNPDARPNAS 363
Cdd:cd07862   218 LgkiLDVIGLPGEE---DWPRDVALP-----------RQAFHSKSAQPIEK-FVTDIdelgKDLLLKCLTFNPAKRISAY 282

                  ....*...
gi 1958659070 364 TLLNHSFF 371
Cdd:cd07862   283 SALSHPYF 290
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
110-373 3.88e-06

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK3 shows a restricted expression pattern; it is found at high levels in the pituary glands and is also expressed in the kidney and brain. It has been shown to regulate many ion transporters including members of the SLC12A family of cation-chloride cotransporters such as NCC and NKCC2, the renal potassium channel ROMK, and the epithelial calcium channels TRPV5 and TRPV6. WNK3 appears to sense low-chloride hypotonic stress and under these conditions, it activates SPAK, which directly interacts and phosphorylates cation-chloride cotransporters. WNK3 has also been shown to promote cell survival, possibly through interaction with procaspase-3 and HSP70. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 48.18  E-value: 3.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 110 ELHVSKLFSHPNIV----PYRATFIADNELWAVTSFMAYGSAKDLIGTHFMdgMSELAIAYILQGVLKALDYIHHMG--Y 183
Cdd:cd14031    59 EAEMLKGLQHPNIVrfydSWESVLKGKKCIVLVTELMTSGTLKTYLKRFKV--MKPKVLRSWCRQILKGLQFLHTRTppI 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 184 VHRSVKASHILIS-TDGKVYLSGLrsNLSMISHGQRQRAVHDFPKYsikvlpwLSPEVLQQNlqgYDAKSDIYSVGITAC 262
Cdd:cd14031   137 IHRDLKCDNIFITgPTGSVKIGDL--GLATLMRTSFAKSVIGTPEF-------MAPEMYEEH---YDESVDVYAFGMCML 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 263 ELANGHVPFKDMPATQMLLEKLngtvpclldtstipaeeltmspsrsianpglndslaAGSLRPANgdspshpYHRTFSP 342
Cdd:cd14031   205 EMATSEYPYSECQNAAQIYRKV------------------------------------TSGIKPAS-------FNKVTDP 241
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958659070 343 HFHNFVEQCLQRNPDARPNASTLLNHSFFKQ 373
Cdd:cd14031   242 EVKEIIEGCIRQNKSERLSIKDLLNHAFFAE 272
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
138-283 3.92e-06

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


Pssm-ID: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 48.48  E-value: 3.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 138 VTSFMAYGSAKDLIGTHFMDGMSELAIAYILQgVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSNLsmish 215
Cdd:cd05108    86 ITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQ-IAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITdfGLAKLL----- 159
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958659070 216 GQRQRAVH-DFPKYSIKvlpWLSPEVLQQNLqgYDAKSDIYSVGITACELAN-GHVPFKDMPATQM--LLEK 283
Cdd:cd05108   160 GAEEKEYHaEGGKVPIK---WMALESILHRI--YTHQSDVWSYGVTVWELMTfGSKPYDGIPASEIssILEK 226
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
61-289 5.67e-06

Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases Sty1 and Hog1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs Sty1 from Schizosaccharomyces pombe, Hog1 from Saccharomyces cerevisiae, and similar proteins. Sty1 and Hog1 are stress-activated MAPKs that partipate in transcriptional regulation in response to stress. Sty1 is activated in response to oxidative stress, osmotic stress, and UV radiation. It is regulated by the MAP2K Wis1, which is activated by the MAP3Ks Wis4 and Win1, which receive signals of the stress condition from membrane-spanning histidine kinases Mak1-3. Activated Sty1 stabilizes the Atf1 transcription factor and induces transcription of Atf1-dependent genes of the core environmetal stress response. Hog1 is the key element in the high osmolarity glycerol (HOG) pathway and is activated upon hyperosmotic stress. Activated Hog1 accumulates in the nucleus and regulates stress-induced transcription. The HOG pathway is mediated by two transmembrane osmosensors, Sln1 and Sho1. MAPKs are important mediators of cellular responses to extracellular signals. The Sty1/Hog1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270843 [Multi-domain]  Cd Length: 328  Bit Score: 47.95  E-value: 5.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGFEDLmtVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNE-LWAVT 139
Cdd:cd07856    12 YSDLQPVGMGAFGL--VCSARDQLTGQNVAVKKIMKPFSTPVLAKRTYRELKLLKHLRHENIISLSDIFISPLEdIYFVT 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 140 SFMAygsaKDLIGTHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLrsNLSMISHGQRQ 219
Cdd:cd07856    90 ELLG----TDLHRLLTSRPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDF--GLARIQDPQMT 163
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958659070 220 RAVHDfpKYsikvlpWLSPEVLqQNLQGYDAKSDIYSVGITACELANGH--VPFKDMPATQMLLEKLNGTVP 289
Cdd:cd07856   164 GYVST--RY------YRAPEIM-LTWQKYDVEVDIWSAGCIFAEMLEGKplFPGKDHVNQFSIITELLGTPP 226
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
106-265 5.82e-06

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I Receptor and Activin Type IB/IC Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR1, also called Activin receptor-Like Kinase 5 (ALK5), functions as a receptor for TGFbeta and phoshorylates SMAD2/3. TGFbeta proteins are cytokines that regulate cell growth, differentiation, and survival, and are critical in the development and progression of many human cancers. Mutations in TGFbR1 (and TGFbR2) can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. ACVR1b (also called ALK4) and ACVR1c (also called ALK7) act as receptors for activin A and B, respectively. TGFbR1, ACVR1b, and ACVR1c belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like TGFbR1, ACVR1b, and ACVR1c, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The TGFbR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271045 [Multi-domain]  Cd Length: 288  Bit Score: 47.82  E-value: 5.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 106 FLQGELHVSKLFSHPNIVPYRAtfiADN-------ELWAVTSFMAYGSAKDLIGTHFMD--GMSELAIAyILQGvLKALd 176
Cdd:cd14143    35 FREAEIYQTVMLRHENILGFIA---ADNkdngtwtQLWLVSDYHEHGSLFDYLNRYTVTveGMIKLALS-IASG-LAHL- 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 177 yihHMGYV---------HRSVKASHILISTDGKVYLSGLrsNLSmISHGQRQRAVHDFPKYSIKVLPWLSPEVLQQ--NL 245
Cdd:cd14143   109 ---HMEIVgtqgkpaiaHRDLKSKNILVKKNGTCCIADL--GLA-VRHDSATDTIDIAPNHRVGTKRYMAPEVLDDtiNM 182
                         170       180
                  ....*....|....*....|..
gi 1958659070 246 QGYDA--KSDIYSVGITACELA 265
Cdd:cd14143   183 KHFESfkRADIYALGLVFWEIA 204
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
61-285 6.67e-06

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


Pssm-ID: 270753 [Multi-domain]  Cd Length: 339  Bit Score: 47.70  E-value: 6.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEAC--SNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAV 138
Cdd:cd05602     9 FHFLKVIGKG--SFGKVLLARHKSDEKFYAVKVLQKKAIlkKKEEKHIMSERNVLLKNVKHPFLVGLHFSFQTTDKLYFV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 139 TSFMAYGSAKDLIGTH--FMDGMSELAIAYILQgvlkALDYIHHMGYVHRSVKASHILISTDGKVYLSGLRSNLSMISHG 216
Cdd:cd05602    87 LDYINGGELFYHLQRErcFLEPRARFYAAEIAS----ALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENIEPN 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958659070 217 QRQRAVHDFPKYsikvlpwLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLN 285
Cdd:cd05602   163 GTTSTFCGTPEY-------LAPEVLHK--QPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILN 222
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
61-265 7.35e-06

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


Pssm-ID: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 47.54  E-value: 7.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKG-----FEDLMTVNLAR-----YKPtgeyVTVRRINLEACsnemvtFLQgelhvsKLFSHPNIV------- 123
Cdd:cd14132    20 YEIIRKIGRGkysevFEGINIGNNEKvvikvLKP----VKKKKIKREIK------ILQ------NLRGGPNIVklldvvk 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 124 ---PYRATFI---ADNELWavtsfmaygsaKDLIGThfmdgMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILIST 197
Cdd:cd14132    84 dpqSKTPSLIfeyVNNTDF-----------KTLYPT-----LTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMIDH 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958659070 198 DgkvylsglRSNLSMISHGqrqraVHDF----PKYSIKV--LPWLSPEVLqQNLQGYDAKSDIYSVGitaCELA 265
Cdd:cd14132   148 E--------KRKLRLIDWG-----LAEFyhpgQEYNVRVasRYYKGPELL-VDYQYYDYSLDMWSLG---CMLA 204
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
110-273 7.45e-06

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


Pssm-ID: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 47.25  E-value: 7.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 110 ELHVSKLFSHPNIVPYRATF--IADNELWAVTSFMAYGSAKDLIGTHfmdGMSELAIAYILQGVLKALDYIHHMGYVHRS 187
Cdd:cd14200    73 EIAILKKLDHVNIVKLIEVLddPAEDNLYMVFDLLRKGPVMEVPSDK---PFSEDQARLYFRDIVLGIEYLHYQKIVHRD 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 188 VKASHILISTDGKVYLSGLR-SNlsmishgqrQRAVHDFPKYSIKVLP-WLSPEVLQQNLQGYDAKS-DIYSVGITACEL 264
Cdd:cd14200   150 IKPSNLLLGDDGHVKIADFGvSN---------QFEGNDALLSSTAGTPaFMAPETLSDSGQSFSGKAlDVWAMGVTLYCF 220

                  ....*....
gi 1958659070 265 ANGHVPFKD 273
Cdd:cd14200   221 VYGKCPFID 229
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
167-277 7.46e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 47.56  E-value: 7.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 167 ILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLrsnlsmishGQRQRAVHDFPKYSIK-VLPWLSPEVLQQNl 245
Cdd:PHA03209  162 IEKQILEGLRYLHAQRIIHRDVKTENIFINDVDQVCIGDL---------GAAQFPVVAPAFLGLAgTVETNAPEVLARD- 231
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958659070 246 qGYDAKSDIYSVGITACE-LANGHVPFKDMPAT 277
Cdd:PHA03209  232 -KYNSKADIWSAGIVLFEmLAYPSTIFEDPPST 263
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
61-272 7.53e-06

Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). This subfamily includes Aurora-B and Aurora-C. Aurora-B is most active at the transition during metaphase to the end of mitosis. It associates with centromeres, relocates to the midzone of the central spindle, and concentrates at the midbody during cell division. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. INCENP participates in the activation of Aurora-B in a two-step process: first by binding to form an intermediate state of activation and the phosphorylation of its C-terminal TSS motif to generate the fully active kinase. The Aurora-B subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271019 [Multi-domain]  Cd Length: 270  Bit Score: 47.17  E-value: 7.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTF-LQGELHVSKLFSHPNIVPYRATFIADNELWAVT 139
Cdd:cd14117     8 FDIGRPLGKG--KFGNVYLAREKQSKFIVALKVLFKSQIEKEGVEHqLRREIEIQSHLRHPNILRLYNYFHDRKRIYLIL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 140 SFMAYGSA-KDLIGTHFMDgmsELAIAYILQGVLKALDYIHHMGYVHRSVKASHILIstdgkvylsGLRSNLSMISHGQR 218
Cdd:cd14117    86 EYAPRGELyKELQKHGRFD---EQRTATFMEELADALHYCHEKKVIHRDIKPENLLM---------GYKGELKIADFGWS 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958659070 219 QRAVHDFPKYSIKVLPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFK 272
Cdd:cd14117   154 VHAPSLRRRTMCGTLDYLPPEMIEG--RTHDEKVDLWCIGVLCYELLVGMPPFE 205
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
86-371 8.31e-06

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-2 is also referred to as ALS2CR7 (amyotrophic lateral sclerosis 2 (juvenile) chromosome region candidate 7). It may be associated with amyotrophic lateral sclerosis 2 (ALS2), an autosomal recessive form of juvenile ALS. The function of PFTAIRE-2 is not yet known. It shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270852 [Multi-domain]  Cd Length: 286  Bit Score: 47.26  E-value: 8.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  86 GEYVTVRRINLEAcsNEMVTFLQ-GELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGSAKDLIgtHFMDGMSELAI 164
Cdd:cd07870    25 GQLVALKVISMKT--EEGVPFTAiREASLLKGLKHANIVLLHDIIHTKETLTFVFEYMHTDLAQYMI--QHPGGLHPYNV 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 165 AYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSNLSMISHgqrqravhdfpKYSIKVLP-WLSPEVL 241
Cdd:cd07870   101 RLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLAdfGLARAKSIPSQ-----------TYSSEVVTlWYRPPDV 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 242 QQNLQGYDAKSDIYSVGITACELANGHVPFkdmPATQMLLEKLNGTVPCLldtsTIPAEELTmspsrsianPGLNDslaA 321
Cdd:cd07870   170 LLGATDYSSALDIWGAGCIFIEMLQGQPAF---PGVSDVFEQLEKIWTVL----GVPTEDTW---------PGVSK---L 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958659070 322 GSLRPANGDSPSHPYHRTF------SPHFHNFVEQCLQRNPDARPNASTLLNHSFF 371
Cdd:cd07870   231 PNYKPEWFLPCKPQQLRVVwkrlsrPPKAEDLASQMLMMFPKDRISAQDALLHPYF 286
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
120-272 1.02e-05

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK3, also called beta-adrenergic receptor kinase 2 (beta-ARK2), is widely expressed in many tissues. It is involved in modulating the cholinergic response of airway smooth muscles, and also plays a role in dopamine receptor regulation. GRK3-deficient mice show a lack of olfactory receptor desensitization and altered regulation of the M2 muscarinic airway. GRK3 promoter polymorphisms may also be associated with bipolar disorder. GRK3 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 47.36  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 120 PNIVPYRATFIADNELWAVTSFMAYGSAKDLIGTHFMdgMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDG 199
Cdd:cd05633    68 PFIVCMTYAFHTPDKLCFILDLMNGGDLHYHLSQHGV--FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHG 145
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958659070 200 KVYLSglrsNLSMISHGQRQRavhdfPKYSIKVLPWLSPEVLQQNlQGYDAKSDIYSVGITACELANGHVPFK 272
Cdd:cd05633   146 HVRIS----DLGLACDFSKKK-----PHASVGTHGYMAPEVLQKG-TAYDSSADWFSLGCMLFKLLRGHSPFR 208
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
110-371 1.15e-05

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK4 shows a restricted expression pattern and is usually found in epithelial cells. It is expressed in nephrons and in extrarenal tissues including intestine, eye, mammary glands, and prostate. WNK4 regulates a variety of ion transport proteins including apical or basolateral ion transporters, ion channels in the transcellular pathway, and claudins in the paracellular pathway. Mutations in WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK4 inhibits the activity of the thiazide-sensitive Na-Cl cotransporter (NCC), which is responsible for about 15% of NaCl reabsorption in the kidney. It also inhibits the renal outer medullary potassium channel (ROMK) and decreases its surface expression. Hypertension and hyperkalemia in PHAII patients with WNK4 mutations may be partly due to increased NaCl reabsorption through NCC and impaired renal potassium secretion by ROMK, respectively. The WNK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 46.53  E-value: 1.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 110 ELHVSKLFSHPNIV----PYRATFIADNELWAVTSFMAYGSAKDLIgTHFMDGMSELAIAYILQgVLKALDYIHHMG--Y 183
Cdd:cd14033    50 EVEMLKGLQHPNIVrfydSWKSTVRGHKCIILVTELMTSGTLKTYL-KRFREMKLKLLQRWSRQ-ILKGLHFLHSRCppI 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 184 VHRSVKASHILIS-TDGKVYLSGLrsNLSMISHGQRQRAVHDFPKYsikvlpwLSPEVLQQNlqgYDAKSDIYSVGITAC 262
Cdd:cd14033   128 LHRDLKCDNIFITgPTGSVKIGDL--GLATLKRASFAKSVIGTPEF-------MAPEMYEEK---YDEAVDVYAFGMCIL 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 263 ELANGHVPFKDMPATQMLLEKLngtvpclldtstipaeeltmspsrsianpglndslaagslrpANGDSPShPYHRTFSP 342
Cdd:cd14033   196 EMATSEYPYSECQNAAQIYRKV------------------------------------------TSGIKPD-SFYKVKVP 232
                         250       260
                  ....*....|....*....|....*....
gi 1958659070 343 HFHNFVEQCLQRNPDARPNASTLLNHSFF 371
Cdd:cd14033   233 ELKEIIEGCIRTDKDERFTIQDLLEHRFF 261
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
89-274 1.21e-05

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


Pssm-ID: 271052 [Multi-domain]  Cd Length: 265  Bit Score: 46.55  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  89 VTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNelWAVTSFMAYGSAK----DLIGTHFmDGMSELAI 164
Cdd:cd14150    25 VAVKILKVTEPTPEQLQAFKNEMQVLRKTRHVNILLFMGFMTRPN--FAIITQWCEGSSLyrhlHVTETRF-DTMQLIDV 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 165 AyilQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSNLSMISHGQRQRAvhdfPKYSIKvlpWLSPEVLQ 242
Cdd:cd14150   102 A---RQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGdfGLATVKTRWSGSQQVEQ----PSGSIL---WMAPEVIR 171
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1958659070 243 -QNLQGYDAKSDIYSVGITACELANGHVPFKDM 274
Cdd:cd14150   172 mQDTNPYSFQSDVYAYGVVLYELMSGTLPYSNI 204
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
106-280 1.21e-05

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


Pssm-ID: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 46.63  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 106 FLQgELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGSAKDLI----GTHFMDGMSELAiAYILQGvlkaLDYIHHM 181
Cdd:cd05068    50 FLR-EAQIMKKLRHPKLIQLYAVCTLEEPIYIITELMKHGSLLEYLqgkgRSLQLPQLIDMA-AQVASG----MAYLESQ 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 182 GYVHRSVKASHILISTDG--KVYLSGLrSNLSMISHGQRQRAVHDFPkysIKvlpWLSPEVLqqNLQGYDAKSDIYSVGI 259
Cdd:cd05068   124 NYIHRDLAARNVLVGENNicKVADFGL-ARVIKVEDEYEAREGAKFP---IK---WTAPEAA--NYNRFSIKSDVWSFGI 194
                         170       180
                  ....*....|....*....|..
gi 1958659070 260 TACELAN-GHVPFKDMPATQML 280
Cdd:cd05068   195 LLTEIVTyGRIPYPGMTNAEVL 216
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
61-371 1.44e-05

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


Pssm-ID: 270825 [Multi-domain]  Cd Length: 282  Bit Score: 46.50  E-value: 1.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKG-FEDlmtVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVpyRAT-FIADNELWAV 138
Cdd:cd07831     1 YKILGKIGEGtFSE---VLKAQSRKTGKYYAIKCMKKHFKSLEQVNNLREIQALRRLSPHPNIL--RLIeVLFDRKTGRL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 139 TSFMaygsakdligtHFMDG------------MSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILIStDGKVYLSGL 206
Cdd:cd07831    76 ALVF-----------ELMDMnlyelikgrkrpLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIK-DDILKLADF 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 207 RSnlsmishgqrQRAVHDFPKYSIKV-LPWL-SPEVLQQNlqG-YDAKSDIYSVGITACELANGHVPFkdmPATQML--L 281
Cdd:cd07831   144 GS----------CRGIYSKPPYTEYIsTRWYrAPECLLTD--GyYGPKMDIWAVGCVFFEILSLFPLF---PGTNELdqI 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 282 EKLNgtvpclldtstipaeELTMSPSRSIANpglndslaagSLRPANGDSPSHPyHRT---FSPHFHNFVEQC------- 351
Cdd:cd07831   209 AKIH---------------DVLGTPDAEVLK----------KFRKSRHMNYNFP-SKKgtgLRKLLPNASAEGldllkkl 262
                         330       340
                  ....*....|....*....|
gi 1958659070 352 LQRNPDARPNASTLLNHSFF 371
Cdd:cd07831   263 LAYDPDERITAKQALRHPYF 282
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
82-271 1.48e-05

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


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 46.64  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  82 YKPTGE------YVTVRR-INLEACSNEMVTFLQGELHV--SKLF----------SHPNIVPYRATFIADNELWAVTSFM 142
Cdd:cd14090     3 YKLTGEllgegaYASVQTcINLYTGKEYAVKIIEKHPGHsrSRVFrevetlhqcqGHPNILQLIEYFEDDERFYLVFEKM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 143 AYGSAKDLIGT--HFmdgmSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVY---------LSGLRSNls 211
Cdd:cd14090    83 RGGPLLSHIEKrvHF----TEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKVSpvkicdfdlGSGIKLS-- 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958659070 212 mishGQRQRAVHDfPKYSIKV--LPWLSPEVLQ----QNLQgYDAKSDIYSVGITACELANGHVPF 271
Cdd:cd14090   157 ----STSMTPVTT-PELLTPVgsAEYMAPEVVDafvgEALS-YDKRCDLWSLGVILYIMLCGYPPF 216
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
62-283 1.49e-05

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


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 46.25  E-value: 1.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  62 ELLSVIGKGfeDLMTVNLARYKPTGEYVTVR---RINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADnELWAV 138
Cdd:cd05057    10 EKGKVLGSG--AFGTVYKGVWIPEGEKVKIPvaiKVLREETGPKANEEILDEAYVMASVDHPHLVRLLGICLSS-QVQLI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 139 TSFMAYGSAKDLIGTHFMDGMSELAIAYILQgVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSnlsMISHG 216
Cdd:cd05057    87 TQLMPLGCLLDYVRNHRDNIGSQLLLNWCVQ-IAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITdfGLAK---LLDVD 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 217 QRQRAVhDFPKYSIKvlpWLSPEVLQqnLQGYDAKSDIYSVGITACELAN-GHVPFKDMPATQM--LLEK 283
Cdd:cd05057   163 EKEYHA-EGGKVPIK---WMALESIQ--YRIYTHKSDVWSYGVTVWELMTfGAKPYEGIPAVEIpdLLEK 226
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
131-306 1.80e-05

Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS2 is an essential mitotic regulator responsible for coordinating accurate cytokinesis completion and governing the stabilization of other mitotic regulators. It is also critical in the maintenance of proper chromosome number, genomic stability, mitotic fidelity, and the integrity of centrosome duplication. Downregulation of LATS2 is associated with poor prognosis in acute lymphoblastic leukemia and breast cancer. The LATS2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 46.54  E-value: 1.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 131 ADNElWAVTSFMAYGSAKDLigtHFM-------DGMS----------ELAIAYILQGVLkALDYIHHMGYVHRSVKASHI 193
Cdd:cd05626    58 ADNE-WVVKLYYSFQDKDNL---YFVmdyipggDMMSllirmevfpeVLARFYIAELTL-AIESVHKMGFIHRDIKPDNI 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 194 LISTDGKVYL-------------------------------SGLRSNLSMISHGQR-----QRAVHDFPK---YSIKVLP 234
Cdd:cd05626   133 LIDLDGHIKLtdfglctgfrwthnskyyqkgshirqdsmepSDLWDDVSNCRCGDRlktleQRATKQHQRclaHSLVGTP 212
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958659070 235 -WLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTvpcllDTSTIPAeELTMSP 306
Cdd:cd05626   213 nYIAPEVLLR--KGYTQLCDWWSVGVILFEMLVGQPPFLAPTPTETQLKVINWE-----NTLHIPP-QVKLSP 277
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
60-371 1.95e-05

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


Pssm-ID: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 46.06  E-value: 1.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  60 CYELLSVIGKGfedlmT---VNLARYKPTGEYVTVRRINLEacsNEM----VTFLQgELHVSKLFSHPNIVPYRATFIAD 132
Cdd:cd07843     6 EYEKLNRIEEG-----TygvVYRARDKKTGEIVALKKLKME---KEKegfpITSLR-EINILLKLQHPNIVTVKEVVVGS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 133 N--ELWAVTSFMAYgSAKDLIgTHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGkvylsglrsnl 210
Cdd:cd07843    77 NldKIYMVMEYVEH-DLKSLM-ETMKQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRG----------- 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 211 smishgqrQRAVHDF----------PKYSIKV--LPWLSPEVLqqnL--QGYDAKSDIYSVGITACELANGHVPFKDmpa 276
Cdd:cd07843   144 --------ILKICDFglareygsplKPYTQLVvtLWYRAPELL---LgaKEYSTAIDMWSVGCIFAELLTKKPLFPG--- 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 277 tQMLLEKLNgTVPCLLDTstipaeeltmsPSRSIAnPGLNDSLAAGSLRPangdsPSHPY--------HRTFSPHFHNFV 348
Cdd:cd07843   210 -KSEIDQLN-KIFKLLGT-----------PTEKIW-PGFSELPGAKKKTF-----TKYPYnqlrkkfpALSLSDNGFDLL 270
                         330       340
                  ....*....|....*....|...
gi 1958659070 349 EQCLQRNPDARPNASTLLNHSFF 371
Cdd:cd07843   271 NRLLTYDPAKRISAEDALKHPYF 293
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
119-271 2.25e-05

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: 45.79  E-value: 2.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 119 HPNIVPYRATFIADNELWAVTSFMAYGSAkdLIGTHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTD 198
Cdd:cd14173    59 HRNVLELIEFFEEEDKFYLVFEKMRGGSI--LSHIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHP 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 199 GKVYL---------SG--LRSNLSMISHGQRQRavhdfPKYSIKvlpWLSPEVLQ---QNLQGYDAKSDIYSVGITACEL 264
Cdd:cd14173   137 NQVSPvkicdfdlgSGikLNSDCSPISTPELLT-----PCGSAE---YMAPEVVEafnEEASIYDKRCDLWSLGVILYIM 208

                  ....*..
gi 1958659070 265 ANGHVPF 271
Cdd:cd14173   209 LSGYPPF 215
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
61-295 2.32e-05

Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. Its mRNA levels is low at birth, increases at puberty, and remains high throughout adulthood. The TSSK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 45.75  E-value: 2.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVT-FLQGELHVSKLFSHPNIVP-YRATFIADNELWAV 138
Cdd:cd14163     2 YQLGKTIGEG--TYSKVKEAFSKKHQRKVAIKIIDKSGGPEEFIQrFLPRELQIVERLDHKNIIHvYEMLESADGKIYLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 139 TSFMAYGSAKDLIgTHFMDGMSELAIAYILQgVLKALDYIHHMGYVHRSVKASHIListdgkvyLSGLRSNLSMISHGQR 218
Cdd:cd14163    80 MELAEDGDVFDCV-LHGGPLPEHRAKALFRQ-LVEAIRYCHGCGVAHRDLKCENAL--------LQGFTLKLTDFGFAKQ 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958659070 219 QRAVH-DFPKYSIKVLPWLSPEVLQqNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNG-TVPCLLDTS 295
Cdd:cd14163   150 LPKGGrELSQTFCGSTAYAAPEVLQ-GVPHDSRKGDIWSMGVVLYVMLCAQLPFDDTDIPKMLCQQQKGvSLPGHLGVS 227
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
80-266 2.55e-05

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


Pssm-ID: 270845 [Multi-domain]  Cd Length: 285  Bit Score: 45.87  E-value: 2.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  80 ARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGSAK---DLIGTHFM 156
Cdd:cd07861    19 GRNKKTGQIVAMKKIRLESEEEGVPSTAIREISLLKELQHPNIVCLEDVLMQENRLYLVFEFLSMDLKKyldSLPKGKYM 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 157 DgmSELAIAYILQgVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSnlsmiSHGQRQRAVhdfpKYSIKVLP 234
Cdd:cd07861    99 D--AELVKSYLYQ-ILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLAdfGLAR-----AFGIPVRVY----THEVVTLW 166
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1958659070 235 WLSPEVLQQNlQGYDAKSDIYSVGITACELAN 266
Cdd:cd07861   167 YRAPEVLLGS-PRYSTPVDIWSIGTIFAEMAT 197
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
115-373 2.55e-05

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


Pssm-ID: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 45.81  E-value: 2.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 115 KLFSHPNIV----PYRATFIADNELWAVTSFMAYGSAKDLIgTHFMDGMSELAIAYILQgVLKALDYIHHMG--YVHRSV 188
Cdd:cd14030    79 KGLQHPNIVrfydSWESTVKGKKCIVLVTELMTSGTLKTYL-KRFKVMKIKVLRSWCRQ-ILKGLQFLHTRTppIIHRDL 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 189 KASHILIS-TDGKVYLSGLrsNLSMISHGQRQRAVHDFPKYsikvlpwLSPEVLQQNlqgYDAKSDIYSVGITACELANG 267
Cdd:cd14030   157 KCDNIFITgPTGSVKIGDL--GLATLKRASFAKSVIGTPEF-------MAPEMYEEK---YDESVDVYAFGMCMLEMATS 224
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 268 HVPFKD-MPATQMLLEKLNGTVPCLLDTSTIpaeeltmspsrsianpglndslaagslrpangdspshpyhrtfsPHFHN 346
Cdd:cd14030   225 EYPYSEcQNAAQIYRRVTSGVKPASFDKVAI--------------------------------------------PEVKE 260
                         250       260
                  ....*....|....*....|....*..
gi 1958659070 347 FVEQCLQRNPDARPNASTLLNHSFFKQ 373
Cdd:cd14030   261 IIEGCIRQNKDERYAIKDLLNHAFFQE 287
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
66-278 2.56e-05

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


Pssm-ID: 271106 [Multi-domain]  Cd Length: 284  Bit Score: 45.70  E-value: 2.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  66 VIGKG-FEDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADN-----ELWAVT 139
Cdd:cd14204    14 VLGEGeFGSVMEGELQQPDGTNHKVAVKTMKLDNFSQREIEEFLSEAACMKDFNHPNVIRLLGVCLEVGsqripKPMVIL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 140 SFMAYGSakdlIGTHFMDGMSELAIAYI-LQGVLK-------ALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSN 209
Cdd:cd14204    94 PFMKYGD----LHSFLLRSRLGSGPQHVpLQTLLKfmidialGMEYLSSRNFLHRDLAARNCMLRDDMTVCVAdfGLSKK 169
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958659070 210 lsmISHGQ--RQRAVHDFPkysikvLPWLSPEVLQQNLqgYDAKSDIYSVGITACELAN-GHVPFkdmPATQ 278
Cdd:cd14204   170 ---IYSGDyyRQGRIAKMP------VKWIAVESLADRV--YTVKSDVWAFGVTMWEIATrGMTPY---PGVQ 227
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
61-273 2.81e-05

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK7 (also called iodopsin kinase) belongs to the visual group of GRKs. It is primarily found in the retina and plays a role in the regulation of opsin light receptors. GRK7 is located in retinal cone outer segments and plays an important role in regulating photoresponse of the cones. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270758 [Multi-domain]  Cd Length: 286  Bit Score: 45.67  E-value: 2.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELlSVIGKG-FEDLMTVNLaryKPTGEYVTVRRIN---LEACSNEMVTFLQGElhVSKLFSHPNIVPYRATFIADNELW 136
Cdd:cd05607     5 YEF-RVLGKGgFGEVCAVQV---KNTGQMYACKKLDkkrLKKKSGEKMALLEKE--ILEKVNSPFIVSLAYAFETKTHLC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 137 AVTSFMAYGSAKDLI---GTHFMDgMSELAI--AYILQGVLkaldYIHHMGYVHRSVKASHILISTDGKVYLSGLRSNLS 211
Cdd:cd05607    79 LVMSLMNGGDLKYHIynvGERGIE-MERVIFysAQITCGIL----HLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVE 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958659070 212 MiSHGQ--RQRAVHDfpkysikvlPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKD 273
Cdd:cd05607   154 V-KEGKpiTQRAGTN---------GYMAPEILKE--ESYSYPVDWFAMGCSIYEMVAGRTPFRD 205
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
61-271 3.39e-05

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


Pssm-ID: 270853 [Multi-domain]  Cd Length: 288  Bit Score: 45.39  E-value: 3.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQgELHVSKLFSHPNIVPYRATFIADNELWAVTS 140
Cdd:cd07871     7 YVKLDKLGEG--TYATVFKGRSKLTENLVALKEIRLEHEEGAPCTAIR-EVSLLKNLKHANIVTLHDIIHTERCLTLVFE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 141 FMAygsaKDLigTHFMDG----MSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLrsnlsmis 214
Cdd:cd07871    84 YLD----SDL--KQYLDNcgnlMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLAdfGL-------- 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958659070 215 hgQRQRAVHDfPKYSIKV--LPWLSPEVLQQNLQgYDAKSDIYSVGITACELANGHVPF 271
Cdd:cd07871   150 --ARAKSVPT-KTYSNEVvtLWYRPPDVLLGSTE-YSTPIDMWGVGCILYEMATGRPMF 204
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
66-284 3.78e-05

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


Pssm-ID: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 45.03  E-value: 3.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  66 VIGKGfeDLMTVNLARYKPTGEYVT--VRRINLEACSNEMVTFlQGELHV-SKLFSHPNIVPYRATFIADNELWAVTSFM 142
Cdd:cd05047     2 VIGEG--NFGQVLKARIKKDGLRMDaaIKRMKEYASKDDHRDF-AGELEVlCKLGHHPNIINLLGACEHRGYLYLAIEYA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 143 AYGSAKDLI-GTHFMDGMSELAIAY----------ILQ---GVLKALDYIHHMGYVHRSVKASHILISTD--GKVYLSGL 206
Cdd:cd05047    79 PHGNLLDFLrKSRVLETDPAFAIANstastlssqqLLHfaaDVARGMDYLSQKQFIHRDLAARNILVGENyvAKIADFGL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 207 rsnlsmiSHGQRQravhdFPKYSIKVLP--WLSPEVLqqNLQGYDAKSDIYSVGITACELAN-GHVPFKDMPATQmLLEK 283
Cdd:cd05047   159 -------SRGQEV-----YVKKTMGRLPvrWMAIESL--NYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAE-LYEK 223

                  .
gi 1958659070 284 L 284
Cdd:cd05047   224 L 224
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
164-280 4.77e-05

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


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 44.94  E-value: 4.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 164 IAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSNLSMISHGQRQRAVHDFPkysikvLPWLSPEVL 241
Cdd:cd05115   106 VVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISdfGLSKALGADDSYYKARSAGKWP------LKWYAPECI 179
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1958659070 242 qqNLQGYDAKSDIYSVGITACE-LANGHVPFKDMPATQML 280
Cdd:cd05115   180 --NFRKFSSRSDVWSYGVTMWEaFSYGQKPYKKMKGPEVM 217
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
69-284 4.91e-05

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


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 44.98  E-value: 4.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  69 KGFEDLMTVNLARYKPTGE--YVTVRRINLEACSNEMVTFLQgELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGS 146
Cdd:cd05095    27 EGMEKFMDKDFALEVSENQpvLVAVKMLRADANKNARNDFLK-EIKIMSRLKDPNIIRLLAVCITDDPLCMITEYMENGD 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 147 AKDLIGTHFMDGMSELA----------IAYILQGVLKALDYIHHMGYVHRSVKASHILIstdGKVYLSGLrSNLSMishg 216
Cdd:cd05095   106 LNQFLSRQQPEGQLALPsnaltvsysdLRFMAAQIASGMKYLSSLNFVHRDLATRNCLV---GKNYTIKI-ADFGM---- 177
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958659070 217 qrQRAVHDFPKYSIK---VLP--WLSPEVLQqnLQGYDAKSDIYSVGITACELANghvpF-KDMPATQMLLEKL 284
Cdd:cd05095   178 --SRNLYSGDYYRIQgraVLPirWMSWESIL--LGKFTTASDVWAFGVTLWETLT----FcREQPYSQLSDEQV 243
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
61-221 4.91e-05

Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group is composed of fungal NDR-like proteins including Saccharomyces cerevisiae CBK1 (or CBK1p), Schizosaccharomyces pombe Orb6 (or Orb6p), Ustilago maydis Ukc1 (or Ukc1p), and Neurospora crassa Cot1. Like NDR kinase, group members contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. CBK1 is an essential component in the RAM (regulation of Ace2p activity and cellular morphogenesis) network. CBK1 and Orb6 play similar roles in coordinating cell morphology with cell cycle progression. Ukc1 is involved in morphogenesis, pathogenicity, and pigment formation. Cot1 plays a role in polar tip extension.The fungal NDR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270778 [Multi-domain]  Cd Length: 377  Bit Score: 45.23  E-value: 4.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKG-FEDlmtVNLARYKPTGE-YVTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAV 138
Cdd:cd05629     3 FHTVKVIGKGaFGE---VRLVQKKDTGKiYAMKTLLKSEMFKKDQLAHVKAERDVLAESDSPWVVSLYYSFQDAQYLYLI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 139 TSFMAYGsakDLIgTHFM--DGMSE-LAIAYILQGVLkALDYIHHMGYVHRSVKASHILISTDGKVYLSGLrsNLSMISH 215
Cdd:cd05629    80 MEFLPGG---DLM-TMLIkyDTFSEdVTRFYMAECVL-AIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDF--GLSTGFH 152

                  ....*.
gi 1958659070 216 GQRQRA 221
Cdd:cd05629   153 KQHDSA 158
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
116-281 6.21e-05

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


Pssm-ID: 270633 [Multi-domain]  Cd Length: 259  Bit Score: 44.39  E-value: 6.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 116 LFSHPNIVP-YRATFIADNELwaVTSFMAYGS-------AKDLIGTH-FMDGMSELAiayilqgvlKALDYIHHMGYVHR 186
Cdd:cd05037    58 QISHKHLVKlYGVCVADENIM--VQEYVRYGPldkylrrMGNNVPLSwKLQVAKQLA---------SALHYLEDKKLIHG 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 187 SVKASHILISTDGkvylsgLRSNLSMISHGQrqravhdfPKYSIKVL---------PWLSPEVLQQNLQGYDAKSDIYSV 257
Cdd:cd05037   127 NVRGRNILLAREG------LDGYPPFIKLSD--------PGVPITVLsreervdriPWIAPECLRNLQANLTIAADKWSF 192
                         170       180
                  ....*....|....*....|....*
gi 1958659070 258 GITACEL-ANGHVPFKDMPATQMLL 281
Cdd:cd05037   193 GTTLWEIcSGGEEPLSALSSQEKLQ 217
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
119-275 6.87e-05

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


Pssm-ID: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 44.24  E-value: 6.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 119 HPNIVpyraTFIA--------DNELWAVTSFMAYGSAKDLIGTHFMDGMSELAIAyilQGVLKALDYIH------HMGY- 183
Cdd:cd14053    48 HENIL----QFIGaekhgeslEAEYWLITEFHERGSLCDYLKGNVISWNELCKIA---ESMARGLAYLHedipatNGGHk 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 184 ---VHRSVKASHILISTDGKVYLSGLrsNLSMI-SHGQRQRAVHDfpkySIKVLPWLSPEVLQQNLQ-GYDA--KSDIYS 256
Cdd:cd14053   121 psiAHRDFKSKNVLLKSDLTACIADF--GLALKfEPGKSCGDTHG----QVGTRRYMAPEVLEGAINfTRDAflRIDMYA 194
                         170       180
                  ....*....|....*....|....*
gi 1958659070 257 VG------ITACELANGHVPFKDMP 275
Cdd:cd14053   195 MGlvlwelLSRCSVHDGPVDEYQLP 219
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
89-271 8.45e-05

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


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 44.25  E-value: 8.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  89 VTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNelWAVTSFMAYGSA--KDLigtHFMDGMSEL-AIA 165
Cdd:cd14149    37 VAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGYMTKDN--LAIVTQWCEGSSlyKHL---HVQETKFQMfQLI 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 166 YILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLsglrSNLSMISHGQRQRAVHDFPKYSIKVLpWLSPEVLQ-QN 244
Cdd:cd14149   112 DIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKI----GDFGLATVKSRWSGSQQVEQPTGSIL-WMAPEVIRmQD 186
                         170       180
                  ....*....|....*....|....*..
gi 1958659070 245 LQGYDAKSDIYSVGITACELANGHVPF 271
Cdd:cd14149   187 NNPFSFQSDVYSYGIVLYELMTGELPY 213
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
66-272 9.52e-05

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-eta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 44.13  E-value: 9.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  66 VIGKG-FEDLMtvnLARYKPTGEYVTVRRINLEAC-SNEMVTFLQGELHVSKL-FSHPNIVPYRATFIADNELWAVTSFM 142
Cdd:cd05590     2 VLGKGsFGKVM---LARLKESGRLYAVKVLKKDVIlQDDDVECTMTEKRILSLaRNHPFLTQLYCCFQTPDRLFFVMEFV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 143 AYGsakDLIgTHFMDG--MSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLRSNLSMISHGQRQR 220
Cdd:cd05590    79 NGG---DLM-FHIQKSrrFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGIFNGKTTS 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958659070 221 AVHDFPKYsikvlpwLSPEVLQQNLQGYDAksDIYSVGITACELANGHVPFK 272
Cdd:cd05590   155 TFCGTPDY-------IAPEILQEMLYGPSV--DWWAMGVLLYEMLCGHAPFE 197
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
63-274 9.80e-05

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


Pssm-ID: 271044 [Multi-domain]  Cd Length: 298  Bit Score: 43.97  E-value: 9.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  63 LLSVIGKGfedlmtvnlaRYKPT------GEYVTVRRINleaCSNEMVTFLQGELHVSKLFSHPNIVPYRATFIA----D 132
Cdd:cd14142     9 LVECIGKG----------RYGEVwrgqwqGESVAVKIFS---SRDEKSWFRETEIYNTVLLRHENILGFIASDMTsrnsC 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 133 NELWAVTSFMAYGSAKDLIGTHFMDGMSELAIAyilqgvLKALDYIHHM-----------GYVHRSVKASHILISTDGKV 201
Cdd:cd14142    76 TQLWLITHYHENGSLYDYLQRTTLDHQEMLRLA------LSAASGLVHLhteifgtqgkpAIAHRDLKSKNILVKSNGQC 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 202 YLSGLrsNLS-MISHGQRQRAVHDFPKYSIKvlPWLSPEVLQQ--NLQGYDA--KSDIYSVGITACELA-----NGHV-- 269
Cdd:cd14142   150 CIADL--GLAvTHSQETNQLDVGNNPRVGTK--RYMAPEVLDEtiNTDCFESykRVDIYAFGLVLWEVArrcvsGGIVee 225

                  ....*...
gi 1958659070 270 ---PFKDM 274
Cdd:cd14142   226 ykpPFYDV 233
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
89-275 1.14e-04

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


Pssm-ID: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 43.80  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  89 VTVRRINLEACSNEMVTFLQgELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGSAKDLI----------------- 151
Cdd:cd05045    33 VAVKMLKENASSSELRDLLS-EFNLLKQVNHPHVIKLYGACSQDGPLLLIVEYAKYGSLRSFLresrkvgpsylgsdgnr 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 152 --GTHFMDGMSELAIAYILQ---GVLKALDYIHHMGYVHRSVKASHILIStDGKVylsglrsnlSMISHGQRQRAVHD-- 224
Cdd:cd05045   112 nsSYLDNPDERALTMGDLISfawQISRGMQYLAEMKLVHRDLAARNVLVA-EGRK---------MKISDFGLSRDVYEed 181
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958659070 225 -FPKYSIKVLP--WLSPEVLQQNLqgYDAKSDIYSVGITACELAN-GHVPFKDMP 275
Cdd:cd05045   182 sYVKRSKGRIPvkWMAIESLFDHI--YTTQSDVWSFGVLLWEIVTlGGNPYPGIA 234
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
66-287 1.34e-04

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


Pssm-ID: 270631 [Multi-domain]  Cd Length: 273  Bit Score: 43.29  E-value: 1.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  66 VIGKG-FEDLMTVNLARYKPTGEYVTVRRINLEACS-NEMVTFLQgELHVSKLFSHPNIVPYRATFIADNEL------WA 137
Cdd:cd05035     6 ILGEGeFGSVMEAQLKQDDGSQLKVAVKTMKVDIHTySEIEEFLS-EAACMKDFDHPNVMRLIGVCFTASDLnkppspMV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 138 VTSFMAYGsakDLIGTHFMDGMSELAIAYILQGVLK-------ALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRS 208
Cdd:cd05035    85 ILPFMKHG---DLHSYLLYSRLGGLPEKLPLQTLLKfmvdiakGMEYLSNRNFIHRDLAARNCMLDENMTVCVAdfGLSR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 209 NlsmISHGQRQRAVHdFPKYSIKvlpWLSPEVLQQNLqgYDAKSDIYSVGITACELAN-GHVPFKDMPATQMLLEKLNGT 287
Cdd:cd05035   162 K---IYSGDYYRQGR-ISKMPVK---WIALESLADNV--YTSKSDVWSFGVTMWEIATrGQTPYPGVENHEIYDYLRNGN 232
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
119-368 1.38e-04

Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1b (also called Wee2), Xenopus laevis Wee1a (XeWee1a) and similar vertebrate proteins. XeWee1a accumulates after exiting the metaphase II stage in oocytes and in early mitotic cells. It functions during the first zygotic cell division and not during subsequent divisions. Mammalian Wee2/Wee1b is an oocyte-specific inhibitor of meiosis that functions downstream of cAMP. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1b subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271041 [Multi-domain]  Cd Length: 274  Bit Score: 43.38  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 119 HPNIVPYRATFIADNELWAVTSFMAYGSAKDLI------GTHFmdgmSELAIAYILQGVLKALDYIHHMGYVHRSVKASH 192
Cdd:cd14139    59 HPHVVRYYSAWAEDDHMIIQNEYCNGGSLQDAIsentksGNHF----EEPELKDILLQVSMGLKYIHNSGLVHLDIKPSN 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 193 ILISTdgKVYLSGlrsnlsmiSHGQRQRAVHDfpkysikvlpWLSPEVLqqnlqgydaksdIYSVGitacELanGHVPFK 272
Cdd:cd14139   135 IFICH--KMQSSS--------GVGEEVSNEED----------EFLSANV------------VYKIG----DL--GHVTSI 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 273 DMPATQmlleklNGTVPCLldTSTIPAEELTMSPSRSIANPGLNDSLAAG-SLRPANGDSPSH-------PYHRTFSPHF 344
Cdd:cd14139   177 NKPQVE------EGDSRFL--ANEILQEDYRHLPKADIFALGLTVALAAGaEPLPTNGAAWHHirkgnfpDVPQELPESF 248
                         250       260
                  ....*....|....*....|....
gi 1958659070 345 HNFVEQCLQRNPDARPNASTLLNH 368
Cdd:cd14139   249 SSLLKNMIQPDPEQRPSATALARH 272
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
61-271 1.48e-04

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-2 is specifically expressed in neurons in the central nervous system, mainly in terminally differentiated neurons. It associates with Trap (Tudor repeat associator with PCTAIRE-2) and could play a role in regulating mitochondrial function in neurons. PCTAIRE-2 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 43.44  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQgELHVSKLFSHPNIVPYRATFIADNELWAVTS 140
Cdd:cd07872     8 YIKLEKLGEG--TYATVFKGRSKLTENLVALKEIRLEHEEGAPCTAIR-EVSLLKDLKHANIVTLHDIVHTDKSLTLVFE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 141 FMAygsaKDLigTHFMDG----MSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLrsnlsmis 214
Cdd:cd07872    85 YLD----KDL--KQYMDDcgniMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLAdfGL-------- 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958659070 215 hgQRQRAVHDfPKYSIKVLP-WLSPEVLQQNLQGYDAKSDIYSVGITACELANGHVPF 271
Cdd:cd07872   151 --ARAKSVPT-KTYSNEVVTlWYRPPDVLLGSSEYSTQIDMWGVGCIFFEMASGRPLF 205
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
155-272 1.58e-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: 43.29  E-value: 1.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 155 FMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTdgkvylsgLRS-NLSMISHGQRQRAVHDFPKYSIKVL 233
Cdd:cd14112    92 SNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQS--------VRSwQVKLVDFGRAQKVSKLGKVPVDGDT 163
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1958659070 234 PWLSPEVLQQNLQGYdAKSDIYSVGITACELANGHVPFK 272
Cdd:cd14112   164 DWASPEFHNPETPIT-VQSDIWGLGVLTFCLLSGFHPFT 201
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
110-373 1.66e-04

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


Pssm-ID: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 43.14  E-value: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 110 ELHVSKLFSHPNIVPY----RATFIADNELWAVTSFMAYGSAKDLIGTHFMdgMSELAIAYILQGVLKALDYIHHMG--Y 183
Cdd:cd14032    50 EAEMLKGLQHPNIVRFydfwESCAKGKRCIVLVTELMTSGTLKTYLKRFKV--MKPKVLRSWCRQILKGLLFLHTRTppI 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 184 VHRSVKASHILIS-TDGKVYLSGLrsNLSMISHGQRQRAVHDFPKYsikvlpwLSPEVLQQNlqgYDAKSDIYSVGITAC 262
Cdd:cd14032   128 IHRDLKCDNIFITgPTGSVKIGDL--GLATLKRASFAKSVIGTPEF-------MAPEMYEEH---YDESVDVYAFGMCML 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 263 ELANGHVPFKDMPATQMLLEKlngtVPClldtstipaeeltmspsrsianpglndslaagSLRPANgdspshpYHRTFSP 342
Cdd:cd14032   196 EMATSEYPYSECQNAAQIYRK----VTC--------------------------------GIKPAS-------FEKVTDP 232
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958659070 343 HFHNFVEQCLQRNPDARPNASTLLNHSFFKQ 373
Cdd:cd14032   233 EIKEIIGECICKNKEERYEIKDLLSHAFFAE 263
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
66-279 1.78e-04

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK2 shows a more restricted distribution than SGK1 and is most abundantly expressed in epithelial tissues including kidney, liver, pancreas, and the choroid plexus of the brain. In vitro cellular assays show that SGK2 can stimulate the activity of ion channels, the glutamate transporter EEAT4, and the glutamate receptors, GluR6 and GLUR1. The SGK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270754 [Multi-domain]  Cd Length: 321  Bit Score: 43.42  E-value: 1.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  66 VIGKGfeDLMTVNLARYKPTGEYVTVRRINLEAC-SNEMVTFLQGELHVS-KLFSHPNIVPYRATFIADNELWAVTSFMA 143
Cdd:cd05603     2 VIGKG--SFGKVLLAKRKCDGKFYAVKVLQKKTIlKKKEQNHIMAERNVLlKNLKHPFLVGLHYSFQTSEKLYFVLDYVN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 144 YGSakdlIGTHFMDG--MSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSglrsNLSMISHG-QRQR 220
Cdd:cd05603    80 GGE----LFFHLQRErcFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLT----DFGLCKEGmEPEE 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958659070 221 AVHDF---PKYsikvlpwLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQM 279
Cdd:cd05603   152 TTSTFcgtPEY-------LAPEVLRK--EPYDRTVDWWCLGAVLYEMLYGLPPFYSRDVSQM 204
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
61-272 2.09e-04

Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2, which also localizes the kinase to spindle microtubules. Aurora-A is overexpressed in many cancer types such as prostate, ovarian, breast, bladder, gastric, and pancreatic. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 42.64  E-value: 2.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGfeDLMTVNLARYKPTGEYVTVR---RINLEACSNEMVtfLQGELHVSKLFSHPNIVPYRATFIADNELWA 137
Cdd:cd14116     7 FEIGRPLGKG--KFGNVYLAREKQSKFILALKvlfKAQLEKAGVEHQ--LRREVEIQSHLRHPNILRLYGYFHDATRVYL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 138 VTSFMAYGSA-KDLIG-THFMDGMSELaiaYILQgVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLrsNLSMISH 215
Cdd:cd14116    83 ILEYAPLGTVyRELQKlSKFDEQRTAT---YITE-LANALSYCHSKRVIHRDIKPENLLLGSAGELKIADF--GWSVHAP 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958659070 216 GQRQRAVhdfpkysIKVLPWLSPEVLQQNLqgYDAKSDIYSVGITACELANGHVPFK 272
Cdd:cd14116   157 SSRRTTL-------CGTLDYLPPEMIEGRM--HDEKVDLWSLGVLCYEFLVGKPPFE 204
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
110-271 3.30e-04

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 42.21  E-value: 3.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 110 ELHVSKLFSHPNIVPYRATFIADNELWAVTSFMaygSAKDLI-GTHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSV 188
Cdd:cd14110    49 EYQVLRRLSHPRIAQLHSAYLSPRHLVLIEELC---SGPELLyNLAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDL 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 189 KASHILISTDGKVYLSGLRSNLSMishGQRQRAVHDFPKYSikVLPwLSPEVLQQnlQGYDAKSDIYSVGITACELANGH 268
Cdd:cd14110   126 RSENMIITEKNLLKIVDLGNAQPF---NQGKVLMTDKKGDY--VET-MAPELLEG--QGAGPQTDIWAIGVTAFIMLSAD 197

                  ...
gi 1958659070 269 VPF 271
Cdd:cd14110   198 YPV 200
STKc_VRK cd14015
Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase; STKs ...
171-203 3.36e-04

Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. VRKs were initially discovered due to its similarity to vaccinia virus B1R STK, which is important for viral replication. They play important roles in cell signaling, nuclear envelope dynamics, apoptosis, and stress responses. Vertebrates contain three VRK proteins (VRK1, VRK2, and VRK3) while invertebrates, specifically fruit flies and nematodes, seem to carry only a single ortholog. Mutations of VRK in Drosophila and Caenorhabditis elegans showed varying phenotypes ranging from embryonic lethality to mitotic and meiotic defects resulting in sterility. In vertebrates, VRK1 is implicated in cell cycle progression and proliferation, nuclear envelope assembly, and chromatin condensation. VRK2 is involved in modulating JNK signaling. VRK3 is an inactive pseudokinase that inhibits ERK signaling. The VRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270917 [Multi-domain]  Cd Length: 300  Bit Score: 42.27  E-value: 3.36e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1958659070 171 VLKALDYIHHMGYVHRSVKASHILIS---TDGKVYL 203
Cdd:cd14015   136 ILDVLEYIHENGYVHADIKASNLLLGfgkNKDQVYL 171
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
119-368 3.87e-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: 41.87  E-value: 3.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 119 HPNIVPYRATFIADNELWAVTSFMAYGSAKDLIGTHfmDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTD 198
Cdd:cd14115    48 HPQYITLHDTYESPTSYILVLELMDDGRLLDYLMNH--DELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLR 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 199 ---GKVYLSGLRSNLSMISHgqrqRAVHDF---PKYSikvlpwlSPEVLQQNlqGYDAKSDIYSVGITACELANGHVPFK 272
Cdd:cd14115   126 ipvPRVKLIDLEDAVQISGH----RHVHHLlgnPEFA-------APEVIQGT--PVSLATDIWSIGVLTYVMLSGVSPFL 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 273 DMPATQMLLEKlngtvpCLLDTStIPAEeltmspsrsianpglndslaagslrpangdspshpYHRTFSPHFHNFVEQCL 352
Cdd:cd14115   193 DESKEETCINV------CRVDFS-FPDE-----------------------------------YFGDVSQAARDFINVIL 230
                         250
                  ....*....|....*.
gi 1958659070 353 QRNPDARPNASTLLNH 368
Cdd:cd14115   231 QEDPRRRPTAATCLQH 246
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
164-272 4.22e-04

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK2 is expressed in every cell and tissue type. It is specifically translocated to the mitochondria during dopaminergic cell death. Specific substrates include the microtubule-associated proteins DCX and Tau, as well as TIF-IA which is involved in ribosomal RNA synthesis regulation. Mice deficient in Jnk2 show protection against arthritis, type 1 diabetes, atherosclerosis, abdominal aortic aneurysm, cardiac cell death, TNF-induced liver damage, and tumor growth, indicating that JNK2 may play roles in the pathogenesis of these diseases. Initially it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 42.32  E-value: 4.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 164 IAYILQGVLKALDYIHHMGYVHRSVKASHILISTDgkvylsglrSNLSMISHGQRQRAVHDFPKYSIKVLPWL-SPEVLQ 242
Cdd:cd07876   125 MSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSD---------CTLKILDFGLARTACTNFMMTPYVVTRYYrAPEVIL 195
                          90       100       110
                  ....*....|....*....|....*....|
gi 1958659070 243 QnlQGYDAKSDIYSVGITACELANGHVPFK 272
Cdd:cd07876   196 G--MGYKENVDIWSVGCIMGELVKGSVIFQ 223
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
61-271 4.97e-04

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKN has a C-terminal catalytic domain that is highly homologous to PKCs. Its unique N-terminal regulatory region contains antiparallel coiled-coil (ACC) domains. In mammals, there are three PKN isoforms from different genes (designated PKN-alpha, beta, and gamma), which show different enzymatic properties, tissue distribution, and varied functions. PKN can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytokeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. The PKN subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 41.90  E-value: 4.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKG-FEDLMtvnLARYKPTGEYVTVRRINL-EACSNEMVTFLQGE---LHVSKLFSHPNIVPYRATFIADNEL 135
Cdd:cd05589     1 FRCIAVLGRGhFGKVL---LAEYKPTGELFAIKALKKgDIIARDEVESLMCEkriFETVNSARHPFLVNLFACFQTPEHV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 136 WAVTSFMAYGsakDLIGTHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GL-RSNlsm 212
Cdd:cd05589    78 CFVMEYAAGG---DLMMHIHEDVFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIAdfGLcKEG--- 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958659070 213 ISHGQRQRAVHDFPKYsikvlpwLSPEVLQQNlqGYDAKSDIYSVGITACELANGHVPF 271
Cdd:cd05589   152 MGFGDRTSTFCGTPEF-------LAPEVLTDT--SYTRAVDWWGLGVLIYEMLVGESPF 201
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
86-272 5.39e-04

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: 41.55  E-value: 5.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  86 GEYVTVRRINLEACSNEMVTF--LQGELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGS-AKDLIGTHFmdgMSEL 162
Cdd:cd14147    26 GELVAVKAARQDPDEDISVTAesVRQEARLFAMLAHPNIIALKAVCLEEPNLCLVMEYAAGGPlSRALAGRRV---PPHV 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 163 AIAYILQgVLKALDYIHHMGYV---HRSVKASHILISTDGKvylSGLRSNLSM-ISHGQRQRAVHDFPKYSIK-VLPWLS 237
Cdd:cd14147   103 LVNWAVQ-IARGMHYLHCEALVpviHRDLKSNNILLLQPIE---NDDMEHKTLkITDFGLAREWHKTTQMSAAgTYAWMA 178
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1958659070 238 PEVLQQNLqgYDAKSDIYSVGITACELANGHVPFK 272
Cdd:cd14147   179 PEVIKAST--FSKGSDVWSFGVLLWELLTGEVPYR 211
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
107-271 5.49e-04

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. MLCK4 (or MYLK4 or SgK085) contains a single kinase domain near the C-terminus. The MLCK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 41.44  E-value: 5.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 107 LQGELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGSAKD-LIGTHFmdGMSELAIAYILQGVLKALDYIHHMGYVH 185
Cdd:cd14193    48 VKNEIEVMNQLNHANLIQLYDAFESRNDIVLVMEYVDGGELFDrIIDENY--NLTELDTILFIKQICEGIQYMHQMYILH 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 186 RSVKASHIL-ISTDGKvylsglrsNLSMISHGQRQRAVhdfPKYSIKVlPWLSPEVLQQNLQGYDAKS---DIYSVGITA 261
Cdd:cd14193   126 LDLKPENILcVSREAN--------QVKIIDFGLARRYK---PREKLRV-NFGTPEFLAPEVVNYEFVSfptDMWSLGVIA 193
                         170
                  ....*....|
gi 1958659070 262 CELANGHVPF 271
Cdd:cd14193   194 YMLLSGLSPF 203
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
110-271 5.72e-04

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


Pssm-ID: 271023 [Multi-domain]  Cd Length: 252  Bit Score: 41.50  E-value: 5.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 110 ELHVSKLFSHPNIVPYRATFIADNELWAVtsfMAYGSAKDLIGT-HFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSV 188
Cdd:cd14121    45 EIELLKKLKHPHIVELKDFQWDEEHIYLI---MEYCSGGDLSRFiRSRRTLPESTVRRFLQQLASALQFLREHNISHMDL 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 189 KASHILISTDGKVYLS----GLRSNLSmisHGQRQRAVHDFPKYsikvlpwLSPEVLQQnlQGYDAKSDIYSVGITACEL 264
Cdd:cd14121   122 KPQNLLLSSRYNPVLKladfGFAQHLK---PNDEAHSLRGSPLY-------MAPEMILK--KKYDARVDLWSVGVILYEC 189

                  ....*..
gi 1958659070 265 ANGHVPF 271
Cdd:cd14121   190 LFGRAPF 196
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
77-200 5.94e-04

Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIK, also called mitogen activated protein kinase kinase kinase 14 (MAP3K14), phosphorylates and activates Inhibitor of NF-KappaB Kinase (IKK) alpha, which is a regulator of NF-kB proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. NIK is essential in the IKKalpha-mediated non-canonical NF-kB signaling pathway, in which IKKalpha processes the IkB-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus where it regulates gene transcription. NIK also plays an important role in Toll-like receptor 7/9 signaling cascades. The NIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 41.34  E-value: 5.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  77 VNLARYKPTGEYVTVRRINLEACSNEmvtflqgELHVSKLFSHPNIVPYratFIADNELWAVTSFM---AYGSAKDLIGT 153
Cdd:cd13991    22 VHRMEDKQTGFQCAVKKVRLEVFRAE-------ELMACAGLTSPRVVPL---YGAVREGPWVNIFMdlkEGGSLGQLIKE 91
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958659070 154 hfMDGMSE-LAIAYILQgVLKALDYIHHMGYVHRSVKASHILISTDGK 200
Cdd:cd13991    92 --QGCLPEdRALHYLGQ-ALEGLEYLHSRKILHGDVKADNVLLSSDGS 136
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
110-267 6.08e-04

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: 41.41  E-value: 6.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 110 ELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGSAKDLIGTHFMDG-MSELAIAYILQGVLKALDYIHHM---GYVH 185
Cdd:cd14160    42 ELEVLLLFQHPNILELAAYFTETEKFCLVYPYMQNGTLFDRLQCHGVTKpLSWHERINILIGIAKAIHYLHNSqpcTVIC 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 186 RSVKASHILISTDGKVYLSGLrSNLSMISHGQRQRAVHDFPKYSIKVLPWLSPEVLQQNlqGYDAKSDIYSVGITACELA 265
Cdd:cd14160   122 GNISSANILLDDQMQPKLTDF-ALAHFRPHLEDQSCTINMTTALHKHLWYMPEEYIRQG--KLSVKTDVYSFGIVIMEVL 198

                  ..
gi 1958659070 266 NG 267
Cdd:cd14160   199 TG 200
PHA02988 PHA02988
hypothetical protein; Provisional
174-286 6.08e-04

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 41.27  E-value: 6.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 174 ALDYIHHMGYVHRSVKASHILISTDgkVYLSGLRSNLSMISHGqRQRAVHDFPKYSIKVLPWLSPEVLQQNLQGYDAKSD 253
Cdd:PHA02988  128 AIDCCKGLYNLYKYTNKPYKNLTSV--SFLVTENYKLKIICHG-LEKILSSPPFKNVNFMVYFSYKMLNDIFSEYTIKDD 204
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958659070 254 IYSVGITACELANGHVPFKDMPATQ---MLLEKLNG 286
Cdd:PHA02988  205 IYSLGVVLWEIFTGKIPFENLTTKEiydLIINKNNS 240
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
107-271 6.75e-04

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK1 (or MYLK1) phosphorylates myosin regulatory light chain and controls the contraction of smooth muscles. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module which results in the expression of telokin in phasic smooth muscles, leading to Ca2+ desensitization by cyclic nucleotides of smooth muscle force. MLCK1 is also responsible for myosin regulatory light chain phosphorylation in nonmuscle cells and may play a role in regulating myosin II ATPase activity. The MLCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271093 [Multi-domain]  Cd Length: 259  Bit Score: 41.14  E-value: 6.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 107 LQGELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGSAKDLIGTHFMDGMSELAIAYILQgVLKALDYIHHMGYVHR 186
Cdd:cd14191    46 IRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEMVSGGELFERIIDEDFELTERECIKYMRQ-ISEGVEYIHKQGIVHL 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 187 SVKASHILIstdgkVYLSGlrSNLSMISHGQRQRAVHdfpKYSIKVL----PWLSPEVLQQNLQGYDakSDIYSVGITAC 262
Cdd:cd14191   125 DLKPENIMC-----VNKTG--TKIKLIDFGLARRLEN---AGSLKVLfgtpEFVAPEVINYEPIGYA--TDMWSIGVICY 192

                  ....*....
gi 1958659070 263 ELANGHVPF 271
Cdd:cd14191   193 ILVSGLSPF 201
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
76-267 7.05e-04

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 41.28  E-value: 7.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  76 TVNLARYKPTGEYVTVRRINLEACSNEMVTFLQG------------ELHVSKLFSHPNIVPYRATFIADNELWAVTSFMA 143
Cdd:PTZ00024   24 KVEKAYDTLTGKIVAIKKVKIIEISNDVTKDRQLvgmcgihfttlrELKIMNEIKHENIMGLVDVYVEGDFINLVMDIMA 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 144 YGSAKdligthFMDGMSELAIAY---ILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRS---------N 209
Cdd:PTZ00024  104 SDLKK------VVDRKIRLTESQvkcILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIAdfGLARrygyppysdT 177
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 210 LSMISHGQRQRavhdfpKYSIKV--LPWLSPEVLqQNLQGYDAKSDIYSVGITACELANG 267
Cdd:PTZ00024  178 LSKDETMQRRE------EMTSKVvtLWYRAPELL-MGAEKYHFAVDMWSVGCIFAELLTG 230
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
110-276 8.43e-04

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


Pssm-ID: 270978 [Multi-domain]  Cd Length: 270  Bit Score: 40.93  E-value: 8.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 110 ELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGSAKDLIGTH--FMDGMSELAIAYILQGVlkalDYIHHMGYVHRS 187
Cdd:cd14076    56 EINILKGLTHPNIVRLLDVLKTKKYIGIVLEFVSGGELFDYILARrrLKDSVACRLFAQLISGV----AYLHKKGVVHRD 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 188 VKASHILISTDgkvylsglrSNLSMISHGQRQRAVHDFP---KYSIKVLPWLSPEVLQQNLQGYDAKSDIYSVGITACEL 264
Cdd:cd14076   132 LKLENLLLDKN---------RNLVITDFGFANTFDHFNGdlmSTSCGSPCYAAPELVVSDSMYAGRKADIWSCGVILYAM 202
                         170
                  ....*....|..
gi 1958659070 265 ANGHVPFKDMPA 276
Cdd:cd14076   203 LAGYLPFDDDPH 214
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
67-265 9.97e-04

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1a, also called Activin receptor-Like Kinase 3 (ALK3), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Germline mutations in BMPR1a are associated with an increased risk to Juvenile Polyposis Syndrome, a hamartomatous disorder that may lead to gastrointestinal cancer. BMPR1a may also play an indirect role in the development of hematopoietic stem cells (HSCs) as osteoblasts are a major component of the HSC niche within the bone marrow. BMPR1a belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1a, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271122 [Multi-domain]  Cd Length: 287  Bit Score: 40.79  E-value: 9.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  67 IGKGfeDLMTVNLARYKptGEYVTVRrinLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFI----ADNELWAVTSFM 142
Cdd:cd14220     3 IGKG--RYGEVWMGKWR--GEKVAVK---VFFTTEEASWFRETEIYQTVLMRHENILGFIAADIkgtgSWTQLYLITDYH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 143 AYGSAKDLIGTHFMDGMSELAIAYilqGVLKALDYIHHMGY--------VHRSVKASHILISTDGKVYLSGLRSNLSMIS 214
Cdd:cd14220    76 ENGSLYDFLKCTTLDTRALLKLAY---SAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGTCCIADLGLAVKFNS 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958659070 215 HGQRQravhDFP-KYSIKVLPWLSPEVLQQNL-----QGYdAKSDIYSVGITACELA 265
Cdd:cd14220   153 DTNEV----DVPlNTRVGTKRYMAPEVLDESLnknhfQAY-IMADIYSFGLIIWEMA 204
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
138-283 1.03e-03

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


Pssm-ID: 270684 [Multi-domain]  Cd Length: 279  Bit Score: 40.78  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 138 VTSFMAYG-------SAKDLIGTHFMdgmselaIAYILQgVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRS 208
Cdd:cd05109    86 VTQLMPYGclldyvrENKDRIGSQDL-------LNWCVQ-IAKGMSYLEEVRLVHRDLAARNVLVKSPNHVKITdfGLAR 157
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958659070 209 NLSMishgqRQRAVH-DFPKYSIKvlpWLSPEVLQQnlQGYDAKSDIYSVGITACELAN-GHVPFKDMPATQM--LLEK 283
Cdd:cd05109   158 LLDI-----DETEYHaDGGKVPIK---WMALESILH--RRFTHQSDVWSYGVTVWELMTfGAKPYDGIPAREIpdLLEK 226
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
83-286 1.04e-03

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: 40.67  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  83 KPTGEYVTVRRINLEACSNEMVTFLqgELHVSKLFSHPNIVPYRATFIADNElwaVTSFMAYGSAKDLIgTHFMDGMSEL 162
Cdd:cd14190    26 KRTGLKLAAKVINKQNSKDKEMVLL--EIQVMNQLNHRNLIQLYEAIETPNE---IVLFMEYVEGGELF-ERIVDEDYHL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 163 ----AIAYILQgVLKALDYIHHMGYVHRSVKASHIL-ISTDGKVylsglrsnLSMISHGQRQRAVhdfPKYSIKV---LP 234
Cdd:cd14190   100 tevdAMVFVRQ-ICEGIQFMHQMRVLHLDLKPENILcVNRTGHQ--------VKIIDFGLARRYN---PREKLKVnfgTP 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958659070 235 -WLSPEVLqqNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNG 286
Cdd:cd14190   168 eFLSPEVV--NYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETLNNVLMG 218
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
164-273 1.05e-03

Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 40.58  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 164 IAYILQgVLKALDYIHHMGYVHRSVKASHILISTDgkvylsglrSNLSMISHGQRQRavhdFPKYSIK-------VLPWL 236
Cdd:cd14111   102 VGYLVQ-ILQGLEYLHGRRVLHLDIKPDNIMVTNL---------NAIKIVDFGSAQS----FNPLSLRqlgrrtgTLEYM 167
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1958659070 237 SPEVLQQNLQGYDAksDIYSVGITACELANGHVPFKD 273
Cdd:cd14111   168 APEMVKGEPVGPPA--DIWSIGVLTYIMLSGRSPFED 202
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
89-280 1.15e-03

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


Pssm-ID: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 40.77  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  89 VTVRRINLEACSNEMVTFLQgELHVSKLF-SHPNIVPYRATFIADNELWAVTSFMAYGSAKDLIGTHFMDGM-------- 159
Cdd:cd05098    48 VAVKMLKSDATEKDLSDLIS-EMEMMKMIgKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPGMeycynpsh 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 160 ---SELAIAYILQ---GVLKALDYIHHMGYVHRSVKASHILISTDG--KVYLSGLRSNLSMISHgqrqravhdFPKYSIK 231
Cdd:cd05098   127 npeEQLSSKDLVScayQVARGMEYLASKKCIHRDLAARNVLVTEDNvmKIADFGLARDIHHIDY---------YKKTTNG 197
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958659070 232 VLP--WLSPEVLQQNLqgYDAKSDIYSVGITACELAN-GHVPFKDMPATQML 280
Cdd:cd05098   198 RLPvkWMAPEALFDRI--YTHQSDVWSFGVLLWEIFTlGGSPYPGVPVEELF 247
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
89-265 1.23e-03

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


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 40.40  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  89 VTVRRINLEACSNEMVTFLQgELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGSAKDLIGTH-----FMDGMSELA 163
Cdd:cd05032    39 VAIKTVNENASMRERIEFLN-EASVMKEFNCHHVVRLLGVVSTGQPTLVVMELMAKGDLKSYLRSRrpeaeNNPGLGPPT 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 164 IAYILQGVLKALD---YIHHMGYVHRSVKASHILISTDGKVYLS--GLrsnlsmishgQRQRAVHDFPKYSIK-VLP--W 235
Cdd:cd05032   118 LQKFIQMAAEIADgmaYLAAKKFVHRDLAARNCMVAEDLTVKIGdfGM----------TRDIYETDYYRKGGKgLLPvrW 187
                         170       180       190
                  ....*....|....*....|....*....|
gi 1958659070 236 LSPEVLQQNLqgYDAKSDIYSVGITACELA 265
Cdd:cd05032   188 MAPESLKDGV--FTTKSDVWSFGVVLWEMA 215
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
119-376 1.32e-03

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


Pssm-ID: 270945 [Multi-domain]  Cd Length: 267  Bit Score: 40.47  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 119 HPNIVPYRATFIADNELWAVTSFMAYGSAKDLIGTHFM--DGMSELAIayiLQGVLKALDYIHHMGYVHRSVKASHILIs 196
Cdd:cd14043    55 HENVNLFLGLFVDCGILAIVSEHCSRGSLEDLLRNDDMklDWMFKSSL---LLDLIKGMRYLHHRGIVHGRLKSRNCVV- 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 197 tDGKVYLSGLRSNLSMISHGQRQRAvhdfPKYSIKVLPWLSPEVLQQNLQGYDA--KSDIYSVGITACELANGHVPFkdm 274
Cdd:cd14043   131 -DGRFVLKITDYGYNEILEAQNLPL----PEPAPEELLWTAPELLRDPRLERRGtfPGDVFSFAIIMQEVIVRGAPY--- 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 275 patqmlleklngtvpCLLDtstIPAEEL---TMSPsrsianPGLndslaagsLRPA--NGDSPshpyhrtfsPHFHNFVE 349
Cdd:cd14043   203 ---------------CMLG---LSPEEIiekVRSP------PPL--------CRPSvsMDQAP---------LECIQLMK 241
                         250       260
                  ....*....|....*....|....*....
gi 1958659070 350 QCLQRNPDARPNastlLNHSF--FKQIKR 376
Cdd:cd14043   242 QCWSEAPERRPT----FDQIFdqFKSINK 266
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
134-283 1.81e-03

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


Pssm-ID: 173656 [Multi-domain]  Cd Length: 279  Bit Score: 39.94  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 134 ELWAVTSFMAYGSAKDLIGTHFMDGMSELAIAYILQgVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLrsNLSMI 213
Cdd:cd05111    82 SLQLVTQLLPLGSLLDHVRQHRGSLGPQLLLNWCVQ-IAKGMYYLEEHRMVHRNLAARNVLLKSPSQVQVADF--GVADL 158
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958659070 214 SHGQRQRAVHDFPKYSIKvlpWLSPEVLQqnLQGYDAKSDIYSVGITACELAN-GHVPFKDM--PATQMLLEK 283
Cdd:cd05111   159 LYPDDKKYFYSEAKTPIK---WMALESIH--FGKYTHQSDVWSYGVTVWEMMTfGAEPYAGMrlAEVPDLLEK 226
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
158-267 1.95e-03

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


Pssm-ID: 270922 [Multi-domain]  Cd Length: 285  Bit Score: 39.92  E-value: 1.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 158 GMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYlsglrsnlSMISHGQRQRAVHDFPKYsIKVLPWLS 237
Cdd:cd14020   106 GCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAEDECF--------KLIDFGLSFKEGNQDVKY-IQTDGYRA 176
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1958659070 238 PEVLQQN------LQ---GYDAKSDIYSVGITACELANG 267
Cdd:cd14020   177 PEAELQNclaqagLQsetECTSAVDLWSLGIVLLEMFSG 215
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
61-272 1.98e-03

Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs MPK1 from Saccharomyces cerevisiae, Pmk1 from Schizosaccharomyces pombe, and similar proteins. MPK1 (also called Slt2) and Pmk1 (also called Spm1) are stress-activated MAPKs that regulate the cell wall integrity pathway, and are therefore important in the maintainance of cell shape, cell wall construction, morphogenesis, and ion homeostasis. MPK1 is activated in response to cell wall stress including heat stimulation, osmotic shock, UV irradiation, and any agents that interfere with cell wall biogenesis such as chitin antagonists, caffeine, or zymolase. MPK1 is regulated by the MAP2Ks Mkk1/2, which are regulated by the MAP3K Bck1. Pmk1 is also activated by multiple stresses including elevated temperatures, hyper- or hypotonic stress, glucose deprivation, exposure to cell-wall damaging compounds, and oxidative stress. It is regulated by the MAP2K Pek1, which is regulated by the MAP3K Mkh1. MAPKs are important mediators of cellular responses to extracellular signals. The MPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173750 [Multi-domain]  Cd Length: 332  Bit Score: 40.08  E-value: 1.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGFEDLmtVNLARYKPT--GEYVTVRRINlEACSNEMVT--FLQgELHVSKLF-SHPNIVPYRATFIAD--- 132
Cdd:cd07857     2 YELIKELGQGAYGI--VCSARNAETseEETVAIKKIT-NVFSKKILAkrALR-ELKLLRHFrGHKNITCLYDMDIVFpgn 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 133 -NELWAVTSFMAYGSAKDLigtHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLS--GLRSN 209
Cdd:cd07857    78 fNELYLYEELMEADLHQII---RSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICdfGLARG 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958659070 210 LSmISHGQRQravhDFPKYSIKVLPWLSPEVLQQNlQGYDAKSDIYSVGITACELANGHVPFK 272
Cdd:cd07857   155 FS-ENPGENA----GFMTEYVATRWYRAPEIMLSF-QSYTKAIDVWSVGCILAELLGRKPVFK 211
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
117-286 2.47e-03

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


Pssm-ID: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 39.48  E-value: 2.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 117 FSHPNIVPYRATFIADNELWAVTSFMAYGSAKDLIGTHfMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILIS 196
Cdd:cd05113    56 LSHEKLVQLYGVCTKQRPIFIITEYMANGCLLNYLREM-RKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVN 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 197 TDGKVYLSGLRSNLSMISHGQRQRAVHDFPkysikvLPWLSPEVLQQNlqGYDAKSDIYSVGITACELAN-GHVPFKDMP 275
Cdd:cd05113   135 DQGVVKVSDFGLSRYVLDDEYTSSVGSKFP------VRWSPPEVLMYS--KFSSKSDVWAFGVLMWEVYSlGKMPYERFT 206
                         170
                  ....*....|.
gi 1958659070 276 ATQMLLEKLNG 286
Cdd:cd05113   207 NSETVEHVSQG 217
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
159-265 2.96e-03

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 39.88  E-value: 2.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 159 MSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLRSnlSMISHGQRQRAVHdfpkYSIK-VLPWLS 237
Cdd:PHA03211  257 LGLAQVTAVARQLLSAIDYIHGEGIIHRDIKTENVLVNGPEDICLGDFGA--ACFARGSWSTPFH----YGIAgTVDTNA 330
                          90       100
                  ....*....|....*....|....*...
gi 1958659070 238 PEVLQQNlqGYDAKSDIYSVGITACELA 265
Cdd:PHA03211  331 PEVLAGD--PYTPSVDIWSAGLVIFEAA 356
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
61-266 5.30e-03

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 38.65  E-value: 5.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  61 YELLSVIGKGFEDLmtVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTS 140
Cdd:PLN00009    4 YEKVEKIGEGTYGV--VYKARDRVTNETIALKKIRLEQEDEGVPSTAIREISLLKEMQHGNIVRLQDVVHSEKRLYLVFE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 141 FMaygsakDLIGTHFMDGMSELA-----IAYILQGVLKALDYIHHMGYVHRSVKASHILISTdgkvylsglRSNLSMISH 215
Cdd:PLN00009   82 YL------DLDLKKHMDSSPDFAknprlIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDR---------RTNALKLAD 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958659070 216 GQRQRA----VHDFpKYSIKVLPWLSPEVLQQNLQgYDAKSDIYSVGITACELAN 266
Cdd:PLN00009  147 FGLARAfgipVRTF-THEVVTLWYRAPEILLGSRH-YSTPVDIWSVGCIFAEMVN 199
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
63-271 5.83e-03

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. Although T-cells also express other PKC isoforms, PKC-theta is unique in that upon antigen stimulation, it is translocated to the plasma membrane at the immunological synapse, where it mediates signals essential for T-cell activation. It is essential for TCR-induced proliferation, cytokine production, T-cell survival, and the differentiation and effector function of T-helper (Th) cells, particularly Th2 and Th17. PKC-theta is being developed as a therapeutic target for Th2-mediated allergic inflammation and Th17-mediated autoimmune diseases. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 38.75  E-value: 5.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070  63 LLSVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEAC-SNEMVTFLQGELHVSKL-FSHPNIVPYRATFIADNELWAVts 140
Cdd:cd05619     9 LHKMLGKG--SFGKVFLAELKGTNQFFAIKALKKDVVlMDDDVECTMVEKRVLSLaWEHPFLTHLFCTFQTKENLFFV-- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 141 fMAYGSAKDLI----GTHFMD-GMSELAIAYILQGvlkaLDYIHHMGYVHRSVKASHILISTDGKVYLSGLRSNLSMISH 215
Cdd:cd05619    85 -MEYLNGGDLMfhiqSCHKFDlPRATFYAAEIICG----LQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKENMLG 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958659070 216 GQRQRAVHDFPKYsikvlpwLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPF 271
Cdd:cd05619   160 DAKTSTFCGTPDY-------IAPEILLG--QKYNTSVDWWSFGVLLYEMLIGQSPF 206
PK_MADML cd14035
Pseudokinase domain of MLF1-ADaptor Molecule-Like; The pseudokinase domain shows similarity to ...
116-368 7.02e-03

Pseudokinase domain of MLF1-ADaptor Molecule-Like; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. MADML has been shown to be expressed throughout development in Xenopus laevis with highest expression found in the developing lens and retina. It may play an important role in embryonic eye development. The MADML 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: 270937 [Multi-domain]  Cd Length: 263  Bit Score: 37.98  E-value: 7.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 116 LFSHPNIVPYRATFIADNELWA----VTSFMAYGSAKDLIGTHFMD--GMSELAIAYILQGVLKALDYIHHMG--YVHRS 187
Cdd:cd14035    51 LVDHPNIVKFHKYWLDVKDNHArvvfITEYVSSGSLKQFLKKTKKNhkTMNARAWKRWCTQILSALSYLHSCEppIIHGN 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 188 VKASHILISTDGKVYL--------------SGLRSNLSMisHGQRQRAVHDFPkysikvlpwlsPEVLQQNlqgYDAKSD 253
Cdd:cd14035   131 LTSDTIFIQHNGLIKIgsvwhrlfvnvlpeGGVRGPLRQ--EREELRNLHFFP-----------PEYGSCE---DGTAVD 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 254 IYSVGITACELAnghvpfkdmpatqmLLE-KLNGtvpclldtSTIPAEELTMSPSRSIANPGLNDslaagslrpangdsp 332
Cdd:cd14035   195 IFSFGMCALEMA--------------VLEiQANG--------DTRVSEEAIARARHSLEDPNMRE--------------- 237
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1958659070 333 shpyhrtfsphfhnFVEQCLQRNPDARPNASTLLNH 368
Cdd:cd14035   238 --------------FILSCLRHNPCKRPTAHDLLFH 259
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
172-203 7.60e-03

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. TTBK1 has been linked to Alzheimer's disease (AD) while TTBK2 is associated with spinocerebellar ataxia type 11 (SCA11). Both AD and SCA11 patients show the presence of neurofibrillary tangles in the brain. The Drosophila TTBK homolog, Asator, is an essential protein that localizes to the mitotic spindle during mitosis and may be involved in regulating microtubule dynamics and function. The TTBK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 38.01  E-value: 7.60e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1958659070 172 LKALDYIHHMGYVHRSVKASHILI----STDGKVYL 203
Cdd:cd14017   107 LKAIEDIHEVGFLHRDVKPSNFAIgrgpSDERTVYI 142
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
177-274 7.90e-03

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


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 37.71  E-value: 7.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659070 177 YIHHMGYVHRSVKASHILISTDGKVYLS--GLRSNLSMISHGQRQRAVHDFPkysikvLPWLSPEVLqqNLQGYDAKSDI 254
Cdd:cd05060   110 YLESKHFVHRDLAARNVLLVNRHQAKISdfGMSRALGAGSDYYRATTAGRWP------LKWYAPECI--NYGKFSSKSDV 181
                          90       100
                  ....*....|....*....|.
gi 1958659070 255 YSVGITACE-LANGHVPFKDM 274
Cdd:cd05060   182 WSYGVTLWEaFSYGAKPYGEM 202
 
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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