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Conserved domains on  [gi|1394533236|ref|NP_001350716|]
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STE20-related kinase adapter protein alpha isoform 8 [Homo sapiens]

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 ...
41-367 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: 693.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  41 ELLTVIGKGFEDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSF 120
Cdd:cd08227     1 ELLTVIGRGFEDLMTVNLARYKPTGEYVTVRRINLEACTNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 121 MAYGSAKDLICTHFMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMISHGQRQRV 200
Cdd:cd08227    81 MAYGSAKDLICTHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMINHGQRLRV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 201 VHDFPKYSVKVLPWLSPEVLQQNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPCLLDTSTIPAEE 280
Cdd:cd08227   161 VHDFPKYSVKVLPWLSPEVLQQNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPCLLDTTTIPAEE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 281 LTMSPSRSVANSGLSDSLTTSTPRPSNGDSPSHPYHRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQIKRRASEA 360
Cdd:cd08227   241 LTMKPSRSGANSGLGESTTVSTPRPSNGESSSHPYNRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQIKRRASEA 320

                  ....*..
gi 1394533236 361 LPELLRP 367
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 ...
41-367 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: 693.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  41 ELLTVIGKGFEDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSF 120
Cdd:cd08227     1 ELLTVIGRGFEDLMTVNLARYKPTGEYVTVRRINLEACTNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 121 MAYGSAKDLICTHFMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMISHGQRQRV 200
Cdd:cd08227    81 MAYGSAKDLICTHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMINHGQRLRV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 201 VHDFPKYSVKVLPWLSPEVLQQNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPCLLDTSTIPAEE 280
Cdd:cd08227   161 VHDFPKYSVKVLPWLSPEVLQQNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPCLLDTTTIPAEE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 281 LTMSPSRSVANSGLSDSLTTSTPRPSNGDSPSHPYHRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQIKRRASEA 360
Cdd:cd08227   241 LTMKPSRSGANSGLGESTTVSTPRPSNGESSSHPYNRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQIKRRASEA 320

                  ....*..
gi 1394533236 361 LPELLRP 367
Cdd:cd08227   321 LPELLRP 327
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
40-350 7.55e-53

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 176.57  E-value: 7.55e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236   40 YELLTVIGKG-FEdlmTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQgELHVSKLFNHPNIVPYRATFIADNELWVVT 118
Cdd:smart00220   1 YEILEKLGEGsFG---KVYLARDKKTGKLVAIKVIKKKKIKKDRERILR-EIKILKKLKHPNIVRLYDVFEDEDKLYLVM 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  119 SFMAYGSAKDLICTHfmDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRsnlsmishgq 196
Cdd:smart00220  77 EYCEGGDLFDLLKKR--GRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLAdfGLA---------- 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  197 rqRVVHDFPKYSVKV--LPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLngtvpclldts 274
Cdd:smart00220 145 --RQLDPGEKLTTFVgtPEYMAPEVLLG--KGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKI----------- 209
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1394533236  275 tipaeeltmspsrsvansglsdslttstprpSNGDSPSHPYHRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFF 350
Cdd:smart00220 210 -------------------------------GKPKPPFPPPEWDISPEAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
30-345 1.33e-29

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 119.73  E-value: 1.33e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  30 MSSflPEGGCYELLTVIGKGFedlM-TVNLARYKPTGEYVTVRRINLEACSNE--MVTFLQgELHVSKLFNHPNIVPYRA 106
Cdd:COG0515     1 MSA--LLLGRYRILRLLGRGG---MgVVYLARDLRLGRPVALKVLRPELAADPeaRERFRR-EARALARLNHPNIVRVYD 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 107 TFIADNELWVVTSFMAYGSAKDLICTHfmDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--G 184
Cdd:COG0515    75 VGEEDGRPYLVMEYVEGESLADLLRRR--GPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIdfG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 185 LRSNLSMISHGQRQRVVHDfpkysvkvLPWLSPEVLQqnLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLN 264
Cdd:COG0515   153 IARALGGATLTQTGTVVGT--------PGYMAPEQAR--GEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLR 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 265 GTVPclldtstipaeeltmspsrsvansglsdslttstprpsngdsPSHPYHRTFSPHFHHFVEQCLQRNPDARP-SAST 343
Cdd:COG0515   223 EPPP------------------------------------------PPSELRPDLPPALDAIVLRALAKDPEERYqSAAE 260

                  ..
gi 1394533236 344 LL 345
Cdd:COG0515   261 LA 262
Pkinase pfam00069
Protein kinase domain;
40-350 2.04e-24

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 100.01  E-value: 2.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKG-FEdlmTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVT 118
Cdd:pfam00069   1 YEVLRKLGSGsFG---TVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 119 SFMAYGSAKDLICTHFMDGMNElAIAYILQgVLKALDyihhmgyvhRSVKASHILISVDgkvylsglrsnlsmishgqrq 198
Cdd:pfam00069  78 EYVEGGSLFDLLSEKGAFSERE-AKFIMKQ-ILEGLE---------SGSSLTTFVGTPW--------------------- 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 199 rvvhdfpkysvkvlpWLSPEVLQQNlqGYDAKSDIYSVGITACELANGHVPFKDmpatqmlleklngtvpcllDTSTIPA 278
Cdd:pfam00069 126 ---------------YMAPEVLGGN--PYGPKVDVWSLGCILYELLTGKPPFPG-------------------INGNEIY 169
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1394533236 279 EELTMSPSRsvansglsdslttstprpsngdSPSHPYhrTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFF 350
Cdd:pfam00069 170 ELIIDQPYA----------------------FPELPS--NLSEEAKDLLKKLLKKDPSKRLTATQALQHPWF 217
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
55-370 1.40e-16

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 80.25  E-value: 1.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  55 TVNLARYKPTGEYVTVRRI--NLEACSNEMVTflqGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSakdLICT 132
Cdd:PLN00034   89 TVYKVIHRPTGRLYALKVIygNHEDTVRRQIC---REIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGS---LEGT 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 133 HFMDgmnELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISvdgkvylSGLRSNLSMISHGQRQRVVHDFPKYSVKVL 212
Cdd:PLN00034  163 HIAD---EQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLIN-------SAKNVKIADFGVSRILAQTMDPCNSSVGTI 232
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 213 PWLSPEVLQQNL-QG-YDAKS-DIYSVGITACELANGHVPFkdmpatqmlleklngtvpclldtstipaeeltmspsrSV 289
Cdd:PLN00034  233 AYMSPERINTDLnHGaYDGYAgDIWSLGVSILEFYLGRFPF-------------------------------------GV 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 290 ANSGLSDSLTTSTprpSNGDSPSHPyhRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQIKRRASEALPElLRPVT 369
Cdd:PLN00034  276 GRQGDWASLMCAI---CMSQPPEAP--ATASREFRHFISCCLQREPAKRWSAMQLLQHPFILRAQPGQGQGGPN-LHQLL 349

                  .
gi 1394533236 370 P 370
Cdd:PLN00034  350 P 350
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
37-250 3.37e-11

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 64.82  E-value: 3.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  37 GGCYELLTVIGKG-------FEDL----------MTVNLARyKPTgeyvTVRRINLEACSnemvtflqgelhVSKLfNHP 99
Cdd:NF033483    6 GGRYEIGERIGRGgmaevylAKDTrldrdvavkvLRPDLAR-DPE----FVARFRREAQS------------AASL-SHP 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 100 NIV-----------PYratfIAdnelwvvtsfMAY--GSA-KDLICTHFMdgMNELAIAYILQGVLKALDYIHHMGYVHR 165
Cdd:NF033483   68 NIVsvydvgedggiPY----IV----------MEYvdGRTlKDYIREHGP--LSPEEAVEIMIQILSALEHAHRNGIVHR 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 166 SVKASHILISVDGKVYLS--GL-R--SNLSMIshgQRQRV---VHdfpkYsvkvlpwLSPEvlqQNLQGY-DAKSDIYSV 236
Cdd:NF033483  132 DIKPQNILITKDGRVKVTdfGIaRalSSTTMT---QTNSVlgtVH----Y-------LSPE---QARGGTvDARSDIYSL 194
                         250
                  ....*....|....
gi 1394533236 237 GITACELANGHVPF 250
Cdd:NF033483  195 GIVLYEMLTGRPPF 208
 
Name Accession Description Interval E-value
PK_STRAD_alpha cd08227
Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain ...
41-367 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: 693.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  41 ELLTVIGKGFEDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSF 120
Cdd:cd08227     1 ELLTVIGRGFEDLMTVNLARYKPTGEYVTVRRINLEACTNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 121 MAYGSAKDLICTHFMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMISHGQRQRV 200
Cdd:cd08227    81 MAYGSAKDLICTHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMINHGQRLRV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 201 VHDFPKYSVKVLPWLSPEVLQQNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPCLLDTSTIPAEE 280
Cdd:cd08227   161 VHDFPKYSVKVLPWLSPEVLQQNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPCLLDTTTIPAEE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 281 LTMSPSRSVANSGLSDSLTTSTPRPSNGDSPSHPYHRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQIKRRASEA 360
Cdd:cd08227   241 LTMKPSRSGANSGLGESTTVSTPRPSNGESSSHPYNRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQIKRRASEA 320

                  ....*..
gi 1394533236 361 LPELLRP 367
Cdd:cd08227   321 LPELLRP 327
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
41-367 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: 528.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  41 ELLTVIGKGFEDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSF 120
Cdd:cd08216     1 ELLYEIGKCFKGGGVVHLAKHKPTNTLVAVKKINLESDSKEDLKFLQQEILTSRQLQHPNILPYVTSFVVDNDLYVVTPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 121 MAYGSAKDLICTHFMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMISHGQRQRV 200
Cdd:cd08216    81 MAYGSCRDLLKTHFPEGLPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGLRYAYSMVKHGKRQRV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 201 VHDFPKYSVKVLPWLSPEVLQQNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPCLLDTSTIPAEE 280
Cdd:cd08216   161 VHDFPKSSEKNLPWLSPEVLQQNLLGYNEKSDIYSVGITACELANGVVPFSDMPATQMLLEKVRGTTPQLLDCSTYPLEE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 281 LTMSPSRSvansglsdsltTSTPRPSNGDSPSHPYHRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQIkRRASEA 360
Cdd:cd08216   241 DSMSQSED-----------SSTEHPNNRDTRDIPYQRTFSEAFHQFVELCLQRDPELRPSASQLLAHSFFKQC-RRSNTS 308

                  ....*..
gi 1394533236 361 LPELLRP 367
Cdd:cd08216   309 LLDLLKP 315
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
41-367 2.46e-139

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: 400.40  E-value: 2.46e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  41 ELLTVIGKGFEDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSF 120
Cdd:cd08226     1 ELQVELGKGFCNLTSVYLARHTPTGTLVTVKITNLDNCSEEHLKALQNEVVLSHFFRHPNIMTHWTVFTEGSWLWVISPF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 121 MAYGSAKDLICTHFMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMISHGQRQRV 200
Cdd:cd08226    81 MAYGSARGLLKTYFPEGMNEALIGNILYGAIKALNYLHQNGCIHRSVKASHILISGDGLVSLSGLSHLYSMVTNGQRSKV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 201 VHDFPKYSVKVLPWLSPEVLQQNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPCLLDTSTIPAEE 280
Cdd:cd08226   161 VYDFPQFSTSVLPWLSPELLRQDLHGYNVKSDIYSVGITACELARGQVPFQDMRRTQMLLQKLKGPPYSPLDIFPFPELE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 281 LTMSPSRSVANSGLSDSLTTSTPRPSNGDSPSH-PYHRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQIKRRASE 359
Cdd:cd08226   241 SRMKNSQSGMDSGIGESVATSSMTRTMTSERLQtPSSKTFSPAFHNLVELCLQQDPEKRPSASSLLSHSFFKQVKEQTQA 320

                  ....*...
gi 1394533236 360 ALPELLRP 367
Cdd:cd08226   321 SLLSLLPP 328
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
40-350 2.15e-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: 2.15e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGFEdlMTVNLARYKPTGEYVTVRRINLEACSNEMvTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTS 119
Cdd:cd06610     3 YELIEVIGSGAT--AVVYAAYCLPKKEKVAIKRIDLEKCQTSM-DELRKEIQAMSQCNHPNVVSYYTSFVVGDELWLVMP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 120 FMAYGSAKDLICTHF-MDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMISHGQRQ 198
Cdd:cd06610    80 LLSGGSLLDIMKSSYpRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVSASLATGGDRT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 199 -RVVHDFpkysVKVLPWLSPEVLQQnLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPCLldtstip 277
Cdd:cd06610   160 rKVRKTF----VGTPCWMAPEVMEQ-VRGYDFKADIWSFGITAIELATGAAPYSKYPPMKVLMLTLQNDPPSL------- 227
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1394533236 278 aeeltmspsrsvansglsdslttstprPSNGDspshpyHRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFF 350
Cdd:cd06610   228 ---------------------------ETGAD------YKKYSKSFRKMISLCLQKDPSKRPTAEELLKHKFF 267
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
39-350 6.10e-60

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: 194.73  E-value: 6.10e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  39 CYELLTVIGKG-FEdlmTVNLARYKPTGEYVTVRRINLEACSNEmvTFLQGELHVSKLFNHPNIVPYRATFIADNELWVV 117
Cdd:cd05122     1 LFEILEKIGKGgFG---VVYKARHKKTGQIVAIKKINLESKEKK--ESILNEIAILKKCKHPNIVKYYGSYLKKDELWIV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 118 TSFMAYGSAKDLIcTHFMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNLSmiSHG 195
Cdd:cd05122    76 MEFCSGGSLKDLL-KNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIdfGLSAQLS--DGK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 196 QRQRVvhdfpkysVKVLPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEklngtvpclldTST 275
Cdd:cd05122   153 TRNTF--------VGTPYWMAPEVIQG--KPYGFKADIWSLGITAIEMAEGKPPYSELPPMKALFL-----------IAT 211
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1394533236 276 IPAEELtmspsrsvansglsdslttstPRPSNgdspshpyhrtFSPHFHHFVEQCLQRNPDARPSASTLLNHSFF 350
Cdd:cd05122   212 NGPPGL---------------------RNPKK-----------WSKEFKDFLKKCLQKDPEKRPTAEQLLKHPFI 254
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
40-366 4.56e-53

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: 177.82  E-value: 4.56e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKG-FEDlmtVNLARYKPTGEYVTVRRINLEAcSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVT 118
Cdd:cd06609     3 FTLLERIGKGsFGE---VYKGIDKRTNQVVAIKVIDLEE-AEDEIEDIQQEIQFLSQCDSPYITKYYGSFLKGSKLWIIM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 119 SFMAYGSAKDLIcthFMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNLsmiSHGQ 196
Cdd:cd06609    79 EYCGGGSVLDLL---KPGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLAdfGVSGQL---TSTM 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 197 RQRvvHDFpkysVKVLPWLSPEVLQQNlqGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEklngtvpclldtstI 276
Cdd:cd06609   153 SKR--NTF----VGTPFWMAPEVIKQS--GYDEKADIWSLGITAIELAKGEPPLSDLHPMRVLFL--------------I 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 277 PAEEltmspsrsvansglSDSLTtstprpsngdspshpyHRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQIKRR 356
Cdd:cd06609   211 PKNN--------------PPSLE----------------GNKFSKPFKDFVELCLNKDPKERPSAKELLKHKFIKKAKKT 260
                         330
                  ....*....|
gi 1394533236 357 ASeaLPELLR 366
Cdd:cd06609   261 SY--LTLLIE 268
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
40-350 7.55e-53

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 176.57  E-value: 7.55e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236   40 YELLTVIGKG-FEdlmTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQgELHVSKLFNHPNIVPYRATFIADNELWVVT 118
Cdd:smart00220   1 YEILEKLGEGsFG---KVYLARDKKTGKLVAIKVIKKKKIKKDRERILR-EIKILKKLKHPNIVRLYDVFEDEDKLYLVM 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  119 SFMAYGSAKDLICTHfmDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRsnlsmishgq 196
Cdd:smart00220  77 EYCEGGDLFDLLKKR--GRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLAdfGLA---------- 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  197 rqRVVHDFPKYSVKV--LPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLngtvpclldts 274
Cdd:smart00220 145 --RQLDPGEKLTTFVgtPEYMAPEVLLG--KGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKI----------- 209
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1394533236  275 tipaeeltmspsrsvansglsdslttstprpSNGDSPSHPYHRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFF 350
Cdd:smart00220 210 -------------------------------GKPKPPFPPPEWDISPEAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
40-351 9.18e-48

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: 163.15  E-value: 9.18e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGFEDlmTVNLARYKPTGEYVTVRRINLEACSNEMvtfLQGELHVSKLFNHPNIVPYRATFIADNELWVVTS 119
Cdd:cd06614     2 YKNLEKIGEGASG--EVYKATDRATGKEVAIKKMRLRKQNKEL---IINEILIMKECKHPNIVDYYDSYLVGDELWVVME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 120 FMAYGSAKDLIcTHFMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNLSMiSHGQR 197
Cdd:cd06614    77 YMDGGSLTDII-TQNPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLAdfGFAAQLTK-EKSKR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 198 QRVVHDfpkysvkvlP-WLSPEVLQQNLqgYDAKSDIYSVGITACELANGHVPFKDMPatqmlleklngtvpclldtsti 276
Cdd:cd06614   155 NSVVGT---------PyWMAPEVIKRKD--YGPKVDIWSLGIMCIEMAEGEPPYLEEP---------------------- 201
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1394533236 277 PAEELTMspsrsVANSGlsdslttsTPRPSNGDSpshpyhrtFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFK 351
Cdd:cd06614   202 PLRALFL-----ITTKG--------IPPLKNPEK--------WSPEFKDFLNKCLVKDPEKRPSAEELLQHPFLK 255
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
40-350 1.03e-47

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: 163.25  E-value: 1.03e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKG-FEDlmtVNLARYKPTGEYVTVRRINLEAcsNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVT 118
Cdd:cd06613     2 YELIQRIGSGtYGD---VYKARNIATGELAAVKVIKLEP--GDDFEIIQQEISMLKECRHPNIVAYFGSYLRRDKLWIVM 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 119 SFMAYGSAKDLIctHFMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRsnlSMISHGQ 196
Cdd:cd06613    77 EYCGGGSLQDIY--QVTGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLAdfGVS---AQLTATI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 197 RQRvvhdfpKYSVKVLPWLSPEVLQQNLQ-GYDAKSDIYSVGITACELANGHVPFKDMPatqmlleklngtvpclldtst 275
Cdd:cd06613   152 AKR------KSFIGTPYWMAPEVAAVERKgGYDGKCDIWALGITAIELAELQPPMFDLH--------------------- 204
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1394533236 276 iPAEELTMSPSrsvansglsdslttstprpSNGDSPSHPYHRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFF 350
Cdd:cd06613   205 -PMRALFLIPK-------------------SNFDPPKLKDKEKWSPDFHDFIKKCLTKNPKKRPTATKLLQHPFV 259
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
40-350 6.41e-46

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: 158.58  E-value: 6.41e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEmvtfLQGELHVSKLFNHPNIVPYRATFIADNELWVVTS 119
Cdd:cd06612     5 FDILEKLGEG--SYGSVYKAIHKETGQVVAIKVVPVEEDLQE----IIKEISILKQCDSPYIVKYYGSYFKNTDLWIVME 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 120 FMAYGSAKDL--ICThfmDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNLsmiSHG 195
Cdd:cd06612    79 YCGAGSVSDImkITN---KTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLAdfGVSGQL---TDT 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 196 QRQRvvhdfpkYSVKVLP-WLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLeklngtvpclldts 274
Cdd:cd06612   153 MAKR-------NTVIGTPfWMAPEVIQE--IGYNNKADIWSLGITAIEMAEGKPPYSDIHPMRAIF-------------- 209
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1394533236 275 TIPaeelTMSPsrsvanSGLSDslttstprpsngdsPSHpyhrtFSPHFHHFVEQCLQRNPDARPSASTLLNHSFF 350
Cdd:cd06612   210 MIP----NKPP------PTLSD--------------PEK-----WSPEFNDFVKKCLVKDPEERPSAIQLLQHPFI 256
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
45-350 4.09e-41

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: 145.74  E-value: 4.09e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  45 VIGKG-FEdlmTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAY 123
Cdd:cd06606     7 LLGKGsFG---SVYLALNLDTGELMAVKEVELSGDSEEELEALEREIRILSSLKHPNIVRYLGTERTENTLNIFLEYVPG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 124 GSAKDLICThFmDGMNE-LAIAYILQgVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNLSMISHGQRQRV 200
Cdd:cd06606    84 GSLASLLKK-F-GKLPEpVVRKYTRQ-ILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLAdfGCAKRLAEIATGEGTKS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 201 VHDFPkysvkvlPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLngtvpclldtstipaee 280
Cdd:cd06606   161 LRGTP-------YWMAPEVIRG--EGYGRAADIWSLGCTVIEMATGKPPWSELGNPVAALFKI----------------- 214
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1394533236 281 ltmspsrsvansglsdslttstprpsnGDSPSHPY-HRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFF 350
Cdd:cd06606   215 ---------------------------GSSGEPPPiPEHLSEEAKDFLRKCLQRDPKKRPTADELLQHPFL 258
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
46-348 1.17e-40

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: 143.57  E-value: 1.17e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  46 IGKG-FedlMTVNLARYKPTGEYVTVRRINLEaCSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYG 124
Cdd:cd00180     1 LGKGsF---GKVYKARDKETGKKVAVKVIPKE-KLKKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 125 SAKDLICTHFmDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMISHGqrqrvvhDF 204
Cdd:cd00180    77 SLKDLLKENK-GPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDD-------SL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 205 PKYSVKVLPWLSPEVLQQNLQGYDAKSDIYSVGITACELanghvpfkdmpatqmlleklngtvpclldtstipaeeltms 284
Cdd:cd00180   149 LKTTGGTTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL----------------------------------------- 187
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1394533236 285 psrsvansglsdslttstprpsngdspshpyhrtfsPHFHHFVEQCLQRNPDARPSASTLLNHS 348
Cdd:cd00180   188 ------------------------------------EELKDLIRRMLQYDPKKRPSAKELLEHL 215
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
39-350 1.25e-39

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: 141.98  E-value: 1.25e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  39 CYELLTVIGKG-FEdlmTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVV 117
Cdd:cd06627     1 NYQLGDLIGRGaFG---SVYKGLNLNTGEFVAIKQISLEKIPKSDLKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYII 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 118 TSFMAYGSAKDLICTHfmDGMNE-LAIAYILQgVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNLSMiSH 194
Cdd:cd06627    78 LEYVENGSLASIIKKF--GKFPEsLVAVYIYQ-VLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLAdfGVATKLNE-VE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 195 GQRQRVVHDfpkysvkvlP-WLSPEVLQqnLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLeklngtvpclldt 273
Cdd:cd06627   154 KDENSVVGT---------PyWMAPEVIE--MSGVTTASDIWSVGCTVIELLTGNPPYYDLQPMAALF------------- 209
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1394533236 274 stipaeeltmspsRSVANsglsdsltTSTPRPSNgdspshpyhrtFSPHFHHFVEQCLQRNPDARPSASTLLNHSFF 350
Cdd:cd06627   210 -------------RIVQD--------DHPPLPEN-----------ISPELRDFLLQCFQKDPTLRPSAKELLKHPWL 254
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
41-353 3.41e-37

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: 135.80  E-value: 3.41e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  41 ELLTVIGKGFEDlmTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQgELHVSKLFNHPNIVPYRATFIADNELWVVTSF 120
Cdd:cd06623     4 ERVKVLGQGSSG--VVYKVRHKPTGKIYALKKIHVDGDEEFRKQLLR-ELKTLRSCESPYVVKCYGAFYKEGEISIVLEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 121 MAYGSAKDLICTHfmDGMNELAIAYILQGVLKALDYIH---HMgyVHRSVKASHILISVDGKVYLS--GLRSNLSmishg 195
Cdd:cd06623    81 MDGGSLADLLKKV--GKIPEPVLAYIARQILKGLDYLHtkrHI--IHRDIKPSNLLINSKGEVKIAdfGISKVLE----- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 196 QRQRVVHDFpkysVKVLPWLSPEVLQQNLQGYDakSDIYSVGITACELANGHVPFKdmPATQM----LLEKLNgtvpcll 271
Cdd:cd06623   152 NTLDQCNTF----VGTVTYMSPERIQGESYSYA--ADIWSLGLTLLECALGKFPFL--PPGQPsffeLMQAIC------- 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 272 dtstipaeeltmspsrsvansglsdslttstprpsNGDSPSHPYHrTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFK 351
Cdd:cd06623   217 -----------------------------------DGPPPSLPAE-EFSPEFRDFISACLQKDPKKRPSAAELLQHPFIK 260

                  ..
gi 1394533236 352 QI 353
Cdd:cd06623   261 KA 262
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
41-352 1.13e-36

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: 134.39  E-value: 1.13e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  41 ELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQgELHVSKLFNHPNIVPYRATFIADNELWVVTSF 120
Cdd:cd06605     4 EYLGELGEG--NGGVVSKVRHRPSGQIMAVKVIRLEIDEALQKQILR-ELDVLHKCNSPYIVGFYGAFYSEGDISICMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 121 MAYGSAKDLIctHFMDGMNELAIAYILQGVLKALDYIHH-MGYVHRSVKASHILISVDGKVYLSGLrsnlsmishGQRQR 199
Cdd:cd06605    81 MDGGSLDKIL--KEVGRIPERILGKIAVAVVKGLIYLHEkHKIIHRDVKPSNILVNSRGQVKLCDF---------GVSGQ 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 200 VVHDFPKYSVKVLPWLSPEVLQQNlqGYDAKSDIYSVGITACELANGHVPFKdmpatqmlleklngtvPCLLDTSTIPAE 279
Cdd:cd06605   150 LVDSLAKTFVGTRSYMAPERISGG--KYTVKSDIWSLGLSLVELATGRFPYP----------------PPNAKPSMMIFE 211
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1394533236 280 ELTmspsrsvansglsdslttstpRPSNGDSPSHPYHRtFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQ 352
Cdd:cd06605   212 LLS---------------------YIVDEPPPLLPSGK-FSPDFQDFVSQCLQKDPTERPSYKELMEHPFIKR 262
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
34-349 3.71e-36

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: 133.20  E-value: 3.71e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  34 LPE-GGCYELLTVIGKGFEDLmtVNLARYKPTGEYVTVRRINLEAcsnEMVTFLQGELHVSKLF-NHPNIVPYRATFI-- 109
Cdd:cd06608     1 LPDpAGIFELVEVIGEGTYGK--VYKARHKKTGQLAAIKIMDIIE---DEEEEIKLEINILRKFsNHPNIATFYGAFIkk 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 110 ----ADNELWVVTSFMAYGSAKDLICTHFMDG--MNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS 183
Cdd:cd06608    76 dppgGDDQLWLVMEYCGGGSVTDLVKGLRKKGkrLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 184 --GLRSNLSMiSHGQRQRVVHDfpkysvkvlP-WLSPEVL---QQNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQ 257
Cdd:cd06608   156 dfGVSAQLDS-TLGRRNTFIGT---------PyWMAPEVIacdQQPDASYDARCDVWSLGITAIELADGKPPLCDMHPMR 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 258 MLLEKLNGTVPCLldtstipaeeltMSPSRsvansglsdslttstprpsngdspshpyhrtFSPHFHHFVEQCLQRNPDA 337
Cdd:cd06608   226 ALFKIPRNPPPTL------------KSPEK-------------------------------WSKEFNDFISECLIKNYEQ 262
                         330
                  ....*....|..
gi 1394533236 338 RPSASTLLNHSF 349
Cdd:cd06608   263 RPFTEELLEHPF 274
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
55-351 5.25e-34

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: 127.17  E-value: 5.25e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  55 TVNLARYKPTGEYVTVRRINLEACSNEMVTFlqGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLIcTHF 134
Cdd:cd06648    22 IVCIATDKSTGRQVAVKKMDLRKQQRRELLF--NEVVIMRDYQHPNIVEMYSSYLVGDELWVVMEFLEGGALTDIV-THT 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 135 MdgMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNLSmishgqrqrvvHDFPKYSVKV- 211
Cdd:cd06648    99 R--MNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSdfGFCAQVS-----------KEVPRRKSLVg 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 212 LP-WLSPEVLQQNLqgYDAKSDIYSVGITACELANGHVPFKDMPatqmlleklngtvpclldtstiPAEELTMspsrsva 290
Cdd:cd06648   166 TPyWMAPEVISRLP--YGTEVDIWSLGIMVIEMVDGEPPYFNEP----------------------PLQAMKR------- 214
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1394533236 291 nsglsdsLTTSTPRPSNgdspshpYHRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFK 351
Cdd:cd06648   215 -------IRDNEPPKLK-------NLHKVSPRLRSFLDRMLVRDPAQRATAAELLNHPFLA 261
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
40-352 6.49e-34

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: 126.80  E-value: 6.49e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEA-CSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVt 118
Cdd:cd06607     3 FEDLREIGHG--SFGAVYYARNKRTSEVVAIKKMSYSGkQSTEKWQDIIKEVKFLRQLRHPNTIEYKGCYLREHTAWLV- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 119 sfMAY--GSAKDLICTHfMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSnLSMIShgq 196
Cdd:cd06607    80 --MEYclGSASDIVEVH-KKPLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFGS-ASLVC--- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 197 rqrvvhdfPKYSVKVLP-WLSPEVLQQNLQG-YDAKSDIYSVGITACELANGHVPFKDMPAtqmlleklngtvpclldts 274
Cdd:cd06607   153 --------PANSFVGTPyWMAPEVILAMDEGqYDGKVDVWSLGITCIELAERKPPLFNMNA------------------- 205
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1394533236 275 tipaeeltMSPSRSVANSglsdslttstprpsngDSPSHPyHRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQ 352
Cdd:cd06607   206 --------MSALYHIAQN----------------DSPTLS-SGEWSDDFRNFVDSCLQKIPQDRPSAEDLLKHPFVTR 258
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
56-365 9.08e-34

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: 127.17  E-value: 9.08e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  56 VNLARYKPTGEYVTVRRINLEAcSNEMVTFLQgELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAyGSAKDLICTHFM 135
Cdd:cd06611    21 VYKAQHKETGLFAAAKIIQIES-EEELEDFMV-EIDILSECKHPNIVGLYEAYFYENKLWILIEFCD-GGALDSIMLELE 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 136 DGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMISHGQRQrvvHDFpkysVKVLPWL 215
Cdd:cd06611    98 RGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSAKNKSTLQKR---DTF----IGTPYWM 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 216 SPEVLQQNL---QGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPCLldtstipaeeltmspsrsvans 292
Cdd:cd06611   171 APEVVACETfkdNPYDYKADIWSLGITLIELAQMEPPHHELNPMRVLLKILKSEPPTL---------------------- 228
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1394533236 293 glsdslttstprpsngDSPSHpyhrtFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQIKRRasEALPELL 365
Cdd:cd06611   229 ----------------DQPSK-----WSSSFNDFLKSCLVKDPDDRPTAAELLKHPFVSDQSDN--KAIKDLL 278
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
40-365 5.72e-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: 122.20  E-value: 5.72e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEmVTFLQGELHVSKLFNH---PNIVPYRATFIADNELWV 116
Cdd:cd06917     3 YRRLELVGRG--SYGAVYRGYHVKTGRVVALKVLNLDTDDDD-VSDIQKEVALLSQLKLgqpKNIIKYYGSYLKGPSLWI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 117 VTSFMAYGSAKDLICTHFMDgmnELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNLSmISH 194
Cdd:cd06917    80 IMDYCEGGSIRTLMRAGPIA---ERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCdfGVAASLN-QNS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 195 GQRQRVVHdfPKYsvkvlpWLSPEVLQQNlQGYDAKSDIYSVGITACELANGHVPFKDMPATQ--MLLEKlngtvpclld 272
Cdd:cd06917   156 SKRSTFVG--TPY------WMAPEVITEG-KYYDTKADIWSLGITTYEMATGNPPYSDVDALRavMLIPK---------- 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 273 tstipaeeltmspsrsvansglsdsltTSTPR-PSNGdspshpyhrtFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFK 351
Cdd:cd06917   217 ---------------------------SKPPRlEGNG----------YSPLLKEFVAACLDEEPKDRLSADELLKSKWIK 259
                         330
                  ....*....|....
gi 1394533236 352 QIKRRASEALPELL 365
Cdd:cd06917   260 QHSKTPTSVLKELI 273
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
64-365 1.93e-31

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: 120.93  E-value: 1.93e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  64 TGEYVTVRRINLEACSNEmVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTHFMDgmnELAI 143
Cdd:cd06640    28 TQQVVAIKIIDLEEAEDE-IEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIMEYLGGGSALDLLRAGPFD---EFQI 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 144 AYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNLSMISHGQRQRVVHDFpkysvkvlpWLSPEVLQ 221
Cdd:cd06640   104 ATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLAdfGVAGQLTDTQIKRNTFVGTPF---------WMAPEVIQ 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 222 QNlqGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPCLLdtstipaeeltmspsrsvansglsdsltts 301
Cdd:cd06640   175 QS--AYDSKADIWSLGITAIELAKGEPPNSDMHPMRVLFLIPKNNPPTLV------------------------------ 222
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1394533236 302 tprpsnGDspshpyhrtFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQIKRRASeALPELL 365
Cdd:cd06640   223 ------GD---------FSKPFKEFIDACLNKDPSFRPTAKELLKHKFIVKNAKKTS-YLTELI 270
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
40-347 2.86e-31

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: 119.54  E-value: 2.86e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKG-FEdlmTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVt 118
Cdd:cd14003     2 YELGKTLGEGsFG---KVKLARHKLTGEKVAIKIIDKSKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVIETENKIYLV- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 119 sfMAYGSAKDL---ICTHfmDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLrSNLSMIs 193
Cdd:cd14003    78 --MEYASGGELfdyIVNN--GRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIdfGL-SNEFRG- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 194 hgqrqrvvHDFPKYSVKVLPWLSPEVLQQnlQGYDA-KSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPClld 272
Cdd:cd14003   152 --------GSLLKTFCGTPAYAAPEVLLG--RKYDGpKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYPI--- 218
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1394533236 273 tstipaeeltmspsrsvansglsdslttstprpsngdsPSHpyhrtFSPHFHHFVEQCLQRNPDARPSASTLLNH 347
Cdd:cd14003   219 --------------------------------------PSH-----LSPDARDLIRRMLVVDPSKRITIEEILNH 250
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
64-365 3.82e-31

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: 119.79  E-value: 3.82e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  64 TGEYVTVRRINLEACSNEmVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTHFMDgmnELAI 143
Cdd:cd06641    28 TQKVVAIKIIDLEEAEDE-IEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYLGGGSALDLLEPGPLD---ETQI 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 144 AYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNLSMISHGQRQRVVHDFpkysvkvlpWLSPEVLQ 221
Cdd:cd06641   104 ATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLAdfGVAGQLTDTQIKRN*FVGTPF---------WMAPEVIK 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 222 QNlqGYDAKSDIYSVGITACELANGHVPFKDM-PATQMLLEKLNGtvPCLLDTStipaeeltmspsrsvansglsdsltt 300
Cdd:cd06641   175 QS--AYDSKADIWSLGITAIELARGEPPHSELhPMKVLFLIPKNN--PPTLEGN-------------------------- 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1394533236 301 stprpsngdspshpyhrtFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQIKRRASeALPELL 365
Cdd:cd06641   225 ------------------YSKPLKEFVEACLNKEPSFRPTAKELLKHKFILRNAKKTS-YLTELI 270
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
64-358 9.90e-31

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: 119.01  E-value: 9.90e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  64 TGEYVTVRRINLEACSNEmVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICThfmDGMNELAI 143
Cdd:cd06642    28 TKEVVAIKIIDLEEAEDE-IEDIQQEITVLSQCDSPYITRYYGSYLKGTKLWIIMEYLGGGSALDLLKP---GPLEETYI 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 144 AYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNLSMISHGQRQRVVHDFpkysvkvlpWLSPEVLQ 221
Cdd:cd06642   104 ATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLAdfGVAGQLTDTQIKRNTFVGTPF---------WMAPEVIK 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 222 QNlqGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLeklngtvpclldtsTIPAEeltmSPsrsvansglsdsltts 301
Cdd:cd06642   175 QS--AYDFKADIWSLGITAIELAKGEPPNSDLHPMRVLF--------------LIPKN----SP---------------- 218
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1394533236 302 tprPSNGDSPSHPyhrtfsphFHHFVEQCLQRNPDARPSASTLLNHSFFKQIKRRAS 358
Cdd:cd06642   219 ---PTLEGQHSKP--------FKEFVEACLNKDPRFRPTAKELLKHKFITRYTKKTS 264
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
64-349 1.42e-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: 117.89  E-value: 1.42e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  64 TGEYVTVRRINL---EACSNEMVTFLQGELHV-SKLfNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLIctHFMDGMN 139
Cdd:cd06632    24 TGDFFAVKEVSLvddDKKSRESVKQLEQEIALlSKL-RHPNIVQYYGTEREEDNLYIFLEYVPGGSIHKLL--QRYGAFE 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 140 ELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSglrsNLSMISHGQRQRvvhdFPKySVKVLP-WLSPE 218
Cdd:cd06632   101 EPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLA----DFGMAKHVEAFS----FAK-SFKGSPyWMAPE 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 219 VLQQNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEklngtvpclldtstipaeeltmspsrsVANSglsdsl 298
Cdd:cd06632   172 VIMQKNSGYGLAVDIWSLGCTVLEMATGKPPWSQYEGVAAIFK---------------------------IGNS------ 218
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1394533236 299 ttstprpsnGDSPSHPYHrtFSPHFHHFVEQCLQRNPDARPSASTLLNHSF 349
Cdd:cd06632   219 ---------GELPPIPDH--LSPDAKDFIRLCLQRDPEDRPTASQLLEHPF 258
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
40-351 5.74e-30

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: 116.18  E-value: 5.74e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGFEDlmTVNLARYKPTGEYVTVRRINL-EACSNEMVTflqGELHVSKLFNHPNIVPYRATFIADNELWVVT 118
Cdd:cd06647     9 YTRFEKIGQGASG--TVYTAIDVATGQEVAIKQMNLqQQPKKELII---NEILVMRENKNPNIVNYLDSYLVGDELWVVM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 119 SFMAYGSAKDLICTHFMDgmnELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLrSNLSMISHGQRQ 198
Cdd:cd06647    84 EYLAGGSLTDVVTETCMD---EGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDF-GFCAQITPEQSK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 199 RVVHDFPKYsvkvlpWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPF-KDMPATQMLLEKLNGTvpclldtstip 277
Cdd:cd06647   160 RSTMVGTPY------WMAPEVVTR--KAYGPKVDIWSLGIMAIEMVEGEPPYlNENPLRALYLIATNGT----------- 220
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1394533236 278 aeeltmspsrsvansglsdslttstprpsngdsPSHPYHRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFK 351
Cdd:cd06647   221 ---------------------------------PELQNPEKLSAIFRDFLNRCLEMDVEKRGSAKELLQHPFLK 261
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
30-345 1.33e-29

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 119.73  E-value: 1.33e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  30 MSSflPEGGCYELLTVIGKGFedlM-TVNLARYKPTGEYVTVRRINLEACSNE--MVTFLQgELHVSKLFNHPNIVPYRA 106
Cdd:COG0515     1 MSA--LLLGRYRILRLLGRGG---MgVVYLARDLRLGRPVALKVLRPELAADPeaRERFRR-EARALARLNHPNIVRVYD 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 107 TFIADNELWVVTSFMAYGSAKDLICTHfmDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--G 184
Cdd:COG0515    75 VGEEDGRPYLVMEYVEGESLADLLRRR--GPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIdfG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 185 LRSNLSMISHGQRQRVVHDfpkysvkvLPWLSPEVLQqnLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLN 264
Cdd:COG0515   153 IARALGGATLTQTGTVVGT--------PGYMAPEQAR--GEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLR 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 265 GTVPclldtstipaeeltmspsrsvansglsdslttstprpsngdsPSHPYHRTFSPHFHHFVEQCLQRNPDARP-SAST 343
Cdd:COG0515   223 EPPP------------------------------------------PPSELRPDLPPALDAIVLRALAKDPEERYqSAAE 260

                  ..
gi 1394533236 344 LL 345
Cdd:COG0515   261 LA 262
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
30-351 2.52e-29

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: 115.47  E-value: 2.52e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  30 MSSFLPEGGCYELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINleaCSNEMVTFLQGELHVSK-LFNHPNIVP----- 103
Cdd:cd06639    14 LESLADPSDTWDIIETIGKG--TYGKVYKVTNKKDGSLAAVKILD---PISDVDEEIEAEYNILRsLPNHPNVVKfygmf 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 104 YRATFIADNELWVVTSFMAYGSAKDLICTHFMDG--MNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVY 181
Cdd:cd06639    89 YKADQYVGGQLWLVLELCNGGSVTELVKGLLKCGqrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVK 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 182 LSGLRSNLSMISHGQRQRVvhdfpkySVKVLPWLSPEVL---QQNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQM 258
Cdd:cd06639   169 LVDFGVSAQLTSARLRRNT-------SVGTPFWMAPEVIaceQQYDYSYDARCDVWSLGITAIELADGDPPLFDMHPVKA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 259 LLEKLNGTVPCLLdtstipaeeltmspsrsvansglsdslttstprpsngdspsHPyhRTFSPHFHHFVEQCLQRNPDAR 338
Cdd:cd06639   242 LFKIPRNPPPTLL-----------------------------------------NP--EKWCRGFSHFISQCLIKDFEKR 278
                         330
                  ....*....|...
gi 1394533236 339 PSASTLLNHSFFK 351
Cdd:cd06639   279 PSVTHLLEHPFIK 291
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
40-349 3.30e-29

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: 114.36  E-value: 3.30e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKG-FEDlmtVNLARYKPTGEYVTVRRINLEACSNemVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVT 118
Cdd:cd06646    11 YELIQRVGSGtYGD---VYKARNLHTGELAAVKIIKLEPGDD--FSLIQQEIFMVKECKHCNIVAYFGSYLSREKLWICM 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 119 SFMAYGSAKDLIctHFMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMISHGQRQ 198
Cdd:cd06646    86 EYCGGGSLQDIY--HVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVAAKITATIAKR 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 199 RVVHDFPKysvkvlpWLSPEV--LQQNlQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLleklngtvpclldtsti 276
Cdd:cd06646   164 KSFIGTPY-------WMAPEVaaVEKN-GGYNQLCDIWAVGITAIELAELQPPMFDLHPMRAL----------------- 218
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1394533236 277 paeeLTMSpsrsvansglsdslttstprPSNGDSPSHPYHRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSF 349
Cdd:cd06646   219 ----FLMS--------------------KSNFQPPKLKDKTKWSSTFHNFVKISLTKNPKKRPTAERLLTHLF 267
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
40-352 7.40e-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: 113.60  E-value: 7.40e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKG-FEDlmtVNLARYKPTGEYVTVRRINLEacSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVT 118
Cdd:cd06645    13 FELIQRIGSGtYGD---VYKARNVNTGELAAIKVIKLE--PGEDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKLWICM 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 119 SFMAYGSAKDLIctHFMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMISHGQRQ 198
Cdd:cd06645    88 EFCGGGSLQDIY--HVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQITATIAKR 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 199 RVVHDFPKysvkvlpWLSPEVLQ-QNLQGYDAKSDIYSVGITACELANGHVPFKDM-PATQMLLeklngtvpclldtsti 276
Cdd:cd06645   166 KSFIGTPY-------WMAPEVAAvERKGGYNQLCDIWAVGITAIELAELQPPMFDLhPMRALFL---------------- 222
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1394533236 277 paeeltmspsrsvansglsdsLTTSTPRPsngdsPSHPYHRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQ 352
Cdd:cd06645   223 ---------------------MTKSNFQP-----PKLKDKMKWSNSFHHFVKMALTKNPKKRPTAEKLLQHPFVTQ 272
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
59-365 1.62e-28

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: 113.20  E-value: 1.62e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  59 ARYKPTGEYVTVRRI---NLEACSNEMVtflqgELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAyGSAKDLICTHFM 135
Cdd:cd06644    31 AKNKETGALAAAKVIetkSEEELEDYMV-----EIEILATCNHPYIVKLLGAFYWDGKLWIMIEFCP-GGAVDAIMLELD 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 136 DGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMISHGQRQRVVHDFPKysvkvlpWL 215
Cdd:cd06644   105 RGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSAKNVKTLQRRDSFIGTPY-------WM 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 216 SPEVLQ-QNLQG--YDAKSDIYSVGITACELANGHVPFKDMPATQMLLEklngtvpclldtstipaeeltmspsrsVANS 292
Cdd:cd06644   178 APEVVMcETMKDtpYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLK---------------------------IAKS 230
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1394533236 293 glsdslttstpRPSNGDSPShpyhrTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQIKrrASEALPELL 365
Cdd:cd06644   231 -----------EPPTLSQPS-----KWSMEFRDFLKTALDKHPETRPSAAQLLEHPFVSSVT--SNRPLRELV 285
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
46-366 6.55e-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: 112.05  E-value: 6.55e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  46 IGKGfeDLMTVNLARYKPTGEYVTVRRINLEA-CSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFmAYG 124
Cdd:cd06633    29 IGHG--SFGAVYFATNSHTNEVVAIKKMSYSGkQTNEKWQDIIKEVKFLQQLKHPNTIEYKGCYLKDHTAWLVMEY-CLG 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 125 SAKDLICTHfMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSnLSMIShgqrqrvvhdf 204
Cdd:cd06633   106 SASDLLEVH-KKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGS-ASIAS----------- 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 205 PKYSVKVLP-WLSPEVLQQNLQG-YDAKSDIYSVGITACELANGHVPFKDMPAtqmlleklngtvpclldtstipaeelt 282
Cdd:cd06633   173 PANSFVGTPyWMAPEVILAMDEGqYDGKVDIWSLGITCIELAERKPPLFNMNA--------------------------- 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 283 MSPSRSVANSglsdslttstprpsngDSPSHPYHRtFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKqiKRRASEALP 362
Cdd:cd06633   226 MSALYHIAQN----------------DSPTLQSNE-WTDSFRGFVDYCLQKIPQERPSSAELLRHDFVR--RERPPRVLI 286

                  ....
gi 1394533236 363 ELLR 366
Cdd:cd06633   287 DLIQ 290
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
46-368 8.21e-28

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: 111.23  E-value: 8.21e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  46 IGKGFEDLmtVNLARYKPTGEYVTVRRINLEACSNEMVTFlqGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGS 125
Cdd:cd06659    29 IGEGSTGV--VCIAREKHSGRQVAVKMMDLRKQQRRELLF--NEVVIMRDYQHPNVVEMYKSYLVGEELWVLMEYLQGGA 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 126 AKDLICThfmDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLrsnlsmishGQRQRVVHDFP 205
Cdd:cd06659   105 LTDIVSQ---TRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDF---------GFCAQISKDVP 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 206 KYSVKV-LP-WLSPEVLQQNLqgYDAKSDIYSVGITACELANGHVP-FKDMPATQMlleklngtvpclldtstipaEELT 282
Cdd:cd06659   173 KRKSLVgTPyWMAPEVISRCP--YGTEVDIWSLGIMVIEMVDGEPPyFSDSPVQAM--------------------KRLR 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 283 MSPSRSVANSglsdslttstprpsngdspshpyHRTfSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQIkrraseALP 362
Cdd:cd06659   231 DSPPPKLKNS-----------------------HKA-SPVLRDFLERMLVRDPQERATAQELLDHPFLLQT------GLP 280

                  ....*.
gi 1394533236 363 ELLRPV 368
Cdd:cd06659   281 ECLVPL 286
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
64-350 4.49e-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: 4.49e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  64 TGEYVTVRRINLEACSNEM---VTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTHfmDGMNE 140
Cdd:cd06625    24 TGRELAVKQVEIDPINTEAskeVKALECEIQLLKNLQHERIVQYYGCLQDEKSLSIFMEYMPGGSVKDEIKAY--GALTE 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 141 -LAIAYILQgVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNLSMISHGQRQRVVHDFPkYsvkvlpWLSP 217
Cdd:cd06625   102 nVTRKYTRQ-ILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGdfGASKRLQTICSSTGMKSVTGTP-Y------WMSP 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 218 EVLqqNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEklngtvpclldtstipaeeltmspsrsvansglsds 297
Cdd:cd06625   174 EVI--NGEGYGRKADIWSVGCTVVEMLTTKPPWAEFEPMAAIFK------------------------------------ 215
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1394533236 298 LTTSTPRPsngDSPSHpyhrtFSPHFHHFVEQCLQRNPDARPSASTLLNHSFF 350
Cdd:cd06625   216 IATQPTNP---QLPPH-----VSEDARDFLSLIFVRNKKQRPSAEELLSHSFV 260
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
40-358 7.72e-27

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: 108.66  E-value: 7.72e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGFEDlmTVNLARYKPTGEYVTVRRINLEACSNEmvTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTS 119
Cdd:cd06656    21 YTRFEKIGQGASG--TVYTAIDIATGQEVAIKQMNLQQQPKK--ELIINEILVMRENKNPNIVNYLDSYLVGDELWVVME 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 120 FMAYGSAKDLICTHFMDgmnELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLrSNLSMISHGQRQR 199
Cdd:cd06656    97 YLAGGSLTDVVTETCMD---EGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDF-GFCAQITPEQSKR 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 200 VVHDFPKYsvkvlpWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPF-KDMPATQMLLEKLNGTvpclldtstipa 278
Cdd:cd06656   173 STMVGTPY------WMAPEVVTR--KAYGPKVDIWSLGIMAIEMVEGEPPYlNENPLRALYLIATNGT------------ 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 279 EELtMSPSRsvansglsdslttstprpsngdspshpyhrtFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQIKRRAS 358
Cdd:cd06656   233 PEL-QNPER-------------------------------LSAVFRDFLNRCLEMDVDRRGSAKELLQHPFLKLAKPLSS 280
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
40-345 9.46e-27

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: 107.29  E-value: 9.46e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfedLM-TVNLARYKPTGEYVTVRRINLEACSN-EMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVV 117
Cdd:cd14014     2 YRLVRLLGRG---GMgEVYRARDTLLGRPVAIKVLRPELAEDeEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 118 tsfMAYGSAKDLicTHFMDGMNEL----AIAYILQgVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNLSM 191
Cdd:cd14014    79 ---MEYVEGGSL--ADLLRERGPLppreALRILAQ-IADALAAAHRAGIVHRDIKPANILLTEDGRVKLTdfGIARALGD 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 192 ISHGQRQRVVhdfpkYSvkvLPWLSPEVLQqnLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVpcll 271
Cdd:cd14014   153 SGLTQTGSVL-----GT---PAYMAPEQAR--GGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAP---- 218
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1394533236 272 dtstipaeeltmsPSRSVANSGLSDSLTTstprpsngdspshpyhrtfsphfhhFVEQCLQRNPDARP-SASTLL 345
Cdd:cd14014   219 -------------PPPSPLNPDVPPALDA-------------------------IILRALAKDPEERPqSAAELL 255
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
40-350 1.23e-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: 107.16  E-value: 1.23e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKG-FEdlmTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVt 118
Cdd:cd08215     2 YEKIRVIGKGsFG---SAYLVRRKSDGKLYVLKEIDLSNMSEKEREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIV- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 119 sfMAYGSAKDL---ICTHFMDG--MNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GL-RsnlS 190
Cdd:cd08215    78 --MEYADGGDLaqkIKKQKKKGqpFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGdfGIsK---V 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 191 MISHGQRQRVVHDFPKYsvkvlpwLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPF--KDMPAtqmLLEK-LNGTV 267
Cdd:cd08215   153 LESTTDLAKTVVGTPYY-------LSPELCEN--KPYNYKSDIWALGCVLYELCTLKHPFeaNNLPA---LVYKiVKGQY 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 268 PclldtsTIPAeeltmspsrsvansglsdslttstprpsngdspshpyhrTFSPHFHHFVEQCLQRNPDARPSASTLLNH 347
Cdd:cd08215   221 P------PIPS---------------------------------------QYSSELRDLVNSMLQKDPEKRPSANEILSS 255

                  ...
gi 1394533236 348 SFF 350
Cdd:cd08215   256 PFI 258
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
30-349 6.37e-26

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: 105.86  E-value: 6.37e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  30 MSSFLPEGGCYELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVtflQGELHVSKLFNH-PNIVPYRATF 108
Cdd:cd06636     8 LSALRDPAGIFELVEVVGNG--TYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEI---KLEINMLKKYSHhRNIATYYGAF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 109 IA------DNELWVVTSFMAYGSAKDLICTHFMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYL 182
Cdd:cd06636    83 IKksppghDDQLWLVMEFCGAGSVTDLVKNTKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 183 S--GLRSNLSMiSHGQRQRVVHDfpKYsvkvlpWLSPEVL--QQNLQG-YDAKSDIYSVGITACELANGHVPFKDM-PAT 256
Cdd:cd06636   163 VdfGVSAQLDR-TVGRRNTFIGT--PY------WMAPEVIacDENPDAtYDYRSDIWSLGITAIEMAEGAPPLCDMhPMR 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 257 QMLLeklngtvpclldtstipaeeltmspsrsvansglsdslttsTPRpsngDSPSHPYHRTFSPHFHHFVEQCLQRNPD 336
Cdd:cd06636   234 ALFL-----------------------------------------IPR----NPPPKLKSKKWSKKFIDFIEGCLVKNYL 268
                         330
                  ....*....|...
gi 1394533236 337 ARPSASTLLNHSF 349
Cdd:cd06636   269 SRPSTEQLLKHPF 281
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
26-349 9.45e-26

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: 105.48  E-value: 9.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  26 KQEVMSSFLPEGGCYELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVtflQGELHVSK-LFNHPNIVP- 103
Cdd:cd06638     6 KTIIFDSFPDPSDTWEIIETIGKG--TYGKVFKVLNKKNGSKAAVKILDPIHDIDEEI---EAEYNILKaLSDHPNVVKf 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 104 ----YRATFIADNELWVVTSFMAYGSAKDLICTHFMDG--MNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVD 177
Cdd:cd06638    81 ygmyYKKDVKNGDQLWLVLELCNGGSVTDLVKGFLKRGerMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 178 GKVYLS--GLRSNLSMISHGQRQRVVHDFpkysvkvlpWLSPEVL---QQNLQGYDAKSDIYSVGITACELANGHVPFKD 252
Cdd:cd06638   161 GGVKLVdfGVSAQLTSTRLRRNTSVGTPF---------WMAPEVIaceQQLDSTYDARCDVWSLGITAIELGDGDPPLAD 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 253 MPATQMLLEklngtvpclldtstIPaeeltmspsrsvansglsdslttSTPRPsngdSPSHPyhRTFSPHFHHFVEQCLQ 332
Cdd:cd06638   232 LHPMRALFK--------------IP-----------------------RNPPP----TLHQP--ELWSNEFNDFIRKCLT 268
                         330
                  ....*....|....*..
gi 1394533236 333 RNPDARPSASTLLNHSF 349
Cdd:cd06638   269 KDYEKRPTVSDLLQHVF 285
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
40-358 1.00e-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: 105.58  E-value: 1.00e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGFEDlmTVNLARYKPTGEYVTVRRINLEACSNEmvTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTS 119
Cdd:cd06654    22 YTRFEKIGQGASG--TVYTAMDVATGQEVAIRQMNLQQQPKK--ELIINEILVMRENKNPNIVNYLDSYLVGDELWVVME 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 120 FMAYGSAKDLICTHFMDgmnELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLrSNLSMISHGQRQR 199
Cdd:cd06654    98 YLAGGSLTDVVTETCMD---EGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDF-GFCAQITPEQSKR 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 200 VVHDFPKYsvkvlpWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFkdmpatqmlleklngtvpclldtstipae 279
Cdd:cd06654   174 STMVGTPY------WMAPEVVTR--KAYGPKVDIWSLGIMAIEMIEGEPPY----------------------------- 216
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1394533236 280 eLTMSPSRSvansgLSDSLTTSTPRPSNGDSpshpyhrtFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQIKRRAS 358
Cdd:cd06654   217 -LNENPLRA-----LYLIATNGTPELQNPEK--------LSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLKIAKPLSS 281
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
43-366 2.44e-25

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: 105.13  E-value: 2.44e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  43 LTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEA-CSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFm 121
Cdd:cd06635    30 LREIGHG--SFGAVYFARDVRTSEVVAIKKMSYSGkQSNEKWQDIIKEVKFLQRIKHPNSIEYKGCYLREHTAWLVMEY- 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 122 AYGSAKDLICTHfMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSnLSMIShgqrqrvv 201
Cdd:cd06635   107 CLGSASDLLEVH-KKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGS-ASIAS-------- 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 202 hdfPKYSVKVLP-WLSPEVLQQNLQG-YDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPCLLDTStipae 279
Cdd:cd06635   177 ---PANSFVGTPyWMAPEVILAMDEGqYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNESPTLQSNE----- 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 280 eltmspsrsvansglsdslttstprpsngdspshpyhrtFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFkqIKRRASE 359
Cdd:cd06635   249 ---------------------------------------WSDYFRNFVDSCLQKIPQDRPTSEELLKHMFV--LRERPET 287

                  ....*..
gi 1394533236 360 ALPELLR 366
Cdd:cd06635   288 VLIDLIQ 294
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
97-349 6.94e-25

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


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 102.80  E-value: 6.94e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  97 NHPNIVPYRATFIADNELWVVTSFMAyGSAKDLICTHFMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISV 176
Cdd:cd06643    60 DHPNIVKLLDAFYYENNLWILIEFCA-GGAVDAVMLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTL 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 177 DGKVYLSGLRSNLSMISHGQRQRVVHDFPKysvkvlpWLSPEVLQ---QNLQGYDAKSDIYSVGITACELANGHVPFKDM 253
Cdd:cd06643   139 DGDIKLADFGVSAKNTRTLQRRDSFIGTPY-------WMAPEVVMcetSKDRPYDYKADVWSLGVTLIEMAQIEPPHHEL 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 254 PATQMLLEKLNGTVPCLldtstipaeeltMSPSRsvansglsdslttstprpsngdspshpyhrtFSPHFHHFVEQCLQR 333
Cdd:cd06643   212 NPMRVLLKIAKSEPPTL------------AQPSR-------------------------------WSPEFKDFLRKCLEK 248
                         250
                  ....*....|....*.
gi 1394533236 334 NPDARPSASTLLNHSF 349
Cdd:cd06643   249 NVDARWTTSQLLQHPF 264
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
37-351 7.12e-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: 103.26  E-value: 7.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  37 GGCYELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVtflQGELHVSKLFNH-PNIVPYRATFIA----- 110
Cdd:cd06637     5 AGIFELVELVGNG--TYGQVYKGRHVKTGQLAAIKVMDVTGDEEEEI---KQEINMLKKYSHhRNIATYYGAFIKknppg 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 111 -DNELWVVTSFMAYGSAKDLICTHFMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNL 189
Cdd:cd06637    80 mDDQLWLVMEFCGAGSVTDLIKNTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 190 SMISHGQRQRVVHDFPKysvkvlpWLSPEVL--QQNLQG-YDAKSDIYSVGITACELANGHVPFKDMPatqmlleklngt 266
Cdd:cd06637   160 QLDRTVGRRNTFIGTPY-------WMAPEVIacDENPDAtYDFKSDLWSLGITAIEMAEGAPPLCDMH------------ 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 267 vpclldtstiPAEELTMSPSrsvansglsdsltTSTPRPSNgdspshpyhRTFSPHFHHFVEQCLQRNPDARPSASTLLN 346
Cdd:cd06637   221 ----------PMRALFLIPR-------------NPAPRLKS---------KKWSKKFQSFIESCLVKNHSQRPSTEQLMK 268

                  ....*
gi 1394533236 347 HSFFK 351
Cdd:cd06637   269 HPFIR 273
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
43-352 1.41e-24

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: 102.79  E-value: 1.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  43 LTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEA-CSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFm 121
Cdd:cd06634    20 LREIGHG--SFGAVYFARDVRNNEVVAIKKMSYSGkQSNEKWQDIIKEVKFLQKLRHPNTIEYRGCYLREHTAWLVMEY- 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 122 AYGSAKDLICTHfMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSnLSMIShgqrqrvv 201
Cdd:cd06634    97 CLGSASDLLEVH-KKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFGS-ASIMA-------- 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 202 hdfPKYSVKVLP-WLSPEVLQQNLQG-YDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPCLLDTStipae 279
Cdd:cd06634   167 ---PANSFVGTPyWMAPEVILAMDEGqYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNESPALQSGH----- 238
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1394533236 280 eltmspsrsvansglsdslttstprpsngdspshpyhrtFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQ 352
Cdd:cd06634   239 ---------------------------------------WSEYFRNFVDSCLQKIPQDRPTSDVLLKHRFLLR 272
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
46-358 1.81e-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: 102.11  E-value: 1.81e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  46 IGKGFEDlmTVNLARYKPTGEYVTVRRINLEACSNEmvTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGS 125
Cdd:cd06655    27 IGQGASG--TVFTAIDVATGQEVAIKQINLQKQPKK--ELIINEILVMKELKNPNIVNFLDSFLVGDELFVVMEYLAGGS 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 126 AKDLICTHFMDgmnELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLrSNLSMISHGQRQRVVHDFP 205
Cdd:cd06655   103 LTDVVTETCMD---EAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDF-GFCAQITPEQSKRSTMVGT 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 206 KYsvkvlpWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFkdmpatqmlleklngtvpclldtstipaeeLTMSP 285
Cdd:cd06655   179 PY------WMAPEVVTR--KAYGPKVDIWSLGIMAIEMVEGEPPY------------------------------LNENP 220
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1394533236 286 SRSvansgLSDSLTTSTPRPSNGDSpshpyhrtFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQIKRRAS 358
Cdd:cd06655   221 LRA-----LYLIATNGTPELQNPEK--------LSPIFRDFLNRCLEMDVEKRGSAKELLQHPFLKLAKPLSS 280
Pkinase pfam00069
Protein kinase domain;
40-350 2.04e-24

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 100.01  E-value: 2.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKG-FEdlmTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVT 118
Cdd:pfam00069   1 YEVLRKLGSGsFG---TVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 119 SFMAYGSAKDLICTHFMDGMNElAIAYILQgVLKALDyihhmgyvhRSVKASHILISVDgkvylsglrsnlsmishgqrq 198
Cdd:pfam00069  78 EYVEGGSLFDLLSEKGAFSERE-AKFIMKQ-ILEGLE---------SGSSLTTFVGTPW--------------------- 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 199 rvvhdfpkysvkvlpWLSPEVLQQNlqGYDAKSDIYSVGITACELANGHVPFKDmpatqmlleklngtvpcllDTSTIPA 278
Cdd:pfam00069 126 ---------------YMAPEVLGGN--PYGPKVDVWSLGCILYELLTGKPPFPG-------------------INGNEIY 169
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1394533236 279 EELTMSPSRsvansglsdslttstprpsngdSPSHPYhrTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFF 350
Cdd:pfam00069 170 ELIIDQPYA----------------------FPELPS--NLSEEAKDLLKKLLKKDPSKRLTATQALQHPWF 217
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
64-349 2.30e-24

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: 100.97  E-value: 2.30e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  64 TGEYVTVRRINLEACSNEMVTF----LQGELHVSKLFNHPNIVPYRATFIADNelwVVTSFMAY---GSAKDLIcTHFMD 136
Cdd:cd06631    24 TGQLIAVKQVELDTSDKEKAEKeyekLQEEVDLLKTLKHVNIVGYLGTCLEDN---VVSIFMEFvpgGSIASIL-ARFGA 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 137 GMNELAIAY---ILQGVlkalDYIHHMGYVHRSVKASHILISVDGKVYL------SGLRSNLSMISHGQRQRVVHDFPkY 207
Cdd:cd06631   100 LEEPVFCRYtkqILEGV----AYLHNNNVIHRDIKGNNIMLMPNGVIKLidfgcaKRLCINLSSGSQSQLLKSMRGTP-Y 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 208 svkvlpWLSPEVLqqNLQGYDAKSDIYSVGITACELANGHVPFKDMPatqmlleklngtvpclldtstipaeeltmsPSR 287
Cdd:cd06631   175 ------WMAPEVI--NETGHGRKSDIWSIGCTVFEMATGKPPWADMN------------------------------PMA 216
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1394533236 288 SVANSGlsdslttstprpsNGDSPSHPYHRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSF 349
Cdd:cd06631   217 AIFAIG-------------SGRKPVPRLPDKFSPEARDFVHACLTRDQDERPSAEQLLKHPF 265
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
40-349 3.39e-24

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: 100.24  E-value: 3.39e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKG-FEdlmTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVT 118
Cdd:cd05117     2 YELGKVLGRGsFG---VVRLAVHKKTGEEYAVKIIDKKKLKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 119 SFMAYGSAKDLICTHFMdgMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILI---SVDGKVYLS--GLRsnlSMIS 193
Cdd:cd05117    79 ELCTGGELFDRIVKKGS--FSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLaskDPDSPIKIIdfGLA---KIFE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 194 HGQRQRVVHDFPKYsvkvlpwLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFkDMPATQMLLEK-LNGtvpclld 272
Cdd:cd05117   154 EGEKLKTVCGTPYY-------VAPEVLKG--KGYGKKCDIWSLGVILYILLCGYPPF-YGETEQELFEKiLKG------- 216
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1394533236 273 tstipaeELTMSPsrsvansglsdslttstprpsngdspshPYHRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSF 349
Cdd:cd05117   217 -------KYSFDS----------------------------PEWKNVSEEAKDLIKRLLVVDPKKRLTAAEALNHPW 258
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
55-353 6.25e-24

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: 99.15  E-value: 6.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  55 TVNLARYKptGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLIctHF 134
Cdd:cd13999     8 EVYKGKWR--GTDVAIKKLKVEDDNDELLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSLYDLL--HK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 135 MDG-MNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNLSmishgqrqrvvHDFPKYSVKV 211
Cdd:cd13999    84 KKIpLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIAdfGLSRIKN-----------STTEKMTGVV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 212 --LPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEklngtvpclldtstipaeeltmspsrsV 289
Cdd:cd13999   153 gtPRWMAPEVLRG--EPYTEKADVYSFGIVLWELLTGEVPFKELSPIQIAAA---------------------------V 203
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1394533236 290 ANSGLsdslttstpRPsngdspshPYHRTFSPHFHHFVEQCLQRNPDARPSastllnhsfFKQI 353
Cdd:cd13999   204 VQKGL---------RP--------PIPPDCPPELSKLIKRCWNEDPEKRPS---------FSEI 241
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
46-259 4.05e-23

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: 98.19  E-value: 4.05e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  46 IGKGFEDLmtVNLARYKPTGEYVTVRRINLEACSNEMVTFlqGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGS 125
Cdd:cd06658    30 IGEGSTGI--VCIATEKHTGKQVAVKKMDLRKQQRRELLF--NEVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLEGGA 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 126 AKDLIcTHfmDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLrsnlsmishGQRQRVVHDFP 205
Cdd:cd06658   106 LTDIV-TH--TRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDF---------GFCAQVSKEVP 173
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1394533236 206 KYS--VKVLPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQML 259
Cdd:cd06658   174 KRKslVGTPYWMAPEVISR--LPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAM 227
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
46-356 7.19e-23

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: 97.44  E-value: 7.19e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  46 IGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVP-YRATFiADNELWVVTSFM--- 121
Cdd:cd06616    14 IGRG--AFGTVNKMLHKPSGTIMAVKRIRSTVDEKEQKRLLMDLDVVMRSSDCPYIVKfYGALF-REGDCWICMELMdis 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 122 -------AYGSAKDLIcthfmdgmNELAIAYILQGVLKALDYI---HHMgyVHRSVKASHILISVDGKVYLSGLRsnlsm 191
Cdd:cd06616    91 ldkfykyVYEVLDSVI--------PEEILGKIAVATVKALNYLkeeLKI--IHRDVKPSNILLDRNGNIKLCDFG----- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 192 IShGQRQRVV---HDfpkysVKVLPWLSPEVLQQN--LQGYDAKSDIYSVGITACELANGHVPFkdmPATQMLLEKLNGT 266
Cdd:cd06616   156 IS-GQLVDSIaktRD-----AGCRPYMAPERIDPSasRDGYDVRSDVWSLGITLYEVATGKFPY---PKWNSVFDQLTQV 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 267 VpclldtstipaeeltmspsrsvansglsdslttstprpsNGDSP--SHPYHRTFSPHFHHFVEQCLQRNPDARPSASTL 344
Cdd:cd06616   227 V---------------------------------------KGDPPilSNSEEREFSPSFVNFVNLCLIKDESKRPKYKEL 267
                         330
                  ....*....|..
gi 1394533236 345 LNHSFFKQIKRR 356
Cdd:cd06616   268 LKHPFIKMYEER 279
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
56-352 4.03e-22

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: 95.18  E-value: 4.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  56 VNLARYKPTGEYVTVRRINLEACSNEMVTFLQgELHVSKLFNH-PNIVPYRATFIADNELWvvtsfmaygsakdlICTHF 134
Cdd:cd06617    17 VDKMRHVPTGTIMAVKRIRATVNSQEQKRLLM-DLDISMRSVDcPYTVTFYGALFREGDVW--------------ICMEV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 135 MDG---------------MNELAIAYILQGVLKALDYIH-HMGYVHRSVKASHILISVDGKVYLS--GLRSNL--SM--- 191
Cdd:cd06617    82 MDTsldkfykkvydkgltIPEDILGKIAVSIVKALEYLHsKLSVIHRDVKPSNVLINRNGQVKLCdfGISGYLvdSVakt 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 192 ISHGQRqrvvhdfpkysvkvlPWLSPEVL--QQNLQGYDAKSDIYSVGITACELANGHVPFkdmpatqmlleklngtvpc 269
Cdd:cd06617   162 IDAGCK---------------PYMAPERInpELNQKGYDVKSDVWSLGITMIELATGRFPY------------------- 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 270 llDTSTIPAEELtmspsRSVAnsglsdslttstprpsNGDSPSHPyHRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSF 349
Cdd:cd06617   208 --DSWKTPFQQL-----KQVV----------------EEPSPQLP-AEKFSPEFQDFVNKCLKKNYKERPNYPELLQHPF 263

                  ...
gi 1394533236 350 FKQ 352
Cdd:cd06617   264 FEL 266
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
40-346 4.57e-22

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: 94.64  E-value: 4.57e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINL---------EACSNEmVTFLQGelhvsklFNHPNIVPYRATFIA 110
Cdd:cd08224     2 YEIEKKIGKG--QFSVVYRARCLLDGRLVALKKVQIfemmdakarQDCLKE-IDLLQQ-------LNHPNIIKYLASFIE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 111 DNELWVVTSFMAYGSAKDLIcTHFMD---GMNELAI-AYILQgVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGL- 185
Cdd:cd08224    72 NNELNIVLELADAGDLSRLI-KHFKKqkrLIPERTIwKYFVQ-LCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLg 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 186 --R--SNLSMISH---GQrqrvvhdfPKYsvkvlpwLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDmpatqm 258
Cdd:cd08224   150 lgRffSSKTTAAHslvGT--------PYY-------MSPERIRE--QGYDFKSDIWSLGCLLYEMAALQSPFYG------ 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 259 llEKLNgtvpclldtstipaeeltmspsrsvansglsdsLTTSTPRPSNGDSPSHPYHRtFSPHFHHFVEQCLQRNPDAR 338
Cdd:cd08224   207 --EKMN---------------------------------LYSLCKKIEKCEYPPLPADL-YSQELRDLVAACIQPDPEKR 250

                  ....*...
gi 1394533236 339 PSASTLLN 346
Cdd:cd08224   251 PDISYVLD 258
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
45-349 5.96e-22

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


Pssm-ID: 270798 [Multi-domain]  Cd Length: 267  Bit Score: 94.52  E-value: 5.96e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  45 VIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNE-------MVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVV 117
Cdd:cd06628     7 LIGSG--SFGSVYLGMNASSGELMAVKQVELPSVSAEnkdrkksMLDALQREIALLRELQHENIVQYLGSSSDANHLNIF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 118 TSFMAYGSAKDLICTHfmDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSG------LRSN-LS 190
Cdd:cd06628    85 LEYVPGGSVATLLNNY--GAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDfgiskkLEANsLS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 191 MISHGQRqrvvhdfPKYSVKVLpWLSPEVLQQNLqgYDAKSDIYSVGITACELANGHVPFKDMPATQMLLeKLNGTVpcl 270
Cdd:cd06628   163 TKNNGAR-------PSLQGSVF-WMAPEVVKQTS--YTRKADIWSLGCLVVEMLTGTHPFPDCTQMQAIF-KIGENA--- 228
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1394533236 271 ldTSTIPaeeltmspsrsvansglsdSLTTSTPRpsngdspshpyhrtfsphfhHFVEQCLQRNPDARPSASTLLNHSF 349
Cdd:cd06628   229 --SPTIP-------------------SNISSEAR--------------------DFLEKTFEIDHNKRPTADELLKHPF 266
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
55-351 7.57e-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: 94.75  E-value: 7.57e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  55 TVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTHf 134
Cdd:cd06618    30 QVYKMRHKKTGHVMAVKQMRRSGNKEENKRILMDLDVVLKSHDCPYIVKCYGYFITDSDVFICMELMSTCLDKLLKRIQ- 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 135 mDGMNELAIAYILQGVLKALDYI--HHmGYVHRSVKASHILISVDGKVYLSGLRSNLSMISHGQRQRvvhdfpkySVKVL 212
Cdd:cd06618   109 -GPIPEDILGKMTVSIVKALHYLkeKH-GVIHRDVKPSNILLDESGNVKLCDFGISGRLVDSKAKTR--------SAGCA 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 213 PWLSPEVLQ-QNLQGYDAKSDIYSVGITACELANGHVPFkdmpatqmlleKLNGTvpclldtstipaeELTMspsrsvan 291
Cdd:cd06618   179 AYMAPERIDpPDNPKYDIRADVWSLGISLVELATGQFPY-----------RNCKT-------------EFEV-------- 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 292 sglsdsLTtstpRPSNGDSPSHPYHRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFK 351
Cdd:cd06618   227 ------LT----KILNEEPPSLPPNEGFSPDFCSFVDLCLTKDHRYRPKYRELLQHPFIR 276
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
46-349 9.40e-22

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: 93.99  E-value: 9.40e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  46 IGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNE--------MVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVV 117
Cdd:cd06629     9 IGKG--TYGRVYLAMNATTGEMLAVKQVELPKTSSDradsrqktVVDALKSEIDTLKDLDHPNIVQYLGFEETEDYFSIF 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 118 TSFMAYGSAKDLICTHfmDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS------------GL 185
Cdd:cd06629    87 LEYVPGGSIGSCLRKY--GKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISdfgiskksddiyGN 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 186 RSNLSMishgqrqrvvhdfpKYSVkvlPWLSPEVLQQNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNg 265
Cdd:cd06629   165 NGATSM--------------QGSV---FWMAPEVIHSQGQGYSAKVDIWSLGCVVLEMLAGRRPWSDDEAIAAMFKLGN- 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 266 tvpclldtstipaeeltmspSRSvansglsdslttstprpsngdSPSHPYHRTFSPHFHHFVEQCLQRNPDARPSASTLL 345
Cdd:cd06629   227 --------------------KRS---------------------APPVPEDVNLSPEALDFLNACFAIDPRDRPTAAELL 265

                  ....
gi 1394533236 346 NHSF 349
Cdd:cd06629   266 SHPF 269
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
46-352 1.22e-21

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: 93.93  E-value: 1.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  46 IGKGFEDLmtVNLARYKPTGEYVTVRRINLEACSNEMVTFlqGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGS 125
Cdd:cd06657    28 IGEGSTGI--VCIATVKSSGKLVAVKKMDLRKQQRRELLF--NEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGA 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 126 AKDLIcTHfmDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMISHGQRQRVVHDFP 205
Cdd:cd06657   104 LTDIV-TH--TRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTP 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 206 KysvkvlpWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPatqmlleklngtvpclldtstiPAEELTMsp 285
Cdd:cd06657   181 Y-------WMAPELISR--LPYGPEVDIWSLGIMVIEMVDGEPPYFNEP----------------------PLKAMKM-- 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1394533236 286 srsvansgLSDSLttsTPRPSNGdspshpyhRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQ 352
Cdd:cd06657   228 --------IRDNL---PPKLKNL--------HKVSPSLKGFLDRLLVRDPAQRATAAELLKHPFLAK 275
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
40-351 1.32e-21

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: 94.04  E-value: 1.32e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLE---ACSNEMVTflqgELHVSKLFNHPNIVPYRATFIADNELwv 116
Cdd:cd06615     3 FEKLGELGAG--NGGVVTKVLHRPSGLIMARKLIHLEikpAIRNQIIR----ELKVLHECNSPYIVGFYGAFYSDGEI-- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 117 vtsfmaygsakdLICTHFMDG------------MNELAIAYILQGVLKALDYI---HHMgyVHRSVKASHILISVDGKVY 181
Cdd:cd06615    75 ------------SICMEHMDGgsldqvlkkagrIPENILGKISIAVLRGLTYLrekHKI--MHRDVKPSNILVNSRGEIK 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 182 LS--GLRSNL--SMISH--GQRQrvvhdfpkysvkvlpWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKdmPA 255
Cdd:cd06615   141 LCdfGVSGQLidSMANSfvGTRS---------------YMSPERLQG--THYTVQSDIWSLGLSLVEMAIGRYPIP--PP 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 256 TQMLLEKLNGTvpclldtstiPAEELTMSPSRSVANSGLSDSlttstPRPS----------NGDSPSHPyHRTFSPHFHH 325
Cdd:cd06615   202 DAKELEAMFGR----------PVSEGEAKESHRPVSGHPPDS-----PRPMaifelldyivNEPPPKLP-SGAFSDEFQD 265
                         330       340
                  ....*....|....*....|....*.
gi 1394533236 326 FVEQCLQRNPDARPSASTLLNHSFFK 351
Cdd:cd06615   266 FVDKCLKKNPKERADLKELTKHPFIK 291
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
40-347 1.51e-21

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: 93.31  E-value: 1.51e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRIN-----LEACSNEMVtflQGELHVSKLFNHPNIVPYRATFIADNEL 114
Cdd:cd14098     2 YQIIDRLGSG--TFAEVKKAVEVETGKMRAIKQIVkrkvaGNDKNLQLF---QREINILKSLEHPGIVRLIDWYEDDQHI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 115 WVVTSFMAYGSAKDLICTHfmDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMISH 194
Cdd:cd14098    77 YLVMEYVEGGDLMDFIMAW--GAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDPVIVKISDFGLAKVIH 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 195 GQrqrvvhDFPKYSVKVLPWLSPEVL---QQNLQ-GYDAKSDIYSVGITACELANGHVPFKDmpATQMLLEKLngtvpcl 270
Cdd:cd14098   155 TG------TFLVTFCGTMAYLAPEILmskEQNLQgGYSNLVDMWSVGCLVYVMLTGALPFDG--SSQLPVEKR------- 219
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1394533236 271 ldtstIPAEELTMSPSRSVansglsdslttstprpsngdspshpyhrTFSPHFHHFVEQCLQRNPDARPSASTLLNH 347
Cdd:cd14098   220 -----IRKGRYTQPPLVDF----------------------------NISEEAIDFILRLLDVDPEKRMTAAQALDH 263
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
40-350 1.62e-21

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: 93.37  E-value: 1.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKG-FEdlmTVNLARYKPTGEYVTVRRI-----NLEACSN--EmVTFLQgelhvsKLFNHPNIVPYRATFIAD 111
Cdd:cd07830     1 YKVIKQLGDGtFG---SVYLARNKETGELVAIKKMkkkfySWEECMNlrE-VKSLR------KLNEHPNIVKLKEVFREN 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 112 NELWVVTSFMAyGSAKDLICTHFMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLrsnl 189
Cdd:cd07830    71 DELYFVFEYME-GNLYQLMKDRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIAdfGL---- 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 190 smishgqrQRVVHDFPKYSVKV-LPWL-SPEVLQQNlQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLE--KLNG 265
Cdd:cd07830   146 --------AREIRSRPPYTDYVsTRWYrAPEILLRS-TSYSSPVDIWALGCIMAELYTLRPLFPGSSEIDQLYKicSVLG 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 266 TvpclldtstiPAEElTMSPSRSVANSgLSDSLTTSTPRPSNGDSPSHpyhrtfSPHFHHFVEQCLQRNPDARPSASTLL 345
Cdd:cd07830   217 T----------PTKQ-DWPEGYKLASK-LGFRFPQFAPTSLHQLIPNA------SPEAIDLIKDMLRWDPKKRPTASQAL 278

                  ....*
gi 1394533236 346 NHSFF 350
Cdd:cd07830   279 QHPYF 283
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
55-356 2.32e-21

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


Pssm-ID: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 93.27  E-value: 2.32e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  55 TVNLARYKPTGEYVTVRRINLEAcSNEMVTFLQGELHVSKLFNHPNIVPYRATFIAD-NELWVVTSFMAYGSakdlicth 133
Cdd:cd06620    20 SVSKVLHIPTGTIMAKKVIHIDA-KSSVRKQILRELQILHECHSPYIVSFYGAFLNEnNNIIICMEYMDCGS-------- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 134 fMDGM-------NELAIAYILQGVLKALDYI---HHMgyVHRSVKASHILISVDGKVYLSGLrsnlsmishGQRQRVVHD 203
Cdd:cd06620    91 -LDKIlkkkgpfPEEVLGKIAVAVLEGLTYLynvHRI--IHRDIKPSNILVNSKGQIKLCDF---------GVSGELINS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 204 FPKYSVKVLPWLSPEVLQQNlqGYDAKSDIYSVGITACELANGHVPFkdmpatqmlleklngtvpclldtstipaeelTM 283
Cdd:cd06620   159 IADTFVGTSTYMSPERIQGG--KYSVKSDVWSLGLSIIELALGEFPF-------------------------------AG 205
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1394533236 284 SPSRSVANSGlSDSLTTSTPRPSNGDSPSHPYHRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQIKRR 356
Cdd:cd06620   206 SNDDDDGYNG-PMGILDLLQRIVNEPPPRLPKDRIFPKDLRDFVDRCLLKDPRERPSPQLLLDHDPFIQAVRA 277
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
41-346 1.22e-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: 90.30  E-value: 1.22e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236   41 ELLTVIGKGFedLMTVNLARYKPTGEY----VTVRRINLEACSNEMVTFLQgELHVSKLFNHPNIVPYRATFIADNELWV 116
Cdd:smart00221   2 TLGKKLGEGA--FGEVYKGTLKGKGDGkeveVAVKTLKEDASEQQIEEFLR-EARIMRKLDHPNIVKLLGVCTEEEPLMI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  117 VTSFMAYGSAKDLI--CTHFMDGMNELaIAYILQgVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLrsnlsmi 192
Cdd:smart00221  79 VMEYMPGGDLLDYLrkNRPKELSLSDL-LSFALQ-IARGMEYLESKNFIHRDLAARNCLVGENLVVKISdfGL------- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  193 shgqrQRVVHDFPKYSVKV--LP--WLSPEVLQQNLqgYDAKSDIYSVGITACELA-NGHVPFKDMPATQMLleklngtv 267
Cdd:smart00221 150 -----SRDLYDDDYYKVKGgkLPirWMAPESLKEGK--FTSKSDVWSFGVLLWEIFtLGEEPYPGMSNAEVL-------- 214
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1394533236  268 pclldtstipaeELTMSPSRsvansglsdslttsTPRPSNgdspshpyhrtFSPHFHHFVEQCLQRNPDARPSASTLLN 346
Cdd:smart00221 215 ------------EYLKKGYR--------------LPKPPN-----------CPPELYKLMLQCWAEDPEDRPTFSELVE 256
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
41-259 1.41e-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: 90.25  E-value: 1.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  41 ELLTVIGKG-FEdlmTVNLARYKPTGEY----VTVRRINLEACSNEMVTFLQgELHVSKLFNHPNIVPYRATFIADNELW 115
Cdd:pfam07714   2 TLGEKLGEGaFG---EVYKGTLKGEGENtkikVAVKTLKEGADEEEREDFLE-EASIMKKLDHPNIVKLLGVCTQGEPLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 116 VVTSFMAYGSAKDLICTHFmDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLrsnlsmis 193
Cdd:pfam07714  78 IVTEYMPGGDLLDFLRKHK-RKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISdfGL-------- 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1394533236 194 hgqrQRVVHDFPKYSVK---VLP--WLSPEVLQQNLqgYDAKSDIYSVGITACELA-NGHVPFKDMPATQML 259
Cdd:pfam07714 149 ----SRDIYDDDYYRKRgggKLPikWMAPESLKDGK--FTSKSDVWSFGVLLWEIFtLGEQPYPGMSNEEVL 214
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
55-352 4.86e-20

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: 89.17  E-value: 4.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  55 TVNLARYKPTGEYVTVRRINLEAcSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELwvvtsfmaygsakdLICTHF 134
Cdd:cd06619    16 TVYKAYHLLTRRILAVKVIPLDI-TVELQKQIMSELEILYKCDSPYIIGFYGAFFVENRI--------------SICTEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 135 MDG--------MNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLrsnlsmishGQRQRVVHDFPK 206
Cdd:cd06619    81 MDGgsldvyrkIPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDF---------GVSTQLVNSIAK 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 207 YSVKVLPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNgTVPCLLDTstipaeeltmsps 286
Cdd:cd06619   152 TYVGTNAYMAPERISG--EQYGIHSDVWSLGISFMELALGRFPYPQIQKNQGSLMPLQ-LLQCIVDE------------- 215
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1394533236 287 rsvansglsdslttstprpsngDSPSHPYHRtFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQ 352
Cdd:cd06619   216 ----------------------DPPVLPVGQ-FSEKFVHFITQCMRKQPKERPAPENLMDHPFIVQ 258
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
45-347 6.67e-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: 88.36  E-value: 6.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  45 VIGKG-FEDlmtVNLARYKPTGEY---VTVRRINLEACSNEMVTFLQgELHVSKLFNHPNIVPYRATFIADNELWVVTSF 120
Cdd:cd00192     2 KLGEGaFGE---VYKGKLKGGDGKtvdVAVKTLKEDASESERKDFLK-EARVMKKLGHPNVVRLLGVCTEEEPLYLVMEY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 121 MAYGSAKDLICTHFMD---------GMNELaIAYILQgVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GL-RSn 188
Cdd:cd00192    78 MEGGDLLDFLRKSRPVfpspepstlSLKDL-LSFAIQ-IAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISdfGLsRD- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 189 lsmISHGQRQRVVHDFPkysvkvLP--WLSPEVLQQNLqgYDAKSDIYSVGITACEL-ANGHVPFKDMPATQMlLEKL-N 264
Cdd:cd00192   155 ---IYDDDYYRKKTGGK------LPirWMAPESLKDGI--FTSKSDVWSFGVLLWEIfTLGATPYPGLSNEEV-LEYLrK 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 265 GTVPclldtstipaeeltmspsrsvansglsdslttstPRPSNgdspshpyhrtFSPHFHHFVEQCLQRNPDARPSASTL 344
Cdd:cd00192   223 GYRL----------------------------------PKPEN-----------CPDELYELMLSCWQLDPEDRPTFSEL 257

                  ...
gi 1394533236 345 LNH 347
Cdd:cd00192   258 VER 260
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
89-356 7.36e-20

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: 89.02  E-value: 7.36e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  89 ELHVSKLFNHPNIVPYRATFIADNE--LWVVTSFMAYGSAKDLICTHFMDGM--NELAIAYILQGVLKALDYIHHMGYVH 164
Cdd:cd06621    49 ELEINKSCASPYIVKYYGAFLDEQDssIGIAMEYCEGGSLDSIYKKVKKKGGriGEKVLGKIAESVLKGLSYLHSRKIIH 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 165 RSVKASHILISVDGKVYLSGLrsnlsmishGQRQRVVHDFPKYSVKVLPWLSPEVLQQnlQGYDAKSDIYSVGITACELA 244
Cdd:cd06621   129 RDIKPSNILLTRKGQVKLCDF---------GVSGELVNSLAGTFTGTSYYMAPERIQG--GPYSITSDVWSLGLTLLEVA 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 245 NGHVPF-KDMPATQMLLEKLNGTVpclldtsTIPAEELtmspsrsvansglsdslttsTPRPSNGdspshpyhRTFSPHF 323
Cdd:cd06621   198 QNRFPFpPEGEPPLGPIELLSYIV-------NMPNPEL--------------------KDEPENG--------IKWSESF 242
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1394533236 324 HHFVEQCLQRNPDARPSASTLLNHSFFKQIKRR 356
Cdd:cd06621   243 KDFIEKCLEKDGTRRPGPWQMLAHPWIKAQEKK 275
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
40-351 1.05e-19

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: 87.53  E-value: 1.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKG-FEdlmTVNLARYKPTGEYVTVRRINLEA-CSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVV 117
Cdd:cd14007     2 FEIGKPLGKGkFG---NVYLAREKKSGFIVALKVISKSQlQKSGLEHQLRREIEIQSHLRHPNILRLYGYFEDKKRIYLI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 118 TSFMAYGSAKDLI--CTHFMDgmnELAIAYILQgVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSglrsnlsmishg 195
Cdd:cd14007    79 LEYAPNGELYKELkkQKRFDE---KEAAKYIYQ-LALALDYLHSKNIIHRDIKPENILLGSNGELKLA------------ 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 196 qrqrvvhDFpKYSVKV-----------LPWLSPEVLqqNLQGYDAKSDIYSVGITACELANGHVPFKdMPATQMLLEKln 264
Cdd:cd14007   143 -------DF-GWSVHApsnrrktfcgtLDYLPPEMV--EGKEYDYKVDIWSLGVLCYELLVGKPPFE-SKSHQETYKR-- 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 265 gtvpclldtstIPAEELTMSPSrsvansglsdslttstprpsngdspshpyhrtFSPHFHHFVEQCLQRNPDARPSASTL 344
Cdd:cd14007   210 -----------IQNVDIKFPSS--------------------------------VSPEAKDLISKLLQKDPSKRLSLEQV 246

                  ....*..
gi 1394533236 345 LNHSFFK 351
Cdd:cd14007   247 LNHPWIK 253
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
41-345 2.30e-19

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 86.82  E-value: 2.30e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236   41 ELLTVIGKGFedLMTVNLARYKP----TGEYVTVRRINLEACSNEMVTFLQgELHVSKLFNHPNIVPYRATFIADNELWV 116
Cdd:smart00219   2 TLGKKLGEGA--FGEVYKGKLKGkggkKKVEVAVKTLKEDASEQQIEEFLR-EARIMRKLDHPNVVKLLGVCTEEEPLYI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  117 VTSFMAYGSAKDLICTHFMD-GMNELaIAYILQgVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLrsnlsmis 193
Cdd:smart00219  79 VMEYMEGGDLLSYLRKNRPKlSLSDL-LSFALQ-IARGMEYLESKNFIHRDLAARNCLVGENLVVKISdfGL-------- 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  194 hgqrQRVVHDFPKYSVKV--LP--WLSPEVLQQNLqgYDAKSDIYSVGITACELA-NGHVPFKDMPATQMLleklngtvp 268
Cdd:smart00219 149 ----SRDLYDDDYYRKRGgkLPirWMAPESLKEGK--FTSKSDVWSFGVLLWEIFtLGEQPYPGMSNEEVL--------- 213
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1394533236  269 clldtstipaeELTMSPSRsvansglsdslttsTPRPSNGdspshpyhrtfSPHFHHFVEQCLQRNPDARPSASTLL 345
Cdd:smart00219 214 -----------EYLKNGYR--------------LPQPPNC-----------PPELYDLMLQCWAEDPEDRPTFSELV 254
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
40-348 1.17e-18

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


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 84.75  E-value: 1.17e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTS 119
Cdd:cd08530     2 FKVLKKLGKG--SYGSVYKVKRLSDNQVYALKEVNLGSLSQKEREDSVNEIRLLASVNHPNIIRYKEAFLDGNRLCIVME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 120 FMAYGSAKDLICTHFMDG--MNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLrsNLSMISHGQR 197
Cdd:cd08530    80 YAPFGDLSKLISKRKKKRrlFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDL--GISKVLKKNL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 198 QRVVHDFPKYsvkvlpwLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPF--KDMpatqmllEKLNGTVpclldtst 275
Cdd:cd08530   158 AKTQIGTPLY-------AAPEVWKG--RPYDYKSDIWSLGCLLYEMATFRPPFeaRTM-------QELRYKV-------- 213
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1394533236 276 ipaeeltmspsrsvansglsdsLTTSTPRPSNgdspshpyhrTFSPHFHHFVEQCLQRNPDARPSASTLLNHS 348
Cdd:cd08530   214 ----------------------CRGKFPPIPP----------VYSQDLQQIIRSLLQVNPKKRPSCDKLLQSP 254
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
61-352 3.24e-18

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: 84.72  E-value: 3.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  61 YKPTGEYVTVRRINLE---ACSNEMVTflqgELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDliCTHFMDG 137
Cdd:cd06650    26 HKPSGLVMARKLIHLEikpAIRNQIIR----ELQVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQ--VLKKAGR 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 138 MNELAIAYILQGVLKALDYIHHMGYV-HRSVKASHILISVDGKVYLSGLrsnlsmishGQRQRVVHDFPKYSVKVLPWLS 216
Cdd:cd06650   100 IPEQILGKVSIAVIKGLTYLREKHKImHRDVKPSNILVNSRGEIKLCDF---------GVSGQLIDSMANSFVGTRSYMS 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 217 PEVLQQNlqGYDAKSDIYSVGITACELANGHVPFKdmPATQMLLEKLNGtvpCLLDTSTIPAEELTMSPSRSVANSG--- 293
Cdd:cd06650   171 PERLQGT--HYSVQSDIWSMGLSLVEMAVGRYPIP--PPDAKELELMFG---CQVEGDAAETPPRPRTPGRPLSSYGmds 243
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1394533236 294 --------LSDSLTTSTPrpsngdsPSHPyHRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQ 352
Cdd:cd06650   244 rppmaifeLLDYIVNEPP-------PKLP-SGVFSLEFQDFVNKCLIKNPAERADLKQLMVHAFIKR 302
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
64-349 4.72e-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: 83.12  E-value: 4.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  64 TGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVvtsFMAY---GSAKDLiCTHfMDGMNE 140
Cdd:cd06626    24 TGELMAMKEIRFQDNDPKTIKEIADEMKVLEGLDHPNLVRYYGVEVHREEVYI---FMEYcqeGTLEEL-LRH-GRILDE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 141 LAI-AYILQgVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSG------LRSNLSMISHGQRQRVVHDfPKYsvkvlp 213
Cdd:cd06626    99 AVIrVYTLQ-LLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDfgsavkLKNNTTTMAPGEVNSLVGT-PAY------ 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 214 wLSPEV-LQQNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLngtvpclldtstipaeeltmspsrsvans 292
Cdd:cd06626   171 -MAPEViTGNKGEGHGRAADIWSLGCVVLEMATGKRPWSELDNEWAIMYHV----------------------------- 220
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1394533236 293 glsdslttstprpSNGDSPSHPYHRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSF 349
Cdd:cd06626   221 -------------GMGHKPPIPDSLQLSPEGKDFLSRCLESDPKKRPTASELLDHPF 264
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
40-350 1.46e-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: 82.37  E-value: 1.46e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRInLEACSNEMV--TFLQgELHVSKLFNHPNIVPYRATFIADNELWVV 117
Cdd:cd07833     3 YEVLGVVGEG--AYGVVLKCRNKATGEIVAIKKF-KESEDDEDVkkTALR-EVKVLRQLRHENIVNLKEAFRRKGRLYLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 118 TSFMAYGSAKDLicTHFMDGMNELAI-AYILQgVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNLsmisH 194
Cdd:cd07833    79 FEYVERTLLELL--EASPGGLPPDAVrSYIWQ-LLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCdfGFARAL----T 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 195 GQRQRVVHDFpkysVKVLPWLSPEVLQQNLQgYDAKSDIYSVGITACELANGHVPFkdmPAT----QM-LLEKLNGTVPc 269
Cdd:cd07833   152 ARPASPLTDY----VATRWYRAPELLVGDTN-YGKPVDVWAIGCIMAELLDGEPLF---PGDsdidQLyLIQKCLGPLP- 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 270 lldtstiPAE-ELTMSPSRsvaNSGLsdslttSTPRPSNGDSPSHPYHRTFSPHFHHFVEQCLQRNPDARPSASTLLNHS 348
Cdd:cd07833   223 -------PSHqELFSSNPR---FAGV------AFPEPSQPESLERRYPGKVSSPALDFLKACLRMDPKERLTCDELLQHP 286

                  ..
gi 1394533236 349 FF 350
Cdd:cd07833   287 YF 288
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
46-251 1.75e-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: 81.50  E-value: 1.75e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  46 IGKG-FEdlmTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYG 124
Cdd:cd14009     1 IGRGsFA---TVWKGRHKQTGEVVAIKEISRKKLNKKLQENLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAGG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 125 SAKDLICTHFmdGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDG-----KVYLSGL-RSnlsmISHGQRQ 198
Cdd:cd14009    78 DLSQYIRKRG--RLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGddpvlKIADFGFaRS----LQPASMA 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1394533236 199 RVVHDFPKYsvkvlpwLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFK 251
Cdd:cd14009   152 ETLCGSPLY-------MAPEILQF--QKYDAKADLWSVGAILFEMLVGKPPFR 195
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
40-268 1.83e-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: 81.57  E-value: 1.83e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGFEDlmTVNLARYKPTGEYVTVRRINL-EACSNEMVTFLQGELHVSklFNHPNIVPYRATFIADNELWVVT 118
Cdd:cd13996     8 FEEIELLGSGGFG--SVYKVRNKVDGVTYAIKKIRLtEKSSASEKVLREVKALAK--LNHPNIVRYYTAWVEEPPLYIQM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 119 SFMAYGSAKDLI--CTHFMDGMNELAIAYILQgVLKALDYIHHMGYVHRSVKASHILISVDGKVY------LSGLRSNLS 190
Cdd:cd13996    84 ELCEGGTLRDWIdrRNSSSKNDRKLALELFKQ-ILKGVSYIHSKGIVHRDLKPSNIFLDNDDLQVkigdfgLATSIGNQK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 191 MISHGQRQRVVHDFPKYSVKV--LPWLSPEVLQQNLqgYDAKSDIYSVGITACELangHVPFKdmpaTQM----LLEKL- 263
Cdd:cd13996   163 RELNNLNNNNNGNTSNNSVGIgtPLYASPEQLDGEN--YNEKADIYSLGIILFEM---LHPFK----TAMerstILTDLr 233

                  ....*
gi 1394533236 264 NGTVP 268
Cdd:cd13996   234 NGILP 238
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
40-269 1.88e-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: 81.30  E-value: 1.88e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLE-ACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVT 118
Cdd:cd14663     2 YELGRTLGEG--TFAKVKFARNTKTGESVAIKIIDKEqVAREGMVEQIKREIAIMKLLRHPNIVELHEVMATKTKIFFVM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 119 SFMAYGSAKDLICTHfmDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLrSNLSmiSHGQ 196
Cdd:cd14663    80 ELVTGGELFSKIAKN--GRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISdfGL-SALS--EQFR 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1394533236 197 RQRVVHDF---PKYsvkvlpwLSPEVLQQNlqGYD-AKSDIYSVGITACELANGHVPFKDmPATQMLLEKL-NGTVPC 269
Cdd:cd14663   155 QDGLLHTTcgtPNY-------VAPEVLARR--GYDgAKADIWSCGVILFVLLAGYLPFDD-ENLMALYRKImKGEFEY 222
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
40-350 2.07e-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. 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: 81.76  E-value: 2.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfedlmT---VNLARYKPTGEYVTVRRINLEACSNEM-VTFLQgELHVSKLFNHPNIVPYRATFIADNELW 115
Cdd:cd07829     1 YEKLEKLGEG-----TygvVYKAKDKKTGEIVALKKIRLDNEEEGIpSTALR-EISLLKELKHPNIVKLLDVIHTENKLY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 116 VVTSFMAYgsakDLicTHFMD----GMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GL-RSn 188
Cdd:cd07829    75 LVFEYCDQ----DL--KKYLDkrpgPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLAdfGLaRA- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 189 lsmishgqrqrVVHDFPKYSVKVL-PW-LSPEVLQQNlQGYDAKSDIYSVG-ITAcELANGHVPFkdmPATQ---MLLE- 261
Cdd:cd07829   148 -----------FGIPLRTYTHEVVtLWyRAPEILLGS-KHYSTAVDIWSVGcIFA-ELITGKPLF---PGDSeidQLFKi 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 262 -KLNGTvpclldtstiPAEE----LTMSPSRSVansglsdslttSTPRPsngdsPSHPYHRTFSPHFHHFVE---QCLQR 333
Cdd:cd07829   212 fQILGT----------PTEEswpgVTKLPDYKP-----------TFPKW-----PKNDLEKVLPRLDPEGIDllsKMLQY 265
                         330
                  ....*....|....*..
gi 1394533236 334 NPDARPSASTLLNHSFF 350
Cdd:cd07829   266 NPAKRISAKEALKHPYF 282
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
56-352 3.06e-17

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: 82.02  E-value: 3.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  56 VNLARYKPTGEYVTVRRINLE---ACSNEMVTflqgELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICT 132
Cdd:cd06649    21 VTKVQHKPSGLIMARKLIHLEikpAIRNQIIR----ELQVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQVLKE 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 133 hfMDGMNELAIAYILQGVLKALDYIHHMGYV-HRSVKASHILISVDGKVYLSGLrsnlsmishGQRQRVVHDFPKYSVKV 211
Cdd:cd06649    97 --AKRIPEEILGKVSIAVLRGLAYLREKHQImHRDVKPSNILVNSRGEIKLCDF---------GVSGQLIDSMANSFVGT 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 212 LPWLSPEVLQQNlqGYDAKSDIYSVGITACELANGHVPFKdmPATQMLLEKLNGTVpcLLDTSTipAEELTMSP-----S 286
Cdd:cd06649   166 RSYMSPERLQGT--HYSVQSDIWSMGLSLVELAIGRYPIP--PPDAKELEAIFGRP--VVDGEE--GEPHSISPrprppG 237
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1394533236 287 RSVANSGLsDSlttstpRPS-----------NGDSPSHPyHRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQ 352
Cdd:cd06649   238 RPVSGHGM-DS------RPAmaifelldyivNEPPPKLP-NGVFTPDFQEFVNKCLIKNPAERADLKMLMNHTFIKR 306
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
40-370 4.39e-17

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: 81.45  E-value: 4.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGFEDLmtVNLARYKPTGEYVTVRRInLEACSNEM--------VTFLQgelhvsKLFNHPNIVPYRATFIAD 111
Cdd:cd07852     9 YEILKKLGKGAYGI--VWKAIDKKTGEVVALKKI-FDAFRNATdaqrtfreIMFLQ------ELNDHPNIIKLLNVIRAE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 112 N--ELWVVTSFMAygsaKDL-------IcthfmdgMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYL 182
Cdd:cd07852    80 NdkDIYLVFEYME----TDLhaviranI-------LEDIHKQYIMYQLLKALKYLHSGGVIHRDLKPSNILLNSDCRVKL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 183 S--GLRSNLSMISHGQRQRVVHDFpkysVKVLPWLSPEVLQQNlQGYDAKSDIYSVGitaCELAnghvpfkdmpatQMLL 260
Cdd:cd07852   149 AdfGLARSLSQLEEDDENPVLTDY----VATRWYRAPEILLGS-TRYTKGVDMWSVG---CILG------------EMLL 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 261 EKlngtvPCLLDTSTIPAEELTMS----PSRS---VANSGLSDSLTTSTPRPsngdsPSHPYHRTF---SPHFHHFVEQC 330
Cdd:cd07852   209 GK-----PLFPGTSTLNQLEKIIEvigrPSAEdieSIQSPFAATMLESLPPS-----RPKSLDELFpkaSPDALDLLKKL 278
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1394533236 331 LQRNPDARPSASTLLNHSFFKQIKRRASEalPELLRPVTP 370
Cdd:cd07852   279 LVFNPNKRLTAEEALRHPYVAQFHNPADE--PSLPGPIVI 316
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
56-347 7.30e-17

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: 80.03  E-value: 7.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  56 VNLARYKPTGEYVTVRRInleAC-SNEMVTFLQGELHVSKLFNHPNIVPYRATFI-----ADNELWVVTSFMAYGSAKDL 129
Cdd:cd13986    16 VYLVEDLSTGRLYALKKI---LChSKEDVKEAMREIENYRLFNHPNILRLLDSQIvkeagGKKEVYLLLPYYKRGSLQDE 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 130 ICTHFMDG--MNELAIAYILQGVLKALDYIHHM---GYVHRSVKASHILISVDGKVYLSGLRS-NLSMIS-HGQRQ-RVV 201
Cdd:cd13986    93 IERRLVKGtfFPEDRILHIFLGICRGLKAMHEPelvPYAHRDIKPGNVLLSEDDEPILMDLGSmNPARIEiEGRREaLAL 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 202 HDFPKYSVKvLPWLSPEVLQ-QNLQGYDAKSDIYSVGITACELANGHVPFkdmpatqmlleklngtvpclldtstipaeE 280
Cdd:cd13986   173 QDWAAEHCT-MPYRAPELFDvKSHCTIDEKTDIWSLGCTLYALMYGESPF-----------------------------E 222
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 281 LTMSPSRSVA---NSGLSdslttSTPRPSNgdspshpyhrtFSPHFHHFVEQCLQRNPDARPSASTLLNH 347
Cdd:cd13986   223 RIFQKGDSLAlavLSGNY-----SFPDNSR-----------YSEELHQLVKSMLVVNPAERPSIDDLLSR 276
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
46-350 1.29e-16

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


Pssm-ID: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 78.71  E-value: 1.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  46 IGKGFEDlmTVNLARYKPTGEYVTVRRINLEAC-SNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYG 124
Cdd:cd05123     1 LGKGSFG--KVLLVRKKDTGKLYAMKVLRKKEIiKRKEVEHTLNERNILERVNHPFIVKLHYAFQTEEKLYLVLDYVPGG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 125 SAKDLICTHFMdgMNELAIA-YILQGVLkALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSnlSMISHGQRqrvV 201
Cdd:cd05123    79 ELFSHLSKEGR--FPEERARfYAAEIVL-ALEYLHSLGIIYRDLKPENILLDSDGHIKLTdfGLAK--ELSSDGDR---T 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 202 HDF---PKYsvkvlpwLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQMlleklngtvpclldTSTIPA 278
Cdd:cd05123   151 YTFcgtPEY-------LAPEVLLG--KGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEI--------------YEKILK 207
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1394533236 279 EELTMspsrsvansglsdslttstprpsngdsPSHpyhrtFSPHFHHFVEQCLQRNPDAR---PSASTLLNHSFF 350
Cdd:cd05123   208 SPLKF---------------------------PEY-----VSPEAKSLISGLLQKDPTKRlgsGGAEEIKAHPFF 250
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
55-370 1.40e-16

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 80.25  E-value: 1.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  55 TVNLARYKPTGEYVTVRRI--NLEACSNEMVTflqGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSakdLICT 132
Cdd:PLN00034   89 TVYKVIHRPTGRLYALKVIygNHEDTVRRQIC---REIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGS---LEGT 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 133 HFMDgmnELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISvdgkvylSGLRSNLSMISHGQRQRVVHDFPKYSVKVL 212
Cdd:PLN00034  163 HIAD---EQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLIN-------SAKNVKIADFGVSRILAQTMDPCNSSVGTI 232
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 213 PWLSPEVLQQNL-QG-YDAKS-DIYSVGITACELANGHVPFkdmpatqmlleklngtvpclldtstipaeeltmspsrSV 289
Cdd:PLN00034  233 AYMSPERINTDLnHGaYDGYAgDIWSLGVSILEFYLGRFPF-------------------------------------GV 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 290 ANSGLSDSLTTSTprpSNGDSPSHPyhRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQIKRRASEALPElLRPVT 369
Cdd:PLN00034  276 GRQGDWASLMCAI---CMSQPPEAP--ATASREFRHFISCCLQREPAKRWSAMQLLQHPFILRAQPGQGQGGPN-LHQLL 349

                  .
gi 1394533236 370 P 370
Cdd:PLN00034  350 P 350
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
40-345 1.88e-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: 78.61  E-value: 1.88e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTS 119
Cdd:cd08529     2 FEILNKLGKG--SFGVVYKVVRKVDGRVYALKQIDISRMSRKMREEAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIVME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 120 FMAYGSAKDLICTHFMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNLSMIShgqr 197
Cdd:cd08529    80 YAENGDLHSLIKSQRGRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGdlGVAKILSDTT---- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 198 qrvvhDFPKYSVKVLPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPclldtstip 277
Cdd:cd08529   156 -----NFAQTIVGTPYYLSPELCED--KPYNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIVRGKYP--------- 219
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1394533236 278 aeeltmspsrsvansglsdslttstprpsngdspshPYHRTFSPHFHHFVEQCLQRNPDARPSASTLL 345
Cdd:cd08529   220 ------------------------------------PISASYSQDLSQLIDSCLTKDYRQRPDTTELL 251
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
41-355 3.86e-16

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


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 77.97  E-value: 3.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  41 ELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQgELHVSKLFNHPNIVPYRATFIADNELWVVTSF 120
Cdd:cd06622     4 EVLDELGKG--NYGSVYKVLHRPTGVTMAMKEIRLELDESKFNQIIM-ELDILHKAVSPYIVDFYGAFFIEGAVYMCMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 121 MAYGSAKDLIC-THFMDGMNELAIAYILQGVLKALDYI-HHMGYVHRSVKASHILISVDGKVYLS--GLRSNLsmishgq 196
Cdd:cd06622    81 MDAGSLDKLYAgGVATEGIPEDVLRRITYAVVKGLKFLkEEHNIIHRDVKPTNVLVNGNGQVKLCdfGVSGNL------- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 197 rqrvVHDFPKYSVKVLPWLSPEVLQ-----QNLQgYDAKSDIYSVGITACELANGHVPFkdmpatqmlleklngtvpcll 271
Cdd:cd06622   154 ----VASLAKTNIGCQSYMAPERIKsggpnQNPT-YTVQSDVWSLGLSILEMALGRYPY--------------------- 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 272 dtstiPAEeltmspsrsvansgLSDSLTTSTPRPSNGDSPSHPyhRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFK 351
Cdd:cd06622   208 -----PPE--------------TYANIFAQLSAIVDGDPPTLP--SGYSDDAQDFVAKCLNKIPNRRPTYAQLLEHPWLV 266

                  ....
gi 1394533236 352 QIKR 355
Cdd:cd06622   267 KYKN 270
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
40-256 7.84e-16

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: 76.60  E-value: 7.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKG-FEDlmtVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVT 118
Cdd:cd14069     3 WDLVQTLGEGaFGE---VFLAVNRNTEEAVAVKFVDMKRAPGDCPENIKKEVCIQKMLSHKNVVRFYGHRREGEFQYLFL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 119 SFMAYGSAKDLIctHFMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRsnlSMISHGQ 196
Cdd:cd14069    80 EYASGGELFDKI--EPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISdfGLA---TVFRYKG 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1394533236 197 RQRVVHDfpkySVKVLPWLSPEVLQQnlQGYDA-KSDIYSVGITACELANGHVPFkDMPAT 256
Cdd:cd14069   155 KERLLNK----MCGTLPYVAPELLAK--KKYRAePVDVWSCGIVLFAMLAGELPW-DQPSD 208
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
40-350 1.24e-15

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: 76.12  E-value: 1.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGFEDlmTVNLARYKPTGEYVTVRRInleACSNEMVTFLQGEL----HVSKLFNHPNIV--PYRATFIADNE 113
Cdd:cd05118     1 YEVLRKIGEGAFG--TVWLARDKVTGEKVAIKKI---KNDFRHPKAALREIkllkHLNDVEGHPNIVklLDVFEHRGGNH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 114 LWVVTSFMAYgSAKDLIcTHFMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILIS-VDGKVYLS--GLrsnls 190
Cdd:cd05118    76 LCLVFELMGM-NLYELI-KDYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINlELGQLKLAdfGL----- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 191 mishgqrQRVVHDfPKYSVKV--LPWLSPEVLQQnLQGYDAKSDIYSVGITACELANGhVPF----KDMPATQMLLEKLn 264
Cdd:cd05118   149 -------ARSFTS-PPYTPYVatRWYRAPEVLLG-AKPYGSSIDIWSLGCILAELLTG-RPLfpgdSEVDQLAKIVRLL- 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 265 GTvPCLLDtstipaeeltmspsrsvansglsdslttstprpsngdspshpyhrtfsphfhhFVEQCLQRNPDARPSASTL 344
Cdd:cd05118   218 GT-PEALD-----------------------------------------------------LLSKMLKYDPAKRITASQA 243

                  ....*.
gi 1394533236 345 LNHSFF 350
Cdd:cd05118   244 LAHPYF 249
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
40-350 1.52e-15

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: 76.55  E-value: 1.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSK---LFNHPNIVPYR---ATFIADNE 113
Cdd:cd07838     1 YEEVAEIGEG--AYGTVYKARDLQDGRFVALKKVRVPLSEEGIPLSTIREIALLKqleSFEHPNVVRLLdvcHGPRTDRE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 114 LwVVTSFMAYgSAKDLicTHFMD-----GMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLR 186
Cdd:cd07838    79 L-KLTLVFEH-VDQDL--ATYLDkcpkpGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLAdfGLA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 187 SnlsmishgqrqrvVHDF--PKYSVKVLPWL-SPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKL 263
Cdd:cd07838   155 R-------------IYSFemALTSVVVTLWYrAPEVLLQ--SSYATPVDMWSVGCIFAELFNRRPLFRGSSEADQLGKIF 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 264 ngtvpclldtstipaeELTMSPSRS--VANSGLS-DSLTTSTPRPSNGDSPShpyhrtFSPHFHHFVEQCLQRNPDARPS 340
Cdd:cd07838   220 ----------------DVIGLPSEEewPRNSALPrSSFPSYTPRPFKSFVPE------IDEEGLDLLKKMLTFNPHKRIS 277
                         330
                  ....*....|
gi 1394533236 341 ASTLLNHSFF 350
Cdd:cd07838   278 AFEALQHPYF 287
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
40-250 1.73e-15

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: 75.63  E-value: 1.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTS 119
Cdd:cd14072     2 YRLLKTIGKG--NFAKVKLARHVLTGREVAIKIIDKTQLNPSSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 120 FMAYGSAKDLICTHfmDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLR-SNlsMISHGQRQ 198
Cdd:cd14072    80 YASGGEVFDYLVAH--GRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGfSN--EFTPGNKL 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1394533236 199 RVVHDFPkysvkvlPWLSPEVLQQnlQGYDA-KSDIYSVGITACELANGHVPF 250
Cdd:cd14072   156 DTFCGSP-------PYAAPELFQG--KKYDGpEVDVWSLGVILYTLVSGSLPF 199
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
40-250 1.88e-15

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: 75.37  E-value: 1.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTS 119
Cdd:cd14002     3 YHVLELIGEG--SFGKVYKGRRKYTGQVVALKFIPKRGKSEKELRNLRQEIEILRKLNHPNIIEMLDSFETKKEFVVVTE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 120 FmAYGSAKDLICThfmDG-MNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNLSMISHgq 196
Cdd:cd14002    81 Y-AQGELFQILED---DGtLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCdfGFARAMSCNTL-- 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1394533236 197 rqrVVHdfpkySVKVLP-WLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPF 250
Cdd:cd14002   155 ---VLT-----SIKGTPlYMAPELVQE--QPYDHTADLWSLGCILYELFVGQPPF 199
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
40-348 2.47e-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: 75.40  E-value: 2.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLfNHPNIVPYRATFIADNELWVVts 119
Cdd:cd08219     2 YNVLRVVGEG--SFGRALLVQHVNSDQKYAMKEIRLPKSSSAVEDSRKEAVLLAKM-KHPNIVAFKESFEADGHLYIV-- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 120 fMAYGSAKDLIcTHFMDGMNEL-----AIAYILQGVLkALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSnlsmish 194
Cdd:cd08219    77 -MEYCDGGDLM-QKIKLQRGKLfpedtILQWFVQMCL-GVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGS------- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 195 gqrQRVVHDFPKYSVKVL--PWLSPEVLQQNLQgYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPCLld 272
Cdd:cd08219   147 ---ARLLTSPGAYACTYVgtPYYVPPEIWENMP-YNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGSYKPL-- 220
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1394533236 273 tstipaeeltmspsrsvansglsdslttstprpsngdsPSHpyhrtFSPHFHHFVEQCLQRNPDARPSASTLLNHS 348
Cdd:cd08219   221 --------------------------------------PSH-----YSYELRSLIKQMFKRNPRSRPSATTILSRG 253
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
40-250 4.90e-15

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: 75.88  E-value: 4.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKG-FEDlmtVNLARYKPTGEYVTVRRIN-LEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVV 117
Cdd:cd05596    28 FDVIKVIGRGaFGE---VQLVRHKSTKKVYAMKLLSkFEMIKRSDSAFFWEERDIMAHANSEWIVQLHYAFQDDKYLYMV 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 118 TSFMAYGsakDLIctHFMDGMN---ELAIAYILQGVLkALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMISH 194
Cdd:cd05596   105 MDYMPGG---DLV--NLMSNYDvpeKWARFYTAEVVL-ALDAIHSMGFVHRDVKPDNMLLDASGHLKLADFGTCMKMDKD 178
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1394533236 195 GQrqrVVHDFPkysVKVLPWLSPEVLQ-QNLQG-YDAKSDIYSVGITACELANGHVPF 250
Cdd:cd05596   179 GL---VRSDTA---VGTPDYISPEVLKsQGGDGvYGRECDWWSVGVFLYEMLVGDTPF 230
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
40-252 6.01e-15

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: 74.25  E-value: 6.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVtflQGELHVSKLFNHPNIVPYRATFIADNELWVVTS 119
Cdd:cd14665     2 YELVKDIGSG--NFGVARLMRDKQTKELVAVKYIERGEKIDENV---QREIINHRSLRHPNIVRFKEVILTPTHLAIVME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 120 FMAYGSAKDLICThfMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILIsvDGKVylsglRSNLSMISHG-QRQ 198
Cdd:cd14665    77 YAAGGELFERICN--AGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLL--DGSP-----APRLKICDFGySKS 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1394533236 199 RVVHDFPKYSVKVLPWLSPEVLQQnlQGYDAK-SDIYSVGITACELANGHVPFKD 252
Cdd:cd14665   148 SVLHSQPKSTVGTPAYIAPEVLLK--KEYDGKiADVWSCGVTLYVMLVGAYPFED 200
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
63-355 8.07e-15

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: 73.96  E-value: 8.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  63 PTGEYVTVRRINLEACSNEMVTFlqgELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICT--HFMDGMNE 140
Cdd:cd13992    23 YGGRTVAIKHITFSRTEKRTILQ---ELNQLKELVHDNLNKFIGICINPPNIAVVTEYCTRGSLQDVLLNreIKMDWMFK 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 141 LAIAYilqGVLKALDYIH-HMGYVHRSVKASHILISVDGKVYLSGLrsNLSMISHGQRQRVVHDFPKYSVKVlpWLSPEV 219
Cdd:cd13992   100 SSFIK---DIVKGMNYLHsSSIGYHGRLKSSNCLVDSRWVVKLTDF--GLRNLLEEQTNHQLDEDAQHKKLL--WTAPEL 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 220 LQQNLQGY--DAKSDIYSVGITACELANGHVPFkdmpatqmlleklngtvpclldtstipAEELTMSPSRSVANSGlsds 297
Cdd:cd13992   173 LRGSLLEVrgTQKGDVYSFAIILYEILFRSDPF---------------------------ALEREVAIVEKVISGG---- 221
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1394533236 298 ltTSTPRPsngdSPSHPYHRtFSPHFHHFVEQCLQRNPDARPSastllnhsfFKQIKR 355
Cdd:cd13992   222 --NKPFRP----ELAVLLDE-FPPRLVLLVKQCWAENPEKRPS---------FKQIKK 263
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
41-254 1.07e-14

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: 73.48  E-value: 1.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  41 ELLTVIGKG-FEDLMtvnLARYKptGEYVTVRRINLEACSNEMVtflqGELHVSKLFNHPNIVPYRATFIADN-ELWVVT 118
Cdd:cd05082     9 KLLQTIGKGeFGDVM---LGDYR--GNKVAVKCIKNDATAQAFL----AEASVMTQLRHSNLVQLLGVIVEEKgGLYIVT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 119 SFMAYGSAKDLICTHFMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVD--GKVYLSGLRSNLSMIshgq 196
Cdd:cd05082    80 EYMAKGSLVDYLRSRGRSVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDnvAKVSDFGLTKEASST---- 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1394533236 197 rqrvvHDFPKYSVKvlpWLSPEVLQQNLqgYDAKSDIYSVGITACELAN-GHVPFKDMP 254
Cdd:cd05082   156 -----QDTGKLPVK---WTAPEALREKK--FSTKSDVWSFGILLWEIYSfGRVPYPRIP 204
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
86-350 1.82e-14

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: 72.97  E-value: 1.82e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  86 LQGELHVSKLFNHPNIV--------PYratfiaDNELWVVTSFMAYGSAKDLICTHFMDGMNELAIAYILQGVLKALDYI 157
Cdd:cd14008    51 VRREIAIMKKLDHPNIVrlyeviddPE------SDKLYLVLEYCEGGPVMELDSGDRVPPLPEETARKYFRDLVLGLEYL 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 158 HHMGYVHRSVKASHILISVDGKVYLS--GlrsnlsmISHgqrqrVVHDFPKYSVKVL--P-WLSPEVLQQNLQGYDAK-S 231
Cdd:cd14008   125 HENGIVHRDIKPENLLLTADGTVKISdfG-------VSE-----MFEDGNDTLQKTAgtPaFLAPELCDGDSKTYSGKaA 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 232 DIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPclldtstipaeeltmspsrsvansglsdslttstprpsngdsp 311
Cdd:cd14008   193 DIWALGVTLYCLVFGRLPFNGDNILELYEAIQNQNDE------------------------------------------- 229
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1394533236 312 sHPYHRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFF 350
Cdd:cd14008   230 -FPIPPELSPELKDLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
89-354 2.04e-14

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: 72.75  E-value: 2.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  89 ELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLIcTHFMDG---MNELAI-AYILQgVLKALDYIHHMGYVH 164
Cdd:cd08228    52 EIDLLKQLNHPNVIKYLDSFIEDNELNIVLELADAGDLSQMI-KYFKKQkrlIPERTVwKYFVQ-LCSAVEHMHSRRVMH 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 165 RSVKASHILISVDGKVYLSGLRSNLSMISHGQRQRVVHDFPKYsvkvlpwLSPEVLQQNlqGYDAKSDIYSVGITACELA 244
Cdd:cd08228   130 RDIKPANVFITATGVVKLGDLGLGRFFSSKTTAAHSLVGTPYY-------MSPERIHEN--GYNFKSDIWSLGCLLYEMA 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 245 NGHVPFKDmpatqmllEKLNgtvpclldtstipaeeltmspsrsvansglsdsLTTSTPRPSNGDSPSHPYHRtFSPHFH 324
Cdd:cd08228   201 ALQSPFYG--------DKMN---------------------------------LFSLCQKIEQCDYPPLPTEH-YSEKLR 238
                         250       260       270
                  ....*....|....*....|....*....|
gi 1394533236 325 HFVEQCLQRNPDARPSASTLlnHSFFKQIK 354
Cdd:cd08228   239 ELVSMCIYPDPDQRPDIGYV--HQIAKQMH 266
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
94-246 2.13e-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: 72.42  E-value: 2.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  94 KLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTHFMDG-MNELAIAYILQGVLKALDYIHHMGYVHRSVKASHI 172
Cdd:cd13997    55 ALGQHPNIVRYYSSWEEGGHLYIQMELCENGSLQDALEELSPISkLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNI 134
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1394533236 173 LISVDGKVYLS--GLRSNLS---MISHGQrqrvvhdfPKYsvkvlpwLSPEVLQQNLQgYDAKSDIYSVGITACELANG 246
Cdd:cd13997   135 FISNKGTCKIGdfGLATRLEtsgDVEEGD--------SRY-------LAPELLNENYT-HLPKADIFSLGVTVYEAATG 197
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
56-252 2.69e-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: 72.63  E-value: 2.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  56 VNLARYKPTGEYVTVRRINLEACSNE-MVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLIctHF 134
Cdd:cd05579     9 VYLAKKKSTGDLYAIKVIKKRDMIRKnQVDSVLAERNILSQAQNPFVVKLYYSFQGKKNLYLVMEYLPGGDLYSLL--EN 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 135 MDGMNE-LAIAYILQGVLkALDYIHHMGYVHRSVKASHILISVDGKVYLS-------GLRSNLSMISHGQRQRVVHDFPK 206
Cdd:cd05579    87 VGALDEdVARIYIAEIVL-ALEYLHSHGIIHRDLKPDNILIDANGHLKLTdfglskvGLVRRQIKLSIQKKSNGAPEKED 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1394533236 207 YSVKVLP-WLSPEVLqqNLQGYDAKSDIYSVGITACELANGHVPFKD 252
Cdd:cd05579   166 RRIVGTPdYLAPEIL--LGQGHGKTVDWWSLGVILYEFLVGIPPFHA 210
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
46-346 2.72e-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: 72.80  E-value: 2.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  46 IGKGfeDLMTVNLARYKP----TGEYVTVRRINLEACSNEMVTFlQGELHVSKLFNHPNIVPYR--ATFIADNELWVVTS 119
Cdd:cd05038    12 LGEG--HFGSVELCRYDPlgdnTGEQVAVKSLQPSGEEQHMSDF-KREIEILRTLDHEYIVKYKgvCESPGRRSLRLIME 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 120 FMAYGSAKDLICTHFMDGMNELAIAYILQgVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNLSMISHGQR 197
Cdd:cd05038    89 YLPSGSLRDYLQRHRDQIDLKRLLLFASQ-ICKGMEYLGSQRYIHRDLAARNILVESEDLVKISdfGLAKVLPEDKEYYY 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 198 QRVVHDFPKYsvkvlpWLSPEVLQQNLqgYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPCLLDTstip 277
Cdd:cd05038   168 VKEPGESPIF------WYAPECLRESR--FSSASDVWSFGVTLYELFTYGDPSQSPPALFLRMIGIAQGQMIVTRL---- 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1394533236 278 AEELTMSPsrsvansglsdslttSTPRPSNgdSPSHPYhrtfsphfhHFVEQCLQRNPDARPSASTLLN 346
Cdd:cd05038   236 LELLKSGE---------------RLPRPPS--CPDEVY---------DLMKECWEYEPQDRPSFSDLIL 278
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
31-272 2.74e-14

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: 72.54  E-value: 2.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  31 SSFLPEggcYELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIA 110
Cdd:cd14049     2 SRYLNE---FEEIARLGKG--GYGKVYKVRNKLDGQYYAIKKILIKKVTKRDCMKVLREVKVLAGLQHPNIVGYHTAWME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 111 DNEL---------------WVVTSFMAYGSAKDLICTHFMDGMNelAIAYILQGVLKALDYIHHMGYVHRSVKASHILIS 175
Cdd:cd14049    77 HVQLmlyiqmqlcelslwdWIVERNKRPCEEEFKSAPYTPVDVD--VTTKILQQLLEGVTYIHSMGIVHRDLKPRNIFLH 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 176 V-DGKVYL----------------SGLRSNLSMISHGQRqrvvhdfpkysVKVLPWLSPEVLQQNlqGYDAKSDIYSVGI 238
Cdd:cd14049   155 GsDIHVRIgdfglacpdilqdgndSTTMSRLNGLTHTSG-----------VGTCLYAAPEQLEGS--HYDFKSDMYSIGV 221
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1394533236 239 TACELangHVPF-KDMPATQMLLEKLNGTVPCLLD 272
Cdd:cd14049   222 ILLEL---FQPFgTEMERAEVLTQLRNGQIPKSLC 253
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
40-350 3.17e-14

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


Pssm-ID: 270836 [Multi-domain]  Cd Length: 286  Bit Score: 72.46  E-value: 3.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRInLEACSNEMVTFLQ-GELHVSKLFNHPNIVPYRATFIADNELWVVT 118
Cdd:cd07846     3 YENLGLVGEG--SYGMVMKCRHKETGQIVAIKKF-LESEDDKMVKKIAmREIKMLKQLRHENLVNLIEVFRRKKRWYLVF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 119 SFMAYGSAKDLicTHFMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMISHGQrq 198
Cdd:cd07846    80 EFVDHTVLDDL--EKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGE-- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 199 rvvhDFPKYsVKVLPWLSPEVLQQNLQgYDAKSDIYSVGITACELANGHVPFkdmPATQMlLEKLNGTVPCLldTSTIPA 278
Cdd:cd07846   156 ----VYTDY-VATRWYRAPELLVGDTK-YGKAVDVWAVGCLVTEMLTGEPLF---PGDSD-IDQLYHIIKCL--GNLIPR 223
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1394533236 279 EELTMSPSRSVANSGLSDsltTSTPRPSNGDSPshpyhrTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFF 350
Cdd:cd07846   224 HQELFQKNPLFAGVRLPE---VKEVEPLERRYP------KLSGVVIDLAKKCLHIDPDKRPSCSELLHHEFF 286
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
96-253 4.29e-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: 4.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  96 FNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTHfmDG-MNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILI 174
Cdd:cd05064    63 FDHSNIVRLEGVITRGNTMMIVTEYMSNGALDSFLRKH--EGqLVAGQLMGMLPGLASGMKYLSEMGYVHKGLAAHKVLV 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 175 SVDGKVYLSGLRsnlsmisHGQRQRVVHDFPKYSVK-VLPWLSPEVLQqnLQGYDAKSDIYSVGITACE-LANGHVPFKD 252
Cdd:cd05064   141 NSDLVCKISGFR-------RLQEDKSEAIYTTMSGKsPVLWAAPEAIQ--YHHFSSASDVWSFGIVMWEvMSYGERPYWD 211

                  .
gi 1394533236 253 M 253
Cdd:cd05064   212 M 212
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
40-350 5.44e-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: 71.53  E-value: 5.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVts 119
Cdd:cd08225     2 YEIIKKIGEG--SFGKIYLAKAKSDSEHCVIKEIDLTKMPVKEKEASKKEVILLAKMKHPNIVTFFASFQENGRLFIV-- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 120 fMAYGSAKDLicthfMDGMN---------ELAIAYILQGVLkALDYIHHMGYVHRSVKASHILISVDGKVylsglrSNLS 190
Cdd:cd08225    78 -MEYCDGGDL-----MKRINrqrgvlfseDQILSWFVQISL-GLKHIHDRKILHRDIKSQNIFLSKNGMV------AKLG 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 191 MISHGQRQRVVHDFPKYSVKVLPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVpcl 270
Cdd:cd08225   145 DFGIARQLNDSMELAYTCVGTPYYLSPEICQN--RPYNNKTDIWSLGCVLYELCTLKHPFEGNNLHQLVLKICQGYF--- 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 271 ldtstipaeeltmspsrsvansglsdslttstprpsngdspsHPYHRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFF 350
Cdd:cd08225   220 ------------------------------------------APISPNFSRDLRSLISQLFKVSPRDRPSITSILKRPFL 257
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
40-349 7.08e-14

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: 70.92  E-value: 7.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKG-FEDLMTVNLARYKPTGEYVTVRRINL-EACSNEMVTFLQGELHVSKLfNHPNIVPYRATFIADNELWVV 117
Cdd:cd08222     2 YRVVRKLGSGnFGTVYLVSDLKATADEELKVLKEISVgELQPDETVDANREAKLLSKL-DHPAIVKFHDSFVEKESFCIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 118 TSFMAYGSAKDLICTHFMDGM---NELAIAYILQgVLKALDYIHHMGYVHRSVKASHILisvdgkvylsgLRSNLSMISH 194
Cdd:cd08222    81 TEYCEGGDLDDKISEYKKSGTtidENQILDWFIQ-LLLAVQYMHERRILHRDLKAKNIF-----------LKNNVIKVGD 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 195 GQRQRVVH---DFPKYSVKVLPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFkdmpATQMLLEKLNGTVpcll 271
Cdd:cd08222   149 FGISRILMgtsDLATTFTGTPYYMSPEVLKH--EGYNSKSDIWSLGCILYEMCCLKHAF----DGQNLLSVMYKIV---- 218
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1394533236 272 dtstipaeeltmspsrsvansglsdslttstprpsNGDSPSHPYHrtFSPHFHHFVEQCLQRNPDARPSASTLLNHSF 349
Cdd:cd08222   219 -----------------------------------EGETPSLPDK--YSKELNAIYSRMLNKDPALRPSAAEILKIPF 259
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
40-350 1.05e-13

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: 70.65  E-value: 1.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKG-FEdlmTVNLARYKPTGEYVTVRRINLEACSN---EMvtfLQGELHVSKLFNHPNIVPYRATFIaDNELW 115
Cdd:cd08217     2 YEVLETIGKGsFG---TVRKVRRKSDGKILVWKEIDYGKMSEkekQQ---LVSEVNILRELKHPNIVRYYDRIV-DRANT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 116 VVTSFMAYGSAKDL---ICTHFMDG--MNELAIAYILQGVLKALDYIHHMGY-----VHRSVKASHILISVDGKVYLS-- 183
Cdd:cd08217    75 TLYIVMEYCEGGDLaqlIKKCKKENqyIPEEFIWKIFTQLLLALYECHNRSVgggkiLHRDLKPANIFLDSDNNVKLGdf 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 184 GL-RsnlsMISHGQRqrvvhdFPKYSVKVLPWLSPEVLqqNLQGYDAKSDIYSVGITACELANGHVPFKdmPATQMLLEK 262
Cdd:cd08217   155 GLaR----VLSHDSS------FAKTYVGTPYYMSPELL--NEQSYDEKSDIWSLGCLIYELCALHPPFQ--AANQLELAK 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 263 L--NGTVPCLldtstipaeeltmspsrsvansglsdslttstprpsngdsPSHpyhrtFSPHFHHFVEQCLQRNPDARPS 340
Cdd:cd08217   221 KikEGKFPRI----------------------------------------PSR-----YSSELNEVIKSMLNVDPDKRPS 255
                         330
                  ....*....|
gi 1394533236 341 ASTLLNHSFF 350
Cdd:cd08217   256 VEELLQLPLI 265
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
46-243 1.94e-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: 69.97  E-value: 1.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  46 IGKGFedLMTVNLARYKPTGEYVTVRRinLEACSNE-MVTFLQgELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYG 124
Cdd:cd14222     1 LGKGF--FGQAIKVTHKATGKVMVMKE--LIRCDEEtQKTFLT-EVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 125 SAKDLI-CTHFMDGMNELAIAyilQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLrsNLSMISHGQRQRVVHD 203
Cdd:cd14222    76 TLKDFLrADDPFPWQQKVSFA---KGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADF--GLSRLIVEEKKKPPPD 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1394533236 204 FP--------------KYSVKVLP-WLSPEVLqqNLQGYDAKSDIYSVGITACEL 243
Cdd:cd14222   151 KPttkkrtlrkndrkkRYTVVGNPyWMAPEML--NGKSYDEKVDIFSFGIVLCEI 203
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
40-252 1.99e-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: 69.71  E-value: 1.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKG-FEDlmtVNLARYKPTGEYVTVRRINLEACSNEMVTfLQGELHVSKLFNHPNIVPYRATFIADNELWVVT 118
Cdd:cd14083     5 YEFKEVLGTGaFSE---VVLAEDKATGKLVAIKCIDKKALKGKEDS-LENEIAVLRKIKHPNIVQLLDIYESKSHLYLVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 119 SFMAYGSAKDLICTHfmDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILI---SVDGKVYLSGLrsNLSMISHG 195
Cdd:cd14083    81 ELVTGGELFDRIVEK--GSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYyspDEDSKIMISDF--GLSKMEDS 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1394533236 196 QRQRVVHDFPKYsvkvlpwLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKD 252
Cdd:cd14083   157 GVMSTACGTPGY-------VAPEVLAQ--KPYGKAVDCWSIGVISYILLCGYPPFYD 204
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
40-252 2.56e-13

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: 69.41  E-value: 2.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVtflQGELHVSKLFNHPNIVPYRATFIADNELWVVTS 119
Cdd:cd14662     2 YELVKDIGSG--NFGVARLMRNKETKELVAVKYIERGLKIDENV---QREIINHRSLRHPNIIRFKEVVLTPTHLAIVME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 120 FMAYGSAKDLICThfMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILIsvDGKVylsglRSNLSMISHG-QRQ 198
Cdd:cd14662    77 YAAGGELFERICN--AGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLL--DGSP-----APRLKICDFGySKS 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1394533236 199 RVVHDFPKYSVKVLPWLSPEVLQQnlQGYDAK-SDIYSVGITACELANGHVPFKD 252
Cdd:cd14662   148 SVLHSQPKSTVGTPAYIAPEVLSR--KEYDGKvADVWSCGVTLYVMLVGAYPFED 200
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
98-255 3.44e-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: 69.67  E-value: 3.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  98 HPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTHFMdgMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILIsVD 177
Cdd:cd14175    54 HPNIITLKDVYDDGKHVYLVTELMRGGELLDKILRQKF--FSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILY-VD 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 178 GkvylSGLRSNLSMISHGQRQRVVHD-----FPKYSVKvlpWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKD 252
Cdd:cd14175   131 E----SGNPESLRICDFGFAKQLRAEngllmTPCYTAN---FVAPEVLKR--QGYDEGCDIWSLGILLYTMLAGYTPFAN 201

                  ...
gi 1394533236 253 MPA 255
Cdd:cd14175   202 GPS 204
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
40-350 3.51e-13

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: 69.52  E-value: 3.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfedlmT---VNLARYKPTGEYVTVRRINLEACSNEM-VTFLQgELHVSKLFNHPNIVPY------RATFI 109
Cdd:cd07840     1 YEKIAQIGEG-----TygqVYKARNKKTGELVALKKIRMENEKEGFpITAIR-EIKLLQKLDHPNVVRLkeivtsKGSAK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 110 ADNELWVVTSFMAYgsakDLicTHFMDG----MNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS-- 183
Cdd:cd07840    75 YKGSIYMVFEYMDH----DL--TGLLDNpevkFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLAdf 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 184 GLrsnlsmishgQRQRVVHDFPKYSVKV--LPWLSPEVLQQNLQgYDAKSDIYSVGITACELANGHVPFK-DMPATQM-L 259
Cdd:cd07840   149 GL----------ARPYTKENNADYTNRVitLWYRPPELLLGATR-YGPEVDMWSVGCILAELFTGKPIFQgKTELEQLeK 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 260 LEKLNGTvpclldtstiPAEEltmspsrsvANSGLSDSLTTSTPRpsngdsPSHPYHRTFSPHFHHF--------VEQCL 331
Cdd:cd07840   218 IFELCGS----------PTEE---------NWPGVSDLPWFENLK------PKKPYKRRLREVFKNVidpsaldlLDKLL 272
                         330
                  ....*....|....*....
gi 1394533236 332 QRNPDARPSASTLLNHSFF 350
Cdd:cd07840   273 TLDPKKRISADQALQHEYF 291
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
40-352 3.60e-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: 69.58  E-value: 3.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTG-EY-VTVRRINLEACSNEMVTFLqgelhvsKLFNHPNIVPYRATFIADNELWVV 117
Cdd:cd14091     2 YEIKEEIGKG--SYSVCKRCIHKATGkEYaVKIIDKSKRDPSEEIEILL-------RYGQHPNIITLRDVYDDGNSVYLV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 118 TSFMAYGSAKDLICT--HFmdgmNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDgkvylSGLRSNLSMISHG 195
Cdd:cd14091    73 TELLRGGELLDRILRqkFF----SEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADE-----SGDPESLRICDFG 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 196 QRQRVVHD-----FPKYSVKvlpWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPAtqmlleklngtvpcl 270
Cdd:cd14091   144 FAKQLRAEngllmTPCYTAN---FVAPEVLKK--QGYDAACDIWSLGVLLYTMLAGYTPFASGPN--------------- 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 271 lDTstiPAEELTmspsrsvansglsdslttstpRPSNGDSP-SHPYHRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSF 349
Cdd:cd14091   204 -DT---PEVILA---------------------RIGSGKIDlSGGNWDHVSDSAKDLVRKMLHVDPSQRPTAAQVLQHPW 258

                  ...
gi 1394533236 350 FKQ 352
Cdd:cd14091   259 IRN 261
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
46-284 3.80e-13

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


Pssm-ID: 270896 [Multi-domain]  Cd Length: 265  Bit Score: 68.87  E-value: 3.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  46 IGKGFEDLMTVNLARYKPTGEYVTV---RRINLEACSNEMVTFLQGELHVSKLFNHPNIVpyrATFiadnELWVVTS--- 119
Cdd:cd13994     1 IGKGATSVVRIVTKKNPRSGVLYAVkeyRRRDDESKRKDYVKRLTSEYIISSKLHHPNIV---KVL----DLCQDLHgkw 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 120 --FMAYGSAKDLiCTHFMDGMN---ELAIAYILQgVLKALDYIHHMGYVHRSVKASHILISVDGkvylsglrsNLSMISH 194
Cdd:cd13994    74 clVMEYCPGGDL-FTLIEKADSlslEEKDCFFKQ-ILRGVAYLHSHGIAHRDLKPENILLDEDG---------VLKLTDF 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 195 GQRQrVVHDFPKYSVKV-------LPWLSPEVLQQNlqGYDAKS-DIYSVGITACELANGHVPFKD--------MPATQM 258
Cdd:cd13994   143 GTAE-VFGMPAEKESPMsaglcgsEPYMAPEVFTSG--SYDGRAvDVWSCGIVLFALFTGRFPWRSakksdsayKAYEKS 219
                         250       260
                  ....*....|....*....|....*.
gi 1394533236 259 LLEKLNGTVPCLLDTSTIpAEELTMS 284
Cdd:cd13994   220 GDFTNGPYEPIENLLPSE-CRRLIYR 244
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
40-244 3.96e-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: 68.99  E-value: 3.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTS 119
Cdd:cd08220     2 YEKIRVVGRG--AYGTVYLCRRKDDNKLVIIKQIPVEQMTKEERQAALNEVKVLSMLHHPNIIEYYESFLEDKALMIVME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 120 FMAYGSAKDLI---CTHFMDgmNELAIAYILQgVLKALDYIHHMGYVHRSVKASHILISVDGK-VYLS--GLRSNLSMIS 193
Cdd:cd08220    80 YAPGGTLFEYIqqrKGSLLS--EEEILHFFVQ-ILLALHHVHSKQILHRDLKTQNILLNKKRTvVKIGdfGISKILSSKS 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1394533236 194 HGqrqrvvhdfpkYSVKVLP-WLSPEVLQQnlQGYDAKSDIYSVGITACELA 244
Cdd:cd08220   157 KA-----------YTVVGTPcYISPELCEG--KPYNQKSDIWALGCVLYELA 195
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
40-265 4.57e-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: 68.57  E-value: 4.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTS 119
Cdd:cd14071     2 YDIERTIGKG--NFAVVKLARHRITKTEVAIKIIDKSQLDEENLKKIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVTE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 120 FMAYGSAKDLICTHfmDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLR-SNLsmISHGQRQ 198
Cdd:cd14071    80 YASNGEIFDYLAQH--GRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGfSNF--FKPGELL 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1394533236 199 RVVHDFPkysvkvlPWLSPEVLQQnlQGYDA-KSDIYSVGITACELANGHVPFkDMPATQMLLEK-LNG 265
Cdd:cd14071   156 KTWCGSP-------PYAAPEVFEG--KEYEGpQLDIWSLGVVLYVLVCGALPF-DGSTLQTLRDRvLSG 214
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
38-262 4.70e-13

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: 68.43  E-value: 4.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  38 GCYELLTVIGKGfedlMT--VNLARYKPTGEYVTVRRINLEACSNE-MVTFLQGELHVSKLFNHPNIVPYRATFIADNEL 114
Cdd:cd14081     1 GPYRLGKTLGKG----QTglVKLAKHCVTGQKVAIKIVNKEKLSKEsVLMKVEREIAIMKLIEHPNVLKLYDVYENKKYL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 115 WVVTSFMAYGSAKDLICTHfmDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLsglrSNLSMISH 194
Cdd:cd14081    77 YLVLEYVSGGELFDYLVKK--GRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKI----ADFGMASL 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1394533236 195 GQRQRVVHDF---PKYsvkvlpwLSPEVLQQnlQGYD-AKSDIYSVGITACELANGHVPFKDmPATQMLLEK 262
Cdd:cd14081   151 QPEGSLLETScgsPHY-------ACPEVIKG--EKYDgRKADIWSCGVILYALLVGALPFDD-DNLRQLLEK 212
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
40-250 4.73e-13

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: 70.03  E-value: 4.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRIN-LEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVT 118
Cdd:cd05622    75 YEVVKVIGRG--AFGEVQLVRHKSTRKVYAMKLLSkFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVM 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 119 SFMAYGSAKDLICTHfmDGMNELAIAYILQGVLkALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMISHGQ-R 197
Cdd:cd05622   153 EYMPGGDLVNLMSNY--DVPEKWARFYTAEVVL-ALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMvR 229
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1394533236 198 QRVVHDFPKYsvkvlpwLSPEVLQ-QNLQGYDAKS-DIYSVGITACELANGHVPF 250
Cdd:cd05622   230 CDTAVGTPDY-------ISPEVLKsQGGDGYYGREcDWWSVGVFLYEMLVGDTPF 277
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
45-349 4.78e-13

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: 68.59  E-value: 4.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  45 VIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNemVTFLQGELHVSKLFNHPNIVPYRATFIADNelwVVTSFMAY- 123
Cdd:cd06624    15 VLGKG--TFGVVYAARDLSTQVRIAIKEIPERDSRE--VQPLHEEIALHSRLSHKNIVQYLGSVSEDG---FFKIFMEQv 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 124 --GSAKDLICTHF---MDgmNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISV-DGKVYLS--GLRSNLSMIshg 195
Cdd:cd06624    88 pgGSLSALLRSKWgplKD--NENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTySGVVKISdfGTSKRLAGI--- 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 196 qrQRVVHDFpkysVKVLPWLSPEVLQQNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKlngtVPCLLDTST 275
Cdd:cd06624   163 --NPCTETF----TGTLQYMAPEVIDKGQRGYGPPADIWSLGCTIIEMATGKPPFIELGEPQAAMFK----VGMFKIHPE 232
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1394533236 276 IPAEeltmspsrsvansgLSDSLTTstprpsngdspshpyhrtfsphfhhFVEQCLQRNPDARPSASTLLNHSF 349
Cdd:cd06624   233 IPES--------------LSEEAKS-------------------------FILRCFEPDPDKRATASDLLQDPF 267
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
40-375 7.92e-13

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: 68.71  E-value: 7.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINleacsNEMVTFLQG-----ELHVSKLFNHPNIV--------PYRA 106
Cdd:cd07834     2 YELLKPIGSG--AYGVVCSAYDKRTGRKVAIKKIS-----NVFDDLIDAkrilrEIKILRHLKHENIIglldilrpPSPE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 107 TFiadNELWVVTSFMAYGSAKDLICTHFMDgmnELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--G 184
Cdd:cd07834    75 EF---NDVYIVTELMETDLHKVIKSPQPLT---DDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICdfG 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 185 L-RSnlsmISHGQRQRVVHDFpkysVkVLPWL-SPEVLqQNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMlLEK 262
Cdd:cd07834   149 LaRG----VDPDEDKGFLTEY----V-VTRWYrAPELL-LSSKKYTKAIDIWSVGCIFAELLTRKPLFPGRDYIDQ-LNL 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 263 LNGTVPclldtsTIPAEELTMSPSrSVANSGLSdSLTTSTPRPSNGDSPshpyhrTFSPHFHHFVEQCLQRNPDARPSAS 342
Cdd:cd07834   218 IVEVLG------TPSEEDLKFISS-EKARNYLK-SLPKKPKKPLSEVFP------GASPEAIDLLEKMLVFNPKKRITAD 283
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1394533236 343 TLLNHSFFKQIKRRASEALPEllrPVTPITNFE 375
Cdd:cd07834   284 EALAHPYLAQLHDPEDEPVAK---PPFDFPFFD 313
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
40-250 8.14e-13

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: 68.91  E-value: 8.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKG-FEDlmtVNLARYKPTGEYVTVRRIN----LE----ACSNEmvtflqgELHVSKLFNHPNIVPYRATFIA 110
Cdd:cd05597     3 FEILKVIGRGaFGE---VAVVKLKSTEKVYAMKILNkwemLKraetACFRE-------ERDVLVNGDRRWITKLHYAFQD 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 111 DNELWVVtsfMAYGSAKDLIC--THFMDGM-NELAIAYILQGVLkALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRS 187
Cdd:cd05597    73 ENYLYLV---MDYYCGGDLLTllSKFEDRLpEEMARFYLAEMVL-AIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFGS 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1394533236 188 NLSMISHGQRQRVVhdfpkySVKVLPWLSPEVLQQNLQG---YDAKSDIYSVGITACELANGHVPF 250
Cdd:cd05597   149 CLKLREDGTVQSSV------AVGTPDYISPEILQAMEDGkgrYGPECDWWSLGVCMYEMLYGETPF 208
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
41-254 8.28e-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: 67.76  E-value: 8.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  41 ELLTVIGKG-FEDLMtvnLARYKptGEYVTVRRINleaCSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTS 119
Cdd:cd05039     9 KLGELIGKGeFGDVM---LGDYR--GQKVAVKCLK---DDSTAAQAFLAEASVMTTLRHPNLVQLLGVVLEGNGLYIVTE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 120 FMAYGSAKDLICT---HFMDGMNELAIAYilqGVLKALDYIHHMGYVHRSVKASHILISVDG--KVYLSGLrsnlsmish 194
Cdd:cd05039    81 YMAKGSLVDYLRSrgrAVITRKDQLGFAL---DVCEGMEYLESKKFVHRDLAARNVLVSEDNvaKVSDFGL--------- 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1394533236 195 GQRQRVVHDFPKYSVKvlpWLSPEVLQQNLqgYDAKSDIYSVGITACEL-ANGHVPFKDMP 254
Cdd:cd05039   149 AKEASSNQDGGKLPIK---WTAPEALREKK--FSTKSDVWSFGILLWEIySFGRVPYPRIP 204
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
98-254 1.09e-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: 68.12  E-value: 1.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  98 HPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTHfmDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVD 177
Cdd:cd14177    57 HPNIITLKDVYDDGRYVYLVTELMKGGELLDRILRQ--KFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDD 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 178 gkvylSGLRSNLSMISHGQRQRVVHD-----FPKYSVKvlpWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKD 252
Cdd:cd14177   135 -----SANADSIRICDFGFAKQLRGEnglllTPCYTAN---FVAPEVLMR--QGYDAACDIWSLGVLLYTMLAGYTPFAN 204

                  ..
gi 1394533236 253 MP 254
Cdd:cd14177   205 GP 206
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
59-351 1.52e-12

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: 67.45  E-value: 1.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  59 ARYKPTGEYVTVRRINLeaCSN------EMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLIcT 132
Cdd:cd06630    19 ARDVKTGTLMAVKQVSF--CRNssseqeEVVEAIREEIRMMARLNHPNIVRMLGATQHKSHFNIFVEWMAGGSVASLL-S 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 133 HFMDGMNELAIAYILQgVLKALDYIHHMGYVHRSVKASHILISVDGK-VYLSGLRSNLSMISHGQRqrvVHDFPKYSVKV 211
Cdd:cd06630    96 KYGAFSENVIINYTLQ-ILRGLAYLHDNQIIHRDLKGANLLVDSTGQrLRIADFGAAARLASKGTG---AGEFQGQLLGT 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 212 LPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKdmpatqmlleklngtvpclldtstipaeeltmspsrsvaN 291
Cdd:cd06630   172 IAFMAPEVLRG--EQYGRSCDVWSVGCVIIEMATAKPPWN---------------------------------------A 210
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 292 SGLSDSLTTSTPRPSNGDSPSHPYHrtFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFK 351
Cdd:cd06630   211 EKISNHLALIFKIASATTPPPIPEH--LSPGLRDVTLRCLELQPEDRPPARELLKHPVFT 268
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
40-252 1.74e-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: 66.97  E-value: 1.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKG-FEDLMtvnLARYKPTGEYVTVRRINLEACSNEMvTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVT 118
Cdd:cd14167     5 YDFREVLGTGaFSEVV---LAEEKRTQKLVAIKCIAKKALEGKE-TSIENEIAVLHKIKHPNIVALDDIYESGGHLYLIM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 119 SFMAYGSAKDLICTHFMdgMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHIL---ISVDGKVYLSGLrsNLSMIS-H 194
Cdd:cd14167    81 QLVSGGELFDRIVEKGF--YTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDF--GLSKIEgS 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1394533236 195 GQRQRVVHDFPKYsvkvlpwLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKD 252
Cdd:cd14167   157 GSVMSTACGTPGY-------VAPEVLAQ--KPYSKAVDCWSIGVIAYILLCGYPPFYD 205
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
70-346 2.25e-12

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: 67.04  E-value: 2.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  70 VRRINLEACSNEMVTF---LQGELHVSKLFNHPNIVPYRA-TFIADNELWVVtsfMAYG--SAKDLICTHFMDGMNELAI 143
Cdd:cd14001    33 VKKINSKCDKGQRSLYqerLKEEAKILKSLNHPNIVGFRAfTKSEDGSLCLA---MEYGgkSLNDLIEERYEAGLGPFPA 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 144 AYILQ---GVLKALDYIHHMGYV-HRSVKASHILISVDGK--------VYLSgLRSNLSMISHGQRQRVVHDfpkysvkv 211
Cdd:cd14001   110 ATILKvalSIARALEYLHNEKKIlHGDIKSGNVLIKGDFEsvklcdfgVSLP-LTENLEVDSDPKAQYVGTE-------- 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 212 lPWLSPEVLQQNLQGYDaKSDIYSVGITACELanghvpfkdmpatqMLLEklngtvpclldtstIPAEELTMSPSRSVAN 291
Cdd:cd14001   181 -PWKAKEALEEGGVITD-KADIFAYGLVLWEM--------------MTLS--------------VPHLNLLDIEDDDEDE 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1394533236 292 SGLSDSLTTSTPRPSNGDSPSHPYHrTFSPHFHHFVE---QCLQRNPDARPSASTLLN 346
Cdd:cd14001   231 SFDEDEEDEEAYYGTLGTRPALNLG-ELDDSYQKVIElfyACTQEDPKDRPSAAHIVE 287
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
40-358 2.30e-12

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: 67.06  E-value: 2.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTS 119
Cdd:cd14086     3 YDLKEELGKG--AFSVVRRCVQKSTGQEFAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 120 FMAYGSA-KDLICTHFmdgMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGK---VYLSGLrsNLSMISHG 195
Cdd:cd14086    81 LVTGGELfEDIVAREF---YSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSKgaaVKLADF--GLAIEVQG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 196 QRQRvVHDF---PKYsvkvlpwLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVpclld 272
Cdd:cd14086   156 DQQA-WFGFagtPGY-------LSPEVLRK--DPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAY----- 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 273 tstipaeeltmspsrsvansglsdslttstprpsngDSPShPYHRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQ 352
Cdd:cd14086   221 ------------------------------------DYPS-PEWDTVTPEAKDLINQMLTVNPAKRITAAEALKHPWICQ 263

                  ....*.
gi 1394533236 353 IKRRAS 358
Cdd:cd14086   264 RDRVAS 269
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
42-258 2.41e-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: 66.96  E-value: 2.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  42 LLTVIGKGfeDLMTVNLARYKP----TGEYVTVRRinLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIA--DNELW 115
Cdd:cd14205     8 FLQQLGKG--NFGSVEMCRYDPlqdnTGEVVAVKK--LQHSTEEHLRDFEREIEILKSLQHDNIVKYKGVCYSagRRNLR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 116 VVTSFMAYGSAKDLICTHfMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLrsnlsmishG 195
Cdd:cd14205    84 LIMEYLPYGSLRDYLQKH-KERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDF---------G 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1394533236 196 QRQRVVHDFPKYSVK-----VLPWLSPEVLQQNlqGYDAKSDIYSVGITACELANGHVPFKDMPATQM 258
Cdd:cd14205   154 LTKVLPQDKEYYKVKepgesPIFWYAPESLTES--KFSVASDVWSFGVVLYELFTYIEKSKSPPAEFM 219
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
40-349 2.77e-12

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: 66.55  E-value: 2.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRInlEACSNEMVTflqGELHVSKLFNHPNIVPYRATFIADNELWVVTS 119
Cdd:cd14010     2 YVLYDEIGRG--KHSVVYKGRRKGTIEFVAIKCV--DKSKRPEVL---NEVRLTHELKHPNVLKFYEWYETSNHLWLVVE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 120 FMAYGSAKDLICTHfmDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSG----------LRSNL 189
Cdd:cd14010    75 YCTGGDLETLLRQD--GNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDfglarregeiLKELF 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 190 SMISHGQRQRVVHDfpKYSVKVLP-WLSPEVLQQNLQGYDakSDIYSVGITACELANGHVPFKdmpatqmlleklngtvp 268
Cdd:cd14010   153 GQFSDEGNVNKVSK--KQAKRGTPyYMAPELFQGGVHSFA--SDLWALGCVLYEMFTGKPPFV----------------- 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 269 clldtstipAEELTmspsrSVANSGLSDSltTSTPRPSNGDSPshpyhrtfSPHFHHFVEQCLQRNPDARPSASTLLNHS 348
Cdd:cd14010   212 ---------AESFT-----ELVEKILNED--PPPPPPKVSSKP--------SPDFKSLLKGLLEKDPAKRLSWDELVKHP 267

                  .
gi 1394533236 349 F 349
Cdd:cd14010   268 F 268
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
46-249 3.53e-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: 65.98  E-value: 3.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  46 IGKGFedLMTVNLARYKPTGEyVTVRRINLEacSNEMVTFLQgELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGS 125
Cdd:cd14065     1 LGKGF--FGEVYKVTHRETGK-VMVMKELKR--FDEQRSFLK-EVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 126 AKDLICTHfMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISvdgkvylsglrsnlsmISHGQRQRVVHDF- 204
Cdd:cd14065    75 LEELLKSM-DEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVR----------------EANRGRNAVVADFg 137
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1394533236 205 ----------------PKYSVKVLP-WLSPEVLQQNLqgYDAKSDIYSVGITACELAnGHVP 249
Cdd:cd14065   138 larempdektkkpdrkKRLTVVGSPyWMAPEMLRGES--YDEKVDVFSFGIVLCEII-GRVP 196
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
40-250 3.76e-12

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: 66.92  E-value: 3.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKG-FEDlmtVNLARYKPTGEYVTVRRINLEacsnEMVTFLQgELHVsklfnhpnivpyRAT----FIADNEl 114
Cdd:cd05573     3 FEVIKVIGRGaFGE---VWLVRDKDTGQVYAMKILRKS----DMLKREQ-IAHV------------RAErdilADADSP- 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 115 WVVTSFMAYGSAKDL-ICTHFMDG---MN----------ELAIAYILQGVLkALDYIHHMGYVHRSVKASHILISVDGKV 180
Cdd:cd05573    62 WIVRLHYAFQDEDHLyLVMEYMPGgdlMNllikydvfpeETARFYIAELVL-ALDSLHKLGFIHRDIKPDNILLDADGHI 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 181 YLSGLRSNLSMISHGQR-----QRVVHDFPKYSVKVLPWL-----------------SPEVLQQnlQGYDAKSDIYSVGI 238
Cdd:cd05573   141 KLADFGLCTKMNKSGDResylnDSVNTLFQDNVLARRRPHkqrrvraysavgtpdyiAPEVLRG--TGYGPECDWWSLGV 218
                         250
                  ....*....|..
gi 1394533236 239 TACELANGHVPF 250
Cdd:cd05573   219 ILYEMLYGFPPF 230
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
40-250 3.87e-12

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: 67.33  E-value: 3.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRIN-LEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVT 118
Cdd:cd05621    54 YDVVKVIGRG--AFGEVQLVRHKASQKVYAMKLLSkFEMIKRSDSAFFWEERDIMAFANSPWVVQLFCAFQDDKYLYMVM 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 119 SFMAYGSAKDLICTHfmDGMNELAIAYILQGVLkALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMISHGqrq 198
Cdd:cd05621   132 EYMPGGDLVNLMSNY--DVPEKWAKFYTAEVVL-ALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFGTCMKMDETG--- 205
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1394533236 199 rVVHdfPKYSVKVLPWLSPEVLQ-QNLQGYDAKS-DIYSVGITACELANGHVPF 250
Cdd:cd05621   206 -MVH--CDTAVGTPDYISPEVLKsQGGDGYYGREcDWWSVGVFLFEMLVGDTPF 256
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
61-260 3.99e-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: 3.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  61 YK---PTGEYVTVRRINLEACsNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLIctHFMDG 137
Cdd:cd14066    10 YKgvlENGTVVAVKRLNEMNC-AASKKEFLTELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPNGSLEDRL--HCHKG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 138 MNEL---AIAYILQGVLKALDYIHHMGY---VHRSVKASHILISVDGKVYLSGLRSNLSMISHGQRQRVVHdfpkySVKV 211
Cdd:cd14066    87 SPPLpwpQRLKIAKGIARGLEYLHEECPppiIHGDIKSSNILLDEDFEPKLTDFGLARLIPPSESVSKTSA-----VKGT 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1394533236 212 LPWLSPEVLQQNLqgYDAKSDIYSVGITACELANGHVPFKDMPATQMLL 260
Cdd:cd14066   162 IGYLAPEYIRTGR--VSTKSDVYSFGVVLLELLTGKPAVDENRENASRK 208
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
97-349 4.16e-12

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: 65.84  E-value: 4.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  97 NHPNIVPYRA---TFIADNELWVV---TSFMAYGSAKDLICTHF---MDGMNelaiAYILQgVLKALDYIHHMGYVHRSV 167
Cdd:cd14012    56 RHPNLVSYLAfsiERRGRSDGWKVyllTEYAPGGSLSELLDSVGsvpLDTAR----RWTLQ-LLEALEYLHRNGVVHKSL 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 168 KASHILISVD---GKVYLSGL---RSNLSMISHGqrqrvvhdfPKYSVKVLPWLSPEVLQQNLQgYDAKSDIYSVGITAC 241
Cdd:cd14012   131 HAGNVLLDRDagtGIVKLTDYslgKTLLDMCSRG---------SLDEFKQTYWLPPELAQGSKS-PTRKTDVWDLGLLFL 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 242 ELANGHVPFKDMPATQMLLEklngtvpclldtstipaeeltmspsrsvansglSDSLttstprpsngdspshpyhrtfSP 321
Cdd:cd14012   201 QMLFGLDVLEKYTSPNPVLV---------------------------------SLDL---------------------SA 226
                         250       260
                  ....*....|....*....|....*...
gi 1394533236 322 HFHHFVEQCLQRNPDARPSASTLLNHSF 349
Cdd:cd14012   227 SLQDFLSKCLSLDPKKRPTALELLPHEF 254
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
40-238 7.84e-12

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: 65.47  E-value: 7.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKG-FEDlmtVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLfNHPNIVPYRATFIADNELWVVT 118
Cdd:cd14046     8 FEELQVLGKGaFGQ---VVKVRNKLDGRYYAIKKIKLRSESKNNSRILREVMLLSRL-NHQHVVRYYQAWIERANLYIQM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 119 SFMAYGSAKDLICTHFMDGMNElaIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNLSMISHGQ 196
Cdd:cd14046    84 EYCEKSTLRDLIDSGLFQDTDR--LWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGdfGLATSNKLNVELA 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1394533236 197 RQRVVHdfpKYSVKVLP------------WLSPEVLQQNLQGYDAKSDIYSVGI 238
Cdd:cd14046   162 TQDINK---STSAALGSsgdltgnvgtalYVAPEVQSGTKSTYNEKVDMYSLGI 212
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
35-353 7.93e-12

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: 65.60  E-value: 7.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  35 PEGGCYELLTVIGKG-FEdlmTVNLARYKPTGEYVTVRRInleacsnemvtfLQG------ELHVSKLFNHPNIVPYRAT 107
Cdd:cd14137     1 PVEISYTIEKVIGSGsFG---VVYQAKLLETGEVVAIKKV------------LQDkryknrELQIMRRLKHPNIVKLKYF 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 108 FIADNE------LWVVTSFMAYgsakDL--ICTHFMDGMNELAIAYI----LQgVLKALDYIHHMGYVHRSVKASHILIS 175
Cdd:cd14137    66 FYSSGEkkdevyLNLVMEYMPE----TLyrVIRHYSKNKQTIPIIYVklysYQ-LFRGLAYLHSLGICHRDIKPQNLLVD 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 176 VDgkvylsglrsnlSMIShgqrqrVVHDFPkySVKVL----PWLS---------PEVLQQNlQGYDAKSDIYSVGitaC- 241
Cdd:cd14137   141 PE------------TGVL------KLCDFG--SAKRLvpgePNVSyicsryyraPELIFGA-TDYTTAIDIWSAG---Cv 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 242 --ELANGHVPFKDMPATQMLLE--KLNGTvpclldtstiPAEE--LTMSPSRsvansglsdsltTSTPRPsngDSPSHPY 315
Cdd:cd14137   197 laELLLGQPLFPGESSVDQLVEiiKVLGT----------PTREqiKAMNPNY------------TEFKFP---QIKPHPW 251
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1394533236 316 HRTFSPHFHH----FVEQCLQRNPDARPSASTLLNHSFFKQI 353
Cdd:cd14137   252 EKVFPKRTPPdaidLLSKILVYNPSKRLTALEALAHPFFDEL 293
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
89-250 9.33e-12

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: 65.44  E-value: 9.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  89 ELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLIcTHFMDG---MNELAIAYILQGVLKALDYIHHMGYVHR 165
Cdd:cd08229    74 EIDLLKQLNHPNVIKYYASFIEDNELNIVLELADAGDLSRMI-KHFKKQkrlIPEKTVWKYFVQLCSALEHMHSRRVMHR 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 166 SVKASHILISVDGKVYLSGLRSNLSMISHGQRQRVVHDFPKYsvkvlpwLSPEVLQQNlqGYDAKSDIYSVGITACELAN 245
Cdd:cd08229   153 DIKPANVFITATGVVKLGDLGLGRFFSSKTTAAHSLVGTPYY-------MSPERIHEN--GYNFKSDIWSLGCLLYEMAA 223

                  ....*
gi 1394533236 246 GHVPF 250
Cdd:cd08229   224 LQSPF 228
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
64-315 1.00e-11

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


Pssm-ID: 270819 [Multi-domain]  Cd Length: 264  Bit Score: 64.66  E-value: 1.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  64 TGEYVTVRRINLEACSNEM---VTFLQGELHVSKLFNHPNIVPYRATfIADNE---LWVVTSFMAYGSAKDLICTH--FM 135
Cdd:cd06653    26 TGRELAVKQVPFDPDSQETskeVNALECEIQLLKNLRHDRIVQYYGC-LRDPEekkLSIFVEYMPGGSVKDQLKAYgaLT 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 136 DGMNELAIAYILQGVlkalDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNLSMIS-HGQRQRVVHDFPKysvkvl 212
Cdd:cd06653   105 ENVTRRYTRQILQGV----SYLHSNMIVHRDIKGANILRDSAGNVKLGdfGASKRIQTICmSGTGIKSVTGTPY------ 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 213 pWLSPEVLqqNLQGYDAKSDIYSVGITACELANGHVPFKDMPAtqmlleklngtVPCLLDTSTIPAEELTMSPSRSVANS 292
Cdd:cd06653   175 -WMSPEVI--SGEGYGRKADVWSVACTVVEMLTEKPPWAEYEA-----------MAAIFKIATQPTKPQLPDGVSDACRD 240
                         250       260
                  ....*....|....*....|...
gi 1394533236 293 GLSDSLTTSTPRPSNGDSPSHPY 315
Cdd:cd06653   241 FLRQIFVEEKRRPTAEFLLRHPF 263
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
40-251 1.25e-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: 64.20  E-value: 1.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKG-FEdlmTVNLARYKPTGEYVTVRRINLEAC-SNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVV 117
Cdd:cd05578     2 FQILRVIGKGsFG---KVCIVQKKDTKKMFAMKYMNKQKCiEKDSVRNVLNELEILQELEHPFLVNLWYSFQDEEDMYMV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 118 TSFMAYGsakDLIcTHF--MDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLrsNLSMISHG 195
Cdd:cd05578    79 VDLLLGG---DLR-YHLqqKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDF--NIATKLTD 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1394533236 196 QRQRVVhdfpkySVKVLPWLSPEVLQqnLQGYDAKSDIYSVGITACELANGHVPFK 251
Cdd:cd05578   153 GTLATS------TSGTKPYMAPEVFM--RAGYSFAVDWWSLGVTAYEMLRGKRPYE 200
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
42-250 1.85e-11

Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mos (or c-Mos) is a germ-cell specific kinase that plays roles in both the release of primary arrest and the induction of secondary arrest in oocytes. It is expressed towards the end of meiosis I and is quickly degraded upon fertilization. It is a component of the cytostatic factor (CSF), which is responsible for metaphase II arrest. In addition, Mos activates a phoshorylation cascade that leads to the activation of the p34 subunit of MPF (mitosis-promoting factor or maturation promoting factor), a cyclin-dependent kinase that is responsible for the release of primary arrest in meiosis I. The Mos subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270881 [Multi-domain]  Cd Length: 265  Bit Score: 63.94  E-value: 1.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  42 LLTVIGKGfeDLMTVNLARYKptGEYVTVRRINLEACSNEMVTFLQGELHVSKLfNHPNIVPYRA--TFIADNELWVVTs 119
Cdd:cd13979     7 LQEPLGSG--GFGSVYKATYK--GETVAVKIVRRRRKNRASRQSFWAELNAARL-RHENIVRVLAaeTGTDFASLGLII- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 120 fMAYGSAKDLicTHFMDGMNELAIAY----ILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSM---I 192
Cdd:cd13979    81 -MEYCGNGTL--QQLIYEGSEPLPLAhrilISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCSVKLgegN 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1394533236 193 SHGQRQRVVHDFPKYsvkvlpwLSPEVLQQNLQGydAKSDIYSVGITACELANGHVPF 250
Cdd:cd13979   158 EVGTPRSHIGGTYTY-------RAPELLKGERVT--PKADIYSFGITLWQMLTRELPY 206
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
98-254 1.93e-11

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: 64.66  E-value: 1.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  98 HPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTHFMdgMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILIsvd 177
Cdd:cd14176    72 HPNIITLKDVYDDGKYVYVVTELMKGGELLDKILRQKF--FSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILY--- 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 178 gkVYLSGLRSNLSMISHGQRQRVVHD-----FPKYSVKvlpWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKD 252
Cdd:cd14176   147 --VDESGNPESIRICDFGFAKQLRAEngllmTPCYTAN---FVAPEVLER--QGYDAACDIWSLGVLLYTMLTGYTPFAN 219

                  ..
gi 1394533236 253 MP 254
Cdd:cd14176   220 GP 221
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
40-252 1.95e-11

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: 64.14  E-value: 1.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRIN---------LEACSNEmvtflqgeLHVSKLFNHPNIVPYRATFIA 110
Cdd:cd05580     3 FEFLKTLGTG--SFGRVRLVKHKDSGKYYALKILKkakiiklkqVEHVLNE--------KRILSEVRHPFIVNLLGSFQD 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 111 DNELWVVTSFMAYGSAKDLI--CTHFMdgmNELAIAYILQgVLKALDYIHHMGYVHRSVKASHILISVDGkvylsglrsN 188
Cdd:cd05580    73 DRNLYMVMEYVPGGELFSLLrrSGRFP---NDVAKFYAAE-VVLALEYLHSLDIVYRDLKPENLLLDSDG---------H 139
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1394533236 189 LSMISHGQRQRVvhDFPKYSVKVLP-WLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKD 252
Cdd:cd05580   140 IKITDFGFAKRV--KDRTYTLCGTPeYLAPEIILS--KGHGKAVDWWALGILIYEMLAGYPPFFD 200
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
40-263 2.07e-11

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 65.91  E-value: 2.07e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236   40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFI--ADNELWVV 117
Cdd:PTZ00266    15 YEVIKKIGNG--RFGEVFLVKHKRTQEFFCWKAISYRGLKEREKSQLVIEVNVMRELKHKNIVRYIDRFLnkANQKLYIL 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  118 TSFMAYGSAKDLI--CTHFMDGMNELAIAYILQGVLKALDYIHHMG-------YVHRSVKASHILISVD----GKVYLSG 184
Cdd:PTZ00266    93 MEFCDAGDLSRNIqkCYKMFGKIEEHAIVDITRQLLHALAYCHNLKdgpngerVLHRDLKPQNIFLSTGirhiGKITAQA 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  185 LRSNLSMISH----GQRQRVVHDFPKYSVKVLPWL-SPEVLQQNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQML 259
Cdd:PTZ00266   173 NNLNGRPIAKigdfGLSKNIGIESMAHSCVGTPYYwSPELLLHETKSYDDKSDMWALGCIIYELCSGKTPFHKANNFSQL 252

                   ....
gi 1394533236  260 LEKL 263
Cdd:PTZ00266   253 ISEL 256
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
36-253 2.79e-11

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: 63.35  E-value: 2.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  36 EGGCYELLTVIGKGfeDLMTVNLARYKPTGE---YVTVRRINLEACSNEMVTFLqGELHVSKLFNHPNIVPYRATFIADN 112
Cdd:cd05066     2 DASCIKIEKVIGAG--EFGEVCSGRLKLPGKreiPVAIKTLKAGYTEKQRRDFL-SEASIMGQFDHPNIIHLEGVVTRSK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 113 ELWVVTSFMAYGSAKDLICTHfmDG-MNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISvdgkvylsglrSNL-S 190
Cdd:cd05066    79 PVMIVTEYMENGSLDAFLRKH--DGqFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVN-----------SNLvC 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 191 MISHGQRQRVVHDFPK--YSVK--VLP--WLSPEVLQqnLQGYDAKSDIYSVGITACE-LANGHVPFKDM 253
Cdd:cd05066   146 KVSDFGLSRVLEDDPEaaYTTRggKIPirWTAPEAIA--YRKFTSASDVWSYGIVMWEvMSYGERPYWEM 213
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
40-349 2.99e-11

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


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 63.39  E-value: 2.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGFEDlmTVNLARYkPTGEYVTVRRINLEACSNEMVTFLQGEL-HVSKLFNHPNIVP---YRATFiADNELW 115
Cdd:cd14131     3 YEILKQLGKGGSS--KVYKVLN-PKKKIYALKRVDLEGADEQTLQSYKNEIeLLKKLKGSDRIIQlydYEVTD-EDDYLY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 116 VVtsfMAYGSAkDL---ICTHFMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILIsVDGkvylsglrsNLSMI 192
Cdd:cd14131    79 MV---MECGEI-DLatiLKKKRPKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLL-VKG---------RLKLI 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 193 shgqrqrvvhDF------PKYSVKV--------LPWLSPEVLQQNLQGYDAK--------SDIYSVGITACELANGHVPF 250
Cdd:cd14131   145 ----------DFgiakaiQNDTTSIvrdsqvgtLNYMSPEAIKDTSASGEGKpkskigrpSDVWSLGCILYQMVYGKTPF 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 251 KDMPAtqmLLEKLNGtvpcLLDtstiPAEELTMSPsrsVANSGLSDSLttstprpsngdspshpyhrtfsphfhhfvEQC 330
Cdd:cd14131   215 QHITN---PIAKLQA----IID----PNHEIEFPD---IPNPDLIDVM-----------------------------KRC 251
                         330
                  ....*....|....*....
gi 1394533236 331 LQRNPDARPSASTLLNHSF 349
Cdd:cd14131   252 LQRDPKKRPSIPELLNHPF 270
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
46-243 3.34e-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: 63.30  E-value: 3.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  46 IGKG-FEDLMTVNlarYKPTGEYVTVRRinLEACSNE-MVTFLQgELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAY 123
Cdd:cd14154     1 LGKGfFGQAIKVT---HRETGEVMVMKE--LIRFDEEaQRNFLK-EVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 124 GSAKDLIctHFMDG----MNELAIAyilQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GL---------RSN 188
Cdd:cd14154    75 GTLKDVL--KDMARplpwAQRVRFA---KDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVAdfGLarliveerlPSG 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1394533236 189 LSMISHGQRQRVVHDFPK-YSVKVLP-WLSPEVLqqNLQGYDAKSDIYSVGITACEL 243
Cdd:cd14154   150 NMSPSETLRHLKSPDRKKrYTVVGNPyWMAPEML--NGRSYDEKVDIFSFGIVLCEI 204
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
37-250 3.37e-11

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 64.82  E-value: 3.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  37 GGCYELLTVIGKG-------FEDL----------MTVNLARyKPTgeyvTVRRINLEACSnemvtflqgelhVSKLfNHP 99
Cdd:NF033483    6 GGRYEIGERIGRGgmaevylAKDTrldrdvavkvLRPDLAR-DPE----FVARFRREAQS------------AASL-SHP 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 100 NIV-----------PYratfIAdnelwvvtsfMAY--GSA-KDLICTHFMdgMNELAIAYILQGVLKALDYIHHMGYVHR 165
Cdd:NF033483   68 NIVsvydvgedggiPY----IV----------MEYvdGRTlKDYIREHGP--LSPEEAVEIMIQILSALEHAHRNGIVHR 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 166 SVKASHILISVDGKVYLS--GL-R--SNLSMIshgQRQRV---VHdfpkYsvkvlpwLSPEvlqQNLQGY-DAKSDIYSV 236
Cdd:NF033483  132 DIKPQNILITKDGRVKVTdfGIaRalSSTTMT---QTNSVlgtVH----Y-------LSPE---QARGGTvDARSDIYSL 194
                         250
                  ....*....|....
gi 1394533236 237 GITACELANGHVPF 250
Cdd:NF033483  195 GIVLYEMLTGRPPF 208
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
64-349 3.44e-11

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: 63.14  E-value: 3.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  64 TGEYVTVRRINLEACSNEM---VTFLQGELHVSKLFNHPNIVPYRAtFIADNELWVVTSFMAY---GSAKDLICTHfmDG 137
Cdd:cd06652    26 TGRELAVKQVQFDPESPETskeVNALECEIQLLKNLLHERIVQYYG-CLRDPQERTLSIFMEYmpgGSIKDQLKSY--GA 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 138 MNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNLSMIS-HGQRQRVVHDFPKysvkvlpW 214
Cdd:cd06652   103 LTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGdfGASKRLQTIClSGTGMKSVTGTPY-------W 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 215 LSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPAtqmlleklngtvpclldtstipaeeltMSPSRSVANsgl 294
Cdd:cd06652   176 MSPEVISG--EGYGRKADIWSVGCTVVEMLTEKPPWAEFEA---------------------------MAAIFKIAT--- 223
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1394533236 295 sdslttstpRPSNGDSPSH--PYHRTFSPHFhhFVEQCLqrnpdaRPSASTLLNHSF 349
Cdd:cd06652   224 ---------QPTNPQLPAHvsDHCRDFLKRI--FVEAKL------RPSADELLRHTF 263
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
39-264 3.49e-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: 63.16  E-value: 3.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  39 CYELLTVIGKG-FEDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLqGELHVSKLFNHPNIVPYRATFIADNELWVV 117
Cdd:cd05033     5 YVTIEKVIGGGeFGEVCSGSLKLPGKKEIDVAIKTLKSGYSDKQRLDFL-TEASIMGQFDHPNVIRLEGVVTKSRPVMIV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 118 TSFMAYGSAKDLICTHfmDG-MNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVD--GKVYLSGLrsnlsmish 194
Cdd:cd05033    84 TEYMENGSLDKFLREN--DGkFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDlvCKVSDFGL--------- 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1394533236 195 gqrQRVVHDF-PKYSVK----VLPWLSPEVLQqnLQGYDAKSDIYSVGITACE-LANGHVPFKDMPaTQMLLEKLN 264
Cdd:cd05033   153 ---SRRLEDSeATYTTKggkiPIRWTAPEAIA--YRKFTSASDVWSFGIVMWEvMSYGERPYWDMS-NQDVIKAVE 222
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
58-349 3.78e-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: 62.91  E-value: 3.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  58 LARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVtsfMAYGSAKDLIC-THFMD 136
Cdd:cd08218    18 LVKSKEDGKQYVIKEINISKMSPKEREESRKEVAVLSKMKHPNIVQYQESFEENGNLYIV---MDYCDGGDLYKrINAQR 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 137 GMN---ELAIAYILQGVLkALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMISHGQRQRVVHDFPKYsvkvlp 213
Cdd:cd08218    95 GVLfpeDQILDWFVQLCL-ALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARVLNSTVELARTCIGTPYY------ 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 214 wLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPclldtstipaeeltmspsrsvansg 293
Cdd:cd08218   168 -LSPEICEN--KPYNNKSDIWALGCVLYEMCTLKHAFEAGNMKNLVLKIIRGSYP------------------------- 219
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1394533236 294 lsdslttstPRPSNgdspshpyhrtFSPHFHHFVEQCLQRNPDARPSASTLLNHSF 349
Cdd:cd08218   220 ---------PVPSR-----------YSYDLRSLVSQLFKRNPRDRPSINSILEKPF 255
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
38-257 4.76e-11

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: 62.85  E-value: 4.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  38 GCYELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRIN---------------LEACSNEMVTFLqgELHVSKLFNHPNIV 102
Cdd:cd14077     1 GNWEFVKTIGAG--SMGKVKLAKHIRTGEKCAIKIIPrasnaglkkerekrlEKEISRDIRTIR--EAALSSLLNHPHIC 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 103 PYRATFIADNELWVVTSFMAYGSAKDLICTHfmDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYL 182
Cdd:cd14077    77 RLRDFLRTPNHYYMLFEYVDGGQLLDYIISH--GKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 183 --SGLrSNLSmishgQRQRVVHDFpkysVKVLPWLSPEVLQQnlQGYDA-KSDIYSVGITACELANGHVPFKD--MPATQ 257
Cdd:cd14077   155 idFGL-SNLY-----DPRRLLRTF----CGSLYFAAPELLQA--QPYTGpEVDVWSFGVVLYVLVCGKVPFDDenMPALH 222
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
86-350 5.35e-11

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: 62.57  E-value: 5.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  86 LQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTHfmDGMNELAIAYILQGVLKALDYIHHMGYVHR 165
Cdd:cd14099    48 LKSEIKIHRSLKHPNIVKFHDCFEDEENVYILLELCSNGSLMELLKRR--KALTEPEVRYFMRQILSGVKYLHSNRIIHR 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 166 SVKASHILISVDGKVYLS--GLRSNLSmiSHGQRQRVVHDFPKYsvkvlpwLSPEVLqQNLQGYDAKSDIYSVGITACEL 243
Cdd:cd14099   126 DLKLGNLFLDENMNVKIGdfGLAARLE--YDGERKKTLCGTPNY-------IAPEVL-EKKKGHSFEVDIWSLGVILYTL 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 244 ANGHVPFkdmpatqmlleklngtvpcllDTSTIpaeELTMSPSRSVANSglsdslttstprpsngdSPSHPyhrTFSPHF 323
Cdd:cd14099   196 LVGKPPF---------------------ETSDV---KETYKRIKKNEYS-----------------FPSHL---SISDEA 231
                         250       260
                  ....*....|....*....|....*..
gi 1394533236 324 HHFVEQCLQRNPDARPSASTLLNHSFF 350
Cdd:cd14099   232 KDLIRSMLQPDPTKRPSLDEILSHPFF 258
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
124-349 6.39e-11

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: 60.88  E-value: 6.39e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  124 GSAKDLIcTHFMDGMNELAIAYILQGVLKALDYihhmgyVHRSVKASHILISVDGKVYLSGlrsnlsmiSHGQRQRVVHD 203
Cdd:smart00750   1 VSLADIL-EVRGRPLNEEEIWAVCLQCLGALRE------LHRQAKSGNILLTWDGLLKLDG--------SVAFKTPEQSR 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  204 FPKYsvkvlpWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPfkdmpatqmlleklngtvpclldtstiPAEELTM 283
Cdd:smart00750  66 PDPY------FMAPEVIQG--QSYTEKADIYSLGITLYEALDYELP---------------------------YNEEREL 110
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1394533236  284 SPSRsvansglsDSLTTSTPRPSNGDSPShPYHRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSF 349
Cdd:smart00750 111 SAIL--------EILLNGMPADDPRDRSN-LEGVSAARSFEDFMRLCASRLPQRREAANHYLAHCR 167
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
56-345 6.50e-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: 62.61  E-value: 6.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  56 VNLARYKP----TGEYVTVRRINLEaCSNEMVTFLQGELHVSKLFNHPNIVPYRA--TFIADNELWVVTSFMAYGSAKDL 129
Cdd:cd05080    20 VSLYCYDPtndgTGEMVAVKALKAD-CGPQHRSGWKQEIDILKTLYHENIVKYKGccSEQGGKSLQLIMEYVPLGSLRDY 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 130 ICTHfmdgmnELAIAYIL---QGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNLSMISHGQRQRVVHDF 204
Cdd:cd05080    99 LPKH------SIGLAQLLlfaQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGdfGLAKAVPEGHEYYRVREDGDS 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 205 PKYsvkvlpWLSPEVLQQNLQGYdaKSDIYSVGITACELANgHVPFKDMPATQmlLEKLNGTVPCLLdtSTIPAEELTMS 284
Cdd:cd05080   173 PVF------WYAPECLKEYKFYY--ASDVWSFGVTLYELLT-HCDSSQSPPTK--FLEMIGIAQGQM--TVVRLIELLER 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1394533236 285 PSRsvansglsdslttsTPRPSNgdSPSHPYhrtfsphfhHFVEQCLQRNPDARPSASTLL 345
Cdd:cd05080   240 GER--------------LPCPDK--CPQEVY---------HLMKNCWETEASFRPTFENLI 275
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
89-347 7.79e-11

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: 61.90  E-value: 7.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  89 ELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTHFMdgMNELAIAYILQGVLKALDYIHHMGYVHRSVK 168
Cdd:cd14006    39 EISILNQLQHPRIIQLHEAYESPTELVLILELCSGGELLDRLAERGS--LSEEEVRTYMRQLLEGLQYLHNHHILHLDLK 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 169 ASHILISvdgkvylSGLRSNLSMISHGQRQRVVHDFPKYSVKVLP-WLSPEVLQQNLQGYdaKSDIYSVGITACELANGH 247
Cdd:cd14006   117 PENILLA-------DRPSPQIKIIDFGLARKLNPGEELKEIFGTPeFVAPEIVNGEPVSL--ATDMWSIGVLTYVLLSGL 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 248 VPFKDMPAtqmlLEKLNGTVPCLLDtstipAEELTmspsrsvaNSGLSDSLTTstprpsngdspshpyhrtfsphfhhFV 327
Cdd:cd14006   188 SPFLGEDD----QETLANISACRVD-----FSEEY--------FSSVSQEAKD-------------------------FI 225
                         250       260
                  ....*....|....*....|
gi 1394533236 328 EQCLQRNPDARPSASTLLNH 347
Cdd:cd14006   226 RKLLVKEPRKRPTAQEALQH 245
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
23-352 8.72e-11

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: 62.75  E-value: 8.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  23 SFSKQEVMSSFLPEGGCYELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIV 102
Cdd:cd07877     2 TFYRQELNKTIWEVPERYQNLSPVGSG--AYGSVCAAFDTKTGLRVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHENVI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 103 -------PYRaTFIADNELWVVTSFMAYGSAKDLICTHFMDGMNELAIAYILQGvlkaLDYIHHMGYVHRSVKASHILIS 175
Cdd:cd07877    80 glldvftPAR-SLEEFNDVYLVTHLMGADLNNIVKCQKLTDDHVQFLIYQILRG----LKYIHSADIIHRDLKPSNLAVN 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 176 VDgkvylsglrSNLSMISHGQRQRVVHDFPKYsVKVLPWLSPEVLqQNLQGYDAKSDIYSVGITACELANGHVPFkdmPA 255
Cdd:cd07877   155 ED---------CELKILDFGLARHTDDEMTGY-VATRWYRAPEIM-LNWMHYNQTVDIWSVGCIMAELLTGRTLF---PG 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 256 TqmllEKLNGTVPCLLDTSTIPAEELTMSPSRSVANsglsdsLTTSTPRpsngdSPSHPYHRTF---SPHFHHFVEQCLQ 332
Cdd:cd07877   221 T----DHIDQLKLILRLVGTPGAELLKKISSESARN------YIQSLTQ-----MPKMNFANVFigaNPLAVDLLEKMLV 285
                         330       340
                  ....*....|....*....|
gi 1394533236 333 RNPDARPSASTLLNHSFFKQ 352
Cdd:cd07877   286 LDSDKRITAAQALAHAYFAQ 305
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
40-350 9.37e-11

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: 62.35  E-value: 9.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGFEDLmtVNLARYKPTGEYVTVRRI---NLEAC-SNEM---VTFLQgelhvsKLFNHPNIVPYRATFIADN 112
Cdd:cd07832     2 YKILGRIGEGAHGI--VFKAKDRETGETVALKKValrKLEGGiPNQAlreIKALQ------ACQGHPYVVKLRDVFPHGT 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 113 ELWVVTSFMAyGSAKDLIcTHFMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLrsNLSMI 192
Cdd:cd07832    74 GFVLVFEYML-SSLSEVL-RDEERPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADF--GLARL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 193 SHGQRQRVvhdfpkYS--VKVLPWLSPEVLQQNlQGYDAKSDIYSVGITACELANGHVPF---KDMpatqmllEKLNgtv 267
Cdd:cd07832   150 FSEEDPRL------YShqVATRWYRAPELLYGS-RKYDEGVDLWAVGCIFAELLNGSPLFpgeNDI-------EQLA--- 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 268 pCLLDTSTIPAEELTmspsrsvanSGLsdsltTSTPRPSNGDSPSHPYHR------TFSPHFHHFVEQCLQRNPDARPSA 341
Cdd:cd07832   213 -IVLRTLGTPNEKTW---------PEL-----TSLPDYNKITFPESKGIRleeifpDCSPEAIDLLKGLLVYNPKKRLSA 277

                  ....*....
gi 1394533236 342 STLLNHSFF 350
Cdd:cd07832   278 EEALRHPYF 286
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
40-252 9.80e-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: 61.78  E-value: 9.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKG-FEDLMTVnlaRYKPTGEYVTVRRINLEACSNEmvtFLQGELHVSKLFNHPNIVPYRATFIADNELWVVT 118
Cdd:cd14087     3 YDIKALIGRGsFSRVVRV---EHRVTRQPYAIKMIETKCRGRE---VCESELNVLRRVRHTNIIQLIEVFETKERVYMVM 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 119 SFMAYGSAKDLICTHfmDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILisvdgkVYLSGLRSNLSMISHG--- 195
Cdd:cd14087    77 ELATGGELFDRIIAK--GSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLL------YYHPGPDSKIMITDFGlas 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1394533236 196 QRQRVVHDFPKYSVKVLPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKD 252
Cdd:cd14087   149 TRKKGPNCLMKTTCGTPEYIAPEILLR--KPYTQSVDMWAVGVIAYILLSGTMPFDD 203
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
89-350 1.02e-10

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: 61.57  E-value: 1.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  89 ELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTHFMdgMNELAIAYILQGVLKALDYIHHMGYVHRSVK 168
Cdd:cd14188    51 EIELHRILHHKHVVQFYHYFEDKENIYILLEYCSRRSMAHILKARKV--LTEPEVRYYLRQIVSGLKYLHEQEILHRDLK 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 169 ASHILI--SVDGKVYLSGLRSNLSMIshGQRQRVVHDFPKYsvkvlpwLSPEVLqqNLQGYDAKSDIYSVGITACELANG 246
Cdd:cd14188   129 LGNFFIneNMELKVGDFGLAARLEPL--EHRRRTICGTPNY-------LSPEVL--NKQGHGCESDIWALGCVMYTMLLG 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 247 HVPFKDMpatqmlleKLNGTVPCLLDtstipaeeltmspsrsvANSGLSDSLTTSTprpsngdspshpyhrtfsphfHHF 326
Cdd:cd14188   198 RPPFETT--------NLKETYRCIRE-----------------ARYSLPSSLLAPA---------------------KHL 231
                         250       260
                  ....*....|....*....|....
gi 1394533236 327 VEQCLQRNPDARPSASTLLNHSFF 350
Cdd:cd14188   232 IASMLSKNPEDRPSLDEIIRHDFF 255
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
55-258 1.02e-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: 61.51  E-value: 1.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  55 TVNLARYKPTGEYVTVRRINLeacsnemvtfLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTHF 134
Cdd:cd14060     8 SVYRAIWVSQDKEVAVKKLLK----------IEKEAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGSLFDYLNSNE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 135 MDGMNELAIAYILQGVLKALDYIHH---MGYVHRSVKASHILISVDGKVYLSGLRSNlSMISHGQRQRVVHDFpkysvkv 211
Cdd:cd14060    78 SEEMDMDQIMTWATDIAKGMHYLHMeapVKVIHRDLKSRNVVIAADGVLKICDFGAS-RFHSHTTHMSLVGTF------- 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1394533236 212 lPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQM 258
Cdd:cd14060   150 -PWMAPEVIQS--LPVSETCDTYSYGVVLWEMLTREVPFKGLEGLQV 193
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
45-253 1.06e-10

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: 61.90  E-value: 1.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  45 VIGKG-FEDlmtVNLARYKptGEYVTVRRINleacSNEMVTFL-QGELHVSKLFNHPNIVPYRATFIADN----ELWVVT 118
Cdd:cd14056     2 TIGKGrYGE---VWLGKYR--GEKVAVKIFS----SRDEDSWFrETEIYQTVMLRHENILGFIAADIKSTgswtQLWLIT 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 119 SFMAYGSAKDLICTHFMDGMNELAIAY-ILQGvlkaLDYIHH--MGY------VHRSVKASHILISVDGKVYLS--GLrs 187
Cdd:cd14056    73 EYHEHGSLYDYLQRNTLDTEEALRLAYsAASG----LAHLHTeiVGTqgkpaiAHRDLKSKNILVKRDGTCCIAdlGL-- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 188 nlsMISHGQRQRVVHDFPKYSVKVLPWLSPEVLQQNLQG--YDA--KSDIYSVGITACELA-----NGHV-----PFKDM 253
Cdd:cd14056   147 ---AVRYDSDTNTIDIPPNPRVGTKRYMAPEVLDDSINPksFESfkMADIYSFGLVLWEIArrceiGGIAeeyqlPYFGM 223
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
94-348 1.08e-10

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: 62.05  E-value: 1.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  94 KLFNHPNIVPYRATFIADNELWVVTSFMAYGSAkDLICTHFMD--GMNELAIAYILQGVLKALDYIHHMGYVHRSVKASH 171
Cdd:cd14052    58 TLDGHDNIVQLIDSWEYHGHLYIQTELCENGSL-DVFLSELGLlgRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPAN 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 172 ILISVDGKVYLS--GLRSNLSMISHGQRQ--RVvhdfpkysvkvlpWLSPEVLQQnlQGYDAKSDIYSVGITACELANGH 247
Cdd:cd14052   137 VLITFEGTLKIGdfGMATVWPLIRGIEREgdRE-------------YIAPEILSE--HMYDKPADIFSLGLILLEAAANV 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 248 VpfkdMPATQMLLEKL-NGtvpcllDTSTIPaeeltmspsrsvansGLSDSLTTSTPRPSNGDSPSHPYHRTFSPHFHHF 326
Cdd:cd14052   202 V----LPDNGDAWQKLrSG------DLSDAP---------------RLSSTDLHSASSPSSNPPPDPPNMPILSGSLDRV 256
                         250       260
                  ....*....|....*....|..
gi 1394533236 327 VEQCLQRNPDARPSASTLLNHS 348
Cdd:cd14052   257 VRWMLSPEPDRRPTADDVLATP 278
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
68-289 1.09e-10

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: 61.95  E-value: 1.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  68 VTVRRINLEACSNEMvTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLIctHFMDGMNELAIAYIL 147
Cdd:cd14202    31 VAVKCINKKNLAKSQ-TLLGKEIKILKELKHENIVALYDFQEIANSVYLVMEYCNGGDLADYL--HTMRTLSEDTIRLFL 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 148 QGVLKALDYIHHMGYVHRSVKASHILISvdgkvYLSGLRSN-----LSMISHGQRQRVVHDFPKYSVKVLP-WLSPEVLQ 221
Cdd:cd14202   108 QQIAGAMKMLHSKGIIHRDLKPQNILLS-----YSGGRKSNpnnirIKIADFGFARYLQNNMMAATLCGSPmYMAPEVIM 182
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1394533236 222 QnlQGYDAKSDIYSVGITACELANGHVPFK-DMPATQMLLEKLNGTVpclldTSTIPAEelTMSPSRSV 289
Cdd:cd14202   183 S--QHYDAKADLWSIGTIIYQCLTGKAPFQaSSPQDLRLFYEKNKSL-----SPNIPRE--TSSHLRQL 242
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
40-258 1.10e-10

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


Pssm-ID: 271071 [Multi-domain]  Cd Length: 277  Bit Score: 61.83  E-value: 1.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMvTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTS 119
Cdd:cd14169     5 YELKEKLGEG--AFSEVVLAQERGSQRLVALKCIPKKALRGKE-AMVENEIAVLRRINHENIVSLEDIYESPTHLYLAME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 120 FMAYGSAKDLICTHfmDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISV---DGKVYLSGLrsNLSMISHGQ 196
Cdd:cd14169    82 LVTGGELFDRIIER--GSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYATpfeDSKIMISDF--GLSKIEAQG 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1394533236 197 RQRVVHDFPKYsvkvlpwLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQM 258
Cdd:cd14169   158 MLSTACGTPGY-------VAPELLEQ--KPYGKAVDVWAIGVISYILLCGYPPFYDENDSEL 210
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
39-347 1.30e-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: 1.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  39 CYELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNE--MVtflQGELHVSKLFNHPNIVPYRATFIADNELWV 116
Cdd:cd14095     1 KYDIGRVIGDG--NFAVVKECRDKATDKEYALKIIDKAKCKGKehMI---ENEVAILRRVKHPNIVQLIEEYDTDTELYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 117 VtsfMAYGSAKDL-----ICTHFmdgmNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGkvylSGLRSnLSM 191
Cdd:cd14095    76 V---MELVKGGDLfdaitSSTKF----TERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHE----DGSKS-LKL 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 192 ISHGQRQRVVHdfPKYSVKVLP-WLSPEVLQQNlqGYDAKSDIYSVGITACELANGHVPFKDMPATQmllEKLngtvpcl 270
Cdd:cd14095   144 ADFGLATEVKE--PLFTVCGTPtYVAPEILAET--GYGLKVDIWAAGVITYILLCGFPPFRSPDRDQ---EEL------- 209
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1394533236 271 ldTSTIPAEELTMSPsrsvansglsdslttstprpsngdspshPYHRTFSPHFHHFVEQCLQRNPDARPSASTLLNH 347
Cdd:cd14095   210 --FDLILAGEFEFLS----------------------------PYWDNISDSAKDLISRMLVVDPEKRYSAGQVLDH 256
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
98-254 1.39e-10

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: 61.57  E-value: 1.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  98 HPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTHfmDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVD 177
Cdd:cd14178    56 HPNIITLKDVYDDGKFVYLVMELMRGGELLDRILRQ--KCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYMDE 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 178 gkvylSGLRSNLSMISHGQRQRVVHD-----FPKYSVKvlpWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKD 252
Cdd:cd14178   134 -----SGNPESIRICDFGFAKQLRAEngllmTPCYTAN---FVAPEVLKR--QGYDAACDIWSLGILLYTMLAGFTPFAN 203

                  ..
gi 1394533236 253 MP 254
Cdd:cd14178   204 GP 205
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
24-354 1.42e-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: 62.28  E-value: 1.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  24 FSKQEVMSSFLPEGGCYELLTVIGKGFEDLMTVNLARYkpTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVP 103
Cdd:cd07880     1 YYRQEVNKTIWEVPDRYRDLKQVGSGAYGTVCSALDRR--TGAKVAIKKLYRPFQSELFAKRAYRELRLLKHMKHENVIG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 104 YRATFIAD------NELWVVTSFMAygsaKDLICTHFMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVD 177
Cdd:cd07880    79 LLDVFTPDlsldrfHDFYLVMPFMG----TDLGKLMKHEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNED 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 178 gkvylsglrSNLSMISHGQRQRVVHDFPKYSVKvlPWL-SPEVLqQNLQGYDAKSDIYSVGITACELANGHVPFKDMPAT 256
Cdd:cd07880   155 ---------CELKILDFGLARQTDSEMTGYVVT--RWYrAPEVI-LNWMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDHL 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 257 QMLLE--KLNGTvpclldtstiPAEELTMSpsrsvANSGLSDSLTTSTPRPSNGDSPShpYHRTFSPHFHHFVEQCLQRN 334
Cdd:cd07880   223 DQLMEimKVTGT----------PSKEFVQK-----LQSEDAKNYVKKLPRFRKKDFRS--LLPNANPLAVNVLEKMLVLD 285
                         330       340
                  ....*....|....*....|
gi 1394533236 335 PDARPSASTLLNHSFFKQIK 354
Cdd:cd07880   286 AESRITAAEALAHPYFEEFH 305
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
41-279 1.79e-10

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: 61.21  E-value: 1.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  41 ELLTVIGKGfeDLMTVNLARYKptGEyVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSF 120
Cdd:cd14063     3 EIKEVIGKG--RFGRVHRGRWH--GD-VAIKLLNIDYLNEEQLEAFKEEVAAYKNTRHDNLVLFMGACMDPPHLAIVTSL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 121 MAYGSAKDLICTHFMD-GMNElaIAYILQGVLKALDYIHHMGYVHRSVKASHILISvDGKVYLS--GLRSNLSMISHGQR 197
Cdd:cd14063    78 CKGRTLYSLIHERKEKfDFNK--TVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLE-NGRVVITdfGLFSLSGLLQPGRR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 198 Q---RVVHDFpkysvkvLPWLSPEV---LQQNLQG-----YDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGT 266
Cdd:cd14063   155 EdtlVIPNGW-------LCYLAPEIiraLSPDLDFeeslpFTKASDVYAFGTVWYELLAGRWPFKEQPAESIIWQVGCGK 227
                         250
                  ....*....|...
gi 1394533236 267 VPCLLDTStIPAE 279
Cdd:cd14063   228 KQSLSQLD-IGRE 239
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
61-326 1.87e-10

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: 61.59  E-value: 1.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  61 YKPTGEYVTVRRInleacSNEMVTFLQGELHVSKLFN-HPNIVPYRATFIADNELWVVTSFMAYGSAKDLI--CTHFmdg 137
Cdd:cd14179    28 HKKTNQEYAVKIV-----SKRMEANTQREIAALKLCEgHPNIVKLHEVYHDQLHTFLVMELLKGGELLERIkkKQHF--- 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 138 mNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKvylsglRSNLSMISHG-QRQRVVHDFP-KYSVKVLPWL 215
Cdd:cd14179   100 -SETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDESD------NSEIKIIDFGfARLKPPDNQPlKTPCFTLHYA 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 216 SPEVLQQNlqGYDAKSDIYSVGITACELANGHVPFKDMPATQM------LLEKL-NGTVPCLLDTSTIPAEE-------- 280
Cdd:cd14179   173 APELLNYN--GYDESCDLWSLGVILYTMLSGQVPFQCHDKSLTctsaeeIMKKIkQGDFSFEGEAWKNVSQEakdliqgl 250
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1394533236 281 LTMSPSRSVANSGL-------SDSLTTSTP--RPSNGDSPSHPYHRTFSPHFHHF 326
Cdd:cd14179   251 LTVDPNKRIKMSGLrynewlqDGSQLSSNPlmTPDILGSSGASVHTCVKATFHAF 305
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
68-350 1.92e-10

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


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 60.91  E-value: 1.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  68 VTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTHFMDGMNELAIAYIL 147
Cdd:cd08221    28 VVWKEVNLSRLSEKERRDALNEIDILSLLNHDNIITYYNHFLDGESLFIEMEYCNGGNLHDKIAQQKNQLFPEEVVLWYL 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 148 QGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNLSmiSHGQRQRVVHDFPKYsvkvlpwLSPEVLQQNlq 225
Cdd:cd08221   108 YQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGdfGISKVLD--SESSMAESIVGTPYY-------MSPELVQGV-- 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 226 GYDAKSDIYSVGITACELANghvpfkdmpatqmLLEKLNGTVPCLLDTSTIPAEeltmspsRSVANSGLSDSLTTstprp 305
Cdd:cd08221   177 KYNFKSDIWAVGCVLYELLT-------------LKRTFDATNPLRLAVKIVQGE-------YEDIDEQYSEEIIQ----- 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1394533236 306 sngdspshpyhrtfsphfhhFVEQCLQRNPDARPSASTLLNHSFF 350
Cdd:cd08221   232 --------------------LVHDCLHQDPEDRPTAEELLERPLL 256
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
40-259 2.25e-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: 60.66  E-value: 2.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYK--PTGEYVTVRRINLEACSNEMVT-FLQGELHVSKLFNHPNIVPYRATFIADNELWV 116
Cdd:cd14080     2 YRLGKTIGEG--SYSKVKLAEYTksGLKEKVACKIIDKKKAPKDFLEkFLPRELEILRKLRHPNIIQVYSIFERGSKVFI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 117 vtsFMAYGSAKDL---ICTHFMDGMNElAIAYILQgVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSglrsnlsmis 193
Cdd:cd14080    80 ---FMEYAEHGDLleyIQKRGALSESQ-ARIWFRQ-LALAVQYLHSLDIAHRDLKCENILLDSNNNVKLS---------- 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 194 hgqrqrvvhDF------PKYSVKVLP--------WLSPEVlqqnLQG--YDAK-SDIYSVGITACELANGHVPFKDMPAT 256
Cdd:cd14080   145 ---------DFgfarlcPDDDGDVLSktfcgsaaYAAPEI----LQGipYDPKkYDIWSLGVILYIMLCGSMPFDDSNIK 211

                  ...
gi 1394533236 257 QML 259
Cdd:cd14080   212 KML 214
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
56-243 2.47e-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: 2.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  56 VNLARYKP----TGEYVTVRRINLEACSNEMVTfLQGELHVSKLFNHPNIVPYRA--TFIADNELWVVTSFMAYGSAKDL 129
Cdd:cd05079    20 VELCRYDPegdnTGEQVAVKSLKPESGGNHIAD-LKKEIEILRNLYHENIVKYKGicTEDGGNGIKLIMEFLPSGSLKEY 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 130 ICTHFMDGMNELAIAYILQgVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLrsnlsmishGQRQRVVHDFPKYSV 209
Cdd:cd05079    99 LPRNKNKINLKQQLKYAVQ-ICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDF---------GLTKAIETDKEYYTV 168
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1394533236 210 K-----VLPWLSPEVLQQNlQGYDAkSDIYSVGITACEL 243
Cdd:cd05079   169 KddldsPVFWYAPECLIQS-KFYIA-SDVWSFGVTLYEL 205
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
84-243 2.48e-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: 60.74  E-value: 2.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  84 TFLQgELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICThfMDGM----NELAIAyilQGVLKALDYIHH 159
Cdd:cd14221    36 TFLK-EVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGTLRGIIKS--MDSHypwsQRVSFA---KDIASGMAYLHS 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 160 MGYVHRSVKASHILISVDGKVYLS--GLR----SNLSMISHGQRQRVVHDFPKYSVKVLP-WLSPEVLqqNLQGYDAKSD 232
Cdd:cd14221   110 MNIIHRDLNSHNCLVRENKSVVVAdfGLArlmvDEKTQPEGLRSLKKPDRKKRYTVVGNPyWMAPEMI--NGRSYDEKVD 187
                         170
                  ....*....|.
gi 1394533236 233 IYSVGITACEL 243
Cdd:cd14221   188 VFSFGIVLCEI 198
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
85-347 2.60e-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: 60.41  E-value: 2.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  85 FLQGELHVSKLFNHPNIVPYRATFIADNelwVVTSFMAYGSAKDLICTHFMDG-MNELAIAYILQGVLKALDYIHHMGYV 163
Cdd:cd13995    42 FKPSDVEIQACFRHENIAELYGALLWEE---TVHLFMEAGEGGSVLEKLESCGpMREFEIIWVTKHVLKGLDFLHSKNII 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 164 HRSVKASHIlisvdgkVYLSglrSNLSMISHGQRQRVVHD--FPKYSVKVLPWLSPEVLQqnLQGYDAKSDIYSVGITAC 241
Cdd:cd13995   119 HHDIKPSNI-------VFMS---TKAVLVDFGLSVQMTEDvyVPKDLRGTEIYMSPEVIL--CRGHNTKADIYSLGATII 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 242 ELANGHVPF-KDMP--ATQMLLEKLNGTVPclldtstiPAEELTMSpsrsvansglsdslttstprpsngdspshpyhrt 318
Cdd:cd13995   187 HMQTGSPPWvRRYPrsAYPSYLYIIHKQAP--------PLEDIAQD---------------------------------- 224
                         250       260
                  ....*....|....*....|....*....
gi 1394533236 319 FSPHFHHFVEQCLQRNPDARPSASTLLNH 347
Cdd:cd13995   225 CSPAMRELLEAALERNPNHRSSAAELLKH 253
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
40-250 2.63e-10

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: 60.48  E-value: 2.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNE--MVTfLQGELHVSKLFNHPNIVPYRATFIADNELWVV 117
Cdd:cd14073     3 YELLETLGKG--TYGKVKLAIERATGREVAIKSIKKDKIEDEqdMVR-IRREIEIMSSLNHPHIIRIYEVFENKDKIVIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 118 TSFMAYGSAKDLICTHfmDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLrSNlsmisHG 195
Cdd:cd14073    80 MEYASGGELYDYISER--RRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIAdfGL-SN-----LY 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1394533236 196 QRQRVVHDF---PKYS----VKVLPWLSPEVlqqnlqgydaksDIYSVGITACELANGHVPF 250
Cdd:cd14073   152 SKDKLLQTFcgsPLYAspeiVNGTPYQGPEV------------DCWSLGVLLYTLVYGTMPF 201
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
89-350 2.73e-10

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: 60.33  E-value: 2.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  89 ELHVSKLFNHPNIVPYRATFIADNELWVvtsFMAYGSAKDLicTHFMDGMNEL---AIAYILQGVLKALDYIHHMGYVHR 165
Cdd:cd14189    51 EIELHRDLHHKHVVKFSHHFEDAENIYI---FLELCSRKSL--AHIWKARHTLlepEVRYYLKQIISGLKYLHLKGILHR 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 166 SVKASHILI--SVDGKVYLSGLRSNLSMIShgQRQRVVHDFPKYsvkvlpwLSPEVLqqNLQGYDAKSDIYSVGITACEL 243
Cdd:cd14189   126 DLKLGNFFIneNMELKVGDFGLAARLEPPE--QRKKTICGTPNY-------LAPEVL--LRQGHGPESDVWSLGCVMYTL 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 244 ANGHVPFK--DMPATQMLLEKLNGTVPCLLdtsTIPAEELTMSpsrsvansglsdslttstprpsngdspshpyhrtfsp 321
Cdd:cd14189   195 LCGNPPFEtlDLKETYRCIKQVKYTLPASL---SLPARHLLAG------------------------------------- 234
                         250       260
                  ....*....|....*....|....*....
gi 1394533236 322 hfhhfveqCLQRNPDARPSASTLLNHSFF 350
Cdd:cd14189   235 --------ILKRNPGDRLTLDQILEHEFF 255
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
40-250 3.02e-10

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: 60.35  E-value: 3.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARyKPTGEYVTVRRINLEACSNEM-VTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVT 118
Cdd:cd14161     5 YEFLETLGKG--TYGRVKKAR-DSSGRLVAIKSIRKDRIKDEQdLLHIRREIEIMSSLNHPHIISVYEVFENSSKIVIVM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 119 SFMAYGSAKDLICTHfmDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLrsNLSMISHGqrQ 198
Cdd:cd14161    82 EYASRGDLYDYISER--QRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADF--GLSNLYNQ--D 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1394533236 199 RVVHDF---PKYS----VKVLPWLSPEVlqqnlqgydaksDIYSVGITACELANGHVPF 250
Cdd:cd14161   156 KFLQTYcgsPLYAspeiVNGRPYIGPEV------------DSWSLGVLLYILVHGTMPF 202
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
40-260 3.21e-10

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: 60.31  E-value: 3.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGFEDLmtVNLARYKPTGEYVTVRRINLEAcSNEMVTFLQGELH---------VSKLFNHPNIVPYRATFIA 110
Cdd:cd14182     5 YEPKEILGRGVSSV--VRRCIHKPTRQEYAVKIIDITG-GGSFSPEEVQELReatlkeidiLRKVSGHPNIIQLKDTYET 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 111 DNELWVVTSFMAYGSAKDLICTHFMdgMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLS 190
Cdd:cd14182    82 NTFFFLVFDLMKKGELFDYLTEKVT--LSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFSCQ 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1394533236 191 mISHGQRQRVVHDFPKYsvkvlpwLSPEVLQ----QNLQGYDAKSDIYSVGITACELANGHVPF---KDMPATQMLL 260
Cdd:cd14182   160 -LDPGEKLREVCGTPGY-------LAPEIIEcsmdDNHPGYGKEVDMWSTGVIMYTLLAGSPPFwhrKQMLMLRMIM 228
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
40-350 3.44e-10

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: 60.85  E-value: 3.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKG-FEDlmtVNLARYKPTGEYVTVRRINLEacsNEM----VTFLQgELHVSKLFNHPNIVP----------- 103
Cdd:cd07865    14 YEKLAKIGQGtFGE---VFKARHRKTGQIVALKKVLME---NEKegfpITALR-EIKILQLLKHENVVNlieicrtkatp 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 104 ---YRATFiadnelWVVTSFMAYGSAKDLICTHFMdgMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKV 180
Cdd:cd07865    87 ynrYKGSI------YLVFEFCEHDLAGLLSNKNVK--FTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGVL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 181 YLS--GLRSNLSMISHGQRQRvvhdfpkYSVKVLP-WLSPEVLQQNLQGYDAKSDIYSVGITACELANGHVPFK-DMPAT 256
Cdd:cd07865   159 KLAdfGLARAFSLAKNSQPNR-------YTNRVVTlWYRPPELLLGERDYGPPIDMWGAGCIMAEMWTRSPIMQgNTEQH 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 257 QM-LLEKLNGTV-----PCLLDTSTIPAEELTMSPSRSVansglSDSLTtstprpsngdspshPYHRtfSPHFHHFVEQC 330
Cdd:cd07865   232 QLtLISQLCGSItpevwPGVDKLELFKKMELPQGQKRKV-----KERLK--------------PYVK--DPYALDLIDKL 290
                         330       340
                  ....*....|....*....|
gi 1394533236 331 LQRNPDARPSASTLLNHSFF 350
Cdd:cd07865   291 LVLDPAKRIDADTALNHDFF 310
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
64-349 3.92e-10

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: 60.10  E-value: 3.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  64 TGEYVTVRRINLEACSNEM---VTFLQGELHVSKLFNHPNIVPYRATfIADNELWVVTSFMAY---GSAKDLICTHfmDG 137
Cdd:cd06651    31 TGRELAAKQVQFDPESPETskeVSALECEIQLLKNLQHERIVQYYGC-LRDRAEKTLTIFMEYmpgGSVKDQLKAY--GA 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 138 MNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNLSMIS-HGQRQRVVHDFPKysvkvlpW 214
Cdd:cd06651   108 LTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGdfGASKRLQTICmSGTGIRSVTGTPY-------W 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 215 LSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFkdmpatqmlleklngtvpclldtstipAEELTMSPSRSVANsgl 294
Cdd:cd06651   181 MSPEVISG--EGYGRKADVWSLGCTVVEMLTEKPPW---------------------------AEYEAMAAIFKIAT--- 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1394533236 295 sdslttstpRPSNGDSPSHpyhrtFSPHFHHFVeQCLQRNPDARPSASTLLNHSF 349
Cdd:cd06651   229 ---------QPTNPQLPSH-----ISEHARDFL-GCIFVEARHRPSAEELLRHPF 268
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
38-268 3.94e-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: 60.12  E-value: 3.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  38 GCYELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVV 117
Cdd:cd14074     3 GLYDLEETLGRG--HFAVVKLARHVFTGEKVAVKVIDKTKLDDVSKAHLFQEVRCMKLVQHPNVVRLYEVIDTQTKLYLI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 118 TSFMAYGSAKDLICTHfMDGMNE-LAIAYILQgVLKALDYIHHMGYVHRSVKASHILIS-VDGKVYLS--GLrSNLSMis 193
Cdd:cd14074    81 LELGDGGDMYDYIMKH-ENGLNEdLARKYFRQ-IVSAISYCHKLHVVHRDLKPENVVFFeKQGLVKLTdfGF-SNKFQ-- 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1394533236 194 HGQRQRVvhdfpkySVKVLPWLSPEVLQQNlqGYDA-KSDIYSVGITACELANGHVPFKDMPATQMLLEKLNG--TVP 268
Cdd:cd14074   156 PGEKLET-------SCGSLAYSAPEILLGD--EYDApAVDIWSLGVILYMLVCGQPPFQEANDSETLTMIMDCkyTVP 224
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
24-261 5.01e-10

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: 59.71  E-value: 5.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  24 FSKQEVMSSFLPEGGCYElltvigkgfedlmtVNLARYKPTGEYVTVRRIN---LEACS---NEMVTFLQGELHVSKLFN 97
Cdd:cd14084     4 LRKKYIMSRTLGSGACGE--------------VKLAYDKSTCKKVAIKIINkrkFTIGSrreINKPRNIETEIEILKKLS 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  98 HPNIVPYRATFIADNELWVVTSFMAYGSAKDLIcTHFMdGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVD 177
Cdd:cd14084    70 HPCIIKIEDFFDAEDDYYIVLELMEGGELFDRV-VSNK-RLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQ 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 178 G-----KVYLSGLRSNLSMIShgqRQRVVHDFPKYsvkvlpwLSPEVLQQNLQ-GYDAKSDIYSVGITACELANGHVPF- 250
Cdd:cd14084   148 EeecliKITDFGLSKILGETS---LMKTLCGTPTY-------LAPEVLRSFGTeGYTRAVDCWSLGVILFICLSGYPPFs 217
                         250
                  ....*....|....
gi 1394533236 251 ---KDMPATQMLLE 261
Cdd:cd14084   218 eeyTQMSLKEQILS 231
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
55-340 5.03e-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: 59.77  E-value: 5.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  55 TVNLARYKPTGEYVTVRRIN-LEACSNEMVTFLQgELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTH 133
Cdd:cd13978     8 TVSKARHVSWFGMVAIKCLHsSPNCIEERKALLK-EAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGSLKSLLERE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 134 FMDGMNELAIAYILQGVLkALDYIHHM--GYVHRSVKASHILISVDGKVYLS--GLrSNLSMISHGQRQRV----VHDFP 205
Cdd:cd13978    87 IQDVPWSLRFRIIHEIAL-GMNFLHNMdpPLLHHDLKPENILLDNHFHVKISdfGL-SKLGMKSISANRRRgtenLGGTP 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 206 KYsvkvlpwLSPEVLQQNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKlngtvpclldtstipaeeltmsp 285
Cdd:cd13978   165 IY-------MAPEAFDDFNKKPTSKSDVYSFAIVIWAVLTRKEPFENAINPLLIMQI----------------------- 214
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 286 srsvansglsdslttstprPSNGDSPS-----HPYHRTFSPHFHHFVEQCLQRNPDARPS 340
Cdd:cd13978   215 -------------------VSKGDRPSlddigRLKQIENVQELISLMIRCWDGNPDARPT 255
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
61-303 6.27e-10

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: 59.47  E-value: 6.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  61 YKPT--GEYVTVRRINLEA-CSNEMVTFLQGELHVSKLFNHPNIVPYRATFIAD-NELWVVTSFMAYGSAKDLICTH--F 134
Cdd:cd14064    10 YKGRcrNKIVAIKRYRANTyCSKSDVDMFCREVSILCRLNHPCVIQFVGACLDDpSQFAIVTQYVSGGSLFSLLHEQkrV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 135 MDGMNELAIAYilqGVLKALDYIHHMGY--VHRSVKASHILISVDGKvylsglrsnlSMISHGQRQRVVHDFPKYSVKVL 212
Cdd:cd14064    90 IDLQSKLIIAV---DVAKGMEYLHNLTQpiIHRDLNSHNILLYEDGH----------AVVADFGESRFLQSLDEDNMTKQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 213 P----WLSPEVLQQNLQgYDAKSDIYSVGITACELANGHVPFKDM----PATQMLLEKLNGTVPclldtSTIPAEELTMS 284
Cdd:cd14064   157 PgnlrWMAPEVFTQCTR-YSIKADVFSYALCLWELLTGEIPFAHLkpaaAAADMAYHHIRPPIG-----YSIPKPISSLL 230
                         250
                  ....*....|....*....
gi 1394533236 285 PSRSVANSGLSDSLTTSTP 303
Cdd:cd14064   231 MRGWNAEPESRPSFVEIVA 249
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
85-269 6.34e-10

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: 59.16  E-value: 6.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  85 FLQgELHVSKLFNHPNIVPYRATfIADNELWVVTSFMAYGSAKDLIcthfMDGMNE-LAIAYILQ---GVLKALDYIHHM 160
Cdd:cd14203    37 FLE-EAQIMKKLRHDKLVQLYAV-VSEEPIYIVTEFMSKGSLLDFL----KDGEGKyLKLPQLVDmaaQIASGMAYIERM 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 161 GYVHRSVKASHILISvDG---KVYLSGLRSNLSMISHGQRQRVvhdfpKYSVKvlpWLSPEVLqqnLQG-YDAKSDIYSV 236
Cdd:cd14203   111 NYIHRDLRAANILVG-DNlvcKIADFGLARLIEDNEYTARQGA-----KFPIK---WTAPEAA---LYGrFTIKSDVWSF 178
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1394533236 237 GITACEL-ANGHVPFKDMPATQMLLEKLNG-TVPC 269
Cdd:cd14203   179 GILLTELvTKGRVPYPGMNNREVLEQVERGyRMPC 213
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
110-258 6.93e-10

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


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 60.02  E-value: 6.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 110 ADNElWVVT---SF---------MAYGSAKDLICTHFMDGMNE--LAIAYILQGVLkALDYIHHMGYVHRSVKASHILIS 175
Cdd:cd05598    58 ADNE-WVVKlyySFqdkenlyfvMDYIPGGDLMSLLIKKGIFEedLARFYIAELVC-AIESVHKMGFIHRDIKPDNILID 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 176 VDGKVYLS--GLRSNLsmishgqrqRVVHDFPKYSVKVL---P-WLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVP 249
Cdd:cd05598   136 RDGHIKLTdfGLCTGF---------RWTHDSKYYLAHSLvgtPnYIAPEVLLR--TGYTQLCDWWSVGVILYEMLVGQPP 204
                         170
                  ....*....|.
gi 1394533236 250 F-KDMPA-TQM 258
Cdd:cd05598   205 FlAQTPAeTQL 215
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
40-252 1.01e-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: 59.25  E-value: 1.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKG-FEDlmtVNLARYKPTGEYVTVRRIN-LEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVV 117
Cdd:cd05601     3 FEVKNVIGRGhFGE---VQVVKEKATGDIYAMKVLKkSETLAQEEVSFFEEERDIMAKANSPWITKLQYAFQDSENLYLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 118 TSFMAYGSAKDLICTHfmDGMNE--LAIAYILQGVLkALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMISHG 195
Cdd:cd05601    80 MEYHPGGDLLSLLSRY--DDIFEesMARFYLAELVL-AIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGSAAKLSSDK 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1394533236 196 qrqrvvHDFPKYSVKVLPWLSPEVLQ----QNLQGYDAKSDIYSVGITACELANGHVPFKD 252
Cdd:cd05601   157 ------TVTSKMPVGTPDYIAPEVLTsmngGSKGTYGVECDWWSLGIVAYEMLYGKTPFTE 211
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
85-310 1.06e-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: 58.93  E-value: 1.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  85 FLQgELHVSKLFNHPNIVPYRATfIADNELWVVTSFMAYGSAKDLICTHFMDGMNELAIAYILQGVLKALDYIHHMGYVH 164
Cdd:cd05071    51 FLQ-EAQVMKKLRHEKLVQLYAV-VSEEPIYIVTEYMSKGSLLDFLKGEMGKYLRLPQLVDMAAQIASGMAYVERMNYVH 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 165 RSVKASHILI--SVDGKVYLSGLRSNLSMISHGQRQRVvhdfpKYSVKvlpWLSPEVLqqnLQG-YDAKSDIYSVGITAC 241
Cdd:cd05071   129 RDLRAANILVgeNLVCKVADFGLARLIEDNEYTARQGA-----KFPIK---WTAPEAA---LYGrFTIKSDVWSFGILLT 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 242 ELAN-GHVPFKDMPATQMLLEKLNG-TVPClldTSTIPA-----------EELTMSPSRSVANSGLSDSLTTSTPRPSNG 308
Cdd:cd05071   198 ELTTkGRVPYPGMVNREVLDQVERGyRMPC---PPECPEslhdlmcqcwrKEPEERPTFEYLQAFLEDYFTSTEPQYQPG 274

                  ..
gi 1394533236 309 DS 310
Cdd:cd05071   275 EN 276
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
49-353 1.16e-09

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 59.62  E-value: 1.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  49 GFEDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQ-----GELHVSKLFNHPNIVPYRATFIADNelwvVTSFMAY 123
Cdd:PHA03212   88 GIEKAGFSILETFTPGAEGFAFACIDNKTCEHVVIKAGQrggtaTEAHILRAINHPSIIQLKGTFTYNK----FTCLILP 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 124 GSAKDLICthFMDGMNELAIAYIL---QGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMISHGQRqrv 200
Cdd:PHA03212  164 RYKTDLYC--YLAAKRNIAICDILaieRSVLRAIQYLHENRIIHRDIKAENIFINHPGDVCLGDFGAACFPVDINAN--- 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 201 vhdfpkysvKVLPWL------SPEVLQQNlqGYDAKSDIYSVGITACELANGHvpfkdmpatQMLLEK--LNGT------ 266
Cdd:PHA03212  239 ---------KYYGWAgtiatnAPELLARD--PYGPAVDIWSAGIVLFEMATCH---------DSLFEKdgLDGDcdsdrq 298
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 267 VPCLLDTSTIPAEELTMSPSRSVANSGLSDSLTTSTpRPsnGDSPSHPYHRTFSPHFHHFVEQCLQRNPDARPSASTLLN 346
Cdd:PHA03212  299 IKLIIRRSGTHPNEFPIDAQANLDEIYIGLAKKSSR-KP--GSRPLWTNLYELPIDLEYLICKMLAFDAHHRPSAEALLD 375

                  ....*..
gi 1394533236 347 HSFFKQI 353
Cdd:PHA03212  376 FAAFQDI 382
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
85-310 1.24e-09

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: 58.54  E-value: 1.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  85 FLQgELHVSKLFNHPNIVPYRATfIADNELWVVTSFMAYGSAKDLICTHFMDGMNELAIAYILQGVLKALDYIHHMGYVH 164
Cdd:cd05069    54 FLQ-EAQIMKKLRHDKLVPLYAV-VSEEPIYIVTEFMGKGSLLDFLKEGDGKYLKLPQLVDMAAQIADGMAYIERMNYIH 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 165 RSVKASHILISVD--GKVYLSGLRSNLSMISHGQRQRVvhdfpKYSVKvlpWLSPEVLqqnLQG-YDAKSDIYSVGITAC 241
Cdd:cd05069   132 RDLRAANILVGDNlvCKIADFGLARLIEDNEYTARQGA-----KFPIK---WTAPEAA---LYGrFTIKSDVWSFGILLT 200
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1394533236 242 EL-ANGHVPFKDMPATQMLLEKLNG-TVPCLLDTSTIPAEELTM--------SPSRSVANSGLSDSLTTSTPRPSNGDS 310
Cdd:cd05069   201 ELvTKGRVPYPGMVNREVLEQVERGyRMPCPQGCPESLHELMKLcwkkdpdeRPTFEYIQSFLEDYFTATEPQYQPGDN 279
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
68-261 1.39e-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: 1.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  68 VTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRAtFIADNELWVVTSFMAYGSAKDLIctHFMDGMNEL-AIAYI 146
Cdd:cd14151    33 VAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMG-YSTKPQLAIVTQWCEGSSLYHHL--HIIETKFEMiKLIDI 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 147 LQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSglrsNLSMISHGQRQRVVHDFPKYSVKVLpWLSPEVLQ-QNLQ 225
Cdd:cd14151   110 ARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIG----DFGLATVKSRWSGSHQFEQLSGSIL-WMAPEVIRmQDKN 184
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1394533236 226 GYDAKSDIYSVGITACELANGHVPFKDMPATQMLLE 261
Cdd:cd14151   185 PYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIF 220
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
62-281 1.42e-09

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: 58.82  E-value: 1.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  62 KPTGEYVTVRRinleaCSNEMVTFLQG----ELHVSKLFNHPNIV-----PYRATFIADNELWVVTsfMAYGSAKDL--I 130
Cdd:cd14038    16 QETGEQVAIKQ-----CRQELSPKNRErwclEIQIMKRLNHPNVVaardvPEGLQKLAPNDLPLLA--MEYCQGGDLrkY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 131 CTHFMD--GMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISvDGKVYLSGLRSNLSMISHGQRQRVVHDFpkys 208
Cdd:cd14038    89 LNQFENccGLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQ-QGEQRLIHKIIDLGYAKELDQGSLCTSF---- 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 209 VKVLPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFkdMPATQ----------------MLLEKLNGTV----- 267
Cdd:cd14038   164 VGTLQYLAPELLEQ--QKYTVTVDYWSFGTLAFECITGFRPF--LPNWQpvqwhgkvrqksnediVVYEDLTGAVkfssv 239
                         250
                  ....*....|....*
gi 1394533236 268 -PCLLDTSTIPAEEL 281
Cdd:cd14038   240 lPTPNNLNGILAGKL 254
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
62-279 1.56e-09

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: 58.48  E-value: 1.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  62 KPTGEYVTVRRINLEACSNEMVtFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLIctHFMDGMNEL 141
Cdd:cd14201    29 KKTDWEVAIKSINKKNLSKSQI-LLGKEIKILKELQHENIVALYDVQEMPNSVFLVMEYCNGGDLADYL--QAKGTLSED 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 142 AIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDG--KVYLSGLRsnLSMISHGQRQRVVHDFPKYSVKVLP-WLSPE 218
Cdd:cd14201   106 TIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASrkKSSVSGIR--IKIADFGFARYLQSNMMAATLCGSPmYMAPE 183
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1394533236 219 VLQQnlQGYDAKSDIYSVGITACELANGHVPFK-DMPAT-QMLLEKLNGTVPclldtsTIPAE 279
Cdd:cd14201   184 VIMS--QHYDAKADLWSIGTVIYQCLVGKPPFQaNSPQDlRMFYEKNKNLQP------SIPRE 238
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
40-252 1.69e-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: 58.52  E-value: 1.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTfLQGELHVSKLFNHPNIVPYRATFIADNELWVVTS 119
Cdd:cd14168    12 FEFKEVLGTG--AFSEVVLAEERATGKLFAVKCIPKKALKGKESS-IENEIAVLRKIKHENIVALEDIYESPNHLYLVMQ 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 120 FMAYGSAKDLICTHFMdgMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILisvdgkvYLSGLRSNLSMISHGQRQR 199
Cdd:cd14168    89 LVSGGELFDRIVEKGF--YTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLL-------YFSQDEESKIMISDFGLSK 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1394533236 200 V--VHDFPKYSVKVLPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKD 252
Cdd:cd14168   160 MegKGDVMSTACGTPGYVAPEVLAQ--KPYSKAVDCWSIGVIAYILLCGYPPFYD 212
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
40-281 1.92e-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: 58.12  E-value: 1.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMvTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTS 119
Cdd:cd14184     3 YKIGKVIGDG--NFAVVKECVERSTGKEFALKIIDKAKCCGKE-HLIENEVSILRRVKHPNIIMLIEEMDTPAELYLVME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 120 FMAYGSAKDLICTHfmDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISvdgkVYLSGLRSnLSMISHGQRQR 199
Cdd:cd14184    80 LVKGGDLFDAITSS--TKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVC----EYPDGTKS-LKLGDFGLATV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 200 VvhDFPKYSVKVLP-WLSPEVLQQNlqGYDAKSDIYSVGITACELANGHVPFK-------DMpATQMLLEKLNGTVPcLL 271
Cdd:cd14184   153 V--EGPLYTVCGTPtYVAPEIIAET--GYGLKVDIWAAGVITYILLCGFPPFRsennlqeDL-FDQILLGKLEFPSP-YW 226
                         250
                  ....*....|
gi 1394533236 272 DTSTIPAEEL 281
Cdd:cd14184   227 DNITDSAKEL 236
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
59-250 2.51e-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: 57.56  E-value: 2.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  59 ARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICT--HFmd 136
Cdd:cd14097    20 ATHKETQTKWAIKKINREKAGSSAVKLLEREVDILKHVNHAHIIHLEEVFETPKRMYLVMELCEDGELKELLLRkgFF-- 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 137 gmNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILIS---VDGKVYLsglrsNLSMISHG---QRQRVVHDFPKYSVK 210
Cdd:cd14097    98 --SENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKssiIDNNDKL-----NIKVTDFGlsvQKYGLGEDMLQETCG 170
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1394533236 211 VLPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPF 250
Cdd:cd14097   171 TPIYMAPEVISA--HGYSQQCDIWSIGVIMYMLLCGEPPF 208
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
24-363 2.51e-09

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


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 58.38  E-value: 2.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  24 FSKQEVMSSF--LPEGgcYELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNI 101
Cdd:cd07879     1 FYREEVNKTVweLPER--YTSLKQVGSG--AYGSVCSAIDKRTGEKVAIKKLSRPFQSEIFAKRAYRELTLLKHMQHENV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 102 VPYRATFIAD------NELWVVTSFMAYGSAKdLICTHFmdgmNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILIS 175
Cdd:cd07879    77 IGLLDVFTSAvsgdefQDFYLVMPYMQTDLQK-IMGHPL----SEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVN 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 176 VDgkvylsglrSNLSMISHGQRQRVVHDFPKYSVKvlPWL-SPEVLqQNLQGYDAKSDIYSVGITACELANGHVPFKDMP 254
Cdd:cd07879   152 ED---------CELKILDFGLARHADAEMTGYVVT--RWYrAPEVI-LNWMHYNQTVDIWSVGCIMAEMLTGKTLFKGKD 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 255 ATQMLLEklngtvpcLLDTSTIPAEELTMSpsrsvANSGLSDSLTTSTPR-PSNGDSPSHPyhrTFSPHFHHFVEQCLQR 333
Cdd:cd07879   220 YLDQLTQ--------ILKVTGVPGPEFVQK-----LEDKAAKSYIKSLPKyPRKDFSTLFP---KASPQAVDLLEKMLEL 283
                         330       340       350
                  ....*....|....*....|....*....|
gi 1394533236 334 NPDARPSASTLLNHSFFKQIkrRASEALPE 363
Cdd:cd07879   284 DVDKRLTATEALEHPYFDSF--RDADEETE 311
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
55-250 2.74e-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: 57.62  E-value: 2.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  55 TVNLARYKPTGEYVTVRRINLEACSNEM-VTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLIctH 133
Cdd:cd05572     8 RVELVQLKSKGRTFALKCVKKRHIVQTRqQEHIFSEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLGGELWTIL--R 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 134 FMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLsglrsnlsmISHG-----QRQRVVHDF---P 205
Cdd:cd05572    86 DRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKL---------VDFGfakklGSGRKTWTFcgtP 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1394533236 206 KYsvkvlpwLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPF 250
Cdd:cd05572   157 EY-------VAPEIILN--KGYDFSVDYWSLGILLYELLTGRPPF 192
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
31-291 2.80e-09

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: 57.58  E-value: 2.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  31 SSFLPEggcYELLTVIGKG-----FEDLMTVNLARYkptgeyvTVRRI---NLEACSNEMVTflqgELHVSKLFNHPNIV 102
Cdd:cd14048     2 SRFLTD---FEPIQCLGRGgfgvvFEAKNKVDDCNY-------AVKRIrlpNNELAREKVLR----EVRALAKLDHPGIV 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 103 PYratFIADNE--------------LWVVTSFMAYGSAKDLI---CThfMDGMNELAIAYILQGVLKALDYIHHMGYVHR 165
Cdd:cd14048    68 RY---FNAWLErppegwqekmdevyLYIQMQLCRKENLKDWMnrrCT--MESRELFVCLNIFKQIASAVEYLHSKGLIHR 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 166 SVKASHILISVDGKVYLSGLRSNLSMISHGQRQRVVHDFPKYS-----VKVLPWLSPEvlQQNLQGYDAKSDIYSVGITA 240
Cdd:cd14048   143 DLKPSNVFFSLDDVVKVGDFGLVTAMDQGEPEQTVLTPMPAYAkhtgqVGTRLYMSPE--QIHGNQYSEKVDIFALGLIL 220
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1394533236 241 CELAnghVPFkdmpATQM-----LLEKLNGTVPCLLdTSTIPAEE------LTMSPS-RSVAN 291
Cdd:cd14048   221 FELI---YSF----STQMerirtLTDVRKLKFPALF-TNKYPEERdmvqqmLSPSPSeRPEAH 275
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
86-350 2.97e-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: 57.24  E-value: 2.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  86 LQGELHVSKLFNHPNIVpyraTFI------ADNELWVVTSFMAYGSAKDLICTHfmDGMNELAIAYILQGVLKALDYIHH 159
Cdd:cd13983    47 FKQEIEILKSLKHPNII----KFYdsweskSKKEVIFITELMTSGTLKQYLKRF--KRLKLKVIKSWCRQILEGLNYLHT 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 160 MGY--VHRSVKASHILI-SVDGKVYLSGLrsNLS-MISHGQRQRVVHDfPKYsvkvlpwLSPEVLQQNlqgYDAKSDIYS 235
Cdd:cd13983   121 RDPpiIHRDLKCDNIFInGNTGEVKIGDL--GLAtLLRQSFAKSVIGT-PEF-------MAPEMYEEH---YDEKVDIYA 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 236 VGITACELANGHVPFKDMPATQMLLEKLngtvpclldTSTIPAEELtmspsrsvansglsdslttstprpsngdspshpy 315
Cdd:cd13983   188 FGMCLLEMATGEYPYSECTNAAQIYKKV---------TSGIKPESL---------------------------------- 224
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1394533236 316 HRTFSPHFHHFVEQCLqRNPDARPSASTLLNHSFF 350
Cdd:cd13983   225 SKVKDPELKDFIEKCL-KPPDERPSARELLEHPFF 258
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
59-350 3.02e-09

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: 57.51  E-value: 3.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  59 ARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMaygsAKDLicTHFMDGM 138
Cdd:cd07860    19 ARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFL----HQDL--KKFMDAS 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 139 N--ELAIAYI---LQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNLSMISHGQRQRVVhdfpkysvkV 211
Cdd:cd07860    93 AltGIPLPLIksyLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLAdfGLARAFGVPVRTYTHEVV---------T 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 212 LPWLSPEVLqQNLQGYDAKSDIYSVGITACELANGHVPFK-DMPATQML-LEKLNGTvPcllDTSTIPAeeLTMSPsrsv 289
Cdd:cd07860   164 LWYRAPEIL-LGCKYYSTAVDIWSLGCIFAEMVTRRALFPgDSEIDQLFrIFRTLGT-P---DEVVWPG--VTSMP---- 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1394533236 290 ansglsdSLTTSTPR-PSNGDSPSHPyhrTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFF 350
Cdd:cd07860   233 -------DYKPSFPKwARQDFSKVVP---PLDEDGRDLLSQMLHYDPNKRISAKAALAHPFF 284
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
55-250 3.05e-09

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: 57.49  E-value: 3.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  55 TVNLARYKPTGEYVTVRRI-NLEACSNEMVTFLQGE---LHVSKlfNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLI 130
Cdd:cd05611    11 SVYLAKKRSTGDYFAIKVLkKSDMIAKNQVTNVKAEraiMMIQG--ESPYVAKLYYSFQSKDYLYLVMEYLNGGDCASLI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 131 CThfMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLrsNLSMISHGQRQrvvhdfPKYSVK 210
Cdd:cd05611    89 KT--LGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDF--GLSRNGLEKRH------NKKFVG 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1394533236 211 VLPWLSPEVLQQNlqGYDAKSDIYSVGITACELANGHVPF 250
Cdd:cd05611   159 TPDYLAPETILGV--GDDKMSDWWSLGCVIFEFLFGYPPF 196
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
39-253 3.09e-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: 57.57  E-value: 3.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  39 CYELLTVIGKGfeDLMTVNLARYKPTGE---YVTVRRINLEACSNEMVTFLqGELHVSKLFNHPNIVPYRATFIADNELW 115
Cdd:cd05065     5 CVKIEEVIGAG--EFGEVCRGRLKLPGKreiFVAIKTLKSGYTEKQRRDFL-SEASIMGQFDHPNIIHLEGVVTKSRPVM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 116 VVTSFMAYGSAKDLIctHFMDG-MNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISvdgkvylsglrSNL-SMIS 193
Cdd:cd05065    82 IITEFMENGALDSFL--RQNDGqFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVN-----------SNLvCKVS 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1394533236 194 HGQRQRVVHDF---PKYSVKV---LP--WLSPEVLQqnLQGYDAKSDIYSVGITACE-LANGHVPFKDM 253
Cdd:cd05065   149 DFGLSRFLEDDtsdPTYTSSLggkIPirWTAPEAIA--YRKFTSASDVWSYGIVMWEvMSYGERPYWDM 215
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
145-353 3.29e-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: 57.40  E-value: 3.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 145 YILQGVLkALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLrSNLSMISHGQRqrvVHDFpkysVKVLPWLSPEVLQQ 222
Cdd:cd05583   104 YIGEIVL-ALEHLHKLGIIYRDIKLENILLDSEGHVVLTdfGL-SKEFLPGENDR---AYSF----CGTIEYMAPEVVRG 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 223 NLQGYDAKSDIYSVGITACELANGHVPFkdmpatqmlleklngtvpclldtsTIPAEELTMSP-SRSVansglsdsLTTS 301
Cdd:cd05583   175 GSDGHDKAVDWWSLGVLTYELLTGASPF------------------------TVDGERNSQSEiSKRI--------LKSH 222
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1394533236 302 TPRPsngdspshpyhRTFSPHFHHFVEQCLQRNPDAR-----PSASTLLNHSFFKQI 353
Cdd:cd05583   223 PPIP-----------KTFSAEAKDFILKLLEKDPKKRlgagpRGAHEIKEHPFFKGL 268
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
40-250 3.33e-09

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


Pssm-ID: 270750 [Multi-domain]  Cd Length: 324  Bit Score: 57.62  E-value: 3.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKG-FEDlmtVNLARYKPTGEYVTVRRI-NLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVV 117
Cdd:cd05599     3 FEPLKVIGRGaFGE---VRLVRKKDTGHVYAMKKLrKSEMLEKEQVAHVRAERDILAEADNPWVVKLYYSFQDEENLYLI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 118 TSFMAYGS------AKDLI---CTHFmdgmnelaiaYILQGVLkALDYIHHMGYVHRSVKASHILISVDGKVYLS--GL- 185
Cdd:cd05599    80 MEFLPGGDmmtllmKKDTLteeETRF----------YIAETVL-AIESIHKLGYIHRDIKPDNLLLDARGHIKLSdfGLc 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 186 ----RSNLSmishgqrqrvvhdfpkYSVKVLP-WLSPEVLQQNlqGYDAKSDIYSVGITACELANGHVPF 250
Cdd:cd05599   149 tglkKSHLA----------------YSTVGTPdYIAPEVFLQK--GYGKECDWWSLGVIMYEMLIGYPPF 200
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
40-252 3.33e-09

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: 57.18  E-value: 3.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKG-FEDLMTVNLARYKPTgeyVTVRRINLEACSNEMVT-FLQGELHVSKLFNHPNIVPYRATF-IADNELWV 116
Cdd:cd14164     2 YTLGTTIGEGsFSKVKLATSQKYCCK---VAIKIVDRRRASPDFVQkFLPRELSILRRVNHPNIVQMFECIeVANGRLYI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 117 VTSfmayGSAKDLICTHFMDGMNELAIAY-ILQGVLKALDYIHHMGYVHRSVKASHILISVDGKvylsglRSNLSMISHG 195
Cdd:cd14164    79 VME----AAATDLLQKIQEVHHIPKDLARdMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDR------KIKIADFGFA 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1394533236 196 qrqRVVHDFPKYSVKVL---PWLSPEVLQQNlqGYDAKS-DIYSVGITACELANGHVPFKD 252
Cdd:cd14164   149 ---RFVEDYPELSTTFCgsrAYTPPEVILGT--PYDPKKyDVWSLGVVLYVMVTGTMPFDE 204
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
143-350 3.54e-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: 57.28  E-value: 3.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 143 IAYILQGVLKALDYIHHMGYVHRSVKASHILISvdgkvylSGLRSNLSMISHGQRQRVvHDFPKYSVKVLPWLSPEVLQq 222
Cdd:cd14133   104 IRKIAQQILEALVFLHSLGLIHCDLKPENILLA-------SYSRCQIKIIDFGSSCFL-TQRLYSYIQSRYYRAPEVIL- 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 223 nlqG--YDAKSDIYSVGITACELANGHVPFKDMPATQMLleklngtvPCLLDTSTIPaeeltmsPSRSVANSGLSDSLtt 300
Cdd:cd14133   175 ---GlpYDEKIDMWSLGCILAELYTGEPLFPGASEVDQL--------ARIIGTIGIP-------PAHMLDQGKADDEL-- 234
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1394533236 301 stprpsngdspshpyhrtfsphFHHFVEQCLQRNPDARPSASTLLNHSFF 350
Cdd:cd14133   235 ----------------------FVDFLKKLLEIDPKERPTASQALSHPWL 262
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
40-252 3.63e-09

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: 56.92  E-value: 3.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVT-FLQGELHVSKLFNHPNIVPYRATFIADNELWVVT 118
Cdd:cd14162     2 YIVGKTLGHG--SYAVVKKAYSTKHKCKVAIKIVSKKKAPEDYLQkFLPREIEVIKGLKHPNLICFYEAIETTSRVYIIM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 119 SFMAYGSAKDLICTH-FMDgmnELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGkvylsglrsNLSMISHG-- 195
Cdd:cd14162    80 ELAENGDLLDYIRKNgALP---EPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNN---------NLKITDFGfa 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1394533236 196 QRQRVVHD-FPKYSVKV---LPWLSPEVLQQNLqgYDAK-SDIYSVGITACELANGHVPFKD 252
Cdd:cd14162   148 RGVMKTKDgKPKLSETYcgsYAYASPEILRGIP--YDPFlSDIWSMGVVLYTMVYGRLPFDD 207
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
40-251 4.01e-09

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: 56.97  E-value: 4.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRI-----NLEACSNEMVTFLQGELHV-SKLFNHPNIVPYRATFIADNE 113
Cdd:cd13993     2 YQLISPIGEG--AYGVVYLAVDLRTGRKYAIKCLyksgpNSKDGNDFQKLPQLREIDLhRRVSRHPNIITLHDVFETEVA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 114 LWVVtsfMAYGSAKDLI-CTH---FMDGMNELAIAYILQgVLKALDYIHHMGYVHRSVKASHILIS-VDGKVYLS--GL- 185
Cdd:cd13993    80 IYIV---LEYCPNGDLFeAITenrIYVGKTELIKNVFLQ-LIDAVKHCHSLGIYHRDIKPENILLSqDEGTVKLCdfGLa 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1394533236 186 -RSNLSMishgqrqrvvhdfpKYSVKVLPWLSPEVLQQN---LQGYD-AKSDIYSVGITACELANGHVPFK 251
Cdd:cd13993   156 tTEKISM--------------DFGVGSEFYMAPECFDEVgrsLKGYPcAAGDIWSLGIILLNLTFGRNPWK 212
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
125-350 4.39e-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: 56.82  E-value: 4.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 125 SAKDLICTHFMDG-MNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILIsvdgkvyLSGLRSNLSMISHGQRQRVVHD 203
Cdd:cd14107    81 SSEELLDRLFLKGvVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILM-------VSPTREDIKICDFGFAQEITPS 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 204 FPKYSVKVLP-WLSPEVLQQNlqGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVpclldtstipaeelt 282
Cdd:cd14107   154 EHQFSKYGSPeFVAPEIVHQE--PVSAATDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEGVV--------------- 216
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1394533236 283 mspsrsvansglsdslttstprpsngdSPSHPYHRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFF 350
Cdd:cd14107   217 ---------------------------SWDTPEITHLSEDAKDFIKRVLQPDPEKRPSASECLSHEWF 257
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
40-350 5.07e-09

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: 56.91  E-value: 5.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGFEDLmtVNLARYKPTGEYVTVRRINLEAcSNEMV--TFLQgELHVSKLFNHPNIVPYRATFIADNELWVV 117
Cdd:cd07835     1 YQKLEKIGEGTYGV--VYKARDKLTGEIVALKKIRLET-EDEGVpsTAIR-EISLLKELNHPNIVRLLDVVHSENKLYLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 118 TSFMaygsakDLICTHFMDGMNELAI------AYILQgVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNL 189
Cdd:cd07835    77 FEFL------DLDLKKYMDSSPLTGLdpplikSYLYQ-LLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLAdfGLARAF 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 190 SMISHGQRQRVVhdfpkysvkVLPWLSPEVLQQNLQgYDAKSDIYSVGITACELANGHVPFK-DMPATQML-LEKLNGTv 267
Cdd:cd07835   150 GVPVRTYTHEVV---------TLWYRAPEILLGSKH-YSTPVDIWSVGCIFAEMVTRRPLFPgDSEIDQLFrIFRTLGT- 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 268 PcllDTSTIPAEeltmspsrsvanSGLSDsLTTSTPRPSNGDSPSHPYhrTFSPHFHHFVEQCLQRNPDARPSASTLLNH 347
Cdd:cd07835   219 P---DEDVWPGV------------TSLPD-YKPTFPKWARQDLSKVVP--SLDEDGLDLLSQMLVYDPAKRISAKAALQH 280

                  ...
gi 1394533236 348 SFF 350
Cdd:cd07835   281 PYF 283
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
46-243 5.18e-09

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: 56.72  E-value: 5.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  46 IGKGFedLMTVNLARYKPTGEYVTVRRINLEACSNEMVTflqgELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGS 125
Cdd:cd14155     1 IGSGF--FSEVYKVRHRTSGQVMALKMNTLSSNRANMLR----EVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGGN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 126 AKDLICTH-FMDGMNELAIAYilqGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSglrsnlsmishgqrqrVVHDF 204
Cdd:cd14155    75 LEQLLDSNePLSWTVRVKLAL---DIARGLSYLHSKGIFHRDLTSKNCLIKRDENGYTA----------------VVGDF 135
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1394533236 205 ------PKYSVKVLP--------WLSPEVLQQNLqgYDAKSDIYSVGITACEL 243
Cdd:cd14155   136 glaekiPDYSDGKEKlavvgspyWMAPEVLRGEP--YNEKADVFSYGIILCEI 186
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
46-274 6.05e-09

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: 56.37  E-value: 6.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  46 IGKGFedLMTVNLARYKPTGEYVTVRRINLEACSNEMVTflqgELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGS 125
Cdd:cd14156     1 IGSGF--FSKVYKVTHGATGKVMVVKIYKNDVDQHKIVR----EISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGC 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 126 AKDLICTHfmdgmnELAIAYILQGVL-----KALDYIHHMGYVHRSVKASHILISVDGKVyLSGLRSNLSMishgqrQRV 200
Cdd:cd14156    75 LEELLARE------ELPLSWREKVELacdisRGMVYLHSKNIYHRDLNSKNCLIRVTPRG-REAVVTDFGL------ARE 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 201 VHDFP------KYS-VKVLPWLSPEVLQQnlQGYDAKSDIYSVGITACELAnGHVPF--KDMPAT-------QMLLEKLN 264
Cdd:cd14156   142 VGEMPandperKLSlVGSAFWMAPEMLRG--EPYDRKVDVFSFGIVLCEIL-ARIPAdpEVLPRTgdfgldvQAFKEMVP 218
                         250
                  ....*....|
gi 1394533236 265 GTVPCLLDTS 274
Cdd:cd14156   219 GCPEPFLDLA 228
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
86-252 6.26e-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: 56.60  E-value: 6.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  86 LQGELHVSKLFNHPNIV--------PyratfiADNELWVVTSFMAYGSAKDLICTHFMDgmNELAIAYiLQGVLKALDYI 157
Cdd:cd14118    61 VYREIAILKKLDHPNVVklvevlddP------NEDNLYMVFELVDKGAVMEVPTDNPLS--EETARSY-FRDIVLGIEYL 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 158 HHMGYVHRSVKASHILISVDGKVYLSGLrsNLSMISHGqrqrvVHDFPKYSVKVLPWLSPEVLQQNLQGYDAKS-DIYSV 236
Cdd:cd14118   132 HYQKIIHRDIKPSNLLLGDDGHVKIADF--GVSNEFEG-----DDALLSSTAGTPAFMAPEALSESRKKFSGKAlDIWAM 204
                         170
                  ....*....|....*.
gi 1394533236 237 GITACELANGHVPFKD 252
Cdd:cd14118   205 GVTLYCFVFGRCPFED 220
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
85-250 6.55e-09

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


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 56.37  E-value: 6.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  85 FLQGELHVSKLFNHPNIV-PYRATfiaDNELWVVTSFMAYGSAKDLICTHFMDGMN---ELAIAYILQGVLKALDYIHHM 160
Cdd:cd14109    42 FLMREVDIHNSLDHPNIVqMHDAY---DDEKLAVTVIDNLASTIELVRDNLLPGKDyytERQVAVFVRQLLLALKHMHDL 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 161 GYVHRSVKASHILISVDgkvylsglrsNLSMISHGQRQRVVHDFPKYSVKVLP-WLSPEVLqqNLQGYDAKSDIYSVGIT 239
Cdd:cd14109   119 GIAHLDLRPEDILLQDD----------KLKLADFGQSRRLLRGKLTTLIYGSPeFVSPEIV--NSYPVTLATDMWSVGVL 186
                         170
                  ....*....|.
gi 1394533236 240 ACELANGHVPF 250
Cdd:cd14109   187 TYVLLGGISPF 197
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
40-263 6.96e-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: 56.54  E-value: 6.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKG-FEDlmtVNLARYKPTGEYVT---VRRINLEACSNemvtfLQGELHVSKLFNHPNIVPYRATFIADNELW 115
Cdd:cd14166     5 FIFMEVLGSGaFSE---VYLVKQRSTGKLYAlkcIKKSPLSRDSS-----LENEIAVLKRIKHENIVTLEDIYESTTHYY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 116 VVTSFMAYGSAKDLICTHFMdgMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILisvdgkvYLSGLRSNLSMISH- 194
Cdd:cd14166    77 LVMQLVSGGELFDRILERGV--YTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLL-------YLTPDENSKIMITDf 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1394533236 195 GQRQRVVHDFPKYSVKVLPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQmLLEKL 263
Cdd:cd14166   148 GLSKMEQNGIMSTACGTPGYVAPEVLAQ--KPYSKAVDCWSIGVITYILLCGYPPFYEETESR-LFEKI 213
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
93-347 7.27e-09

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: 56.20  E-value: 7.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  93 SKLF---NHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTHFMDgmNELAIAYILQgVLKALDYIHHMGYV---HRS 166
Cdd:cd14145    56 AKLFamlKHPNIIALRGVCLKEPNLCLVMEFARGGPLNRVLSGKRIP--PDILVNWAVQ-IARGMNYLHCEAIVpviHRD 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 167 VKASHILISvdGKVYLSGLRSNLSMISHGQRQRVVHDFPKYSVK-VLPWLSPEVLQQNLqgYDAKSDIYSVGITACELAN 245
Cdd:cd14145   133 LKSSNILIL--EKVENGDLSNKILKITDFGLAREWHRTTKMSAAgTYAWMAPEVIRSSM--FSKGSDVWSYGVLLWELLT 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 246 GHVPFKDMPAtqmlleklngtvpclldtstipaeeltMSPSRSVANSGLSDSLTTSTPRPsngdspshpyhrtfsphFHH 325
Cdd:cd14145   209 GEVPFRGIDG---------------------------LAVAYGVAMNKLSLPIPSTCPEP-----------------FAR 244
                         250       260
                  ....*....|....*....|..
gi 1394533236 326 FVEQCLQRNPDARPSASTLLNH 347
Cdd:cd14145   245 LMEDCWNPDPHSRPPFTNILDQ 266
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
68-263 7.29e-09

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: 56.33  E-value: 7.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  68 VTVRRINLEACSNEMVT-FLQGELHVSKLFNHPNIVP-YRATFIADNELWVVTSFMAYGSAKDLICTHfmDGMNELAIAY 145
Cdd:cd14165    29 VAIKIIDKKKAPDDFVEkFLPRELEILARLNHKSIIKtYEIFETSDGKVYIVMELGVQGDLLEFIKLR--GALPEDVARK 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 146 ILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLrsnlsmishGQRQRVVHD------FPKYSVKVLPWLSPEV 219
Cdd:cd14165   107 MFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDF---------GFSKRCLRDengrivLSKTFCGSAAYAAPEV 177
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1394533236 220 LQQnlQGYDAK-SDIYSVGITACELANGHVPFKDMPATQMLLEKL 263
Cdd:cd14165   178 LQG--IPYDPRiYDIWSLGVILYIMVCGSMPYDDSNVKKMLKIQK 220
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
27-269 7.58e-09

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 57.33  E-value: 7.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  27 QEVMSSFLPEGGCYELLTVIGKGFEDLMTVNLaRYKPTGEYVTVRRINLEacSNEMVTFLQGELHVSKLFNHPNIVPYRA 106
Cdd:PTZ00267   56 EEVPESNNPREHMYVLTTLVGRNPTTAAFVAT-RGSDPKEKVVAKFVMLN--DERQAAYARSELHCLAACDHFGIVKHFD 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 107 TFIADNELWVVtsfMAYGSAKDL---ICTHFMDGM--NELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVY 181
Cdd:PTZ00267  133 DFKSDDKLLLI---MEYGSGGDLnkqIKQRLKEHLpfQEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIK 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 182 LSGLRsnlsmISHGQRQRVVHDFPKYSVKVLPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLE 261
Cdd:PTZ00267  210 LGDFG-----FSKQYSDSVSLDVASSFCGTPYYLAPELWER--KRYSKKADMWSLGVILYELLTLHRPFKGPSQREIMQQ 282
                         250
                  ....*....|.
gi 1394533236 262 KLNGT---VPC 269
Cdd:PTZ00267  283 VLYGKydpFPC 293
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
56-281 8.29e-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: 55.91  E-value: 8.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  56 VNLARYKptGEYVTVRRINLEACSNEMVTFLQgelHVSKLfNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLIctHFM 135
Cdd:cd14058     9 VCKARWR--NQIVAVKIIESESEKKAFEVEVR---QLSRV-DHPNIIKLYGACSNQKPVCLVMEYAEGGSLYNVL--HGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 136 DGMNEL----AIAYILQGVlKALDYIHHMG---YVHRSVKASHILISVDGKVylsglrsnLSMISHGqrqrVVHDFPKYS 208
Cdd:cd14058    81 EPKPIYtaahAMSWALQCA-KGVAYLHSMKpkaLIHRDLKPPNLLLTNGGTV--------LKICDFG----TACDISTHM 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1394533236 209 VK---VLPWLSPEVLQQNLqgYDAKSDIYSVGITACELANGHVPFKDM--PATQMLLEKLNGTVPCLLDTSTIPAEEL 281
Cdd:cd14058   148 TNnkgSAAWMAPEVFEGSK--YSEKCDVFSWGIILWEVITRRKPFDHIggPAFRIMWAVHNGERPPLIKNCPKPIESL 223
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
40-252 8.77e-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: 55.85  E-value: 8.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTfLQGELHVSKLFNHPNIVPYRATFIADNELWVVTS 119
Cdd:cd14078     5 YELHETIGSG--GFAKVKLATHILTGEKVAIKIMDKKALGDDLPR-VKTEIEALKNLSHQHICRLYHVIETDNKIFMVLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 120 FMAYGSAKDLICTHfmDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYL----------SGLRSNL 189
Cdd:cd14078    82 YCPGGELFDYIVAK--DRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLidfglcakpkGGMDHHL 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1394533236 190 sMISHGQrqrvvhdfPKYSvkvlpwlSPEvLQQNLQGYDAKSDIYSVGITACELANGHVPFKD 252
Cdd:cd14078   160 -ETCCGS--------PAYA-------APE-LIQGKPYIGSEADVWSMGVLLYALLCGFLPFDD 205
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
98-259 8.78e-09

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: 55.97  E-value: 8.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  98 HPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTHFMDGMN--ELAIAYILQGVLKALDYIH-HMGYVHRSVKASHILI 174
Cdd:cd08528    68 HPNIVRYYKTFLENDRLYIVMELIEGAPLGEHFSSLKEKNEHftEDRIWNIFVQMVLALRYLHkEKQIVHRDLKPNNIML 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 175 SVDGKVYLS--GLRSnlsmishgQRQRVVHDFpKYSVKVLPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKd 252
Cdd:cd08528   148 GEDDKVTITdfGLAK--------QKGPESSKM-TSVVGTILYSCPEIVQN--EPYGEKADIWALGCILYQMCTLQPPFY- 215

                  ....*..
gi 1394533236 253 mpATQML 259
Cdd:cd08528   216 --STNML 220
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
40-251 8.92e-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: 56.48  E-value: 8.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNE-MVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVT 118
Cdd:cd05574     3 FKKIKLLGKG--DVGRVYLVRLKGTGKLFAMKVLDKEEMIKRnKVKRVLTEREILATLDHPFLPTLYASFQTSTHLCFVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 119 SFMAYGSAKDLICTHFMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLrsNLSMISH---- 194
Cdd:cd05574    81 DYCPGGELFRLLQKQPGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDF--DLSKQSSvtpp 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1394533236 195 --------GQRQRVVHDFPKYSVKVLP------------WLSPEVLQQNlqGYDAKSDIYSVGITACELANGHVPFK 251
Cdd:cd05574   159 pvrkslrkGSRRSSVKSIEKETFVAEPsarsnsfvgteeYIAPEVIKGD--GHGSAVDWWTLGILLYEMLYGTTPFK 233
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
88-264 8.93e-09

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: 8.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  88 GELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTHfmDG-MNELAIAYILQGVLKALDYIHHMGYVHRS 166
Cdd:cd05063    55 SEASIMGQFSHHNIIRLEGVVTKFKPAMIITEYMENGALDKYLRDH--DGeFSSYQLVGMLRGIAAGMKYLSDMNYVHRD 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 167 VKASHILISvdgkvylsglrSNLS-MISHGQRQRVVHDFPKYSVKV------LPWLSPEVLqqNLQGYDAKSDIYSVGIT 239
Cdd:cd05063   133 LAARNILVN-----------SNLEcKVSDFGLSRVLEDDPEGTYTTsggkipIRWTAPEAI--AYRKFTSASDVWSFGIV 199
                         170       180
                  ....*....|....*....|....*.
gi 1394533236 240 ACE-LANGHVPFKDMpATQMLLEKLN 264
Cdd:cd05063   200 MWEvMSFGERPYWDM-SNHEVMKAIN 224
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
40-261 1.00e-08

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: 56.13  E-value: 1.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGFEDlmTVNLARYKPTG-EY------VTVRRINLEACSnEMVTFLQGELHVSKLF-NHPNIVPYRATFIAD 111
Cdd:cd14181    12 YDPKEVIGRGVSS--VVRRCVHRHTGqEFavkiieVTAERLSPEQLE-EVRSSTLKEIHILRQVsGHPSIITLIDSYESS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 112 NELWVVTSFMAYGSAKDLICTHFMdgMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNL 189
Cdd:cd14181    89 TFIFLVFDLMRRGELFDYLTEKVT--LSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSdfGFSCHL 166
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1394533236 190 smiSHGQRQRVVHDFPKYsvkvlpwLSPEVLQQNL----QGYDAKSDIYSVGITACELANGHVPF---KDMPATQMLLE 261
Cdd:cd14181   167 ---EPGEKLRELCGTPGY-------LAPEILKCSMdethPGYGKEVDLWACGVILFTLLAGSPPFwhrRQMLMLRMIME 235
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
97-253 1.07e-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: 55.68  E-value: 1.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  97 NHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTHfmDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISV 176
Cdd:cd05581    59 AHPGIVKLYYTFQDESKLYFVLEYAPNGDLLEYIRKY--GSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDE 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 177 DGKVYL-----SGLRSNLSMISHGQRQRVVHDFPKYS-----VKVLPWLSPEVLQQNLQGYDakSDIYSVGITACELANG 246
Cdd:cd05581   137 DMHIKItdfgtAKVLGPDSSPESTKGDADSQIAYNQAraasfVGTAEYVSPELLNEKPAGKS--SDLWALGCIIYQMLTG 214

                  ....*..
gi 1394533236 247 HVPFKDM 253
Cdd:cd05581   215 KPPFRGS 221
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
40-350 1.08e-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: 55.85  E-value: 1.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQgELHVSKLFNHPNIVPYRATFIADNELWVVTS 119
Cdd:cd07844     2 YKKLDKLGEG--SYATVYKGRSKLTGQLVALKEIRLEHEEGAPFTAIR-EASLLKDLKHANIVTLHDIIHTKKTLTLVFE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 120 FMAygsaKDLicTHFMD----GMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNLSMIS 193
Cdd:cd07844    79 YLD----TDL--KQYMDdcggGLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLAdfGLARAKSVPS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 194 HGQRQRVVhdfpkysvkVLPWLSPEVLQQNLQgYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEK---LNGTvpcl 270
Cdd:cd07844   153 KTYSNEVV---------TLWYRPPDVLLGSTE-YSTSLDMWGVGCIFYEMATGRPLFPGSTDVEDQLHKifrVLGT---- 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 271 ldtstiPAEEltmspsrsvANSGLSDSLTTSTPRpsNGDSPSHPYHRTFS-----PHFHHFVEQCLQRNPDARPSASTLL 345
Cdd:cd07844   219 ------PTEE---------TWPGVSSNPEFKPYS--FPFYPPRPLINHAPrldriPHGEELALKFLQYEPKKRISAAEAM 281

                  ....*
gi 1394533236 346 NHSFF 350
Cdd:cd07844   282 KHPYF 286
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
89-352 1.23e-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: 56.21  E-value: 1.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  89 ELHVSKLFNHPNIV-------PyrATFIAD-NELWVVTSFMAYGSAKDLICTHFMDGMnelaIAYILQGVLKALDYIHHM 160
Cdd:cd07878    64 ELRLLKHMKHENVIglldvftP--ATSIENfNEVYLVTNLMGADLNNIVKCQKLSDEH----VQFLIYQLLRGLKYIHSA 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 161 GYVHRSVKASHILISVDgkvylsglrSNLSMISHGQRQRVVHDFPKYsVKVLPWLSPEVLqQNLQGYDAKSDIYSVGITA 240
Cdd:cd07878   138 GIIHRDLKPSNVAVNED---------CELRILDFGLARQADDEMTGY-VATRWYRAPEIM-LNWMHYNQTVDIWSVGCIM 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 241 CELANGHVPFkdmPATQMlLEKLNGtvpcLLDTSTIPAEELTMSPSRSVANSGLSdslttSTPRPSNGDSPShpYHRTFS 320
Cdd:cd07878   207 AELLKGKALF---PGNDY-IDQLKR----IMEVVGTPSPEVLKKISSEHARKYIQ-----SLPHMPQQDLKK--IFRGAN 271
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1394533236 321 PHFHHFVEQCLQRNPDARPSASTLLNHSFFKQ 352
Cdd:cd07878   272 PLAIDLLEKMLVLDSDKRISASEALAHPYFSQ 303
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
40-243 1.24e-08

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: 55.96  E-value: 1.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEacsNEMVTF---LQGELHVSKLFNHPNIVPYRATFIADNE--- 113
Cdd:cd07864     9 FDIIGIIGEG--TYGQVYKAKDKDTGELVALKKVRLD---NEKEGFpitAIREIKILRQLNHRSVVNLKEIVTDKQDald 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 114 -------LWVVTSFMAYgsakDLI--CTHFMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSG 184
Cdd:cd07864    84 fkkdkgaFYLVFEYMDH----DLMglLESGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLAD 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 185 LrsNLSMISHGQRQRvvhdfpKYSVKVLP-WLSPEVLQQNLQGYDAKSDIYSVGITACEL 243
Cdd:cd07864   160 F--GLARLYNSEESR------PYTNKVITlWYRPPELLLGEERYGPAIDVWSCGCILGEL 211
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
39-250 1.31e-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: 55.63  E-value: 1.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  39 CYELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEA-CSNEMVTF--LQGELHVSKLFNHPNIVPYRATFIADNELW 115
Cdd:cd14094     4 VYELCEVIGKG--PFSVVRRCIHRETGQQFAVKIVDVAKfTSSPGLSTedLKREASICHMLKHPHIVELLETYSSDGMLY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 116 VVTSFMaygSAKDL---ICTHFMDGM--NELAIAYILQGVLKALDYIHHMGYVHRSVKASHILI-SVD--GKVYLSGL-- 185
Cdd:cd14094    82 MVFEFM---DGADLcfeIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaSKEnsAPVKLGGFgv 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1394533236 186 ---RSNLSMISHGQrqrvvhdfpkysVKVLPWLSPEVLQQNLqgYDAKSDIYSVGITACELANGHVPF 250
Cdd:cd14094   159 aiqLGESGLVAGGR------------VGTPHFMAPEVVKREP--YGKPVDVWGCGVILFILLSGCLPF 212
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
40-252 1.39e-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: 55.42  E-value: 1.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKgfEDLMTVNLARYKPTGEYVTVRRInLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVvts 119
Cdd:cd14088     3 YDLGQVIKT--EEFCEIFRAKDKTTGKLYTCKKF-LKRDGRKVRKAAKNEINILKMVKHPNILQLVDVFETRKEYFI--- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 120 FMAYGSAKDLICTHFMDGM-NELAIAYILQGVLKALDYIHHMGYVHRSVKASHIlisvdgkVYLSGLRSNLSMISHGQRQ 198
Cdd:cd14088    77 FLELATGREVFDWILDQGYySERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENL-------VYYNRLKNSKIVISDFHLA 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1394533236 199 RVVHDFPKYSVKVLPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKD 252
Cdd:cd14088   150 KLENGLIKEPCGTPEYLAPEVVGR--QRYGRPVDCWAIGVIMYILLSGNPPFYD 201
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
38-267 1.70e-08

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: 54.97  E-value: 1.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  38 GCYELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSN-EMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWV 116
Cdd:cd14079     2 GNYILGKTLGVG--SFGKVKLAEHELTGHKVAVKILNRQKIKSlDMEEKIRREIQILKLFRHPHIIRLYEVIETPTDIFM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 117 VTSFMAYGSAKDLICTHfmDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLrSNlsMISH 194
Cdd:cd14079    80 VMEYVSGGELFDYIVQK--GRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIAdfGL-SN--IMRD 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1394533236 195 GqrqrvvhDFPKYSVKVLPWLSPEVLQQNL-QGYDAksDIYSVGITACELANGHVPFKDmPATQMLLEKLNGTV 267
Cdd:cd14079   155 G-------EFLKTSCGSPNYAAPEVISGKLyAGPEV--DVWSCGVILYALLCGSLPFDD-EHIPNLFKKIKSGI 218
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
41-250 1.70e-08

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: 55.12  E-value: 1.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  41 ELLTVIGKGFedLMTVNLARY-KPTGEYVTVRRINLEACSNEMVT--FLQgELHVSKLFNHPNIVPYRATfIADNELWVV 117
Cdd:cd05056     9 TLGRCIGEGQ--FGDVYQGVYmSPENEKIAVAVKTCKNCTSPSVRekFLQ-EAYIMRQFDHPHIVKLIGV-ITENPVWIV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 118 TSFMAYGSAKDLICTHFMDGMNELAIAYILQgVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLrsnlsmishg 195
Cdd:cd05056    85 MELAPLGELRSYLQVNKYSLDLASLILYAYQ-LSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGdfGL---------- 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 196 qrQRVVHD--FPKYSVKVLP--WLSPEVLqqNLQGYDAKSDIYSVGITACE-LANGHVPF 250
Cdd:cd05056   154 --SRYMEDesYYKASKGKLPikWMAPESI--NFRRFTSASDVWMFGVCMWEiLMLGVKPF 209
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
68-270 1.80e-08

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: 55.01  E-value: 1.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  68 VTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMA----YGSAKDLICTHFMDGMNELAi 143
Cdd:cd14153    25 VAIRLIDIERDNEEQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKgrtlYSVVRDAKVVLDVNKTRQIA- 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 144 ayilQGVLKALDYIHHMGYVHRSVKASHILISvDGKVYLS--GLRSNLSMISHGQRQ---RVVHDFPKY-SVKVLPWLSP 217
Cdd:cd14153   104 ----QEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITdfGLFTISGVLQAGRREdklRIQSGWLCHlAPEIIRQLSP 178
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1394533236 218 EVLQQNLQgYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPCL 270
Cdd:cd14153   179 ETEEDKLP-FSKHSDVFAFGTIWYELHAREWPFKTQPAEAIIWQVGSGMKPNL 230
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
40-283 2.09e-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: 55.00  E-value: 2.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMvTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTS 119
Cdd:cd14183     8 YKVGRTIGDG--NFAVVKECVERSTGREYALKIINKSKCRGKE-HMIQNEVSILRRVKHPNIVLLIEEMDMPTELYLVME 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 120 FMAYGSAKDLICThfMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILI--SVDGKVYLSGLRSNLSMISHGqr 197
Cdd:cd14183    85 LVKGGDLFDAITS--TNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVyeHQDGSKSLKLGDFGLATVVDG-- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 198 qrvvhdfPKYSVKVLP-WLSPEVLQQNlqGYDAKSDIYSVGITACELANGHVPFK----DMPA--TQMLLEKLNGTVPCL 270
Cdd:cd14183   161 -------PLYTVCGTPtYVAPEIIAET--GYGLKVDIWAAGVITYILLCGFPPFRgsgdDQEVlfDQILMGQVDFPSPYW 231
                         250
                  ....*....|...
gi 1394533236 271 LDTSTIPAEELTM 283
Cdd:cd14183   232 DNVSDSAKELITM 244
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
40-243 2.22e-08

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: 54.80  E-value: 2.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLeacSNEMVtflqgELHVSKLFN--HPNIVPYratfiadNELWVV 117
Cdd:cd14047     8 FKEIELIGSG--GFGQVFKAKHRIDGKTYAIKRVKL---NNEKA-----EREVKALAKldHPNIVRY-------NGCWDG 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 118 TSFMAYGSAKD---------LICTHFMDG---------MN-----ELAIAYILQGVLKALDYIHHMGYVHRSVKASHILI 174
Cdd:cd14047    71 FDYDPETSSSNssrsktkclFIQMEFCEKgtleswiekRNgekldKVLALEIFEQITKGVEYIHSKKLIHRDLKPSNIFL 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1394533236 175 SVDGKVYLSGLRSNLSMISHGQRQRvvhdfpkySVKVLPWLSPEvlQQNLQGYDAKSDIYSVGITACEL 243
Cdd:cd14047   151 VDTGKVKIGDFGLVTSLKNDGKRTK--------SKGTLSYMSPE--QISSQDYGKEVDIYALGLILFEL 209
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
65-345 2.92e-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: 54.22  E-value: 2.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  65 GEYVTVRRINLEACSNEMVTF--LQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGS-----AKDLICTHFMdg 137
Cdd:cd14148    17 GEEVAVKAARQDPDEDIAVTAenVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVMEYARGGAlnralAGKKVPPHVL-- 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 138 mnelaIAYILQgVLKALDYIHHMGYV---HRSVKASHILISvdGKVYLSGLRSNLSMISHGQRQRVVHDFPKYSVK-VLP 213
Cdd:cd14148    95 -----VNWAVQ-IARGMNYLHNEAIVpiiHRDLKSSNILIL--EPIENDDLSGKTLKITDFGLAREWHKTTKMSAAgTYA 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 214 WLSPEVLQQNLqgYDAKSDIYSVGITACELANGHVPFKDMPAtqmlleklngtvpclldtstipaeeltMSPSRSVANSG 293
Cdd:cd14148   167 WMAPEVIRLSL--FSKSSDVWSFGVLLWELLTGEVPYREIDA---------------------------LAVAYGVAMNK 217
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1394533236 294 LSDSLTTSTPRPsngdspshpyhrtfsphFHHFVEQCLQRNPDARPSASTLL 345
Cdd:cd14148   218 LTLPIPSTCPEP-----------------FARLLEECWDPDPHGRPDFGSIL 252
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
40-251 3.64e-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: 54.18  E-value: 3.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMvTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTS 119
Cdd:cd14185     2 YEIGRTIGDG--NFAVVKECRHWNENQEYAMKIIDKSKLKGKE-DMIESEILIIKSLSHPNIVKLFEVYETEKEIYLILE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 120 FMAYGSAKDLICTHFMdgMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILI--SVDGKvylsglrSNLSMISHGQR 197
Cdd:cd14185    79 YVRGGDLFDAIIESVK--FTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVqhNPDKS-------TTLKLADFGLA 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1394533236 198 QRVVHdfPKYSVKVLP-WLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFK 251
Cdd:cd14185   150 KYVTG--PIFTVCGTPtYVAPEILSE--KGYGLEVDMWAAGVILYILLCGFPPFR 200
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
89-252 3.68e-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: 53.80  E-value: 3.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  89 ELHVSKLFNHPNIVPYRATFiADNELWVVTSFMAY--GSAKDLIcthFMDGMNELAI----AYILQgVLKALDYIHHMGY 162
Cdd:cd14119    44 EIQILRRLNHRNVIKLVDVL-YNEEKQKLYMVMEYcvGGLQEML---DSAPDKRLPIwqahGYFVQ-LIDGLEYLHSQGI 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 163 VHRSVKASHILISVDGKVYLS--GLRSNLSMISHGQRQRVVHDFPKYSvkvlpwlSPEVL--QQNLQGYdaKSDIYSVGI 238
Cdd:cd14119   119 IHKDIKPGNLLLTTDGTLKISdfGVAEALDLFAEDDTCTTSQGSPAFQ-------PPEIAngQDSFSGF--KVDIWSAGV 189
                         170
                  ....*....|....
gi 1394533236 239 TACELANGHVPFKD 252
Cdd:cd14119   190 TLYNMTTGKYPFEG 203
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
40-350 3.75e-08

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: 54.30  E-value: 3.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRInLEACSNEMVTFLQ-GELHVSKLFNHPNIVPYRATFIADNELWVVT 118
Cdd:cd07847     3 YEKLSKIGEG--SYGVVFKCRNRETGQIVAIKKF-VESEDDPVIKKIAlREIRMLKQLKHPNLVNLIEVFRRKRKLHLVF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 119 SFMaygsakDLICTHFMD----GMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLrsNLSMISH 194
Cdd:cd07847    80 EYC------DHTVLNELEknprGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDF--GFARILT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 195 GQRQrvvhDFPKYsVKVLPWLSPEVLQQNLQgYDAKSDIYSVGITACELANGHV--PFKDMPATQMLLEKLNGTVpclld 272
Cdd:cd07847   152 GPGD----DYTDY-VATRWYRAPELLVGDTQ-YGPPVDVWAIGCVFAELLTGQPlwPGKSDVDQLYLIRKTLGDL----- 220
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1394533236 273 tstIPAEELTMSPSRSVanSGLsdslttSTPRPSNGDsPSHPYHRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFF 350
Cdd:cd07847   221 ---IPRHQQIFSTNQFF--KGL------SIPEPETRE-PLESKFPNISSPALSFLKGCLQMDPTERLSCEELLEHPYF 286
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
40-359 3.86e-08

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: 54.68  E-value: 3.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGFEDLmtVNLARYKPTGEYVTVRRInleACSNEMVTFLQG---ELHVSKLFNHPNIVPYRATFIAD----- 111
Cdd:cd07855     7 YEPIETIGSGAYGV--VCSAIDTKSGQKVAIKKI---PNAFDVVTTAKRtlrELKILRHFKHDNIIAIRDILRPKvpyad 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 112 -NELWVVTSFMAyGSAKDLIctHFMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLrSN 188
Cdd:cd07855    82 fKDVYVVLDLME-SDLHHII--HSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGdfGM-AR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 189 LSMISHGQRQRVVHDFpkysVKVLPWLSPEVLqQNLQGYDAKSDIYSVG-ITACELANGHV-PFKD-MPATQMLLEKLNg 265
Cdd:cd07855   158 GLCTSPEEHKYFMTEY----VATRWYRAPELM-LSLPEYTQAIDMWSVGcIFAEMLGRRQLfPGKNyVHQLQLILTVLG- 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 266 tvpclldtstipaeeltmSPSRSVANSGLSDSLTTS-TPRPSNGDSPSHPYHRTFSPHFHHFVEQCLQRNPDARPSASTL 344
Cdd:cd07855   232 ------------------TPSQAVINAIGADRVRRYiQNLPNKQPVPWETLYPKADQQALDLLSQMLRFDPSERITVAEA 293
                         330
                  ....*....|....*
gi 1394533236 345 LNHSFFKQIKRRASE 359
Cdd:cd07855   294 LQHPFLAKYHDPDDE 308
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
150-259 4.82e-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: 54.01  E-value: 4.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 150 VLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRsnLSmishgqRQRVVHDFPKYSVKVLP--WLSPEVLQQNLqgY 227
Cdd:cd05046   126 IALGMDHLSNARFVHRDLAARNCLVSSQREVKVSLLS--LS------KDVYNSEYYKLRNALIPlrWLAPEAVQEDD--F 195
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1394533236 228 DAKSDIYSVGITACELAN-GHVPFKDMPATQML 259
Cdd:cd05046   196 STKSDVWSFGVLMWEVFTqGELPFYGLSDEEVL 228
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
40-349 5.01e-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: 53.71  E-value: 5.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNE-MVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVT 118
Cdd:cd14186     3 FKVLNLLGKG--SFACVYRARSLHTGLEVAIKMIDKKAMQKAgMVQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 119 SfMAYGSAKDLICTHFMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNLSMIShgQ 196
Cdd:cd14186    81 E-MCHNGEMSRYLKNRKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIAdfGLATQLKMPH--E 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 197 RQRVVHDFPKYsvkvlpwLSPEVLQQNLQGYDakSDIYSVGITACELANGHVPFKdmpaTQMLLEKLNGTVpclldtsti 276
Cdd:cd14186   158 KHFTMCGTPNY-------ISPEIATRSAHGLE--SDVWSLGCMFYTLLVGRPPFD----TDTVKNTLNKVV--------- 215
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1394533236 277 paeeltmspsrsvansgLSDSlttstprpsngDSPSHpyhrtFSPHFHHFVEQCLQRNPDARPSASTLLNHSF 349
Cdd:cd14186   216 -----------------LADY-----------EMPAF-----LSREAQDLIHQLLRKNPADRLSLSSVLDHPF 255
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
65-255 5.75e-08

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: 53.55  E-value: 5.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  65 GEYVTVRRINLEACSNEMVTfLQGELHVSKLF---NHPNIVPYRATFIADNELWVVTSFMAYGS-----AKDLICTHFMd 136
Cdd:cd14061    17 GEEVAVKAARQDPDEDISVT-LENVRQEARLFwmlRHPNIIALRGVCLQPPNLCLVMEYARGGAlnrvlAGRKIPPHVL- 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 137 gmnelaIAYILQgVLKALDYIHHMGYV---HRSVKASHILISVdgKVYLSGLRSNLSMISHGQRQRVVHDFPKYSVK-VL 212
Cdd:cd14061    95 ------VDWAIQ-IARGMNYLHNEAPVpiiHRDLKSSNILILE--AIENEDLENKTLKITDFGLAREWHKTTRMSAAgTY 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1394533236 213 PWLSPEVLQQNLqgYDAKSDIYSVGITACELANGHVPFKDMPA 255
Cdd:cd14061   166 AWMAPEVIKSST--FSKASDVWSYGVLLWELLTGEVPYKGIDG 206
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
46-257 6.12e-08

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: 53.22  E-value: 6.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  46 IGKG-FEDlmtVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGElHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYG 124
Cdd:cd05041     3 IGRGnFGD---VYRGVLKPDNTEVAVKTCRETLPPDLKRKFLQEA-RILKQYDHPNIVKLIGVCVQKQPIMIVMELVPGG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 125 SakdlICTHFMDGMNELAIAYILQGVLKA---LDYIHHMGYVHRSVKASHILISVDGKVYLsglrSNLSMishgQRQrvv 201
Cdd:cd05041    79 S----LLTFLRKKGARLTVKQLLQMCLDAaagMEYLESKNCIHRDLAARNCLVGENNVLKI----SDFGM----SRE--- 143
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1394533236 202 HDFPKYSV----KVLP--WLSPEVLqqNLQGYDAKSDIYSVGITACEL-ANGHVPFKDMPATQ 257
Cdd:cd05041   144 EEDGEYTVsdglKQIPikWTAPEAL--NYGRYTSESDVWSFGILLWEIfSLGATPYPGMSNQQ 204
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
40-352 6.43e-08

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: 53.84  E-value: 6.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNEL----- 114
Cdd:cd07851    17 YQNLSPVGSG--AYGQVCSAFDTKTGRKVAIKKLSRPFQSAIHAKRTYRELRLLKHMKHENVIGLLDVFTPASSLedfqd 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 115 -WVVTSFMAygsaKDLICTHFMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDgkvylsglrSNLSMIS 193
Cdd:cd07851    95 vYLVTHLMG----ADLNNIVKCQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNED---------CELKILD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 194 HGQRQRVVHDFPKYsVKVLPWLSPEVLqQNLQGYDAKSDIYSVGITACELANGHVPFkdmPATQMlLEKLNgtvpCLLDT 273
Cdd:cd07851   162 FGLARHTDDEMTGY-VATRWYRAPEIM-LNWMHYNQTVDIWSVGCIMAELLTGKTLF---PGSDH-IDQLK----RIMNL 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 274 STIPAEEL----TMSPSRSVAnsglsDSLTTsTPRpsngdSPSHPYHRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSF 349
Cdd:cd07851   232 VGTPDEELlkkiSSESARNYI-----QSLPQ-MPK-----KDFKEVFSGANPLAIDLLEKMLVLDPDKRITAAEALAHPY 300

                  ...
gi 1394533236 350 FKQ 352
Cdd:cd07851   301 LAE 303
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
40-250 7.75e-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: 7.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRI-NLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVT 118
Cdd:cd05628     3 FESLKVIGRG--AFGEVRLVQKKDTGHVYAMKILrKADMLEKEQVGHIRAERDILVEADSLWVVKMFYSFQDKLNLYLIM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 119 SFMAYGSAKDLICTHfmDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNLSMISHGQ 196
Cdd:cd05628    81 EFLPGGDMMTLLMKK--DTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSdfGLCTGLKKAHRTE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 197 RQR-VVHDFPK-------------------------YSVKVLPWLSPEVLQQNlqGYDAKSDIYSVGITACELANGHVPF 250
Cdd:cd05628   159 FYRnLNHSLPSdftfqnmnskrkaetwkrnrrqlafSTVGTPDYIAPEVFMQT--GYNKLCDWWSLGVIMYEMLIGYPPF 236
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
97-350 9.05e-08

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


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 53.04  E-value: 9.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  97 NHPNIVPYRATFIADNELWVVTSFMAyGSAKDLI---CTHFMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHIL 173
Cdd:cd13982    53 EHPNVIRYFCTEKDRQFLYIALELCA-ASLQDLVespRESKLFLRPGLEPVRLLRQIASGLAHLHSLNIVHRDLKPQNIL 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 174 ISVD-----GKVYLS--GLRSNLSMISHGQRQRvvhDFPKYSVKvlpWLSPEVLQQNLQGYDAKS-DIYSVGitaC---- 241
Cdd:cd13982   132 ISTPnahgnVRAMISdfGLCKKLDVGRSSFSRR---SGVAGTSG---WIAPEMLSGSTKRRQTRAvDIFSLG---Cvfyy 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 242 ELANGHVPFKDMPATQMLLEKLNGTVPCLLDTstipaeeltmspsrsvansglsdslttstprpsngdspshpyhRTFSP 321
Cdd:cd13982   203 VLSGGSHPFGDKLEREANILKGKYSLDKLLSL-------------------------------------------GEHGP 239
                         250       260
                  ....*....|....*....|....*....
gi 1394533236 322 HFHHFVEQCLQRNPDARPSASTLLNHSFF 350
Cdd:cd13982   240 EAQDLIERMIDFDPEKRPSAEEVLNHPFF 268
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
38-254 9.50e-08

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: 52.90  E-value: 9.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  38 GCYELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRIN-LEACSNEMVTF-LQGELHVSKLFNHPNIVPYRATFIADNELW 115
Cdd:cd14070     2 GSYLIGRKLGEG--SFAKVREGLHAVTGEKVAIKVIDkKKAKKDSYVTKnLRREGRIQQMIRHPNITQLLDILETENSYY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 116 VVTSFMAYGSAKDLICTHFMDGMNElAIAYILQgVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNLSMIS 193
Cdd:cd14070    80 LVMELCPGGNLMHRIYDKKRLEERE-ARRYIRQ-LVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIdfGLSNCAGILG 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1394533236 194 HGQRQRVVHDFPKYSvkvlpwlSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMP 254
Cdd:cd14070   158 YSDPFSTQCGSPAYA-------APELLAR--KKYGPKVDVWSIGVNMYAMLTGTLPFTVEP 209
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
64-253 1.12e-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: 1.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  64 TGEYVTVRRINleaCSNEMVTFLQGELHVSKLfNHPNIVPYRATfIADNELWVVTSFMAYGSAKDLICTHfmdGMNELAI 143
Cdd:cd05083    28 MGQKVAVKNIK---CDVTAQAFLEETAVMTKL-QHKNLVRLLGV-ILHNGLYIVMELMSKGNLVNFLRSR---GRALVPV 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 144 AYILQ---GVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRsnlsmISHGQRQRVvhDFPKYSVKvlpWLSPEVL 220
Cdd:cd05083   100 IQLLQfslDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFG-----LAKVGSMGV--DNSRLPVK---WTAPEAL 169
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1394533236 221 QQNlqGYDAKSDIYSVGITACEL-ANGHVPFKDM 253
Cdd:cd05083   170 KNK--KFSSKSDVWSYGVLLWEVfSYGRAPYPKM 201
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
91-259 1.19e-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: 52.11  E-value: 1.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  91 HVSKLfNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLIcthfMDGmNELAIAYIL---QGVLKALDYIHHMGYVHRSV 167
Cdd:cd14059    34 HLRKL-NHPNIIKFKGVCTQAPCYCILMEYCPYGQLYEVL----RAG-REITPSLLVdwsKQIASGMNYLHLHKIIHRDL 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 168 KASHILISVDGKVYLS--GLRSNLSMIShgqrqrvvhdfPKYSVK-VLPWLSPEVLQQnlQGYDAKSDIYSVGITACELA 244
Cdd:cd14059   108 KSPNVLVTYNDVLKISdfGTSKELSEKS-----------TKMSFAgTVAWMAPEVIRN--EPCSEKVDIWSFGVVLWELL 174
                         170
                  ....*....|....*
gi 1394533236 245 NGHVPFKDMPATQML 259
Cdd:cd14059   175 TGEIPYKDVDSSAII 189
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
40-351 1.21e-07

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


Pssm-ID: 270833 [Multi-domain]  Cd Length: 298  Bit Score: 52.96  E-value: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEM----------VTFLQgELHvsklfnHPNIVPYRATFI 109
Cdd:cd07841     2 YEKGKKLGEG--TYAVVYKARDKETGRIVAIKKIKLGERKEAKdginftalreIKLLQ-ELK------HPNIIGLLDVFG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 110 ADNELWVVTSFMAYgsakDLicthfmdgmnELAI-------------AYILQgVLKALDYIHHMGYVHRSVKASHILISV 176
Cdd:cd07841    73 HKSNINLVFEFMET----DL----------EKVIkdksivltpadikSYMLM-TLRGLEYLHSNWILHRDLKPNNLLIAS 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 177 DGKVYLS--GL-RsnlsmiSHGQRQRvvhdfpKYSVKVL-PWL-SPEVLqqnlqgYDAKS-----DIYSVGitaCELAng 246
Cdd:cd07841   138 DGVLKLAdfGLaR------SFGSPNR------KMTHQVVtRWYrAPELL------FGARHygvgvDMWSVG---CIFA-- 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 247 hvpfkdmpatQMLLEKlngtvPCLLDTSTIpaeeltmspsrsvansglsDSLTT-----STPRPSN-GDSPSHPYHRTFS 320
Cdd:cd07841   195 ----------ELLLRV-----PFLPGDSDI-------------------DQLGKifealGTPTEENwPGVTSLPDYVEFK 240
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1394533236 321 PH----FHH-----------FVEQCLQRNPDARPSASTLLNHSFFK 351
Cdd:cd07841   241 PFpptpLKQifpaasddaldLLQRLLTLNPNKRITARQALEHPYFS 286
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
74-253 1.25e-07

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: 52.58  E-value: 1.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  74 NLEACSNEMVTFLQgELHVSKLFNHPNIVPYRATfIADNELWVVTSFMAYGSAKDLICThfmDGMNELAIAYILQ---GV 150
Cdd:cd05067    38 SLKQGSMSPDAFLA-EANLMKQLQHQRLVRLYAV-VTQEPIYIITEYMENGSLVDFLKT---PSGIKLTINKLLDmaaQI 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 151 LKALDYIHHMGYVHRSVKASHILIS--VDGKVYLSGLRSNLSMISHGQRQRVvhdfpKYSVKvlpWLSPEVLqqNLQGYD 228
Cdd:cd05067   113 AEGMAFIEERNYIHRDLRAANILVSdtLSCKIADFGLARLIEDNEYTAREGA-----KFPIK---WTAPEAI--NYGTFT 182
                         170       180
                  ....*....|....*....|....*.
gi 1394533236 229 AKSDIYSVGITACELAN-GHVPFKDM 253
Cdd:cd05067   183 IKSDVWSFGILLTEIVThGRIPYPGM 208
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
40-359 1.41e-07

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: 52.86  E-value: 1.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGFEDLmtVNLARYKPTGEYVTVRRIN--LEACSNemVTFLQGELHVSKLFNHPNIV--------PYRATFi 109
Cdd:cd07859     2 YKIQEVIGKGSYGV--VCSAIDTHTGEKVAIKKINdvFEHVSD--ATRILREIKLLRLLRHPDIVeikhimlpPSRREF- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 110 adNELWVVTSFM------AYGSAKDLICTHFMdgmnelaiaYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS 183
Cdd:cd07859    77 --KDIYVVFELMesdlhqVIKANDDLTPEHHQ---------FFLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKIC 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 184 GLRSNLSMISHGQRQRVVHDFpkysVKVLPWLSPEVLQQNLQGYDAKSDIYSVGITACELANGH--VPFKDMPATQMLLE 261
Cdd:cd07859   146 DFGLARVAFNDTPTAIFWTDY----VATRWYRAPELCGSFFSKYTPAIDIWSIGCIFAEVLTGKplFPGKNVVHQLDLIT 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 262 KLNGTvpclldtstiPAEElTMSPSRSVANSGLSDSLTTSTPRPsngdspshpyhrtFSPHFHH-------FVEQCLQRN 334
Cdd:cd07859   222 DLLGT----------PSPE-TISRVRNEKARRYLSSMRKKQPVP-------------FSQKFPNadplalrLLERLLAFD 277
                         330       340
                  ....*....|....*....|....*
gi 1394533236 335 PDARPSASTLLNHSFFKQIKRRASE 359
Cdd:cd07859   278 PKDRPTAEEALADPYFKGLAKVERE 302
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
68-259 1.71e-07

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: 52.01  E-value: 1.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  68 VTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRAtFIADNELWVVTSFMAyGSA--KDLictHFMDGMNEL-AIA 144
Cdd:cd14062    18 VAVKKLNVTDPTPSQLQAFKNEVAVLRKTRHVNILLFMG-YMTKPQLAIVTQWCE-GSSlyKHL---HVLETKFEMlQLI 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 145 YILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLrsNLSMIShgQRQRVVHDFPKYSVKVLpWLSPEVLQ-QN 223
Cdd:cd14062    93 DIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDF--GLATVK--TRWSGSQQFEQPTGSIL-WMAPEVIRmQD 167
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1394533236 224 LQGYDAKSDIYSVGITACELANGHVPFKD-MPATQML 259
Cdd:cd14062   168 ENPYSFQSDVYAFGIVLYELLTGQLPYSHiNNRDQIL 204
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
40-359 1.74e-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: 52.39  E-value: 1.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQgELHVSKLFNHPNIVPYRATFIADNELWVVTS 119
Cdd:cd07869     7 YEKLEKLGEG--SYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTAIR-EASLLKGLKHANIVLLHDIIHTKETLTLVFE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 120 FMAygsaKDLicTHFMD----GMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNLSMIS 193
Cdd:cd07869    84 YVH----TDL--CQYMDkhpgGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLAdfGLARAKSVPS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 194 HGQRQRVVhdfpkysvkVLPWLSPEVLQQNLQgYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKL--------NG 265
Cdd:cd07869   158 HTYSNEVV---------TLWYRPPDVLLGSTE-YSTCLDMWGVGCIFVEMIQGVAAFPGMKDIQDQLERIflvlgtpnED 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 266 TVPCLLDTSTIPAEELTMSPSRSVANSGLSDSlttstprpsngdspshpyhrtFSPHFHHFVEQCLQRNPDARPSASTLL 345
Cdd:cd07869   228 TWPGVHSLPHFKPERFTLYSPKNLRQAWNKLS---------------------YVNHAEDLASKLLQCFPKNRLSAQAAL 286
                         330
                  ....*....|....
gi 1394533236 346 NHSFFKQIKRRASE 359
Cdd:cd07869   287 SHEYFSDLPPRLWE 300
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
40-268 1.78e-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: 52.31  E-value: 1.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGFEDLmtVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTS 119
Cdd:cd07848     3 FEVLGVVGEGAYGV--VLKCRHKETKEIVAIKKFKDSEENEEVKETTLRELKMLRTLKQENIVELKEAFRRRGKLYLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 120 FMAyGSAKDLICTHFMDGMNELAIAYILQgVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNLSMISHGqr 197
Cdd:cd07848    81 YVE-KNMLELLEEMPNGVPPEKVRSYIYQ-LIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCdfGFARNLSEGSNA-- 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1394533236 198 qrvvhDFPKYsVKVLPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQML--LEKLNGTVP 268
Cdd:cd07848   157 -----NYTEY-VATRWYRSPELLLG--APYGKAVDMWSVGCILGELSDGQPLFPGESEIDQLftIQKVLGPLP 221
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
84-308 2.37e-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: 2.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  84 TFLQgELHVSKLFNHPNIVPYRATfIADNELWVVTSFMAYGSAKDLICTHFMDGMNELAIAYILQGVLKALDYIHHMGYV 163
Cdd:cd05070    50 SFLE-EAQIMKKLKHDKLVQLYAV-VSEEPIYIVTEYMSKGSLLDFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYI 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 164 HRSVKASHILI--SVDGKVYLSGLRSNLSMISHGQRQRVvhdfpKYSVKvlpWLSPEVLqqnLQG-YDAKSDIYSVGITA 240
Cdd:cd05070   128 HRDLRSANILVgnGLICKIADFGLARLIEDNEYTARQGA-----KFPIK---WTAPEAA---LYGrFTIKSDVWSFGILL 196
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1394533236 241 CEL-ANGHVPFKDMPATQMLLEKLNG-TVPCLLDTStIPAEELTM---------SPSRSVANSGLSDSLTTSTPRPSNG 308
Cdd:cd05070   197 TELvTKGRVPYPGMNNREVLEQVERGyRMPCPQDCP-ISLHELMIhcwkkdpeeRPTFEYLQGFLEDYFTATEPQYQPG 274
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
39-249 2.60e-07

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: 51.54  E-value: 2.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  39 CYELLTVIGKG-F---------ED--LMTVNLARYKPTGEYVTVRRINlEACSNEmvtflqgelhvsKLFNHPNIVPYRA 106
Cdd:cd14050     2 CFTILSKLGEGsFgevfkvrsrEDgkLYAVKRSRSRFRGEKDRKRKLE-EVERHE------------KLGEHPNCVRFIK 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 107 TFIADNELWVVT-----SFMAYGSAKDLIcthfmdgmNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVY 181
Cdd:cd14050    69 AWEEKGILYIQTelcdtSLQQYCEETHSL--------PESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCK 140
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1394533236 182 LS--GL-----RSNLSMISHGQrqrvvhdfPKYsvkvlpwLSPEVLQQNlqgYDAKSDIYSVGITACELA-NGHVP 249
Cdd:cd14050   141 LGdfGLvveldKEDIHDAQEGD--------PRY-------MAPELLQGS---FTKAADIFSLGITILELAcNLELP 198
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
46-182 2.63e-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: 49.36  E-value: 2.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  46 IGKGFEDlmTVNLARYKPTGEYVTVRRINLEAcsNEMVTFLQGELHVSK-LFNH-PNIVPYRATFIADNELWVVTSFMAY 123
Cdd:cd13968     1 MGEGASA--KVFWAEGECTTIGVAVKIGDDVN--NEEGEDLESEMDILRrLKGLeLNIPKVLVTEDVDGPNILLMELVKG 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1394533236 124 GSAKDLICTHFMDgmnELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYL 182
Cdd:cd13968    77 GTLIAYTQEEELD---EKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKL 132
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
56-251 2.70e-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: 51.40  E-value: 2.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  56 VNLARYKPTGEyVTVRRINLEACSNEmvTFLQgELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTHFM 135
Cdd:cd05114    20 VRLGKWRAQYK-VAIKAIREGAMSEE--DFIE-EAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFMENGCLLNYLRQRRG 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 136 DGMNELAIAyILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLsglrSNLSMISHGQRQRVVHDF-PKYSVKvlpW 214
Cdd:cd05114    96 KLSRDMLLS-MCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKV----SDFGMTRYVLDDQYTSSSgAKFPVK---W 167
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1394533236 215 LSPEVLqqNLQGYDAKSDIYSVGITACEL-ANGHVPFK 251
Cdd:cd05114   168 SPPEVF--NYSKFSSKSDVWSFGVLMWEVfTEGKMPFE 203
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
40-352 2.86e-07

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: 51.60  E-value: 2.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGFEDLmtVNLARYKPTGEYVTVRRINLEACSNEM-VTFLQgELHVSKLFNHPNIVPYRATfIADNELWVVT 118
Cdd:cd07845     9 FEKLNRIGEGTYGI--VYRARDTTSGEIVALKKVRMDNERDGIpISSLR-EITLLLNLRHPNIVELKEV-VVGKHLDSIF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 119 SFMAYgsakdliCTH----FMDGM----NELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSN 188
Cdd:cd07845    85 LVMEY-------CEQdlasLLDNMptpfSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIAdfGLART 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 189 LSMISHGQRQRVVhdfpkysvkVLPWLSPEVLQQNLQgYDAKSDIYSVGITACELAnGHVPFkdMPATQMlLEKLNGTVp 268
Cdd:cd07845   158 YGLPAKPMTPKVV---------TLWYRAPELLLGCTT-YTTAIDMWAVGCILAELL-AHKPL--LPGKSE-IEQLDLII- 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 269 clldtstipaeELTMSPSRSVAnSGLSDslttsTPRPSNGDSPSHPYHrTFSPHFHHFVEQCLQ-------RNPDARPSA 341
Cdd:cd07845   223 -----------QLLGTPNESIW-PGFSD-----LPLVGKFTLPKQPYN-NLKHKFPWLSEAGLRllnfllmYDPKKRATA 284
                         330
                  ....*....|.
gi 1394533236 342 STLLNHSFFKQ 352
Cdd:cd07845   285 EEALESSYFKE 295
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
41-259 3.21e-07

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: 51.51  E-value: 3.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  41 ELLTVIGKGFEDlmtvNLARYKPTGEyVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSF 120
Cdd:cd14152     3 ELGELIGQGRWG----KVHRGRWHGE-VAIRLLEIDGNNQDHLKLFKKEVMNYRQTRHENVVLFMGACMHPPHLAIITSF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 121 ----MAYGSAKDLICTHFMDGMNELAiayilQGVLKALDYIHHMGYVHRSVKASHILISvDGKVYLS--GLRSNLSMISH 194
Cdd:cd14152    78 ckgrTLYSFVRDPKTSLDINKTRQIA-----QEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITdfGLFGISGVVQE 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1394533236 195 GQRQ---RVVHDFpkysvkvLPWLSPEVLQQNLQG-------YDAKSDIYSVGITACELANGHVPFKDMPATQML 259
Cdd:cd14152   152 GRREnelKLPHDW-------LCYLAPEIVREMTPGkdedclpFSKAADVYAFGTIWYELQARDWPLKNQPAEALI 219
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
40-175 3.86e-07

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: 51.28  E-value: 3.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKG-FEDlmtVNLARYKP-TGEYVTVRRINLEACSNEMVTFLQ-----GELHVSKLFNHPNIVPYRATFIADN 112
Cdd:cd14096     3 YRLINKIGEGaFSN---VYKAVPLRnTGKPVAIKVVRKADLSSDNLKGSSranilKEVQIMKRLSHPNIVKLLDFQESDE 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1394533236 113 ELWVVTSFMAYGSAKDLIC--THFMDgmnELAIAYILQgVLKALDYIHHMGYVHRSVKASHILIS 175
Cdd:cd14096    80 YYYIVLELADGGEIFHQIVrlTYFSE---DLSRHVITQ-VASAVKYLHEIGVVHRDIKPENLLFE 140
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
40-349 3.87e-07

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: 50.90  E-value: 3.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADN-ELWVVT 118
Cdd:cd08223     2 YQFLRVIGKG--SYGEVWLVRHKRDRKQYVIKKLNLKNASKRERKAAEQEAKLLSKLKHPNIVSYKESFEGEDgFLYIVM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 119 SFMAYG---------SAKDLICTHFMDGMNELAIayilqgvlkALDYIHHMGYVHRSVKASHILISvdgkvylsglRSNL 189
Cdd:cd08223    80 GFCEGGdlytrlkeqKGVLLEERQVVEWFVQIAM---------ALQYMHERNILHRDLKTQNIFLT----------KSNI 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 190 SMISHGQRQRVVH---DFPKYSVKVLPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPF--KDMPAtqMLLEKLN 264
Cdd:cd08223   141 IKVGDLGIARVLEsssDMATTLIGTPYYMSPELFSN--KPYNHKSDVWALGCCVYEMATLKHAFnaKDMNS--LVYKILE 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 265 GTVPclldtstipaeeltmspsrsvansglsdslttstprpsngdspshPYHRTFSPHFHHFVEQCLQRNPDARPSASTL 344
Cdd:cd08223   217 GKLP---------------------------------------------PMPKQYSPELGELIKAMLHQDPEKRPSVKRI 251

                  ....*
gi 1394533236 345 LNHSF 349
Cdd:cd08223   252 LRQPY 256
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
43-243 3.93e-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: 51.05  E-value: 3.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  43 LTVIGKGfeDLMTVNLARYKP----TGEYVTVRRinLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADN--ELWV 116
Cdd:cd05081     9 ISQLGKG--NFGSVELCRYDPlgdnTGALVAVKQ--LQHSGPDQQRDFQREIQILKALHSDFIVKYRGVSYGPGrrSLRL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 117 VTSFMAYGSAKDLICTHfmdgMNELAIAYIL---QGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLrsNLSMIS 193
Cdd:cd05081    85 VMEYLPSGCLRDFLQRH----RARLDASRLLlysSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADF--GLAKLL 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1394533236 194 HGQRQRVVHDFPKYSvkVLPWLSPEVLQQNLqgYDAKSDIYSVGITACEL 243
Cdd:cd05081   159 PLDKDYYVVREPGQS--PIFWYAPESLSDNI--FSRQSDVWSFGVVLYEL 204
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
140-250 4.18e-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: 50.87  E-value: 4.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 140 ELAIAYILQGVLkALDYIHHMGYVHRSVKASHILISVDGKVYLS-------GLRSNLSMISHGQRQRVVHDFPKYSVKVL 212
Cdd:cd05609   100 DMARMYFAETVL-ALEYLHSYGIVHRDLKPDNLLITSMGHIKLTdfglskiGLMSLTTNLYEGHIEKDTREFLDKQVCGT 178
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1394533236 213 P-WLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPF 250
Cdd:cd05609   179 PeYIAPEVILR--QGYGKPVDWWAMGIILYEFLVGCVPF 215
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
55-349 4.23e-07

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: 51.13  E-value: 4.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  55 TVNLARYKPTGEYVTVRRI------NLEACSNEmVTFLqgelhvSKLFNHPNIVPY---RATFIADN--ELWVVTSFMAY 123
Cdd:cd14037    18 HVYLVKTSNGGNRAALKRVyvndehDLNVCKRE-IEIM------KRLSGHKNIVGYidsSANRSGNGvyEVLLLMEYCKG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 124 GSAKDLICTHFMDGMNELAIAYILQGVLKALDYIHHMG--YVHRSVKASHILISVDGKVYL----SGLRSNLSMISHGQR 197
Cdd:cd14037    91 GGVIDLMNQRLQTGLTESEILKIFCDVCEAVAAMHYLKppLIHRDLKVENVLISDSGNYKLcdfgSATTKILPPQTKQGV 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 198 QRVVHDFPKYSvkVLPWLSPEVLQQNL-QGYDAKSDIYSVGItacelanghvpfkdmpatqmLLEKLngtvpCLLdtsTI 276
Cdd:cd14037   171 TYVEEDIKKYT--TLQYRAPEMIDLYRgKPITEKSDIWALGC--------------------LLYKL-----CFY---TT 220
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1394533236 277 PAEEltmspSRSVAnsglsdslttstprPSNGDSPSHPYHRtFSPHFHHFVEQCLQRNPDARPSASTLLNHSF 349
Cdd:cd14037   221 PFEE-----SGQLA--------------ILNGNFTFPDNSR-YSKRLHKLIRYMLEEDPEKRPNIYQVSYEAF 273
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
94-268 4.53e-07

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: 50.56  E-value: 4.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  94 KLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLIctHFMDGMnelaIAYILQGVLKALDYIHHMGYVHR-------- 165
Cdd:cd14057    47 RIFSHPNVLPVLGACNSPPNLVVISQYMPYGSLYNVL--HEGTGV----VVDQSQAVKFALDIARGMAFLHTlepliprh 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 166 SVKASHILISVDGKVYLSGLRSNLSMISHGQrqrvvhdfpKYSVKvlpWLSPEVLQQNLQGYDAKS-DIYSVGITACELA 244
Cdd:cd14057   121 HLNSKHVMIDEDMTARINMADVKFSFQEPGK---------MYNPA---WMAPEALQKKPEDINRRSaDMWSFAILLWELV 188
                         170       180
                  ....*....|....*....|....*...
gi 1394533236 245 NGHVPFKDMP----ATQMLLEKLNGTVP 268
Cdd:cd14057   189 TREVPFADLSnmeiGMKIALEGLRVTIP 216
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
45-250 4.83e-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: 51.16  E-value: 4.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  45 VIGKGfeDLMTVNLARYKPTGEYVTVRRINLEAC-SNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVtsfMAY 123
Cdd:cd05595     2 LLGKG--TFGKVILVREKATGRYYAMKILRKEVIiAKDEVAHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFV---MEY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 124 GSAKDLIcTHFMDG--MNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMISHGQRQRVV 201
Cdd:cd05595    77 ANGGELF-FHLSRErvFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGITDGATMKTF 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1394533236 202 HDFPKYsvkvlpwLSPEVLQQNlqGYDAKSDIYSVGITACELANGHVPF 250
Cdd:cd05595   156 CGTPEY-------LAPEVLEDN--DYGRAVDWWGLGVVMYEMMCGRLPF 195
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
89-252 4.95e-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: 4.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  89 ELHVSKLFNHPNIVPYRATFIADNE--LWVVTSFMAYGSAKDLICTHfmdGMNELAIAYILQGVLKALDYIHHMGYVHRS 166
Cdd:cd14199    75 EIAILKKLDHPNVVKLVEVLDDPSEdhLYMVFELVKQGPVMEVPTLK---PLSEDQARFYFQDLIKGIEYLHYQKIIHRD 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 167 VKASHILISVDGKVYLSGLrsNLSMISHGQRQrvvhdFPKYSVKVLPWLSPEVLQQNLQGYDAKS-DIYSVGITACELAN 245
Cdd:cd14199   152 VKPSNLLVGEDGHIKIADF--GVSNEFEGSDA-----LLTNTVGTPAFMAPETLSETRKIFSGKAlDVWAMGVTLYCFVF 224

                  ....*..
gi 1394533236 246 GHVPFKD 252
Cdd:cd14199   225 GQCPFMD 231
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
85-259 5.00e-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: 5.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  85 FLQgELHVSKLFNHPNIVPYRATfIADNELWVVTSFMAYGSAKDLICThfmDGMNELAIAYILQ---GVLKALDYIHHMG 161
Cdd:cd05073    53 FLA-EANVMKTLQHDKLVKLHAV-VTKEPIYIITEFMAKGSLLDFLKS---DEGSKQPLPKLIDfsaQIAEGMAFIEQRN 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 162 YVHRSVKASHILIS--VDGKVYLSGLRSNLSmishgQRQRVVHDFPKYSVKvlpWLSPEVLqqNLQGYDAKSDIYSVGIT 239
Cdd:cd05073   128 YIHRDLRAANILVSasLVCKIADFGLARVIE-----DNEYTAREGAKFPIK---WTAPEAI--NFGSFTIKSDVWSFGIL 197
                         170       180
                  ....*....|....*....|.
gi 1394533236 240 ACELAN-GHVPFKDMPATQML 259
Cdd:cd05073   198 LMEIVTyGRIPYPGMSNPEVI 218
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
93-345 5.70e-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: 5.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  93 SKLFN---HPNIVPYRATFIADNELWVVTSFMAYGSA-KDLICTHFMDGMN-------ELAIAYILQgVLKALDYIHHMG 161
Cdd:cd14146    44 AKLFSmlrHPNIIKLEGVCLEEPNLCLVMEFARGGTLnRALAAANAAPGPRrarrippHILVNWAVQ-IARGMLYLHEEA 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 162 YV---HRSVKASHILIsVDGKVYLSGLRSNLSMISHGQrQRVVHDFPKYSVK-VLPWLSPEVLQQNLqgYDAKSDIYSVG 237
Cdd:cd14146   123 VVpilHRDLKSSNILL-LEKIEHDDICNKTLKITDFGL-AREWHRTTKMSAAgTYAWMAPEVIKSSL--FSKGSDIWSYG 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 238 ITACELANGHVPFKDMPAtqmlleklngtvpclldtstipaeeltMSPSRSVANSGLSDSLTTSTPRPsngdspshpyhr 317
Cdd:cd14146   199 VLLWELLTGEVPYRGIDG---------------------------LAVAYGVAVNKLTLPIPSTCPEP------------ 239
                         250       260
                  ....*....|....*....|....*...
gi 1394533236 318 tfsphFHHFVEQCLQRNPDARPSASTLL 345
Cdd:cd14146   240 -----FAKLMKECWEQDPHIRPSFALIL 262
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
99-250 6.03e-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: 50.77  E-value: 6.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  99 PNIVPYRATFIADNELWVVTSFMAYGSakdlICTHFMD----GMNELAIaYILQGVLkALDYIHHMGYVHRSVKASHILI 174
Cdd:cd05613    65 PFLVTLHYAFQTDTKLHLILDYINGGE----LFTHLSQrerfTENEVQI-YIGEIVL-ALEHLHKLGIIYRDIKLENILL 138
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1394533236 175 SVDGKVYLSGLRSNLSMISHgQRQRVvhdfpkYSV-KVLPWLSPEVLQQNLQGYDAKSDIYSVGITACELANGHVPF 250
Cdd:cd05613   139 DSSGHVVLTDFGLSKEFLLD-ENERA------YSFcGTIEYMAPEIVRGGDSGHDKAVDWWSLGVLMYELLTGASPF 208
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
56-238 6.07e-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: 50.40  E-value: 6.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  56 VNLARYKPTGEYVTVRRINLEacSNEMVTFLQgELHVS-KLFNHPNIVPYRATFIADNELWVVTSFMA-YGSAKDLICTH 133
Cdd:cd13987     9 VLLAVHKGSGTKMALKFVPKP--STKLKDFLR-EYNISlELSVHPHIIKTYDVAFETEDYYVFAQEYApYGDLFSIIPPQ 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 134 FmdGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILIsvdgkvylsgLRSNLSMISHGQ--RQRVVHDFPKYSVKV 211
Cdd:cd13987    86 V--GLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLL----------FDKDCRRVKLCDfgLTRRVGSTVKRVSGT 153
                         170       180       190
                  ....*....|....*....|....*....|
gi 1394533236 212 LPWLSPEVLQQNL-QGY--DAKSDIYSVGI 238
Cdd:cd13987   154 IPYTAPEVCEAKKnEGFvvDPSIDVWAFGV 183
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
97-350 7.30e-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: 50.31  E-value: 7.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  97 NHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTHFMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISV 176
Cdd:cd14198    66 SNPRVVNLHEVYETTSEIILILEYAAGGEIFNLCVPDLAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSS 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 177 -----DGKVYLSGLRSNlsmISHGQRQRVVHDFPKYsvkvlpwLSPEVLqqNLQGYDAKSDIYSVGITACELANGHVPF- 250
Cdd:cd14198   146 iyplgDIKIVDFGMSRK---IGHACELREIMGTPEY-------LAPEIL--NYDPITTATDMWNIGVIAYMLLTHESPFv 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 251 -KDMPATQMLLEKLNgtvpclLDTStipaeELTMSPSRSVANSglsdslttstprpsngdspshpyhrtfsphfhhFVEQ 329
Cdd:cd14198   214 gEDNQETFLNISQVN------VDYS-----EETFSSVSQLATD---------------------------------FIQK 249
                         250       260
                  ....*....|....*....|.
gi 1394533236 330 CLQRNPDARPSASTLLNHSFF 350
Cdd:cd14198   250 LLVKNPEKRPTAEICLSHSWL 270
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
89-352 7.60e-07

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


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 50.10  E-value: 7.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  89 ELHVSKLFNHPNIV----PYRATFIADNELWVVTSFMAYGSAKDLIctHFMDGMNELAIAYILQGVLKALDYIHHMG--Y 162
Cdd:cd14031    59 EAEMLKGLQHPNIVrfydSWESVLKGKKCIVLVTELMTSGTLKTYL--KRFKVMKPKVLRSWCRQILKGLQFLHTRTppI 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 163 VHRSVKASHILISvdgkvylsGLRSNLSMISHGQRQRVVHDFPKYSVKVLPWLSPEVLQQNlqgYDAKSDIYSVGITACE 242
Cdd:cd14031   137 IHRDLKCDNIFIT--------GPTGSVKIGDLGLATLMRTSFAKSVIGTPEFMAPEMYEEH---YDESVDVYAFGMCMLE 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 243 LANGHVPFKDMPATQMLLEKLngtvpclldtstipaeeltmspsrsvansglsdsltTSTPRPSNgdspshpYHRTFSPH 322
Cdd:cd14031   206 MATSEYPYSECQNAAQIYRKV------------------------------------TSGIKPAS-------FNKVTDPE 242
                         250       260       270
                  ....*....|....*....|....*....|
gi 1394533236 323 FHHFVEQCLQRNPDARPSASTLLNHSFFKQ 352
Cdd:cd14031   243 VKEIIEGCIRQNKSERLSIKDLLNHAFFAE 272
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
40-250 8.26e-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: 50.46  E-value: 8.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEAC-SNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVT 118
Cdd:cd05593    17 FDYLKLLGKG--TFGKVILVREKASGKYYAMKILKKEVIiAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVM 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 119 SFMAYGSAKDLICTHFMdgMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMISHGQRQ 198
Cdd:cd05593    95 EYVNGGELFFHLSRERV--FSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATM 172
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1394533236 199 RVVHDFPKYsvkvlpwLSPEVLQQNlqGYDAKSDIYSVGITACELANGHVPF 250
Cdd:cd05593   173 KTFCGTPEY-------LAPEVLEDN--DYGRAVDWWGLGVVMYEMMCGRLPF 215
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
55-250 8.75e-07

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The IKK complex functions as a master regulator of Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. It is composed of two kinases, IKKalpha and IKKbeta, and the regulatory subunit IKKgamma or NEMO (NF-kB Essential MOdulator). IKKs facilitate the release of NF-kB dimers from an inactive state, allowing them to migrate to the nucleus where they regulate gene transcription. There are two IKK pathways that regulate NF-kB signaling, called the classical (involving IKKbeta and NEMO) and non-canonical (involving IKKalpha) pathways. The classical pathway regulates the majority of genes activated by NF-kB. The IKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270891 [Multi-domain]  Cd Length: 289  Bit Score: 50.14  E-value: 8.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  55 TVNLARYKPTGEYVTVRRinleaCSNEMVTFLQG------ELHVSKLFNHPNIV-----PYRATFIADNELWVVTsfMAY 123
Cdd:cd13989     8 YVTLWKHQDTGEYVAIKK-----CRQELSPSDKNrerwclEVQIMKKLNHPNVVsardvPPELEKLSPNDLPLLA--MEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 124 GSAKDLicTHFMD------GMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHI-LISVDGKVYLS----GLRSNLSmi 192
Cdd:cd13989    81 CSGGDL--RKVLNqpenccGLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIvLQQGGGRVIYKlidlGYAKELD-- 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1394533236 193 shgqRQRVVHDFpkysVKVLPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPF 250
Cdd:cd13989   157 ----QGSLCTSF----VGTLQYLAPELFES--KKYTCTVDYWSFGTLAFECITGYRPF 204
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
89-350 9.47e-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: 49.93  E-value: 9.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  89 ELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLicTHFMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVK 168
Cdd:cd14187    57 EIAIHRSLAHQHVVGFHGFFEDNDFVYVVLELCRRRSLLEL--HKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLK 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 169 ASHILISVDGKVYLS--GLRSNLSMisHGQRQRVVHDFPKYsvkvlpwLSPEVLQQnlQGYDAKSDIYSVGITACELANG 246
Cdd:cd14187   135 LGNLFLNDDMEVKIGdfGLATKVEY--DGERKKTLCGTPNY-------IAPEVLSK--KGHSFEVDIWSIGCIMYTLLVG 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 247 HVPFKdmpatqmlleklngtVPCLLDTST-IPAEELTMspsrsvansglsdslttstprpsngdsPSHpyhrtFSPHFHH 325
Cdd:cd14187   204 KPPFE---------------TSCLKETYLrIKKNEYSI---------------------------PKH-----INPVAAS 236
                         250       260
                  ....*....|....*....|....*
gi 1394533236 326 FVEQCLQRNPDARPSASTLLNHSFF 350
Cdd:cd14187   237 LIQKMLQTDPTARPTINELLNDEFF 261
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
56-268 1.01e-06

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: 50.26  E-value: 1.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  56 VNLARYKPTGEYVTVRRI-NLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTH- 133
Cdd:cd05610    20 VYLGRKKNNSKLYAVKVVkKADMINKNMVHQVQAERDALALSKSPFIVHLYYSLQSANNVYLVMEYLIGGDVKSLLHIYg 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 134 FMDgmNELAIAYILQGVLkALDYIHHMGYVHRSVKASHILISVDGKVYLSG-------LRSNLSM---ISHGQRQRVVHD 203
Cdd:cd05610   100 YFD--EEMAVKYISEVAL-ALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDfglskvtLNRELNMmdiLTTPSMAKPKND 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 204 FPKYSVKVLP------------------------------------WLSPEVLQQnlQGYDAKSDIYSVGITACELANGH 247
Cdd:cd05610   177 YSRTPGQVLSlisslgfntptpyrtpksvrrgaarvegerilgtpdYLAPELLLG--KPHGPAVDWWALGVCLFEFLTGI 254
                         250       260
                  ....*....|....*....|.
gi 1394533236 248 VPFKDMPATQMLLEKLNGTVP 268
Cdd:cd05610   255 PPFNDETPQQVFQNILNRDIP 275
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
40-244 1.17e-06

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: 50.00  E-value: 1.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGFEDLmtVNLARYKPTGEYVTVRRINleacSNEMVTFLQGELHVSKL---FNHPNIVPYRATFIAD----- 111
Cdd:cd07849     7 YQNLSYIGEGAYGM--VCSAVHKPTGQKVAIKKIS----PFEHQTYCLRTLREIKIllrFKHENIIGILDIQRPPtfesf 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 112 NELWVVTSFMAYGSAKDLICTHFMDGMnelaIAYILQGVLKALDYIHHMGYVHRSVKASHILI--SVDGKVYLSGL-RSN 188
Cdd:cd07849    81 KDVYIVQELMETDLYKLIKTQHLSNDH----IQYFLYQILRGLKYIHSANVLHRDLKPSNLLLntNCDLKICDFGLaRIA 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1394533236 189 LSMISHGQrqrvvhdFPKYSVKVLPWLSPEVLqQNLQGYDAKSDIYSVGitaCELA 244
Cdd:cd07849   157 DPEHDHTG-------FLTEYVATRWYRAPEIM-LNSKGYTKAIDIWSVG---CILA 201
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
61-250 1.53e-06

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: 49.34  E-value: 1.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  61 YKPTGE------YVTVRR-INLEACSNEMVTFLQGELHV--SKLF----------NHPNIVPYRATFIADNELWVVTSFM 121
Cdd:cd14090     3 YKLTGEllgegaYASVQTcINLYTGKEYAVKIIEKHPGHsrSRVFrevetlhqcqGHPNILQLIEYFEDDERFYLVFEKM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 122 AYGSAKDLI--CTHFmdgmNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVY---------LSGLRSNls 190
Cdd:cd14090    83 RGGPLLSHIekRVHF----TEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKVSpvkicdfdlGSGIKLS-- 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1394533236 191 mishGQRQRVVHDfPKYSVKV--LPWLSPEVLQ----QNLQgYDAKSDIYSVGITACELANGHVPF 250
Cdd:cd14090   157 ----STSMTPVTT-PELLTPVgsAEYMAPEVVDafvgEALS-YDKRCDLWSLGVILYIMLCGYPPF 216
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
40-349 2.08e-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: 49.11  E-value: 2.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGFEDLmtVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNE-LWVVT 118
Cdd:cd07856    12 YSDLQPVGMGAFGL--VCSARDQLTGQNVAVKKIMKPFSTPVLAKRTYRELKLLKHLRHENIISLSDIFISPLEdIYFVT 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 119 SFMAygsaKDLICTHFMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILI--SVDGKVYLSGlrsnLSMISHGQ 196
Cdd:cd07856    90 ELLG----TDLHRLLTSRPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVneNCDLKICDFG----LARIQDPQ 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 197 RQRVVHDfpKYsvkvlpWLSPEVLqQNLQGYDAKSDIYSVGITACELANGH--VPFKDMPATQMLLEKLNGTVPCLLdTS 274
Cdd:cd07856   162 MTGYVST--RY------YRAPEIM-LTWQKYDVEVDIWSAGCIFAEMLEGKplFPGKDHVNQFSIITELLGTPPDDV-IN 231
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1394533236 275 TIPAEeltmspsrsvansglsDSLTTSTPRPSNGDSPSHPYHRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSF 349
Cdd:cd07856   232 TICSE----------------NTLRFVQSLPKRERVPFSEKFKNADPDAIDLLEKMLVFDPKKRISAAEALAHPY 290
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
89-252 2.24e-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: 48.79  E-value: 2.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  89 ELHVSKLFNHPNIVPYRATF--IADNELWVVTSFMAYGSAKDLICTH-FMDgmnELAIAYiLQGVLKALDYIHHMGYVHR 165
Cdd:cd14200    73 EIAILKKLDHVNIVKLIEVLddPAEDNLYMVFDLLRKGPVMEVPSDKpFSE---DQARLY-FRDIVLGIEYLHYQKIVHR 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 166 SVKASHILISVDGKVYLSGLR-SNlsmishgqrQRVVHDFPKYSVKVLP-WLSPEVLQQNLQGYDAKS-DIYSVGITACE 242
Cdd:cd14200   149 DIKPSNLLLGDDGHVKIADFGvSN---------QFEGNDALLSSTAGTPaFMAPETLSDSGQSFSGKAlDVWAMGVTLYC 219
                         170
                  ....*....|
gi 1394533236 243 LANGHVPFKD 252
Cdd:cd14200   220 FVYGKCPFID 229
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
40-274 2.27e-06

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: 48.45  E-value: 2.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVT-FLQGELHVSKLFNHPNIVP-YRATFIADNELWVV 117
Cdd:cd14163     2 YQLGKTIGEG--TYSKVKEAFSKKHQRKVAIKIIDKSGGPEEFIQrFLPRELQIVERLDHKNIIHvYEMLESADGKIYLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 118 TSFMAYGSAKDliCTHFMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILisvdgkvyLSGLRSNLSMISHGQR 197
Cdd:cd14163    80 MELAEDGDVFD--CVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENAL--------LQGFTLKLTDFGFAKQ 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1394533236 198 QRVVH-DFPKYSVKVLPWLSPEVLQqNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNG-TVPCLLDTS 274
Cdd:cd14163   150 LPKGGrELSQTFCGSTAYAAPEVLQ-GVPHDSRKGDIWSMGVVLYVMLCAQLPFDDTDIPKMLCQQQKGvSLPGHLGVS 227
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
45-257 2.29e-06

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: 48.78  E-value: 2.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  45 VIGKG-FEDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADN-----ELWVVT 118
Cdd:cd14204    14 VLGEGeFGSVMEGELQQPDGTNHKVAVKTMKLDNFSQREIEEFLSEAACMKDFNHPNVIRLLGVCLEVGsqripKPMVIL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 119 SFMAYGSakdlICTHFMDGMNELAIAYI-LQGVLK-------ALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSN 188
Cdd:cd14204    94 PFMKYGD----LHSFLLRSRLGSGPQHVpLQTLLKfmidialGMEYLSSRNFLHRDLAARNCMLRDDMTVCVAdfGLSKK 169
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 189 LSMISHGQRQRVVhdfpKYSVKvlpWLSPEVLQQNLqgYDAKSDIYSVGITACELAN-GHVPFkdmPATQ 257
Cdd:cd14204   170 IYSGDYYRQGRIA----KMPVK---WIAVESLADRV--YTVKSDVWAFGVTMWEIATrGMTPY---PGVQ 227
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
98-250 2.55e-06

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: 48.87  E-value: 2.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  98 HPNIVPYRATFIADNELWVVTSFMAYGSAKDLIctHFMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVD 177
Cdd:cd14173    59 HRNVLELIEFFEEEDKFYLVFEKMRGGSILSHI--HRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHP 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 178 GKVYL---------SG--LRSNLSMISHGQRQRvvhdfPKYSVKvlpWLSPEVLQ---QNLQGYDAKSDIYSVGITACEL 243
Cdd:cd14173   137 NQVSPvkicdfdlgSGikLNSDCSPISTPELLT-----PCGSAE---YMAPEVVEafnEEASIYDKRCDLWSLGVILYIM 208

                  ....*..
gi 1394533236 244 ANGHVPF 250
Cdd:cd14173   209 LSGYPPF 215
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
46-244 2.63e-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: 48.63  E-value: 2.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  46 IGKGfeDLMTVNLARYKptGEYVTVRrINLEACsnEMVTFLQGELHVSKLFNHPNIVPYRATFIADN----ELWVVTSFM 121
Cdd:cd14144     3 VGKG--RYGEVWKGKWR--GEKVAVK-IFFTTE--EASWFRETEIYQTVLMRHENILGFIAADIKGTgswtQLYLITDYH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 122 AYGSAKDLICTHFMDGMNELAIAYILQGVLKAL-DYIHHM----GYVHRSVKASHILISVDGKVYLSGLRSNLSMISHGQ 196
Cdd:cd14144    76 ENGSLYDFLRGNTLDTQSMLKLAYSAACGLAHLhTEIFGTqgkpAIAHRDIKSKNILVKKNGTCCIADLGLAVKFISETN 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1394533236 197 rqrVVHDFPKYSVKVLPWLSPEVLQQNL--QGYDA--KSDIYSVGITACELA 244
Cdd:cd14144   156 ---EVDLPPNTRVGTKRYMAPEVLDESLnrNHFDAykMADMYSFGLVLWEIA 204
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
89-350 3.01e-06

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: 48.46  E-value: 3.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  89 ELHVSKLFNHPNIV----PYRATFIADNELWVVTSFMAYGSAKDLIcTHFMDGMNELAIAYILQgVLKALDYIHHMG--Y 162
Cdd:cd14033    50 EVEMLKGLQHPNIVrfydSWKSTVRGHKCIILVTELMTSGTLKTYL-KRFREMKLKLLQRWSRQ-ILKGLHFLHSRCppI 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 163 VHRSVKASHILIS-VDGKVYLSGLrsNLSMISHGQRQRVVHDFPKYsvkvlpwLSPEVLQQNlqgYDAKSDIYSVGITAC 241
Cdd:cd14033   128 LHRDLKCDNIFITgPTGSVKIGDL--GLATLKRASFAKSVIGTPEF-------MAPEMYEEK---YDEAVDVYAFGMCIL 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 242 ELANGHVPFKDMPATQMLLEKLngtvpclldtstipaeeltmspsrsvansglsdsltTSTPRPSNgdspshpYHRTFSP 321
Cdd:cd14033   196 EMATSEYPYSECQNAAQIYRKV------------------------------------TSGIKPDS-------FYKVKVP 232
                         250       260
                  ....*....|....*....|....*....
gi 1394533236 322 HFHHFVEQCLQRNPDARPSASTLLNHSFF 350
Cdd:cd14033   233 ELKEIIEGCIRTDKDERFTIQDLLEHRFF 261
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
40-250 3.01e-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: 48.55  E-value: 3.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLE-ACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVT 118
Cdd:cd14209     3 FDRIKTLGTG--SFGRVMLVRHKETGNYYAMKILDKQkVVKLKQVEHTLNEKRILQAINFPFLVKLEYSFKDNSNLYMVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 119 SFMAYGsakDLICTHFMDGM--NELAIAYILQGVLkALDYIHHMGYVHRSVKASHILIsvDGKVYLSglrsnlsmishgq 196
Cdd:cd14209    81 EYVPGG---EMFSHLRRIGRfsEPHARFYAAQIVL-AFEYLHSLDLIYRDLKPENLLI--DQQGYIK------------- 141
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 197 rqrvVHDF----------------PKYsvkvlpwLSPEVLQqnLQGYDAKSDIYSVGITACELANGHVPF 250
Cdd:cd14209   142 ----VTDFgfakrvkgrtwtlcgtPEY-------LAPEIIL--SKGYNKAVDWWALGVLIYEMAAGYPPF 198
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
134-250 3.02e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 49.07  E-value: 3.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 134 FMDGMNELA---IAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMISHgqrqrvvhdfpKYSVK 210
Cdd:PHA03207  175 YVDRSGPLPleqAITIQRRLLEALAYLHGRGIIHRDVKTENIFLDEPENAVLGDFGAACKLDAH-----------PDTPQ 243
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1394533236 211 VLPWL------SPEVLQqnLQGYDAKSDIYSVGITACELANGHVPF 250
Cdd:PHA03207  244 CYGWSgtletnSPELLA--LDPYCAKTDIWSAGLVLFEMSVKNVTL 287
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
150-353 3.30e-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: 3.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 150 VLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNLSmishgqrqrvvHDFPKYSVKVLPWLSPEVLQQNlQGY 227
Cdd:cd05606   107 VILGLEHMHNRFIVYRDLKPANILLDEHGHVRISdlGLACDFS-----------KKKPHASVGTHGYMAPEVLQKG-VAY 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 228 DAKSDIYSVGITACELANGHVPFKDMPATqmlleklngtvpcllDTSTIPAEELTMSPsrsvansglsdslttstprpsn 307
Cdd:cd05606   175 DSSADWFSLGCMLYKLLKGHSPFRQHKTK---------------DKHEIDRMTLTMNV---------------------- 217
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1394533236 308 gDSPShpyhrTFSPHFHHFVEQCLQRNPDAR-----PSASTLLNHSFFKQI 353
Cdd:cd05606   218 -ELPD-----SFSPELKSLLEGLLQRDVSKRlgclgRGATEVKEHPFFKGV 262
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
68-261 3.50e-06

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK4 plays a critical role in NFkB activation by its interaction with MyD88, which acts as a scaffold that enables IRAK4 to phosphorylate and activate IRAK1 and/or IRAK2. It also plays an important role in type I IFN production induced by TLR7/8/9. The IRAK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 48.26  E-value: 3.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  68 VTVRRIN--LEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKD-LICTHFMDGMNELAIA 144
Cdd:cd14158    41 VAVKKLAamVDISTEDLTKQFEQEIQVMAKCQHENLVELLGYSCDGPQLCLVYTYMPNGSLLDrLACLNDTPPLSWHMRC 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 145 YILQGVLKALDYIHHMGYVHRSVKASHILISvDG---KVYLSGL-RSNLSMISHGQRQRVvhdfpkysVKVLPWLSPEVL 220
Cdd:cd14158   121 KIAQGTANGINYLHENNHIHRDIKSANILLD-ETfvpKISDFGLaRASEKFSQTIMTERI--------VGTTAYMAPEAL 191
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1394533236 221 QQNLQgydAKSDIYSVGITACELANGHVPFKDMPATQMLLE 261
Cdd:cd14158   192 RGEIT---PKSDIFSFGVVLLEIITGLPPVDENRDPQLLLD 229
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
91-315 3.73e-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: 48.09  E-value: 3.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  91 HVSKLfNHPNIVPYRATFI-ADNELWVVTSFMAYGSAKDLICTHFMD---------GMNELAIAYILQGVLKALDYIH-- 158
Cdd:cd14011    55 QLTRL-RHPRILTVQHPLEeSRESLAFATEPVFASLANVLGERDNMPspppelqdyKLYDVEIKYGLLQISEALSFLHnd 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 159 -HMgyVHRSVKASHILISVDGKVYLSGL--------RSNLSMISHGQRQRVvHDFPKYSvkvLPWLSPEVLQQNlqGYDA 229
Cdd:cd14011   134 vKL--VHGNICPESVVINSNGEWKLAGFdfcisseqATDQFPYFREYDPNL-PPLAQPN---LNYLAPEYILSK--TCDP 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 230 KSDIYSVGITACELANGHVPFKDMPATQMLLEKLngtvPCLLDTSTIPAEELTMSPSRSVANSGLSdslTTSTPRPSNGD 309
Cdd:cd14011   206 ASDMFSLGVLIYAIYNKGKPLFDCVNNLLSYKKN----SNQLRQLSLSLLEKVPEELRDHVKTLLN---VTPEVRPDAEQ 278

                  ....*.
gi 1394533236 310 SPSHPY 315
Cdd:cd14011   279 LSKIPF 284
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
85-262 3.82e-06

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: 47.80  E-value: 3.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  85 FLQgELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTHFMDGMNELAIAYILQGVLKALDYIHHMGYVH 164
Cdd:cd05052    49 FLK-EAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMPYGNLLDYLRECNREELNAVVLLYMATQIASAMEYLEKKNFIH 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 165 RSVKASHILISVDG--KVYLSGLRSNLSmishgQRQRVVHDFPKYSVKvlpWLSPEVLQQNLqgYDAKSDIYSVGITACE 242
Cdd:cd05052   128 RDLAARNCLVGENHlvKVADFGLSRLMT-----GDTYTAHAGAKFPIK---WTAPESLAYNK--FSIKSDVWAFGVLLWE 197
                         170       180
                  ....*....|....*....|...
gi 1394533236 243 LAN-GHVPFKDMPATQM--LLEK 262
Cdd:cd05052   198 IATyGMSPYPGIDLSQVyeLLEK 220
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
65-350 3.87e-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: 48.03  E-value: 3.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  65 GEYVTVRRINLEAcsNEMVTFLQ-GELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLIctHFMDGMNELAI 143
Cdd:cd07870    25 GQLVALKVISMKT--EEGVPFTAiREASLLKGLKHANIVLLHDIIHTKETLTFVFEYMHTDLAQYMI--QHPGGLHPYNV 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 144 AYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNLSMISHgqrqrvvhdfpKYSVKVLP-WLSPEVL 220
Cdd:cd07870   101 RLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLAdfGLARAKSIPSQ-----------TYSSEVVTlWYRPPDV 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 221 QQNLQGYDAKSDIYSVGITACELANGHVPFkdmPATQMLLEKLNGTVPCLldtsTIPAEELTmspsrsvanSGLSDsLTT 300
Cdd:cd07870   170 LLGATDYSSALDIWGAGCIFIEMLQGQPAF---PGVSDVFEQLEKIWTVL----GVPTEDTW---------PGVSK-LPN 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1394533236 301 STP---RPSNGDSPSHPYHR-TFSPHFHHFVEQCLQRNPDARPSASTLLNHSFF 350
Cdd:cd07870   233 YKPewfLPCKPQQLRVVWKRlSRPPKAEDLASQMLMMFPKDRISAQDALLHPYF 286
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
99-251 4.00e-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: 48.12  E-value: 4.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  99 PNIVPYRATFIADNELWVVTSFMAYGSAKDLICTHFMdgMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDG 178
Cdd:cd14223    63 PFIVCMSYAFHTPDKLSFILDLMNGGDLHYHLSQHGV--FSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFG 140
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1394533236 179 KVYLSglrsNLSMISHGQRQRvvhdfPKYSVKVLPWLSPEVLQQNLqGYDAKSDIYSVGITACELANGHVPFK 251
Cdd:cd14223   141 HVRIS----DLGLACDFSKKK-----PHASVGTHGYMAPEVLQKGV-AYDSSADWFSLGCMLFKLLRGHSPFR 203
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
40-250 4.06e-06

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: 47.96  E-value: 4.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVtfLQGELHVSKLFNHPNIVPYRATFIADNELWVVTS 119
Cdd:cd14114     4 YDILEELGTG--AFGVVHRCTERATGNNFAAKFIMTPHESDKET--VRKEIQIMNQLHHPKLINLHDAFEDDNEMVLILE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 120 FMAYGSAKDLICTHFMDGMNELAIAYILQgVLKALDYIHHMGYVHRSVKASHILISVDGKvylsglrSNLSMISHGQRQR 199
Cdd:cd14114    80 FLSGGELFERIAAEHYKMSEAEVINYMRQ-VCEGLCHMHENNIVHLDIKPENIMCTTKRS-------NEVKLIDFGLATH 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1394533236 200 VVhdfPKYSVKVLP----WLSPEVLQQNLQGYdaKSDIYSVGITACELANGHVPF 250
Cdd:cd14114   152 LD---PKESVKVTTgtaeFAAPEIVEREPVGF--YTDMWAVGVLSYVLLSGLSPF 201
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
143-244 4.40e-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: 47.92  E-value: 4.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 143 IAYILQGVLKALDYIHHMGYVHRSVKASHILIsvDGKvylsglRSNLSMISHGqrqrvVHDF----PKYSVKV--LPWLS 216
Cdd:cd14132   114 IRYYMYELLKALDYCHSKGIMHRDVKPHNIMI--DHE------KRKLRLIDWG-----LAEFyhpgQEYNVRVasRYYKG 180
                          90       100
                  ....*....|....*....|....*...
gi 1394533236 217 PEVLqQNLQGYDAKSDIYSVGitaCELA 244
Cdd:cd14132   181 PELL-VDYQYYDYSLDMWSLG---CMLA 204
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
110-315 4.55e-06

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: 48.47  E-value: 4.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 110 ADNElWVVTSFMAYGSAKDL-ICTHFMDGMN-------------ELAIAYILQGVLkALDYIHHMGYVHRSVKASHILIS 175
Cdd:cd05626    58 ADNE-WVVKLYYSFQDKDNLyFVMDYIPGGDmmsllirmevfpeVLARFYIAELTL-AIESVHKMGFIHRDIKPDNILID 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 176 VDGKVYL-------------------------------SGLRSNLSMISHGQRQRVVHDFPK--------YSVKVLP-WL 215
Cdd:cd05626   136 LDGHIKLtdfglctgfrwthnskyyqkgshirqdsmepSDLWDDVSNCRCGDRLKTLEQRATkqhqrclaHSLVGTPnYI 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 216 SPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTvpcllDTSTIPAeELTMSPSRSVANSGLS 295
Cdd:cd05626   216 APEVLLR--KGYTQLCDWWSVGVILFEMLVGQPPFLAPTPTETQLKVINWE-----NTLHIPP-QVKLSPEAVDLITKLC 287
                         250       260
                  ....*....|....*....|
gi 1394533236 296 DSLTTSTPRPSNGDSPSHPY 315
Cdd:cd05626   288 CSAEERLGRNGADDIKAHPF 307
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
40-261 4.97e-06

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: 47.73  E-value: 4.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGFEDlmTVNLARYKPTGEYVTVRRINL--EACSNEMVTFLQGELH-----VSKLFNHPNIVPYRATFIADN 112
Cdd:cd14093     5 YEPKEILGRGVSS--TVRRCIEKETGQEFAVKIIDItgEKSSENEAEELREATRreieiLRQVSGHPNIIELHDVFESPT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 113 ELWVVTSFMAYGSAKDLICTHFMdgMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNLs 190
Cdd:cd14093    83 FIFLVFELCRKGELFDYLTEVVT--LSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISdfGFATRL- 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1394533236 191 miSHGQRQRVVHDFPKYsvkvlpwLSPEVLQ----QNLQGYDAKSDIYSVGITACELANGHVPF---KDMPATQMLLE 261
Cdd:cd14093   160 --DEGEKLRELCGTPGY-------LAPEVLKcsmyDNAPGYGKEVDMWACGVIMYTLLAGCPPFwhrKQMVMLRNIME 228
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
59-245 5.23e-06

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: 47.80  E-value: 5.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  59 ARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICT---HFM 135
Cdd:cd07861    19 GRNKKTGQIVAMKKIRLESEEEGVPSTAIREISLLKELQHPNIVCLEDVLMQENRLYLVFEFLSMDLKKYLDSLpkgKYM 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 136 DGMneLAIAYILQgVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSnlsmiSHGQRQRVVhdfpKYSVKVLP 213
Cdd:cd07861    99 DAE--LVKSYLYQ-ILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLAdfGLAR-----AFGIPVRVY----THEVVTLW 166
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1394533236 214 WLSPEVLQQNlQGYDAKSDIYSVGITACELAN 245
Cdd:cd07861   167 YRAPEVLLGS-PRYSTPVDIWSIGTIFAEMAT 197
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
98-251 5.50e-06

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: 47.94  E-value: 5.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  98 HPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTHFMdgMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVD 177
Cdd:cd14180    60 HPNIVALHEVLHDQYHTYLVMELLRGGELLDRIKKKAR--FSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADE 137
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1394533236 178 GKvylsglRSNLSMISHG-QRQRVVHDFPKYS-VKVLPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFK 251
Cdd:cd14180   138 SD------GAVLKVIDFGfARLRPQGSRPLQTpCFTLQYAAPELFSN--QGYDESCDLWSLGVILYTMLSGQVPFQ 205
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
142-370 5.51e-06

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: 47.57  E-value: 5.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 142 AIAYILQgVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMISHGQRQRVVHDFPKYsvkvlpwLSPEVLQ 221
Cdd:cd05608   107 ACFYTAQ-IISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAVELKDGQTKTKGYAGTPGF-------MAPELLL 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 222 QnlQGYDAKSDIYSVGITACELANGHVPFKDMPatqmllEKLNgtvpclldtstipaeeltmspSRSVANSGLSDSLTts 301
Cdd:cd05608   179 G--EEYDYSVDYFTLGVTLYEMIAARGPFRARG------EKVE---------------------NKELKQRILNDSVT-- 227
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1394533236 302 tprpsngdspshpYHRTFSPHFHHFVEQCLQRNPDAR-----PSASTLLNHSFFKQIKRRASEALPeLLRPVTP 370
Cdd:cd05608   228 -------------YSEKFSPASKSICEALLAKDPEKRlgfrdGNCDGLRTHPFFRDINWRKLEAGI-LPPPFVP 287
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
40-253 6.17e-06

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: 47.38  E-value: 6.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGFEDLmtVNLARYKPTGEYVTVRRINLE-ACSNEMVT-----FLQGELHVS---KLFNHPNIVPYRATFIA 110
Cdd:cd14004     2 YTILKEMGEGAYGQ--VNLAIYKSKGKEVVIKFIFKErILVDTWVRdrklgTVPLEIHILdtlNKRSHPNIVKLLDFFED 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 111 DNELWVVTSfmAYGSAKDLI-CTHFMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNl 189
Cdd:cd14004    80 DEFYYLVME--KHGSGMDLFdFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFGSA- 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1394533236 190 SMISHGqrqrvvhdfpKYSVKV--LPWLSPEVLQQNLqgYDAKS-DIYSVGITACELANGHVPFKDM 253
Cdd:cd14004   157 AYIKSG----------PFDTFVgtIDYAAPEVLRGNP--YGGKEqDIWALGVLLYTLVFKENPFYNI 211
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
40-263 6.27e-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: 47.51  E-value: 6.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGFEDLmtVNLARYKPTGEYVTVRRINLEACSNemvtFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTS 119
Cdd:cd14085     5 FEIESELGRGATSV--VYRCRQKGTQKPYAVKKLKKTVDKK----IVRTEIGVLLRLSHPNIIKLKEIFETPTEISLVLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 120 FMAYGSAKDLICTHFMdgMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKvylsglRSNLSMISHGQRQR 199
Cdd:cd14085    79 LVTGGELFDRIVEKGY--YSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAP------DAPLKIADFGLSKI 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1394533236 200 VVHDFPKYSVKVLP-WLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKL 263
Cdd:cd14085   151 VDQQVTMKTVCGTPgYCAPEILRG--CAYGPEVDMWSVGVITYILLCGFEPFYDERGDQYMFKRI 213
STKc_IRAK2 cd14157
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; ...
61-246 6.47e-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: 47.52  E-value: 6.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  61 YKPTGEYVtVRRINLEACS--NEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKD-LICTHFMDG 137
Cdd:cd14157    13 YRHGKQYV-IKRLKETECEspKSTERFFQTEVQICFRCCHPNILPLLGFCVESDCHCLIYPYMPNGSLQDrLQQQGGSHP 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 138 MNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVD--GKVYLSGLRsnlsmiSHGQRQRVVHDFPKYSV--KVLP 213
Cdd:cd14157    92 LPWEQRLSISLGLLKAVQHLHNFGILHGNIKSSNVLLDGNllPKLGHSGLR------LCPVDKKSVYTMMKTKVlqISLA 165
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1394533236 214 WLsPEVLQQNLQgYDAKSDIYSVGITACELANG 246
Cdd:cd14157   166 YL-PEDFVRHGQ-LTEKVDIFSCGVVLAEILTG 196
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
85-259 6.63e-06

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: 47.40  E-value: 6.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  85 FLQgELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGS--------AKDLICTHFMDGMNELAiayilqgvlKALDY 156
Cdd:cd05068    50 FLR-EAQIMKKLRHPKLIQLYAVCTLEEPIYIITELMKHGSlleylqgkGRSLQLPQLIDMAAQVA---------SGMAY 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 157 IHHMGYVHRSVKASHILISVDG--KVYLSGLrSNLSMISHGQRQRVVHDFPkysvkvLPWLSPEVLqqNLQGYDAKSDIY 234
Cdd:cd05068   120 LESQNYIHRDLAARNVLVGENNicKVADFGL-ARVIKVEDEYEAREGAKFP------IKWTAPEAA--NYNRFSIKSDVW 190
                         170       180
                  ....*....|....*....|....*.
gi 1394533236 235 SVGITACELAN-GHVPFKDMPATQML 259
Cdd:cd05068   191 SFGILLTEIVTyGRIPYPGMTNAEVL 216
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
40-350 7.05e-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: 47.33  E-value: 7.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLAR-YKPTGEYVTVRRINLEACSNEMVTFLQGELHVSK---LFNHPNIVP-YRATFIADNEL 114
Cdd:cd07862     3 YECVAEIGEG--AYGKVFKARdLKNGGRFVALKRVRVQTGEEGMPLSTIREVAVLRhleTFEHPNVVRlFDVCTVSRTDR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 115 WVVTSFMAYGSAKDLicTHFMD-----GMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLrsNL 189
Cdd:cd07862    81 ETKLTLVFEHVDQDL--TTYLDkvpepGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADF--GL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 190 SMISHGQrqrvvhdFPKYSVKVLPWL-SPEVLQQNlqGYDAKSDIYSVGITACELanghvpFKDMPatqmlLEKLNGTVP 268
Cdd:cd07862   157 ARIYSFQ-------MALTSVVVTLWYrAPEVLLQS--SYATPVDLWSVGCIFAEM------FRRKP-----LFRGSSDVD 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 269 CL---LDTSTIPAEEltmSPSRSVAnsglsdslttsTPRPSNGDSPSHPYHRtFSPHFHH----FVEQCLQRNPDARPSA 341
Cdd:cd07862   217 QLgkiLDVIGLPGEE---DWPRDVA-----------LPRQAFHSKSAQPIEK-FVTDIDElgkdLLLKCLTFNPAKRISA 281

                  ....*....
gi 1394533236 342 STLLNHSFF 350
Cdd:cd07862   282 YSALSHPYF 290
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
55-363 7.24e-06

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: 47.29  E-value: 7.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  55 TVNLARYKPTGEYVTVRRINLEACSNEMVTFLQgELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAygsaKDLicTHF 134
Cdd:cd07872    21 TVFKGRSKLTENLVALKEIRLEHEEGAPCTAIR-EVSLLKDLKHANIVTLHDIVHTDKSLTLVFEYLD----KDL--KQY 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 135 MDG----MNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNLSMISHGQRQRVVhdfpkys 208
Cdd:cd07872    94 MDDcgniMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLAdfGLARAKSVPTKTYSNEVV------- 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 209 vkVLPWLSPEVLQQNLQgYDAKSDIYSVGITACELANGH--VPFKDMPATQMLLEKLNGTvpclldtstiPAEEltMSPS 286
Cdd:cd07872   167 --TLWYRPPDVLLGSSE-YSTQIDMWGVGCIFFEMASGRplFPGSTVEDELHLIFRLLGT----------PTEE--TWPG 231
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1394533236 287 RSVANSGLSDSLTTSTPRPSNGDSPShpyhrtFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQIKRRAsEALPE 363
Cdd:cd07872   232 ISSNDEFKNYNFPKYKPQPLINHAPR------LDTEGIELLTKFLQYESKKRISAEEAMKHAYFRSLGTRI-HSLPE 301
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
55-352 7.77e-06

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 47.45  E-value: 7.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  55 TVNLARYKPTGEYVTVRRINLEACSNEMVTFLQG------------ELHVSKLFNHPNIVPYRATFIADNELWVVTSFMA 122
Cdd:PTZ00024   24 KVEKAYDTLTGKIVAIKKVKIIEISNDVTKDRQLvgmcgihfttlrELKIMNEIKHENIMGLVDVYVEGDFINLVMDIMA 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 123 YGSAKdlicthFMDGMNELAIAY---ILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRS---------N 188
Cdd:PTZ00024  104 SDLKK------VVDRKIRLTESQvkcILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIAdfGLARrygyppysdT 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 189 LSMISHGQRQRvvhdfpKYSVKV--LPWLSPEVLqQNLQGYDAKSDIYSVGITACELANGHVPFkdmPATQMlLEKLnGT 266
Cdd:PTZ00024  178 LSKDETMQRRE------EMTSKVvtLWYRAPELL-MGAEKYHFAVDMWSVGCIFAELLTGKPLF---PGENE-IDQL-GR 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 267 VPCLLDTstiPAEeltmspsrsvANSGLSDSLTTSTPRpsngdSPSHPyhRTFSPHFHHFVEQC-------LQRNPDARP 339
Cdd:PTZ00024  246 IFELLGT---PNE----------DNWPQAKKLPLYTEF-----TPRKP--KDLKTIFPNASDDAidllqslLKLNPLERI 305
                         330
                  ....*....|...
gi 1394533236 340 SASTLLNHSFFKQ 352
Cdd:PTZ00024  306 SAKEALKHEYFKS 318
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
40-250 9.29e-06

Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group contains fungal kinases including Schizosaccharomyces pombe Sid2p and Saccharomyces cerevisiae Dbf2p. Group members show similarity to NDR kinases in that they contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Sid2p plays a crucial role in the septum initiation network (SIN) and in the initiation of cytokinesis. Dbf2p is important in regulating the mitotic exit network (MEN) and in cytokinesis. The Sid2p-like group is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270751 [Multi-domain]  Cd Length: 386  Bit Score: 47.33  E-value: 9.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRIN---LEAcSNEMVTFLQgELHVSKLFNHPNIVPYRATFIADNELWV 116
Cdd:cd05600    13 FQILTQVGQG--GYGSVFLARKKDTGEICALKIMKkkvLFK-LNEVNHVLT-ERDILTTTNSPWLVKLLYAFQDPENVYL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 117 VTSFMAYGSAKDLICTHfmdGM--NELAIAYILQgVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRS----- 187
Cdd:cd05600    89 AMEYVPGGDFRTLLNNS---GIlsEEHARFYIAE-MFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTdfGLASgtlsp 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 188 --NLSM--------------ISHGQRQRVVHDFPKY------SVKVLP-WLSPEVLqqNLQGYDAKSDIYSVGITACELA 244
Cdd:cd05600   165 kkIESMkirleevkntafleLTAKERRNIYRAMRKEdqnyanSVVGSPdYMAPEVL--RGEGYDLTVDYWSLGCILFECL 242

                  ....*.
gi 1394533236 245 NGHVPF 250
Cdd:cd05600   243 VGFPPF 248
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
45-251 1.08e-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: 46.82  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  45 VIGKG-FEDLMtvnLARYKPTGEYVTVRRINLEAC-SNEMVTFLQGELHVSKL-FNHPNIVPYRATFIADNELWVVTSFM 121
Cdd:cd05590     2 VLGKGsFGKVM---LARLKESGRLYAVKVLKKDVIlQDDDVECTMTEKRILSLaRNHPFLTQLYCCFQTPDRLFFVMEFV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 122 AYGsakDLI-----CTHFmdgmNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMISHGQ 196
Cdd:cd05590    79 NGG---DLMfhiqkSRRF----DEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGIFNGK 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1394533236 197 RQRVVHDFPKYsvkvlpwLSPEVLQQNLQGYDAksDIYSVGITACELANGHVPFK 251
Cdd:cd05590   152 TTSTFCGTPDY-------IAPEILQEMLYGPSV--DWWAMGVLLYEMLCGHAPFE 197
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
45-263 1.79e-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: 46.19  E-value: 1.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  45 VIGKGfeDLMTVNLARYKPTGEYVT--VRRINLEACSNEMVTFlQGELHV-SKLFNHPNIVPYRATFIADNELWVVTSFM 121
Cdd:cd05047     2 VIGEG--NFGQVLKARIKKDGLRMDaaIKRMKEYASKDDHRDF-AGELEVlCKLGHHPNIINLLGACEHRGYLYLAIEYA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 122 AYGSAKDLI-CTHFMDGMNELAIAY----------ILQ---GVLKALDYIHHMGYVHRSVKASHILIsvdGKVYLSGLRS 187
Cdd:cd05047    79 PHGNLLDFLrKSRVLETDPAFAIANstastlssqqLLHfaaDVARGMDYLSQKQFIHRDLAARNILV---GENYVAKIAD 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1394533236 188 nlSMISHGQRQRVVHDFPKYSVKvlpWLSPEVLqqNLQGYDAKSDIYSVGITACELAN-GHVPFKDMPATQmLLEKL 263
Cdd:cd05047   156 --FGLSRGQEVYVKKTMGRLPVR---WMAIESL--NYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAE-LYEKL 224
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
40-251 2.02e-05

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: 45.72  E-value: 2.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVR---RINLEACSNEMVtfLQGELHVSKLFNHPNIVPYRATFIADNELWV 116
Cdd:cd14116     7 FEIGRPLGKG--KFGNVYLAREKQSKFILALKvlfKAQLEKAGVEHQ--LRREVEIQSHLRHPNILRLYGYFHDATRVYL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 117 VTSFMAYGSA-KDLI-CTHFMDgmnELAIAYILQgVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLrsNLSMISH 194
Cdd:cd14116    83 ILEYAPLGTVyRELQkLSKFDE---QRTATYITE-LANALSYCHSKRVIHRDIKPENLLLGSAGELKIADF--GWSVHAP 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1394533236 195 GQRQRVVhdfpkysVKVLPWLSPEVLQQNLqgYDAKSDIYSVGITACELANGHVPFK 251
Cdd:cd14116   157 SSRRTTL-------CGTLDYLPPEMIEGRM--HDEKVDLWSLGVLCYEFLVGKPPFE 204
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
40-251 2.16e-05

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: 45.63  E-value: 2.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTF-LQGELHVSKLFNHPNIVPYRATFIADNELWVVT 118
Cdd:cd14117     8 FDIGRPLGKG--KFGNVYLAREKQSKFIVALKVLFKSQIEKEGVEHqLRREIEIQSHLRHPNILRLYNYFHDRKRIYLIL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 119 SFMAYGSAKDLICTHfmDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLrsNLSMISHGQRQ 198
Cdd:cd14117    86 EYAPRGELYKELQKH--GRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADF--GWSVHAPSLRR 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1394533236 199 RVVhdfpkysVKVLPWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFK 251
Cdd:cd14117   162 RTM-------CGTLDYLPPEMIEG--RTHDEKVDLWCIGVLCYELLVGMPPFE 205
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
99-251 2.18e-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: 46.21  E-value: 2.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  99 PNIVPYRATFIADNELWVVTSFMAYGSAKDLICTHFMdgMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDG 178
Cdd:cd05633    68 PFIVCMTYAFHTPDKLCFILDLMNGGDLHYHLSQHGV--FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHG 145
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1394533236 179 KVYLSglrsNLSMISHGQRQRvvhdfPKYSVKVLPWLSPEVLQQNlQGYDAKSDIYSVGITACELANGHVPFK 251
Cdd:cd05633   146 HVRIS----DLGLACDFSKKK-----PHASVGTHGYMAPEVLQKG-TAYDSSADWFSLGCMLFKLLRGHSPFR 208
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
40-250 2.21e-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: 45.77  E-value: 2.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQgELHVSKLFNHPNIVPYRATFIADNELWVVTS 119
Cdd:cd07871     7 YVKLDKLGEG--TYATVFKGRSKLTENLVALKEIRLEHEEGAPCTAIR-EVSLLKNLKHANIVTLHDIIHTERCLTLVFE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 120 FMAygsaKDLicTHFMDGMNELA----IAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNLSMIS 193
Cdd:cd07871    84 YLD----SDL--KQYLDNCGNLMsmhnVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLAdfGLARAKSVPT 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1394533236 194 HGQRQRVVhdfpkysvkVLPWLSPEVLQQNLQgYDAKSDIYSVGITACELANGHVPF 250
Cdd:cd07871   158 KTYSNEVV---------TLWYRPPDVLLGSTE-YSTPIDMWGVGCILYEMATGRPMF 204
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
97-254 2.39e-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: 45.78  E-value: 2.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  97 NHPNIVpyraTFIA--------DNELWVVTSFMAYGSAKDLICTHFMDgMNELaiAYILQGVLKALDYIH------HMGY 162
Cdd:cd14053    47 KHENIL----QFIGaekhgeslEAEYWLITEFHERGSLCDYLKGNVIS-WNEL--CKIAESMARGLAYLHedipatNGGH 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 163 ----VHRSVKASHILISVDGKVYLSGLrsNLSMI---------SHGQrqrvvhdfpkysVKVLPWLSPEVLQQNLQ-GYD 228
Cdd:cd14053   120 kpsiAHRDFKSKNVLLKSDLTACIADF--GLALKfepgkscgdTHGQ------------VGTRRYMAPEVLEGAINfTRD 185
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1394533236 229 A--KSDIYSVG------ITACELANGHVPFKDMP 254
Cdd:cd14053   186 AflRIDMYAMGlvlwelLSRCSVHDGPVDEYQLP 219
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
40-264 2.39e-05

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: 45.78  E-value: 2.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEAC--SNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVV 117
Cdd:cd05602     9 FHFLKVIGKG--SFGKVLLARHKSDEKFYAVKVLQKKAIlkKKEEKHIMSERNVLLKNVKHPFLVGLHFSFQTTDKLYFV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 118 TSFMAYGSakdlICTH------FMDGMNELAIAYILQgvlkALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSM 191
Cdd:cd05602    87 LDYINGGE----LFYHlqrercFLEPRARFYAAEIAS----ALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKEN 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1394533236 192 ISHGQRQRVVHDFPKYsvkvlpwLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLN 264
Cdd:cd05602   159 IEPNGTTSTFCGTPEY-------LAPEVLHK--QPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILN 222
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
68-253 2.48e-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: 45.39  E-value: 2.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  68 VTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRAtFIADNELWVVTSFMAYGSAK---DLICTHFmDGMNELAIA 144
Cdd:cd14150    25 VAVKILKVTEPTPEQLQAFKNEMQVLRKTRHVNILLFMG-FMTRPNFAIITQWCEGSSLYrhlHVTETRF-DTMQLIDVA 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 145 yilQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNLSMISHGQRQrvvhDFPKYSVKvlpWLSPEVLQ- 221
Cdd:cd14150   103 ---RQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGdfGLATVKTRWSGSQQV----EQPSGSIL---WMAPEVIRm 172
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1394533236 222 QNLQGYDAKSDIYSVGITACELANGHVPFKDM 253
Cdd:cd14150   173 QDTNPYSFQSDVYAYGVVLYELMSGTLPYSNI 204
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
94-352 2.58e-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: 2.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  94 KLFNHPNIV----PYRATFIADNELWVVTSFMAYGSAKDLIcTHFMDGMNELAIAYILQgVLKALDYIHHMG--YVHRSV 167
Cdd:cd14030    79 KGLQHPNIVrfydSWESTVKGKKCIVLVTELMTSGTLKTYL-KRFKVMKIKVLRSWCRQ-ILKGLQFLHTRTppIIHRDL 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 168 KASHILIS-VDGKVYLSGLrsNLSMISHGQRQRVVHDFPKYsvkvlpwLSPEVLQQNlqgYDAKSDIYSVGITACELANG 246
Cdd:cd14030   157 KCDNIFITgPTGSVKIGDL--GLATLKRASFAKSVIGTPEF-------MAPEMYEEK---YDESVDVYAFGMCMLEMATS 224
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 247 HVPFKD-MPATQMLLEKLNGTVPCLLDTSTIpaeeltmspsrsvansglsdslttstprpsngdspshpyhrtfsPHFHH 325
Cdd:cd14030   225 EYPYSEcQNAAQIYRRVTSGVKPASFDKVAI--------------------------------------------PEVKE 260
                         250       260
                  ....*....|....*....|....*..
gi 1394533236 326 FVEQCLQRNPDARPSASTLLNHSFFKQ 352
Cdd:cd14030   261 IIEGCIRQNKDERYAIKDLLNHAFFQE 287
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
45-343 2.98e-05

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: 45.73  E-value: 2.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  45 VIGKGfeDLMTVNLARYKPTGEYVTVRRINLEAC-SNEMVTFLQGELHVS-KLFNHPNIVPYRATFIADNELWVVTSFMA 122
Cdd:cd05603     2 VIGKG--SFGKVLLAKRKCDGKFYAVKVLQKKTIlKKKEQNHIMAERNVLlKNLKHPFLVGLHYSFQTSEKLYFVLDYVN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 123 YGSakdlICTHFMDG--MNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSglrsNLSMISHG-QRQR 199
Cdd:cd05603    80 GGE----LFFHLQRErcFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLT----DFGLCKEGmEPEE 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 200 VVHDF---PKYsvkvlpwLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLleklngtvpclldtSTI 276
Cdd:cd05603   152 TTSTFcgtPEY-------LAPEVLRK--EPYDRTVDWWCLGAVLYEMLYGLPPFYSRDVSQMY--------------DNI 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 277 PAEELTMSPSRSVANSGLSDSLTTSTPR-------------------PSNGDSPSH-----PYH---------RTFSPHF 323
Cdd:cd05603   209 LHKPLHLPGGKTVAACDLLQGLLHKDQRrrlgakadfleiknhvffsPINWDDLYHkritpPYNpnvagpadlRHFDPEF 288
                         330       340
                  ....*....|....*....|.
gi 1394533236 324 -HHFVEQCLQRNPDARPSAST 343
Cdd:cd05603   289 tQEAVPHSVGRTPDLTASSSS 309
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
40-198 3.18e-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: 45.61  E-value: 3.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKG-FEDlmtVNLARYKPTGE-YVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVV 117
Cdd:cd05629     3 FHTVKVIGKGaFGE---VRLVQKKDTGKiYAMKTLLKSEMFKKDQLAHVKAERDVLAESDSPWVVSLYYSFQDAQYLYLI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 118 TSFMAYGSAKDLICTH--FMDGMNELaiaYILQGVLkALDYIHHMGYVHRSVKASHILISVDGKVYLSGLrsNLSMISHG 195
Cdd:cd05629    80 MEFLPGGDLMTMLIKYdtFSEDVTRF---YMAECVL-AIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDF--GLSTGFHK 153

                  ...
gi 1394533236 196 QRQ 198
Cdd:cd05629   154 QHD 156
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
134-251 3.66e-05

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: 44.83  E-value: 3.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 134 FMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILisvdgkvyLSGLRS-NLSMISHGQRQRVVHDFPKYSVKVL 212
Cdd:cd14112    92 SNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIM--------FQSVRSwQVKLVDFGRAQKVSKLGKVPVDGDT 163
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1394533236 213 PWLSPEVLQQNLQGYdAKSDIYSVGITACELANGHVPFK 251
Cdd:cd14112   164 DWASPEFHNPETPIT-VQSDIWGLGVLTFCLLSGFHPFT 201
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
68-254 3.66e-05

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: 45.34  E-value: 3.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  68 VTVRRINLEACSNEMVTFLQgELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLI----------------- 130
Cdd:cd05045    33 VAVKMLKENASSSELRDLLS-EFNLLKQVNHPHVIKLYGACSQDGPLLLIVEYAKYGSLRSFLresrkvgpsylgsdgnr 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 131 --CTHFMDGMNELAIAYILQ---GVLKALDYIHHMGYVHRSVKASHILISvDGKVylsglrsnLSMISHGQRQRVVHD-- 203
Cdd:cd05045   112 nsSYLDNPDERALTMGDLISfawQISRGMQYLAEMKLVHRDLAARNVLVA-EGRK--------MKISDFGLSRDVYEEds 182
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1394533236 204 FPKYSVKVLP--WLSPEVLQQNLqgYDAKSDIYSVGITACELAN-GHVPFKDMP 254
Cdd:cd05045   183 YVKRSKGRIPvkWMAIESLFDHI--YTTQSDVWSFGVLLWEIVTlGGNPYPGIA 234
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
45-266 4.38e-05

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: 44.83  E-value: 4.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  45 VIGKG-FEDLMTVNLARYKPTGEYVTVRRINLEACS-NEMVTFLQgELHVSKLFNHPNIVPYRATFIADNEL------WV 116
Cdd:cd05035     6 ILGEGeFGSVMEAQLKQDDGSQLKVAVKTMKVDIHTySEIEEFLS-EAACMKDFDHPNVMRLIGVCFTASDLnkppspMV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 117 VTSFMAYGsakDLICTHFMDGMNELAIAYILQGVLK-------ALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRS 187
Cdd:cd05035    85 ILPFMKHG---DLHSYLLYSRLGGLPEKLPLQTLLKfmvdiakGMEYLSNRNFIHRDLAARNCMLDENMTVCVAdfGLSR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 188 NLSMISHGQRQRVvhdfPKYSVKvlpWLSPEVLQQNLqgYDAKSDIYSVGITACELAN-GHVPFKDMPATQMLLEKLNGT 266
Cdd:cd05035   162 KIYSGDYYRQGRI----SKMPVK---WIALESLADNV--YTSKSDVWSFGVTMWEIATrGQTPYPGVENHEIYDYLRNGN 232
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
40-350 4.63e-05

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


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 44.84  E-value: 4.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKG-FEdlmTVNLARYKPTGEYVTVRRINleacsNEMVTFLQGELHVSKL--------FNHPNIVPYRATFIA 110
Cdd:cd14210    15 YEVLSVLGKGsFG---QVVKCLDHKTGQLVAIKIIR-----NKKRFHQQALVEVKILkhlndndpDDKHNIVRYKDSFIF 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 111 DNELWVVTSFMA---YgsakDLIC-THFMdGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISvdgkvylSGLR 186
Cdd:cd14210    87 RGHLCIVFELLSinlY----ELLKsNNFQ-GLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLK-------QPSK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 187 SNLSMIshgqrqrvvhDFP---KYSVKVLPWL------SPEVLqqnL-QGYDAKSDIYSVGITACELANGHVPFkdMPAT 256
Cdd:cd14210   155 SSIKVI----------DFGsscFEGEKVYTYIqsrfyrAPEVI---LgLPYDTAIDMWSLGCILAELYTGYPLF--PGEN 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 257 QMllEKLNgtvpCLLdtstipaEELTMSPSRSVANSG-------------LSDSLTTSTPRPSNGDSPSHpyHRTFSPHF 323
Cdd:cd14210   220 EE--EQLA----CIM-------EVLGVPPKSLIDKASrrkkffdsngkprPTTNSKGKKRRPGSKSLAQV--LKCDDPSF 284
                         330       340
                  ....*....|....*....|....*..
gi 1394533236 324 HHFVEQCLQRNPDARPSASTLLNHSFF 350
Cdd:cd14210   285 LDFLKKCLRWDPSERMTPEEALQHPWI 311
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
89-250 5.15e-05

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: 44.52  E-value: 5.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  89 ELHVSKLFNHPNIVPYRATFIADNELWVVTSFMaygSAKDLI-CTHFMDGMNELAIAYILQGVLKALDYIHHMGYVHRSV 167
Cdd:cd14110    49 EYQVLRRLSHPRIAQLHSAYLSPRHLVLIEELC---SGPELLyNLAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDL 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 168 KASHILISVDGKVYLSGLRSNLSMishGQRQRVVHDFPKYSVKVLpwlSPEVLQQnlQGYDAKSDIYSVGITACELANGH 247
Cdd:cd14110   126 RSENMIITEKNLLKIVDLGNAQPF---NQGKVLMTDKKGDYVETM---APELLEG--QGAGPQTDIWAIGVTAFIMLSAD 197

                  ...
gi 1394533236 248 VPF 250
Cdd:cd14110   198 YPV 200
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
98-347 6.12e-05

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: 44.18  E-value: 6.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  98 HPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTHfmDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVD 177
Cdd:cd14115    48 HPQYITLHDTYESPTSYILVLELMDDGRLLDYLMNH--DELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLR 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 178 ---GKVYLSGLRSNLSMISHgqrqRVVHDF---PKYSvkvlpwlSPEVLQQNlqGYDAKSDIYSVGITACELANGHVPFk 251
Cdd:cd14115   126 ipvPRVKLIDLEDAVQISGH----RHVHHLlgnPEFA-------APEVIQGT--PVSLATDIWSIGVLTYVMLSGVSPF- 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 252 dmpatqmlleklngtvpclLDTStipAEELTMSPSRsvansglsdsLTTSTPrpsngdspsHPYHRTFSPHFHHFVEQCL 331
Cdd:cd14115   192 -------------------LDES---KEETCINVCR----------VDFSFP---------DEYFGDVSQAARDFINVIL 230
                         250
                  ....*....|....*.
gi 1394533236 332 QRNPDARPSASTLLNH 347
Cdd:cd14115   231 QEDPRRRPTAATCLQH 246
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
86-250 6.74e-05

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: 44.22  E-value: 6.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  86 LQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTHFMDGMNELAIAYILQgVLKALDYIHHMGYVHR 165
Cdd:cd14191    46 IRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEMVSGGELFERIIDEDFELTERECIKYMRQ-ISEGVEYIHKQGIVHL 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 166 SVKASHILIsvdgkVYLSGlrSNLSMISHGQRQRVVHdfpKYSVKVL----PWLSPEVLQQNLQGYDakSDIYSVGITAC 241
Cdd:cd14191   125 DLKPENIMC-----VNKTG--TKIKLIDFGLARRLEN---AGSLKVLfgtpEFVAPEVINYEPIGYA--TDMWSIGVICY 192

                  ....*....
gi 1394533236 242 ELANGHVPF 250
Cdd:cd14191   193 ILVSGLSPF 201
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
68-244 6.87e-05

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: 44.26  E-value: 6.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  68 VTVRRINLEACSNEMVTFLQgELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDL---------ICTHFMDGM 138
Cdd:cd05032    39 VAIKTVNENASMRERIEFLN-EASVMKEFNCHHVVRLLGVVSTGQPTLVVMELMAKGDLKSYlrsrrpeaeNNPGLGPPT 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 139 NELAIAYILQgVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLrsnlsmishgQRQRVVHDFPKYSVK-VLP-- 213
Cdd:cd05032   118 LQKFIQMAAE-IADGMAYLAAKKFVHRDLAARNCMVAEDLTVKIGdfGM----------TRDIYETDYYRKGGKgLLPvr 186
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1394533236 214 WLSPEVLQQNLqgYDAKSDIYSVGITACELA 244
Cdd:cd05032   187 WMAPESLKDGV--FTTKSDVWSFGVVLWEMA 215
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
98-355 8.91e-05

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: 43.93  E-value: 8.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  98 HPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTHFM--DGMNELAiayILQGVLKALDYIHHMGYVHRSVKASHILis 175
Cdd:cd14043    55 HENVNLFLGLFVDCGILAIVSEHCSRGSLEDLLRNDDMklDWMFKSS---LLLDLIKGMRYLHHRGIVHGRLKSRNCV-- 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 176 VDGKVYLSGLRSNLSMISHGQRQRVvhdfPKYSVKVLPWLSPEVLQQNLQGYDA--KSDIYSVGITACELANGHVPFkdm 253
Cdd:cd14043   130 VDGRFVLKITDYGYNEILEAQNLPL----PEPAPEELLWTAPELLRDPRLERRGtfPGDVFSFAIIMQEVIVRGAPY--- 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 254 patqmlleklngtvpCLLDtstIPAEELTmspsRSVAnsglsdslttSTP---RP--SNGDSPshpyhrtfsPHFHHFVE 328
Cdd:cd14043   203 ---------------CMLG---LSPEEII----EKVR----------SPPplcRPsvSMDQAP---------LECIQLMK 241
                         250       260
                  ....*....|....*....|....*....
gi 1394533236 329 QCLQRNPDARPSastlLNHSF--FKQIKR 355
Cdd:cd14043   242 QCWSEAPERRPT----FDQIFdqFKSINK 266
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
68-250 9.53e-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: 43.87  E-value: 9.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  68 VTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNeLWVVTSFMAYGSAKDLIctHFMDGMNEL-AIAYI 146
Cdd:cd14149    37 VAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGYMTKDN-LAIVTQWCEGSSLYKHL--HVQETKFQMfQLIDI 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 147 LQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNLSMISHGQRQrvvhDFPKYSVKvlpWLSPEVLQ-QN 223
Cdd:cd14149   114 ARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGdfGLATVKSRWSGSQQV----EQPTGSIL---WMAPEVIRmQD 186
                         170       180
                  ....*....|....*....|....*..
gi 1394533236 224 LQGYDAKSDIYSVGITACELANGHVPF 250
Cdd:cd14149   187 NNPFSFQSDVYSYGIVLYELMTGELPY 213
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
86-250 1.03e-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: 43.75  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  86 LQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTHFMDgMNELAIAYILQGVLKALDYIHHMGYVHR 165
Cdd:cd14193    48 VKNEIEVMNQLNHANLIQLYDAFESRNDIVLVMEYVDGGELFDRIIDENYN-LTELDTILFIKQICEGIQYMHQMYILHL 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 166 SVKASHIL-ISVDGKvylsglrsNLSMISHGQRQRVVhdfPKYSVKVlPWLSPEVLQQNLQGYDAKS---DIYSVGITAC 241
Cdd:cd14193   127 DLKPENILcVSREAN--------QVKIIDFGLARRYK---PREKLRV-NFGTPEFLAPEVVNYEFVSfptDMWSLGVIAY 194

                  ....*....
gi 1394533236 242 ELANGHVPF 250
Cdd:cd14193   195 MLLSGLSPF 203
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
59-237 1.39e-04

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: 43.37  E-value: 1.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  59 ARYKPTGEYVTVRRINLEacsNEM----VTFLQgELHVSKLFNHPNIVPYRATFIADN--ELWVVTSFMAYgSAKDLict 132
Cdd:cd07843    24 ARDKKTGEIVALKKLKME---KEKegfpITSLR-EINILLKLQHPNIVTVKEVVVGSNldKIYMVMEYVEH-DLKSL--- 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 133 hfMDGMNE-LAIAYI---LQGVLKALDYIHHMGYVHRSVKASHILISVDGKvylsglrsnLSMISHGQRQRVVHDFPKYS 208
Cdd:cd07843    96 --METMKQpFLQSEVkclMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGI---------LKICDFGLAREYGSPLKPYT 164
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1394533236 209 VKV--LPWLSPEVLqqnL--QGYDAKSDIYSVG 237
Cdd:cd07843   165 QLVvtLWYRAPELL---LgaKEYSTAIDMWSVG 194
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
34-263 1.50e-04

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: 43.44  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  34 LPEGGCYELLTVIGKGFEDLMTVNLARYKPTGE--YVTVRRINLEACSNEMVTFLQgELHVSKLFNHPNIVPYRATFIAD 111
Cdd:cd05095    13 LGEGQFGEVHLCEAEGMEKFMDKDFALEVSENQpvLVAVKMLRADANKNARNDFLK-EIKIMSRLKDPNIIRLLAVCITD 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 112 NELWVVTSFMAYGSAKDLICTHFMDG-----MNELAIAY-----ILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVY 181
Cdd:cd05095    92 DPLCMITEYMENGDLNQFLSRQQPEGqlalpSNALTVSYsdlrfMAAQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIK 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 182 LS--GLRSNLsmiSHGQRQRVvhdfpkYSVKVLP--WLSPEVLQqnLQGYDAKSDIYSVGITACELANghvpF-KDMPAT 256
Cdd:cd05095   172 IAdfGMSRNL---YSGDYYRI------QGRAVLPirWMSWESIL--LGKFTTASDVWAFGVTLWETLT----FcREQPYS 236

                  ....*..
gi 1394533236 257 QMLLEKL 263
Cdd:cd05095   237 QLSDEQV 243
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
143-259 1.68e-04

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: 43.01  E-value: 1.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 143 IAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNLSMISHGQRQRVVHDFPkysvkvLPWLSPEVL 220
Cdd:cd05115   106 VVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISdfGLSKALGADDSYYKARSAGKWP------LKWYAPECI 179
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1394533236 221 qqNLQGYDAKSDIYSVGITACE-LANGHVPFKDMPATQML 259
Cdd:cd05115   180 --NFRKFSSRSDVWSYGVTMWEaFSYGQKPYKKMKGPEVM 217
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
89-250 1.75e-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: 42.66  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  89 ELHVSKLFNHPNIVPYRATFIADNELWVVtsfMAYGSAKDL-ICTHFMDGMNELAIAYILQGVLKALDYIHHMGYVHRSV 167
Cdd:cd14121    45 EIELLKKLKHPHIVELKDFQWDEEHIYLI---MEYCSGGDLsRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDL 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 168 KASHILISvdgkvylSGLRSNLSMISHGQRQRVVHDFPKYSVKVLP-WLSPEVLQQnlQGYDAKSDIYSVGITACELANG 246
Cdd:cd14121   122 KPQNLLLS-------SRYNPVLKLADFGFAQHLKPNDEAHSLRGSPlYMAPEMILK--KKYDARVDLWSVGVILYECLFG 192

                  ....
gi 1394533236 247 HVPF 250
Cdd:cd14121   193 RAPF 196
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
40-313 1.82e-04

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: 43.09  E-value: 1.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVR---RINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIAdNELWV 116
Cdd:cd05108     9 FKKIKVLGSG--AFGTVYKGLWIPEGEKVKIPvaiKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLT-STVQL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 117 VTSFMAYGSAKDLICTHFMDGMNELAIAYILQgVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLrsNLSMISHGQ 196
Cdd:cd05108    86 ITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQ-IAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDF--GLAKLLGAE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 197 RQRVVHDFPKYSVKvlpWLSPEVLQQNLqgYDAKSDIYSVGITACELAN-GHVPFKDMPATQM--LLEK---LNGTVPCL 270
Cdd:cd05108   163 EKEYHAEGGKVPIK---WMALESILHRI--YTHQSDVWSYGVTVWELMTfGSKPYDGIPASEIssILEKgerLPQPPICT 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1394533236 271 LDTSTIPAEELTMSPSRSVANSGLSDSLTTSTPRPS-----NGDSPSH 313
Cdd:cd05108   238 IDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQrylviQGDERMH 285
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
85-253 2.47e-04

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: 42.81  E-value: 2.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  85 FLQGELHVSKLFNHPNIVPYRATFIA----DNELWVVTSFMAYGSAKDLICTHFMDGMNELAIAyilqgvLKALDYIHHM 160
Cdd:cd14142    45 FRETEIYNTVLLRHENILGFIASDMTsrnsCTQLWLITHYHENGSLYDYLQRTTLDHQEMLRLA------LSAASGLVHL 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 161 -----------GYVHRSVKASHILISVDGKVYLSGLrsNLS-MISHGQRQRVVHDFPKYSVKvlPWLSPEVLQQ--NLQG 226
Cdd:cd14142   119 hteifgtqgkpAIAHRDLKSKNILVKSNGQCCIADL--GLAvTHSQETNQLDVGNNPRVGTK--RYMAPEVLDEtiNTDC 194
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1394533236 227 YDA--KSDIYSVGITACELA-----NGHV-----PFKDM 253
Cdd:cd14142   195 FESykRVDIYAFGLVLWEVArrcvsGGIVeeykpPFYDV 233
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
62-243 3.26e-04

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 42.76  E-value: 3.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  62 KPTGEYVTVRRINleaCSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVT--------SFMaYGSAKDlicth 133
Cdd:PHA03210  189 KPKCERLIAKRVK---AGSRAAIQLENEILALGRLNHENILKIEEILRSEANTYMITqkydfdlySFM-YDEAFD----- 259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 134 FMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMishgQRQRVVHDFPkySVKVLP 213
Cdd:PHA03210  260 WKDRPLLKQTRAIMKQLLCAVEYIHDKKLIHRDIKLENIFLNCDGKIVLGDFGTAMPF----EKEREAFDYG--WVGTVA 333
                         170       180       190
                  ....*....|....*....|....*....|
gi 1394533236 214 WLSPEVLQQNlqGYDAKSDIYSVGITACEL 243
Cdd:PHA03210  334 TNSPEILAGD--GYCEITDIWSCGLILLDM 361
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
40-251 3.64e-04

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: 42.39  E-value: 3.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGFEDLmtVNLARYKPT--GEYVTVRRINlEACSNEMVT--FLQgELHVSKLF-NHPNIVPYRATFIAD--- 111
Cdd:cd07857     2 YELIKELGQGAYGI--VCSARNAETseEETVAIKKIT-NVFSKKILAkrALR-ELKLLRHFrGHKNITCLYDMDIVFpgn 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 112 -NELWVVTSFMAYG------SAKDLICTHFMdgmnelaiAYILQgVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS- 183
Cdd:cd07857    78 fNELYLYEELMEADlhqiirSGQPLTDAHFQ--------SFIYQ-ILCGLKYIHSANVLHRDLKPGNLLVNADCELKICd 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1394533236 184 -GLRSNLSmISHGQRQrvvhDFPKYSVKVLPWLSPEVLQQNlQGYDAKSDIYSVGITACELANGHVPFK 251
Cdd:cd07857   149 fGLARGFS-ENPGENA----GFMTEYVATRWYRAPEIMLSF-QSYTKAIDVWSVGCILAELLGRKPVFK 211
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
89-251 4.04e-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: 4.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  89 ELHVSKLFNHPNIVPYRATFIAD------NELWVVTSFMAYGsakdlICTHFMDGMNELAIAYILQGVLKALDYIHHMGY 162
Cdd:cd07876    70 ELVLLKCVNHKNIISLLNVFTPQksleefQDVYLVMELMDAN-----LCQVIHMELDHERMSYLLYQMLCGIKHLHSAGI 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 163 VHRSVKASHILISVDgkvylsglrSNLSMISHGQRQRVVHDFPKYSVKVLPWL-SPEVLQQnlQGYDAKSDIYSVGITAC 241
Cdd:cd07876   145 IHRDLKPSNIVVKSD---------CTLKILDFGLARTACTNFMMTPYVVTRYYrAPEVILG--MGYKENVDIWSVGCIMG 213
                         170
                  ....*....|
gi 1394533236 242 ELANGHVPFK 251
Cdd:cd07876   214 ELVKGSVIFQ 223
PHA02988 PHA02988
hypothetical protein; Provisional
189-265 4.12e-04

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 42.04  E-value: 4.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 189 LSMISHGqRQRVVHDFPKYSVKVLPWLSPEVLQQNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQ---MLLEKLNG 265
Cdd:PHA02988  162 LKIICHG-LEKILSSPPFKNVNFMVYFSYKMLNDIFSEYTIKDDIYSLGVVLWEIFTGKIPFENLTTKEiydLIINKNNS 240
PK_MADML cd14035
Pseudokinase domain of MLF1-ADaptor Molecule-Like; The pseudokinase domain shows similarity to ...
95-347 4.15e-04

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: 41.83  E-value: 4.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  95 LFNHPNIVPYRATF--IADNELWVV--TSFMAYGSAKDLI--CTHFMDGMNELAIAYILQGVLKALDYIHHMG--YVHRS 166
Cdd:cd14035    51 LVDHPNIVKFHKYWldVKDNHARVVfiTEYVSSGSLKQFLkkTKKNHKTMNARAWKRWCTQILSALSYLHSCEppIIHGN 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 167 VKASHILISVDGKVYL--------------SGLRSNLSMisHGQRQRVVHDFPkysvkvlpwlsPEVLQQNlqgYDAKSD 232
Cdd:cd14035   131 LTSDTIFIQHNGLIKIgsvwhrlfvnvlpeGGVRGPLRQ--EREELRNLHFFP-----------PEYGSCE---DGTAVD 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 233 IYSVGITACELAnghvpfkdmpatqmLLEklngtvpclldtstIPAEELTMSPSRSVANSGLSDSlttstprpsngdsps 312
Cdd:cd14035   195 IFSFGMCALEMA--------------VLE--------------IQANGDTRVSEEAIARARHSLE--------------- 231
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1394533236 313 hpyhrtfSPHFHHFVEQCLQRNPDARPSASTLLNH 347
Cdd:cd14035   232 -------DPNMREFILSCLRHNPCKRPTAHDLLFH 259
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
145-260 4.28e-04

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: 41.70  E-value: 4.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 145 YILQGVLKALDYIHHMGYVHRSVKASHILISVDGkvylsgLRSNLSMISHGQrqrvvhdfPKYSVKVL---------PWL 215
Cdd:cd05037   106 QVAKQLASALHYLEDKKLIHGNVRGRNILLAREG------LDGYPPFIKLSD--------PGVPITVLsreervdriPWI 171
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1394533236 216 SPEVLQQNLQGYDAKSDIYSVGITACEL-ANGHVPFKDMPATQMLL 260
Cdd:cd05037   172 APECLRNLQANLTIAADKWSFGTTLWEIcSGGEEPLSALSSQEKLQ 217
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
95-347 4.54e-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: 41.84  E-value: 4.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  95 LFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTHFMDG--MNELAIAYILQGVLKALDYIHHMGYVHRSVKASHI 172
Cdd:cd14139    56 LGHHPHVVRYYSAWAEDDHMIIQNEYCNGGSLQDAISENTKSGnhFEEPELKDILLQVSMGLKYIHNSGLVHLDIKPSNI 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 173 LISVDGKVYLSGLRSNLSMISHGQRQRVVHDF-----------PKYSVKVLPWLSPEVLQQNLQgYDAKSDIYSVGITAC 241
Cdd:cd14139   136 FICHKMQSSSGVGEEVSNEEDEFLSANVVYKIgdlghvtsinkPQVEEGDSRFLANEILQEDYR-HLPKADIFALGLTVA 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 242 eLANGHVPFKDMPATQMLLEKlnGTVPclldtsTIPAEeltmspsrsvansglsdslttstprpsngdspshpyhrtFSP 321
Cdd:cd14139   215 -LAAGAEPLPTNGAAWHHIRK--GNFP------DVPQE---------------------------------------LPE 246
                         250       260
                  ....*....|....*....|....*.
gi 1394533236 322 HFHHFVEQCLQRNPDARPSASTLLNH 347
Cdd:cd14139   247 SFSSLLKNMIQPDPEQRPSATALARH 272
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
83-257 5.17e-04

Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; Fer kinase; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fer kinase is a member of the Fes subfamily of proteins which are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. Fer kinase is expressed in a wide variety of tissues, and is found to reside in both the cytoplasm and the nucleus. It plays important roles in neuronal polarization and neurite development, cytoskeletal reorganization, cell migration, growth factor signaling, and the regulation of cell-cell interactions mediated by adherens junctions and focal adhesions. Fer kinase also regulates cell cycle progression in malignant cells.


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 41.53  E-value: 5.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  83 VTFLQgELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSakdlICTHFMDGMNELAIAYILQGVLKA---LDYIHH 159
Cdd:cd05085    38 IKFLS-EARILKQYDHPNIVKLIGVCTQRQPIYIVMELVPGGD----FLSFLRKKKDELKTKQLVKFSLDAaagMAYLES 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 160 MGYVHRSVKASHILISVDGKVYLsglrSNLSMishgQRQRVVHDFPKYSVKVLP--WLSPEVLqqNLQGYDAKSDIYSVG 237
Cdd:cd05085   113 KNCIHRDLAARNCLVGENNALKI----SDFGM----SRQEDDGVYSSSGLKQIPikWTAPEAL--NYGRYSSESDVWSFG 182
                         170       180
                  ....*....|....*....|.
gi 1394533236 238 ITACE-LANGHVPFKDMPATQ 257
Cdd:cd05085   183 ILLWEtFSLGVCPYPGMTNQQ 203
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
96-265 5.43e-04

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: 41.40  E-value: 5.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  96 FNHPNIVPYRATFIADNELWVVTSFMAYGSakdlICTHFMDGMNELAIAYILQ---GVLKALDYIHHMGYVHRSVKASHI 172
Cdd:cd05113    56 LSHEKLVQLYGVCTKQRPIFIITEYMANGC----LLNYLREMRKRFQTQQLLEmckDVCEAMEYLESKQFLHRDLAARNC 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 173 LISVDGKVYLSGLRSNLSMISHGQRQRVVHDFPkysvkvLPWLSPEVLQQNlqGYDAKSDIYSVGITACELAN-GHVPFK 251
Cdd:cd05113   132 LVNDQGVVKVSDFGLSRYVLDDEYTSSVGSKFP------VRWSPPEVLMYS--KFSSKSDVWAFGVLMWEVYSlGKMPYE 203
                         170
                  ....*....|....
gi 1394533236 252 DMPATQMLLEKLNG 265
Cdd:cd05113   204 RFTNSETVEHVSQG 217
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
68-259 5.55e-04

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: 41.54  E-value: 5.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  68 VTVRRINLEACSNEMVTFLQgELHVSKLF-NHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTHFMDGM-------- 138
Cdd:cd05098    48 VAVKMLKSDATEKDLSDLIS-EMEMMKMIgKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPGMeycynpsh 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 139 ---------NELAIAYilqGVLKALDYIHHMGYVHRSVKASHILISVDG--KVYLSGLRSNLSMISHgqrqrvvhdFPKY 207
Cdd:cd05098   127 npeeqlsskDLVSCAY---QVARGMEYLASKKCIHRDLAARNVLVTEDNvmKIADFGLARDIHHIDY---------YKKT 194
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1394533236 208 SVKVLP--WLSPEVLQQNLqgYDAKSDIYSVGITACELAN-GHVPFKDMPATQML 259
Cdd:cd05098   195 TNGRLPvkWMAPEALFDRI--YTHQSDVWSFGVLLWEIFTlGGSPYPGVPVEELF 247
STKc_VRK cd14015
Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase; STKs ...
150-182 6.41e-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: 41.50  E-value: 6.41e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1394533236 150 VLKALDYIHHMGYVHRSVKASHILISVDG---KVYL 182
Cdd:cd14015   136 ILDVLEYIHENGYVHADIKASNLLLGFGKnkdQVYL 171
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
92-251 7.47e-04

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK1 plays a role in the activation of IRF3/7, STAT, and NFkB. It mediates IL-6 and IFN-gamma responses following IL-1 and IL-18 stimulation, respectively. It also plays an essential role in IFN-alpha induction downstream of TLR7 and TLR9. The IRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 40.96  E-value: 7.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  92 VSKL--FNHPNIVPYrATFIADNELW-VVTSFMAYGSAKD-LICTHFMDGMNELAIAYILQGVLKALDYIHHM--GYVHR 165
Cdd:cd14159    43 VEKLsrFRHPNIVDL-AGYSAQQGNYcLIYVYLPNGSLEDrLHCQVSCPCLSWSQRLHVLLGTARAIQYLHSDspSLIHG 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 166 SVKASHILI--SVDGKVYLSGLR---------SNLSMISHGQRQRvvhdfpkysvKVLPWLSPEVLQQNLQGYDakSDIY 234
Cdd:cd14159   122 DVKSSNILLdaALNPKLGDFGLArfsrrpkqpGMSSTLARTQTVR----------GTLAYLPEEYVKTGTLSVE--IDVY 189
                         170
                  ....*....|....*..
gi 1394533236 235 SVGITACELANGHVPFK 251
Cdd:cd14159   190 SFGVVLLELLTGRRAME 206
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
89-255 8.41e-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: 8.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  89 ELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTH--FMDGMNELAIAYILQGVlkalDYIHHMGYVHRS 166
Cdd:cd14076    56 EINILKGLTHPNIVRLLDVLKTKKYIGIVLEFVSGGELFDYILARrrLKDSVACRLFAQLISGV----AYLHKKGVVHRD 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 167 VKASHILISVDgkvylsglrSNLSMISHGQRQRVVHDFP---KYSVKVLPWLSPEVLQQNLQGYDAKSDIYSVGITACEL 243
Cdd:cd14076   132 LKLENLLLDKN---------RNLVITDFGFANTFDHFNGdlmSTSCGSPCYAAPELVVSDSMYAGRKADIWSCGVILYAM 202
                         170
                  ....*....|..
gi 1394533236 244 ANGHVPFKDMPA 255
Cdd:cd14076   203 LAGYLPFDDDPH 214
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
315-350 9.61e-04

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 and three PIM2 isoforms as a result of alternative translation initiation sites, while there is only one PIM3 protein. Compound knockout mice deficient of all three PIM kinases that survive the perinatal period show a profound reduction in body size, indicating that PIMs are important for body growth. The PIM subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 40.68  E-value: 9.61e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1394533236 315 YHRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFF 350
Cdd:cd14005   220 FRPRLSKECCDLISRCLQFDPSKRPSLEQILSHPWF 255
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
62-265 9.80e-04

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


Pssm-ID: 271092 [Multi-domain]  Cd Length: 261  Bit Score: 40.67  E-value: 9.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  62 KPTGEYVTVRRINLEACSNEMVTFLqgELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLIC---THFMDGM 138
Cdd:cd14190    26 KRTGLKLAAKVINKQNSKDKEMVLL--EIQVMNQLNHRNLIQLYEAIETPNEIVLFMEYVEGGELFERIVdedYHLTEVD 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 139 NELAIAYILQGVLkaldYIHHMGYVHRSVKASHILIsvdgkVYLSGlrSNLSMISHGQRQRVVhdfPKYSVKV---LP-W 214
Cdd:cd14190   104 AMVFVRQICEGIQ----FMHQMRVLHLDLKPENILC-----VNRTG--HQVKIIDFGLARRYN---PREKLKVnfgTPeF 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1394533236 215 LSPEVLqqNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNG 265
Cdd:cd14190   170 LSPEVV--NYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETLNNVLMG 218
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
40-250 9.81e-04

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-1 is expressed ubiquitously and is localized in the cytoplasm. Its kinase activity is cell cycle dependent and peaks at the S and G2 phases. PCTAIRE-1 is highly expressed in the brain and may play a role in regulating neurite outgrowth. It can also associate with Trap (Tudor repeat associator with PCTAIRE-2), a physiological partner of PCTAIRE-2; with p11, a small dimeric protein with similarity to S100; and with 14-3-3 proteins, mediators of phosphorylation-dependent interactions in many different proteins. PCTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270854 [Multi-domain]  Cd Length: 297  Bit Score: 40.76  E-value: 9.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGfeDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQgELHVSKLFNHPNIVPYRATFIADNELWVVTS 119
Cdd:cd07873     4 YIKLDKLGEG--TYATVYKGRSKLTDNLVALKEIRLEHEEGAPCTAIR-EVSLLKDLKHANIVTLHDIIHTEKSLTLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 120 FMAygsaKDLicTHFMDG----MNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNLSMIS 193
Cdd:cd07873    81 YLD----KDL--KQYLDDcgnsINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLAdfGLARAKSIPT 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1394533236 194 HGQRQRVVhdfpkysvkVLPWLSPEVLQQNLQgYDAKSDIYSVGITACELANGHVPF 250
Cdd:cd07873   155 KTYSNEVV---------TLWYRPPDILLGSTD-YSTQIDMWGVGCIFYEMSTGRPLF 201
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
89-246 1.26e-03

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: 40.25  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  89 ELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKD-LICTHFMDGMNELAIAYILQGVLKALDYIHHM---GYVH 164
Cdd:cd14160    42 ELEVLLLFQHPNILELAAYFTETEKFCLVYPYMQNGTLFDrLQCHGVTKPLSWHERINILIGIAKAIHYLHNSqpcTVIC 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 165 RSVKASHILISVDGKVYLSGLrSNLSMISHGQRQRVVHDFPKYSVKVLPWLSPEVLQQNlqGYDAKSDIYSVGITACELA 244
Cdd:cd14160   122 GNISSANILLDDQMQPKLTDF-ALAHFRPHLEDQSCTINMTTALHKHLWYMPEEYIRQG--KLSVKTDVYSFGIVIMEVL 198

                  ..
gi 1394533236 245 NG 246
Cdd:cd14160   199 TG 200
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
68-250 1.34e-03

Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Axl is widely expressed in a variety of organs and cells including epithelial, mesenchymal, hematopoietic, as well as non-transformed cells. It is important in many cellular functions such as survival, anti-apoptosis, proliferation, migration, and adhesion. Axl was originally isolated from patients with chronic myelogenous leukemia and a chronic myeloproliferative disorder. It is overexpressed in many human cancers including colon, squamous cell, thyroid, breast, and lung carcinomas. Axl is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to its ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Axl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270660 [Multi-domain]  Cd Length: 277  Bit Score: 40.38  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  68 VTVRRINLEACS-NEMVTFLQgELHVSKLFNHPNIVPYRATFIADNEL------WVVTSFMAYGSAKD-LICTHFMDG-- 137
Cdd:cd05075    30 VAVKTMKIAICTrSEMEDFLS-EAVCMKEFDHPNVMRLIGVCLQNTESegypspVVILPFMKHGDLHSfLLYSRLGDCpv 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 138 -MNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLS--GLRSNLSMISHGQRQRVVhdfpKYSVKvlpW 214
Cdd:cd05075   109 yLPTQMLVKFMTDIASGMEYLSSKNFIHRDLAARNCMLNENMNVCVAdfGLSKKIYNGDYYRQGRIS----KMPVK---W 181
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1394533236 215 LSPEVLQQNLqgYDAKSDIYSVGITACELAN-GHVPF 250
Cdd:cd05075   182 IAIESLADRV--YTTKSDVWSFGVTMWEIATrGQTPY 216
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
89-250 1.35e-03

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


Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 40.23  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  89 ELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTHFMDgMNELAIAYILQGVLKALDYIHHMGYVHRSVK 168
Cdd:cd14104    46 EISILNIARHRNILRLHESFESHEELVMIFEFISGVDIFERITTARFE-LNEREIVSYVRQVCEALEFLHSKNIGHFDIR 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 169 ASHIlisvdgkVYLSGLRSNLSMISHGQ-RQRVVHDFPKYSVKVLPWLSPEVLQQNLQGydAKSDIYSVGITACELANGH 247
Cdd:cd14104   125 PENI-------IYCTRRGSYIKIIEFGQsRQLKPGDKFRLQYTSAEFYAPEVHQHESVS--TATDMWSLGCLVYVLLSGI 195

                  ...
gi 1394533236 248 VPF 250
Cdd:cd14104   196 NPF 198
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
56-364 1.39e-03

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: 40.19  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  56 VNLARYKPTGEYVTVRRINLEACSNEmvtflqgELHVSKLFNHPNIVPYratFIADNELWVVTSFM---AYGSAKDLIct 132
Cdd:cd13991    22 VHRMEDKQTGFQCAVKKVRLEVFRAE-------ELMACAGLTSPRVVPL---YGAVREGPWVNIFMdlkEGGSLGQLI-- 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 133 HFMDGMNE-LAIAYILQgVLKALDYIHHMGYVHRSVKASHILISVDGK-VYLSGLRSNLSMISHGQRQRVV--HDFPKYS 208
Cdd:cd13991    90 KEQGCLPEdRALHYLGQ-ALEGLEYLHSRKILHGDVKADNVLLSSDGSdAFLCDFGHAECLDPDGLGKSLFtgDYIPGTE 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 209 VKvlpwLSPEVLQQnlQGYDAKSDIYSvgiTACelanghvpfkdmpatqMLLEKLNGTVP---------CLLDTSTIPae 279
Cdd:cd13991   169 TH----MAPEVVLG--KPCDAKVDVWS---SCC----------------MMLHMLNGCHPwtqyysgplCLKIANEPP-- 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 280 eltmsPSRSVansglsdslttstprpsngdsPSHPYHRTFsphfhHFVEQCLQRNPDARPSASTLlnhsffkqiKRRASE 359
Cdd:cd13991   222 -----PLREI---------------------PPSCAPLTA-----QAIQAGLRKEPVHRASAAEL---------RRKTNR 261

                  ....*
gi 1394533236 360 ALPEL 364
Cdd:cd13991   262 ALQEV 266
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
86-259 1.66e-03

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Many FGFR3 splice variants have been reported with the IIIb and IIIc isoforms being the predominant forms. FGFR3 IIIc is the isoform expressed in chondrocytes, the cells affected in dwarfism, while IIIb is expressed in epithelial cells. FGFR3 ligands include FGF1, FGF2, FGF4, FGF8, FGF9, and FGF23. It is a negative regulator of long bone growth. In the cochlear duct and in the lens, FGFR3 is involved in differentiation while it appears to have a role in cell proliferation in epithelial cells. Germline mutations in FGFR3 are associated with skeletal disorders including several forms of dwarfism. Some missense mutations are associated with multiple myeloma and carcinomas of the bladder and cervix. Overexpression of FGFR3 is found in thyroid carcinoma. FGFR3 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 40.00  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  86 LQGELHVSKLF-NHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTHFMDGMNE-----------------LAIAYil 147
Cdd:cd05100    64 LVSEMEMMKMIgKHKNIINLLGACTQDGPLYVLVEYASKGNLREYLRARRPPGMDYsfdtcklpeeqltfkdlVSCAY-- 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 148 qGVLKALDYIHHMGYVHRSVKASHILISVDgkvylsglrsNLSMISHGQRQRVVHDFPKYSVKV---LP--WLSPEVLQQ 222
Cdd:cd05100   142 -QVARGMEYLASQKCIHRDLAARNVLVTED----------NVMKIADFGLARDVHNIDYYKKTTngrLPvkWMAPEALFD 210
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1394533236 223 NLqgYDAKSDIYSVGITACELAN-GHVPFKDMPATQML 259
Cdd:cd05100   211 RV--YTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEELF 246
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
56-252 1.83e-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: 39.81  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  56 VNLARYKPTGEYVTVRRINLEAcsNEMVTFLQgELHVSKLFNHPNIVPYRATFIADNELWVVTSFMaygSAKDLICT--- 132
Cdd:cd14111    19 IRRCRENATGKNFPAKIVPYQA--EEKQGVLQ-EYEILKSLHHERIMALHEAYITPRYLVLIAEFC---SGKELLHSlid 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 133 HFMDGMNELAiAYILQgVLKALDYIHHMGYVHRSVKASHILISVDgkvylsglrSNLSMISHGQRQRvvhdFPKYSVK-- 210
Cdd:cd14111    93 RFRYSEDDVV-GYLVQ-ILQGLEYLHGRRVLHLDIKPDNIMVTNL---------NAIKIVDFGSAQS----FNPLSLRql 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1394533236 211 -----VLPWLSPEVLQQNLQGYDAksDIYSVGITACELANGHVPFKD 252
Cdd:cd14111   158 grrtgTLEYMAPEMVKGEPVGPPA--DIWSIGVLTYIMLSGRSPFED 202
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
89-174 4.36e-03

Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 and BubR1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Bub1 (Budding uninhibited by benzimidazoles 1), BubR1, and similar proteins. They contain an N-terminal Bub1/Mad3 homology domain essential for Cdc20 binding and a C-terminal kinase domain. Bub1 and BubR1 are involved in SAC, a surveillance system that delays metaphase to anaphase transition by blocking the activity of APC/C (the anaphase promoting complex) until all chromosomes achieve proper attachments to the mitotic spindle, to avoid chromosome missegregation. Impaired SAC leads to genomic instabilities and tumor development. Bub1 and BubR1 facilitate the localization of SAC proteins to kinetochores and regulate kinetochore-microtubule (K-MT) attachments. Repression studies of Bub1 and BubR1 show that they exert an additive effect in misalignment phenotypes and may function cooperatively or in parallel pathways in regulating K-MT attachments. The Bub1/BubR1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270883 [Multi-domain]  Cd Length: 298  Bit Score: 38.88  E-value: 4.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  89 ELHvSKLFNHP---NIVPYRATFIADNELWVVTSFMAYGSAKDLICT---HFMDGMNE-LAIAYILQgVLKALDYIHHMG 161
Cdd:cd13981    49 QLH-SRLKNSRlreSISGAHSAHLFQDESILVMDYSSQGTLLDVVNKmknKTGGGMDEpLAMFFTIE-LLKVVEALHEVG 126
                          90
                  ....*....|...
gi 1394533236 162 YVHRSVKASHILI 174
Cdd:cd13981   127 IIHGDIKPDNFLL 139
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
89-250 5.52e-03

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK1 is expressed in every cell and tissue type. It specifically binds with JAMP (JNK1-associated membrane protein), which regulates the duration of JNK1 activity in response to stimuli. Specific JNK1 substrates include Itch and SG10, which are implicated in Th2 responses and airway inflammation, and microtubule dynamics and axodendritic length, respectively. Mice deficient in JNK1 are protected against arthritis, obesity, type 2 diabetes, cardiac cell death, and non-alcoholic liver disease, suggesting that JNK1 may play roles in the pathogenesis of these diseases. Initially, it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 38.49  E-value: 5.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  89 ELHVSKLFNHPNIVPYRATFIAD------NELWVVTSFMAYGsakdlICTHFMDGMNELAIAYILQGVLKALDYIHHMGY 162
Cdd:cd07875    73 ELVLMKCVNHKNIIGLLNVFTPQksleefQDVYIVMELMDAN-----LCQVIQMELDHERMSYLLYQMLCGIKHLHSAGI 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 163 VHRSVKASHILISVDgkvylsglrSNLSMISHGQRQRVVHDFPKYSVKVLPWL-SPEVLQQnlQGYDAKSDIYSVGITAC 241
Cdd:cd07875   148 IHRDLKPSNIVVKSD---------CTLKILDFGLARTAGTSFMMTPYVVTRYYrAPEVILG--MGYKENVDIWSVGCIMG 216

                  ....*....
gi 1394533236 242 ELANGHVPF 250
Cdd:cd07875   217 EMIKGGVLF 225
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
40-245 6.10e-03

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 38.26  E-value: 6.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  40 YELLTVIGKGFEDLmtVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTS 119
Cdd:PLN00009    4 YEKVEKIGEGTYGV--VYKARDRVTNETIALKKIRLEQEDEGVPSTAIREISLLKEMQHGNIVRLQDVVHSEKRLYLVFE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 120 FMaygsakDLICTHFMDGMNELA-----IAYILQGVLKALDYIHHMGYVHRSVKASHILISvdgkvylsgLRSN-LSMIS 193
Cdd:PLN00009   82 YL------DLDLKKHMDSSPDFAknprlIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLID---------RRTNaLKLAD 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1394533236 194 HGQRQRV---VHDFpKYSVKVLPWLSPEVLQQNLQgYDAKSDIYSVGITACELAN 245
Cdd:PLN00009  147 FGLARAFgipVRTF-THEVVTLWYRAPEILLGSRH-YSTPVDIWSVGCIFAEMVN 199
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
71-281 7.08e-03

Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. Vertebrates contain two members, LRRK1 and LRRK2, which show complementary expression in the brain. Mutations in LRRK2 are linked to both familial and sporadic forms of Parkinson's disease. The normal roles of LRRKs are not clearly defined. They may be involved in mitogen-activated protein kinase (MAPK) pathways, protein translation control, programmed cell death pathways, and cytoskeletal dynamics. The LRRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270902 [Multi-domain]  Cd Length: 275  Bit Score: 37.98  E-value: 7.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  71 RRINLEACSNEMVTFLQgELHVSKLFNHPNIVPYRATFIadNELWVVTSFMAYGSAKDLICTHFMDG--MNELAIAYILQ 148
Cdd:cd14000    43 RHLRATDAMKNFRLLRQ-ELTVLSHLHHPSIVYLLGIGI--HPLMLVLELAPLGSLDHLLQQDSRSFasLGRTLQQRIAL 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 149 GVLKALDYIHHMGYVHRSVKASHILI-SVDGKVYLsglrsNLSMISHGQRQRVVHDFPKYSVKVLPWLSPEVLQQNLQgY 227
Cdd:cd14000   120 QVADGLRYLHSAMIIYRDLKSHNVLVwTLYPNSAI-----IIKIADYGISRQCCRMGAKGSEGTPGFRAPEIARGNVI-Y 193
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1394533236 228 DAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPCLLDTSTIPAEEL 281
Cdd:cd14000   194 NEKVDVFSFGMLLYEILSGGAPMVGHLKFPNEFDIHGGLRPPLKQYECAPWPEV 247
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
89-315 9.35e-03

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


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 37.76  E-value: 9.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236  89 ELHVSKLFNHPNIVPYRATFIADNEL------WVVTSFMAYGsakdlICTHFMDGMNELAIAYILQGVLKALDYIHHMGY 162
Cdd:cd07874    66 ELVLMKCVNHKNIISLLNVFTPQKSLeefqdvYLVMELMDAN-----LCQVIQMELDHERMSYLLYQMLCGIKHLHSAGI 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 163 VHRSVKASHILISVDgkvylsglrSNLSMISHGQRQRVVHDFPKYSVKVLPWL-SPEVLQQnlQGYDAKSDIYSVGITAC 241
Cdd:cd07874   141 IHRDLKPSNIVVKSD---------CTLKILDFGLARTAGTSFMMTPYVVTRYYrAPEVILG--MGYKENVDIWSVGCIMG 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533236 242 ELANGHVPF-------------------------KDMPATQMLLE---KLNG-TVPCLLDTSTIPAEELTMSPSRSVANS 292
Cdd:cd07874   210 EMVRHKILFpgrdyidqwnkvieqlgtpcpefmkKLQPTVRNYVEnrpKYAGlTFPKLFPDSLFPADSEHNKLKASQARD 289
                         250       260
                  ....*....|....*....|....
gi 1394533236 293 GLSDSLTTS-TPRPSNGDSPSHPY 315
Cdd:cd07874   290 LLSKMLVIDpAKRISVDEALQHPY 313
 
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.
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