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Conserved domains on  [gi|255958318|ref|NP_001157670|]
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cAMP-dependent protein kinase catalytic subunit beta isoform 2 [Mus musculus]

Protein Classification

cAMP-dependent protein kinase catalytic subunit( domain architecture ID 10197742)

cAMP-dependent protein kinase catalytic subunit is a serine/threonine-protein kinase that catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
29-318 0e+00

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: 626.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVM 108
Cdd:cd14209    1 DDFDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKVVKLKQVEHTLNEKRILQAINFPFLVKLEYSFKDNSNLYMVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 109 EYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTWTLCG 188
Cdd:cd14209   81 EYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKRVKGRTWTLCG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 189 TPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKR 268
Cdd:cd14209  161 TPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKR 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 255958318 269 FGNLKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTSNFDDY 318
Cdd:cd14209  241 FGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKLKGPGDTSNFDDY 290
 
Name Accession Description Interval E-value
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
29-318 0e+00

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: 626.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVM 108
Cdd:cd14209    1 DDFDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKVVKLKQVEHTLNEKRILQAINFPFLVKLEYSFKDNSNLYMVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 109 EYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTWTLCG 188
Cdd:cd14209   81 EYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKRVKGRTWTLCG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 189 TPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKR 268
Cdd:cd14209  161 TPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKR 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 255958318 269 FGNLKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTSNFDDY 318
Cdd:cd14209  241 FGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKLKGPGDTSNFDDY 290
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
19-338 4.56e-153

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 432.70  E-value: 4.56e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  19 ENPPPSNAGLEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSF 98
Cdd:PTZ00263   8 TKPDTSSWKLSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMELSHPFIVNMMCSF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  99 KDNSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKR 178
Cdd:PTZ00263  88 QDENRVYFLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKK 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 179 VKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLR 258
Cdd:PTZ00263 168 VPDRTFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWFDGRARDLVK 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 259 NLLQVDLTKRFGNLKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTSNFDDYEEEEIR--VSITEKCGKEFC 336
Cdd:PTZ00263 248 GLLQTDHTKRLGTLKGGVADVKNHPYFHGANWDKLYARYYPAPIPVRVKSPGDTSNFEKYPDSPVDrlPPLTAAQQAEFA 327

                 ..
gi 255958318 337 EF 338
Cdd:PTZ00263 328 GF 329
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
31-285 5.98e-110

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 320.63  E-value: 5.98e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318    31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKvvKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEY 110
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKK--IKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318   111 VPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVK--GRTWTLCG 188
Cdd:smart00220  79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDpgEKLTTFVG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318   189 TPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFAD-QPIQIYEKIVSGKVRFPSH---FSSDLKDLLRNLLQVD 264
Cdd:smart00220 159 TPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDdQLLELFKKIGKPKPPFPPPewdISPEAKDLIRKLLVKD 238
                          250       260
                   ....*....|....*....|.
gi 255958318   265 LTKRFgnlknGVSDIKTHKWF 285
Cdd:smart00220 239 PEKRL-----TAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
31-285 2.43e-71

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 220.96  E-value: 2.43e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318   31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQiEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEY 110
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKD-KNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  111 VPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYlhsldliyrdlkpenllidhqgyiqvtdfgfakrvKGRTWTLCGTP 190
Cdd:pfam00069  80 VEGGSLFDLLSEKGAFSEREAKFIMKQILEGLES-----------------------------------GSSLTTFVGTP 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  191 EYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRF---PSHFSSDLKDLLRNLLQVDLTK 267
Cdd:pfam00069 125 WYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFpelPSNLSEEAKDLLKKLLKKDPSK 204
                         250
                  ....*....|....*...
gi 255958318  268 RFgnlknGVSDIKTHKWF 285
Cdd:pfam00069 205 RL-----TATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
37-271 1.16e-57

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 193.69  E-value: 1.16e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGGEM 116
Cdd:COG0515   15 LGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLVMEYVEGESL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 117 FSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKG----RTWTLCGTPEY 192
Cdd:COG0515   95 ADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGatltQTGTVVGTPGY 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 193 LAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHF----SSDLKDLLRNLLQVDLTKR 268
Cdd:COG0515  175 MAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELrpdlPPALDAIVLRALAKDPEER 254

                 ...
gi 255958318 269 FGN 271
Cdd:COG0515  255 YQS 257
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
100-234 2.63e-22

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 97.56  E-value: 2.63e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 100 DNSNLYMVMEYVPGgemfSHLRRI----GRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGF 175
Cdd:NF033483  78 DGGIPYIVMEYVDG----RTLKDYirehGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGI 153
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255958318 176 AKRVKGRTWT----LCGTPEYLAPEIIlsKGynKAV----DWWALGVLIYEMAAGYPPFFADQPIQI 234
Cdd:NF033483 154 ARALSSTTMTqtnsVLGTVHYLSPEQA--RG--GTVdarsDIYSLGIVLYEMLTGRPPFDGDSPVSV 216
 
Name Accession Description Interval E-value
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
29-318 0e+00

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: 626.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVM 108
Cdd:cd14209    1 DDFDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKVVKLKQVEHTLNEKRILQAINFPFLVKLEYSFKDNSNLYMVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 109 EYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTWTLCG 188
Cdd:cd14209   81 EYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKRVKGRTWTLCG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 189 TPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKR 268
Cdd:cd14209  161 TPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKR 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 255958318 269 FGNLKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTSNFDDY 318
Cdd:cd14209  241 FGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKLKGPGDTSNFDDY 290
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
29-318 0e+00

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: 536.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVM 108
Cdd:cd05580    1 DDFEFLKTLGTGSFGRVRLVKHKDSGKYYALKILKKAKIIKLKQVEHVLNEKRILSEVRHPFIVNLLGSFQDDRNLYMVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 109 EYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTWTLCG 188
Cdd:cd05580   81 EYVPGGELFSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAKRVKDRTYTLCG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 189 TPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKR 268
Cdd:cd05580  161 TPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKILEGKIRFPSFFDPDAKDLIKRLLVVDLTKR 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 255958318 269 FGNLKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTSNFDDY 318
Cdd:cd05580  241 LGNLKNGVEDIKNHPWFAGIDWDALLQRKIPAPYVPKVRGPGDTSNFDKY 290
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
29-320 8.35e-158

Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include human PRKX (X chromosome-encoded protein kinase), Drosophila DC2, and similar proteins. PRKX is present in many tissues including fetal and adult brain, kidney, and lung. The PRKX gene is located in the Xp22.3 subregion and has a homolog called PRKY on the Y chromosome. An abnormal interchange between PRKX aand PRKY leads to the sex reversal disorder of XX males and XY females. PRKX is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PRKX-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270763 [Multi-domain]  Cd Length: 292  Bit Score: 443.42  E-value: 8.35e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVM 108
Cdd:cd05612    1 DDFERIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPEVIRLKQEQHVHNEKRVLKEVSHPFIIRLFWTEHDQRFLYMLM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 109 EYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTWTLCG 188
Cdd:cd05612   81 EYVPGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAKKLRDRTWTLCG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 189 TPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKR 268
Cdd:cd05612  161 TPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKILAGKLEFPRHLDLYAKDLIKKLLVVDRTRR 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 255958318 269 FGNLKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTSNFDDYEE 320
Cdd:cd05612  241 LGNMKNGADDVKNHRWFKSVDWDDVPQRKLKPPIVPKVSHDGDTSNFDDYPE 292
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
19-338 4.56e-153

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 432.70  E-value: 4.56e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  19 ENPPPSNAGLEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSF 98
Cdd:PTZ00263   8 TKPDTSSWKLSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMELSHPFIVNMMCSF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  99 KDNSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKR 178
Cdd:PTZ00263  88 QDENRVYFLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKK 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 179 VKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLR 258
Cdd:PTZ00263 168 VPDRTFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWFDGRARDLVK 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 259 NLLQVDLTKRFGNLKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTSNFDDYEEEEIR--VSITEKCGKEFC 336
Cdd:PTZ00263 248 GLLQTDHTKRLGTLKGGVADVKNHPYFHGANWDKLYARYYPAPIPVRVKSPGDTSNFEKYPDSPVDrlPPLTAAQQAEFA 327

                 ..
gi 255958318 337 EF 338
Cdd:PTZ00263 328 GF 329
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
37-285 6.70e-147

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: 413.84  E-value: 6.70e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGGEM 116
Cdd:cd05123    1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIIKRKEVEHTLNERNILERVNHPFIVKLHYAFQTEEKLYLVLDYVPGGEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 117 FSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKG---RTWTLCGTPEYL 193
Cdd:cd05123   81 FSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELSSdgdRTYTFCGTPEYL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 194 APEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLk 273
Cdd:cd05123  161 APEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKSPLKFPEYVSPEAKSLISGLLQKDPTKRLGSG- 239
                        250
                 ....*....|..
gi 255958318 274 nGVSDIKTHKWF 285
Cdd:cd05123  240 -GAEEIKAHPFF 250
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
37-290 3.91e-119

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: 344.21  E-value: 3.91e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGGEM 116
Cdd:cd05572    1 LGVGGFGRVELVQLKSKGRTFALKCVKKRHIVQTRQQEHIFSEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLGGEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 117 FSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKG--RTWTLCGTPEYLA 194
Cdd:cd05572   81 WTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKKLGSgrKTWTFCGTPEYVA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 195 PEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQ--PIQIYEKIVSG--KVRFPSHFSSDLKDLLRNLLQVDLTKRFG 270
Cdd:cd05572  161 PEIILNKGYDFSVDYWSLGILLYELLTGRPPFGGDDedPMKIYNIILKGidKIEFPKYIDKNAKNLIKQLLRRNPEERLG 240
                        250       260
                 ....*....|....*....|
gi 255958318 271 NLKNGVSDIKTHKWFATTDW 290
Cdd:cd05572  241 YLKGGIRDIKKHKWFEGFDW 260
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
35-330 1.20e-117

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, classical PKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. Novel PKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. Also included in this subfamily are the PKC-like proteins, called PKNs. The PKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 342.27  E-value: 1.20e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRIL-QAVEFPFLVRLEYSFKDNSNLYMVMEYVPG 113
Cdd:cd05570    1 KVLGKGSFGKVMLAERKKTDELYAIKVLKKEVIIEDDDVECTMTEKRVLaLANRHPFLTGLHACFQTEDRLYFVMEYVNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 114 GEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAK---RVKGRTWTLCGTP 190
Cdd:cd05570   81 GDLMFHIQRARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMCKegiWGGNTTSTFCGTP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 191 EYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFG 270
Cdd:cd05570  161 DYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAILNDEVLYPRWLSREAVSILKGLLTKDPARRLG 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255958318 271 NLKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTSNFD-DYEEEEIRVSITEK 330
Cdd:cd05570  241 CGPKGEADIKAHPFFRNIDWDKLEKKEVEPPFKPKVKSPRDTSNFDpEFTSESPRLTPVDS 301
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
35-317 1.62e-116

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


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 339.72  E-value: 1.62e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGG 114
Cdd:cd05571    1 KVLGKGTFGKVILCREKATGELYAIKILKKEVIIAKDEVAHTLTENRVLQNTRHPFLTSLKYSFQTNDRLCFVMEYVNGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 115 EMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAK---RVKGRTWTLCGTPE 191
Cdd:cd05571   81 ELFFHLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLCKeeiSYGATTKTFCGTPE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 192 YLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGN 271
Cdd:cd05571  161 YLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELILMEEVRFPSTLSPEAKSLLAGLLKKDPKKRLGG 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 255958318 272 LKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTSNFDD 317
Cdd:cd05571  241 GPRDAKEIMEHPFFASINWDDLYQKKIPPPFKPQVTSETDTRYFDE 286
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
35-327 1.95e-114

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGKs are activated by insulin and growth factors via phosphoinositide 3-kinase and PDK1. They activate ion channels, ion carriers, and the Na-K-ATPase, as well as regulate the activity of enzymes and transcription factors. SGKs play important roles in transport, hormone release, neuroexcitability, cell proliferation, and apoptosis. There are three isoforms of SGK, named SGK1, SGK2, and SGK3 (also called cytokine-independent survival kinase CISK). The SGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270727 [Multi-domain]  Cd Length: 323  Bit Score: 334.29  E-value: 1.95e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRIL-QAVEFPFLVRLEYSFKDNSNLYMVMEYVPG 113
Cdd:cd05575    1 KVIGKGSFGKVLLARHKAEGKLYAVKVLQKKAILKRNEVKHIMAERNVLlKNVKHPFLVGLHYSFQTKDKLYFVLDYVNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 114 GEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAK---RVKGRTWTLCGTP 190
Cdd:cd05575   81 GELFFHLQRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLCKegiEPSDTTSTFCGTP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 191 EYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFG 270
Cdd:cd05575  161 EYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRDTAEMYDNILHKPLRLRTNVSPSARDLLEGLLQKDRTKRLG 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 255958318 271 NlKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTSNFD-DYEEEEIRVSI 327
Cdd:cd05575  241 S-GNDFLEIKNHSFFRPINWDDLEAKKIPPPFNPNVSGPLDLRNIDpEFTREPVPASV 297
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
31-285 5.98e-110

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 320.63  E-value: 5.98e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318    31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKvvKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEY 110
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKK--IKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318   111 VPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVK--GRTWTLCG 188
Cdd:smart00220  79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDpgEKLTTFVG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318   189 TPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFAD-QPIQIYEKIVSGKVRFPSH---FSSDLKDLLRNLLQVD 264
Cdd:smart00220 159 TPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDdQLLELFKKIGKPKPPFPPPewdISPEAKDLIRKLLVKD 238
                          250       260
                   ....*....|....*....|.
gi 255958318   265 LTKRFgnlknGVSDIKTHKWF 285
Cdd:smart00220 239 PEKRL-----TAEEALQHPFF 254
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
29-334 3.67e-109

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 321.93  E-value: 3.67e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKaTEQY--YAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYM 106
Cdd:PTZ00426  30 EDFNFIRTLGTGSFGRVILATYK-NEDFppVAIKRFEKSKIIKQKQVDHVFSERKILNYINHPFCVNLYGSFKDESYLYL 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 107 VMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTWTL 186
Cdd:PTZ00426 109 VLEFVIGGEFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGFAKVVDTRTYTL 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 187 CGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLT 266
Cdd:PTZ00426 189 CGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPFYANEPLLIYQKILEGIIYFPKFLDNNCKHLMKKLLSHDLT 268
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255958318 267 KRFGNLKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTSNFDDYEEEeirVSITEKCGKE 334
Cdd:PTZ00426 269 KRYGNLKKGAQNVKEHPWFGNIDWVSLLHKNVEVPYKPKYKNVFDSSNFERVQED---LTIADKITNE 333
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
29-323 1.19e-107

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: 318.07  E-value: 1.19e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVM 108
Cdd:cd05573    1 DDFEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILRKSDMLKREQIAHVRAERDILADADSPWIVRLHYAFQDEDHLYLVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 109 EYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRV--------- 179
Cdd:cd05573   81 EYMPGGDLMNLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCTKMnksgdresy 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 180 --------------KGRTW---------TLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYE 236
Cdd:cd05573  161 lndsvntlfqdnvlARRRPhkqrrvraySAVGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLYGFPPFYSDSLVETYS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 237 KIVSGKV--RFPSH--FSSDLKDLLRNLLqVDLTKRFGNLKngvsDIKTHKWFATTDWIAIYQRKveAPFIPKFRGSGDT 312
Cdd:cd05573  241 KIMNWKEslVFPDDpdVSPEAIDLIRRLL-CDPEDRLGSAE----EIKAHPFFKGIDWENLRESP--PPFVPELSSPTDT 313
                        330
                 ....*....|.
gi 255958318 313 SNFDDYEEEEI 323
Cdd:cd05573  314 SNFDDFEDDLL 324
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
29-334 2.39e-106

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: 313.78  E-value: 2.39e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVM 108
Cdd:cd05599    1 EDFEPLKVIGRGAFGEVRLVRKKDTGHVYAMKKLRKSEMLEKEQVAHVRAERDILAEADNPWVVKLYYSFQDEENLYLIM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 109 EYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGR--TWTL 186
Cdd:cd05599   81 EFLPGGDMMTLLMKKDTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGLCTGLKKShlAYST 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 187 CGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGK--VRFPS--HFSSDLKDLLRNLLq 262
Cdd:cd05599  161 VGTPDYIAPEVFLQKGYGKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKIMNWRetLVFPPevPISPEAKDLIERLL- 239
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255958318 263 VDLTKRFGNlkNGVSDIKTHKWFATTDWIAIYQRKveAPFIPKFRGSGDTSNFDDYEEEEIRVSITEKCGKE 334
Cdd:cd05599  240 CDAEHRLGA--NGVEEIKSHPFFKGVDWDHIRERP--APILPEVKSILDTSNFDEFEEVDLQIPSSPEAGKD 307
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
35-316 2.57e-106

Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p70S6K (or S6K) contains only one catalytic kinase domain, unlike p90 ribosomal S6 kinases (RSKs). It acts as a downstream effector of the STK mTOR (mammalian Target of Rapamycin) and plays a role in the regulation of the translation machinery during protein synthesis. p70S6K also plays a pivotal role in regulating cell size and glucose homeostasis. Its targets include S6, the translation initiation factor eIF3, and the insulin receptor substrate IRS-1, among others. Mammals contain two isoforms of p70S6K, named S6K1 and S6K2 (or S6K-beta). The p70S6K subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 313.96  E-value: 2.57e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKAT---EQYYAMKILDKQKVVK-LKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEY 110
Cdd:cd05584    2 KVLGKGGYGKVFQVRKTTGsdkGKIFAMKVLKKASIVRnQKDTAHTKAERNILEAVKHPFIVDLHYAFQTGGKLYLILEY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 111 VPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAK-RVKG--RTWTLC 187
Cdd:cd05584   82 LSGGELFMHLEREGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLCKeSIHDgtVTHTFC 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 188 GTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTK 267
Cdd:cd05584  162 GTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKGKLNLPPYLTNEARDLLKKLLKRNVSS 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 255958318 268 RFGNLKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTSNFD 316
Cdd:cd05584  242 RLGSGPGDAEEIKAHPFFRHINWDDLLAKKVEPPFKPLLQSEEDVSQFD 290
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
40-290 2.10e-103

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: 304.52  E-value: 2.10e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  40 GSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGGEMFSH 119
Cdd:cd05579    4 GAYGRVYLAKKKSTGDLYAIKVIKKRDMIRKNQVDSVLAERNILSQAQNPFVVKLYYSFQGKKNLYLVMEYLPGGDLYSL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 120 LRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAK-----RVKGRTW---------- 184
Cdd:cd05579   84 LENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSKvglvrRQIKLSIqkksngapek 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 185 ---TLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHF--SSDLKDLLRN 259
Cdd:cd05579  164 edrRIVGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNILNGKIEWPEDPevSDEAKDLISK 243
                        250       260       270
                 ....*....|....*....|....*....|.
gi 255958318 260 LLQVDLTKRFGnlKNGVSDIKTHKWFATTDW 290
Cdd:cd05579  244 LLTPDPEKRLG--AKGIEEIKNHPFFKGIDW 272
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
35-317 8.22e-101

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: 300.00  E-value: 8.22e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGG 114
Cdd:cd05595    1 KLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVAHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 115 EMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKR--VKGRTW-TLCGTPE 191
Cdd:cd05595   81 ELFFHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEgiTDGATMkTFCGTPE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 192 YLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGN 271
Cdd:cd05595  161 YLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLAGLLKKDPKQRLGG 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 255958318 272 LKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTSNFDD 317
Cdd:cd05595  241 GPSDAKEVMEHRFFLSINWQDVVQKKLLPPFKPQVTSEVDTRYFDD 286
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
37-317 1.14e-100

Catalytic domain of Yeast Protein Kinase 1-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 proteins with similarity to the AGC STKs, Saccharomyces cerevisiae YPK1 and Schizosaccharomyces pombe Gad8p. YPK1 is required for cell growth and acts as a downstream kinase in the sphingolipid-mediated signaling pathway of yeast. It also plays a role in efficient endocytosis and in the maintenance of cell wall integrity. Gad8p is a downstream target of Tor1p, the fission yeast homolog of mTOR. It plays a role in cell growth and sexual development. The YPK1-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: 270737 [Multi-domain]  Cd Length: 313  Bit Score: 299.10  E-value: 1.14e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGGEM 116
Cdd:cd05585    2 IGKGSFGKVMQVRKKDTSRIYALKTIRKAHIVSRSEVTHTLAERTVLAQVDCPFIVPLKFSFQSPEKLYLVLAFINGGEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 117 FSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAK---RVKGRTWTLCGTPEYL 193
Cdd:cd05585   82 FHHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLCKlnmKDDDKTNTFCGTPEYL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 194 APEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGnlK 273
Cdd:cd05585  162 APELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQEPLRFPDGFDRDAKDLLIGLLNRDPTKRLG--Y 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 255958318 274 NGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTSNFDD 317
Cdd:cd05585  240 NGAQEIKNHPFFDQIDWKRLLMKKIQPPFKPAVENAIDTSNFDE 283
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
30-324 5.29e-100

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: 298.08  E-value: 5.29e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  30 DFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVME 109
Cdd:cd05598    2 MFEKIKTIGVGAFGEVSLVRKKDTNALYAMKTLRKKDVLKRNQVAHVKAERDILAEADNEWVVKLYYSFQDKENLYFVMD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 110 YVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAkrvKGRTWT---- 185
Cdd:cd05598   82 YIPGGDLMSLLIKKGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLC---TGFRWThdsk 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 186 ------LCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGK--VRFP--SHFSSDLKD 255
Cdd:cd05598  159 yylahsLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFLAQTPAETQLKVINWRttLKIPheANLSPEAKD 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255958318 256 LLRNLLqVDLTKRFGnlKNGVSDIKTHKWFATTDWiaIYQRKVEAPFIPKFRGSGDTSNFDDYEEEEIR 324
Cdd:cd05598  239 LILRLC-CDAEDRLG--RNGADEIKAHPFFAGIDW--EKLRKQKAPYIPTIRHPTDTSNFDPVDPEKLR 302
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
35-328 2.52e-98

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: 293.41  E-value: 2.52e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRIL-QAVEFPFLVRLEYSFKDNSNLYMVMEYVPG 113
Cdd:cd05603    1 KVIGKGSFGKVLLAKRKCDGKFYAVKVLQKKTILKKKEQNHIMAERNVLlKNLKHPFLVGLHYSFQTSEKLYFVLDYVNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 114 GEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAK---RVKGRTWTLCGTP 190
Cdd:cd05603   81 GELFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKegmEPEETTSTFCGTP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 191 EYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFG 270
Cdd:cd05603  161 EYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFYSRDVSQMYDNILHKPLHLPGGKTVAACDLLQGLLHKDQRRRLG 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 255958318 271 NlKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTSNFD-DYEEEEIRVSIT 328
Cdd:cd05603  241 A-KADFLEIKNHVFFSPINWDDLYHKRITPPYNPNVAGPADLRHFDpEFTQEAVPHSVG 298
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
30-311 1.90e-96

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: 288.37  E-value: 1.90e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  30 DFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVME 109
Cdd:cd05574    2 HFKKIKLLGKGDVGRVYLVRLKGTGKLFAMKVLDKEEMIKRNKVKRVLTEREILATLDHPFLPTLYASFQTSTHLCFVMD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 110 YVPGGEMFSHLRR--IGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDF-------------- 173
Cdd:cd05574   82 YCPGGELFRLLQKqpGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFdlskqssvtpppvr 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 174 ------GFAKRVKG------------RTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIY 235
Cdd:cd05574  162 kslrkgSRRSSVKSieketfvaepsaRSNSFVGTEEYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGTTPFKGSNRDETF 241
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255958318 236 EKIVSGKVRFPSH--FSSDLKDLLRNLLQVDLTKRFGNlKNGVSDIKTHKWFATTDWIAIyqRKVEAPFIPKFRGSGD 311
Cdd:cd05574  242 SNILKKELTFPESppVSSEAKDLIRKLLVKDPSKRLGS-KRGASEIKRHPFFRGVNWALI--RNMTPPIIPRPDDPID 316
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
35-330 3.99e-96

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


Pssm-ID: 270744 [Multi-domain]  Cd Length: 320  Bit Score: 287.74  E-value: 3.99e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQ-AVEFPFLVRLEYSFKDNSNLYMVMEYVPG 113
Cdd:cd05592    1 KVLGKGSFGKVMLAELKGTNQYFAIKALKKDVVLEDDDVECTMIERRVLAlASQHPFLTHLFCTFQTESHLFFVMEYLNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 114 GEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAK-RVKG--RTWTLCGTP 190
Cdd:cd05592   81 GDLMFHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMCKeNIYGenKASTFCGTP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 191 EYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFG 270
Cdd:cd05592  161 DYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSICNDTPHYPRWLTKEAASCLSLLLERNPEKRLG 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255958318 271 NLKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTSNFD-DYEEEEIRVSITEK 330
Cdd:cd05592  241 VPECPAGDIRDHPFFKTIDWDKLERREIDPPFKPKVKSANDVSNFDpDFTMEKPVLTPVDK 301
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
29-285 6.36e-95

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: 283.34  E-value: 6.36e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVM 108
Cdd:cd05581    1 NDFKFGKPLGEGSYSTVVLAKEKETGKEYAIKVLDKRHIIKEKKVKYVTIEKEVLSRLAHPGIVKLYYTFQDESKLYFVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 109 EYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKG------- 181
Cdd:cd05581   81 EYAPNGDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGTAKVLGPdsspest 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 182 -------------RTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSH 248
Cdd:cd05581  161 kgdadsqiaynqaRAASFVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQKIVKLEYEFPEN 240
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 255958318 249 FSSDLKDLLRNLLQVDLTKRFG-NLKNGVSDIKTHKWF 285
Cdd:cd05581  241 FPPDAKDLIQKLLVLDPSKRLGvNENGGYDELKAHPFF 278
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
37-317 1.56e-94

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


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 283.81  E-value: 1.56e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAV---EFPFLVRLEYSFKDNSNLYMVMEYVPG 113
Cdd:cd05589    7 LGRGHFGKVLLAEYKPTGELFAIKALKKGDIIARDEVESLMCEKRIFETVnsaRHPFLVNLFACFQTPEHVCFVMEYAAG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 114 GEMFSHLRRiGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKG---RTWTLCGTP 190
Cdd:cd05589   87 GDLMMHIHE-DVFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGfgdRTSTFCGTP 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 191 EYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFG 270
Cdd:cd05589  166 EFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSTEAISIMRRLLRKNPERRLG 245
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 255958318 271 NLKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTSNFDD 317
Cdd:cd05589  246 ASERDAEDVKKQPFFRNIDWEALLARKIKPPFVPTIKSPEDVSNFDE 292
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
30-327 2.03e-94

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: 284.22  E-value: 2.03e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  30 DFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRIL-QAVEFPFLVRLEYSFKDNSNLYMVM 108
Cdd:cd05602    8 DFHFLKVIGKGSFGKVLLARHKSDEKFYAVKVLQKKAILKKKEEKHIMSERNVLlKNVKHPFLVGLHFSFQTTDKLYFVL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 109 EYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAK---RVKGRTWT 185
Cdd:cd05602   88 DYINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKeniEPNGTTST 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 186 LCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDL 265
Cdd:cd05602  168 FCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQLKPNITNSARHLLEGLLQKDR 247
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255958318 266 TKRFGnLKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTSNFD-DYEEEEIRVSI 327
Cdd:cd05602  248 TKRLG-AKDDFTEIKNHIFFSPINWDDLINKKITPPFNPNVSGPNDLRHFDpEFTDEPVPNSI 309
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
37-285 7.30e-94

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: 280.05  E-value: 7.30e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKH---KATEQYYAMKILDKQKVV-KLKQIEHTLNEKRILQAV-EFPFLVRLEYSFKDNSNLYMVMEYV 111
Cdd:cd05583    2 LGTGAYGKVFLVRKvggHDAGKLYAMKVLKKATIVqKAKTAEHTMTERQVLEAVrQSPFLVTLHYAFQTDAKLHLILDYV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 112 PGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRV----KGRTWTLC 187
Cdd:cd05583   82 NGGELFTHLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLSKEFlpgeNDRAYSFC 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 188 GTPEYLAPEIILSK--GYNKAVDWWALGVLIYEMAAGYPPFFAD----QPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLL 261
Cdd:cd05583  162 GTIEYMAPEVVRGGsdGHDKAVDWWSLGVLTYELLTGASPFTVDgernSQSEISKRILKSHPPIPKTFSAEAKDFILKLL 241
                        250       260
                 ....*....|....*....|....
gi 255958318 262 QVDLTKRFGNLKNGVSDIKTHKWF 285
Cdd:cd05583  242 EKDPKKRLGAGPRGAHEIKEHPFF 265
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
35-330 4.36e-93

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


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 280.05  E-value: 4.36e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFP-FLVRLEYSFKDNSNLYMVMEYVPG 113
Cdd:cd05587    2 MVLGKGSFGKVMLAERKGTDELYAIKILKKDVIIQDDDVECTMVEKRVLALSGKPpFLTQLHSCFQTMDRLYFVMEYVNG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 114 GEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAK-RVKG--RTWTLCGTP 190
Cdd:cd05587   82 GDLMYHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCKeGIFGgkTTRTFCGTP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 191 EYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFG 270
Cdd:cd05587  162 DYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSICKGLLTKHPAKRLG 241
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255958318 271 NLKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTSNFD-DYEEEEIRVSITEK 330
Cdd:cd05587  242 CGPTGERDIKEHPFFRRIDWEKLERREIQPPFKPKIKSPRDAENFDkEFTKEPPVLTPTDK 302
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
37-316 6.89e-93

Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Sck1 and similar fungal proteins. Sck1 plays a role in trehalase activation triggered by glucose and a nitrogen source. Trehalase catalyzes the cleavage of the disaccharide trehalose to glucose. Trehalose, as a carbohydrate reserve and stress metabolite, plays an important role in the response of yeast to environmental changes. The Sck1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 279.84  E-value: 6.89e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAV---EFPFLVRLEYSFKDNSNLYMVMEYVPG 113
Cdd:cd05586    1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIVAKKEVAHTIGERNILVRTaldESPFIVGLKFSFQTPTDLYLVTDYMSG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 114 GEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAK---RVKGRTWTLCGTP 190
Cdd:cd05586   81 GELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLSKadlTDNKTTNTFCGTT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 191 EYLAPEIIL-SKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSH-FSSDLKDLLRNLLQVDLTKR 268
Cdd:cd05586  161 EYLAPEVLLdEKGYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIAFGKVRFPKDvLSDEGRSFVKGLLNRNPKHR 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 255958318 269 FGNLKNGVsDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTSNFD 316
Cdd:cd05586  241 LGAHDDAV-ELKEHPFFADIDWDLLSKKKITPPFKPIVDSDTDVSNFD 287
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
30-315 5.26e-91

N-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: 270765 [Multi-domain]  Cd Length: 332  Bit Score: 275.26  E-value: 5.26e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  30 DFERKKTLGTGSFGRVMLVKHKA---TEQYYAMKILDKQKVV-KLKQIEHTLNEKRILQAV-EFPFLVRLEYSFKDNSNL 104
Cdd:cd05614    1 NFELLKVLGTGAYGKVFLVRKVSghdANKLYAMKVLRKAALVqKAKTVEHTRTERNVLEHVrQSPFLVTLHYAFQTDAKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 105 YMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRV----K 180
Cdd:cd05614   81 HLILDYVSGGELFTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLSKEFlteeK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 181 GRTWTLCGTPEYLAPEIILSK-GYNKAVDWWALGVLIYEMAAGYPPFF----ADQPIQIYEKIVSGKVRFPSHFSSDLKD 255
Cdd:cd05614  161 ERTYSFCGTIEYMAPEIIRGKsGHGKAVDWWSLGILMFELLTGASPFTlegeKNTQSEVSRRILKCDPPFPSFIGPVARD 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 256 LLRNLLQVDLTKRFGNLKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTSNF 315
Cdd:cd05614  241 LLQKLLCKDPKKRLGAGPQGAQEIKEHPFFKGLDWEALALRKVNPPFRPSIRSELDVGNF 300
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
35-327 6.65e-91

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK3 (also called cytokine-independent survival kinase or CISK) is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. The SGK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270755 [Multi-domain]  Cd Length: 326  Bit Score: 274.92  E-value: 6.65e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRIL-QAVEFPFLVRLEYSFKDNSNLYMVMEYVPG 113
Cdd:cd05604    2 KVIGKGSFGKVLLAKRKRDGKYYAVKVLQKKVILNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTDKLYFVLDFVNG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 114 GEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKR---VKGRTWTLCGTP 190
Cdd:cd05604   82 GELFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCKEgisNSDTTTTFCGTP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 191 EYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFG 270
Cdd:cd05604  162 EYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENILHKPLVLRPGISLTAWSILEELLEKDRQLRLG 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 255958318 271 nLKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTSNFD-DYEEEEIRVSI 327
Cdd:cd05604  242 -AKEDFLEIKNHPFFESINWTDLVQKKIPPPFNPNVNGPDDISNFDaEFTEEMVPYSV 298
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
22-317 2.77e-90

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


Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 274.21  E-value: 2.77e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  22 PPSNAGLEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDN 101
Cdd:cd05594   18 PKHKVTMNDFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTH 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 102 SNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHS-LDLIYRDLKPENLLIDHQGYIQVTDFGFAKR-- 178
Cdd:cd05594   98 DRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEgi 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 179 VKGRTW-TLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLL 257
Cdd:cd05594  178 KDGATMkTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLSPEAKSLL 257
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 258 RNLLQVDLTKRFGNLKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTSNFDD 317
Cdd:cd05594  258 SGLLKKDPKQRLGGGPDDAKEIMQHKFFAGIVWQDVYEKKLVPPFKPQVTSETDTRYFDE 317
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
30-269 5.78e-90

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: 269.73  E-value: 5.78e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  30 DFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVvKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVME 109
Cdd:cd05117    1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKL-KSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 110 YVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLI---DHQGYIQVTDFGFAKRVKG--RTW 184
Cdd:cd05117   80 LCTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLaskDPDSPIKIIDFGLAKIFEEgeKLK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 185 TLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPS----HFSSDLKDLLRNL 260
Cdd:cd05117  160 TVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFDSpewkNVSEEAKDLIKRL 239

                 ....*....
gi 255958318 261 LQVDLTKRF 269
Cdd:cd05117  240 LVVDPKKRL 248
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
35-284 1.32e-88

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: 265.92  E-value: 1.32e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKlKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGG 114
Cdd:cd14003    6 KTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKE-EIEEKIKREIEIMKLLNHPNIIKLYEVIETENKIYLVMEYASGG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 115 EMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKG--RTWTLCGTPEY 192
Cdd:cd14003   85 ELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNEFRGgsLLKTFCGTPAY 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 193 LAPEIILSKGYN-KAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFgn 271
Cdd:cd14003  165 AAPEVLLGRKYDgPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYPIPSHLSPDARDLIRRMLVVDPSKRI-- 242
                        250
                 ....*....|...
gi 255958318 272 lknGVSDIKTHKW 284
Cdd:cd14003  243 ---TIEEILNHPW 252
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
28-330 3.93e-88

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: 268.49  E-value: 3.93e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  28 LEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMV 107
Cdd:cd05593   14 MNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFV 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 108 MEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKR---VKGRTW 184
Cdd:cd05593   94 MEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEgitDAATMK 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 185 TLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVD 264
Cdd:cd05593  174 TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSADAKSLLSGLLIKD 253
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255958318 265 LTKRFGNLKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTSNFD-DYEEEEIRVSITEK 330
Cdd:cd05593  254 PNKRLGGGPDDAKEIMRHSFFTGVNWQDVYDKKLVPPFKPQVTSETDTRYFDeEFTAQTITITPPEK 320
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
30-318 1.36e-87

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG, and in most cases, phosphatidylserine (PS) for activation. The cPKC-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 266.09  E-value: 1.36e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  30 DFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQ-AVEFPFLVRLEYSFKDNSNLYMVM 108
Cdd:cd05616    1 DFNFLMVLGKGSFGKVMLAERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLAlSGKPPFLTQLHSCFQTMDRLYFVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 109 EYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKR--VKG-RTWT 185
Cdd:cd05616   81 EYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKEniWDGvTTKT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 186 LCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDL 265
Cdd:cd05616  161 FCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHP 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 255958318 266 TKRFGNLKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSgDTSNFDDY 318
Cdd:cd05616  241 GKRLGCGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPKACGR-NAENFDRF 292
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
30-284 3.58e-87

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: 262.41  E-value: 3.58e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  30 DFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVME 109
Cdd:cd14007    1 DFEIGKPLGKGKFGNVYLAREKKSGFIVALKVISKSQLQKSGLEHQLRREIEIQSHLRHPNILRLYGYFEDKKRIYLILE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 110 YVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRV--KGRTwTLC 187
Cdd:cd14007   81 YAPNGELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWSVHApsNRRK-TFC 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 188 GTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTK 267
Cdd:cd14007  160 GTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNVDIKFPSSVSPEAKDLISKLLQKDPSK 239
                        250
                 ....*....|....*..
gi 255958318 268 RFgnlknGVSDIKTHKW 284
Cdd:cd14007  240 RL-----SLEQVLNHPW 251
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
12-322 4.44e-87

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: 265.78  E-value: 4.44e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  12 EDFLRKWENPPPSNAGL----EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVE 87
Cdd:cd05596    5 ENFLNRYEKPVNEITKLrmnaEDFDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLLSKFEMIKRSDSAFFWEERDIMAHAN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  88 FPFLVRLEYSFKDNSNLYMVMEYVPGGEMFSHLRRIgRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGY 167
Cdd:cd05596   85 SEWIVQLHYAFQDDKYLYMVMDYMPGGDLVNLMSNY-DVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGH 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 168 IQVTDFGFAKRV----KGRTWTLCGTPEYLAPEIILSKG----YNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIV 239
Cdd:cd05596  164 LKLADFGTCMKMdkdgLVRSDTAVGTPDYISPEVLKSQGgdgvYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYGKIM 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 240 SGK--VRFPS--HFSSDLKDLLRNLLqVDLTKRFGnlKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTSNF 315
Cdd:cd05596  244 NHKnsLQFPDdvEISKDAKSLICAFL-TDREVRLG--RNGIEEIKAHPFFKNDQWTWDNIRETVPPVVPELSSDIDTSNF 320

                 ....*..
gi 255958318 316 DDYEEEE 322
Cdd:cd05596  321 DDIEEDE 327
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
31-285 7.30e-87

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: 261.81  E-value: 7.30e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEY 110
Cdd:cd05578    2 FQILRVIGKGSFGKVCIVQKKDTKKMFAMKYMNKQKCIEKDSVRNVLNELEILQELEHPFLVNLWYSFQDEEDMYMVVDL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 111 VPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTWT--LCG 188
Cdd:cd05578   82 LLGGDLRYHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIATKLTDGTLAtsTSG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 189 TPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFF--ADQPI-QIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDL 265
Cdd:cd05578  162 TKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEihSRTSIeEIRAKFETASVLYPAGWSEEAIDLINKLLERDP 241
                        250       260
                 ....*....|....*....|
gi 255958318 266 TKRFGNLKngvsDIKTHKWF 285
Cdd:cd05578  242 QKRLGDLS----DLKNHPYF 257
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
35-322 4.09e-86

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: 262.54  E-value: 4.09e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQ-AVEFPFLVRLEYSFKDNSNLYMVMEYVPG 113
Cdd:cd05590    1 RVLGKGSFGKVMLARLKESGRLYAVKVLKKDVILQDDDVECTMTEKRILSlARNHPFLTQLYCCFQTPDRLFFVMEFVNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 114 GEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAK---RVKGRTWTLCGTP 190
Cdd:cd05590   81 GDLMFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKegiFNGKTTSTFCGTP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 191 EYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFG 270
Cdd:cd05590  161 DYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPTWLSQDAVDILKAFMTKNPTMRLG 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 255958318 271 NL-KNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTSNFD-DYEEEE 322
Cdd:cd05590  241 SLtLGGEEAILRHPFFKELDWEKLNRRQIEPPFRPRIKSREDVSNFDpDFIKED 294
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
35-322 7.11e-86

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 261.66  E-value: 7.11e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQ-AVEFPFLVRLEYSFKDNSNLYMVMEYVPG 113
Cdd:cd05591    1 KVLGKGSFGKVMLAERKGTDEVYAIKVLKKDVILQDDDVDCTMTEKRILAlAAKHPFLTALHSCFQTKDRLFFVMEYVNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 114 GEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKR--VKGR-TWTLCGTP 190
Cdd:cd05591   81 GDLMFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgiLNGKtTTTFCGTP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 191 EYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFG 270
Cdd:cd05591  161 DYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPAKRLG 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 255958318 271 NLK--NGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTSNFD-DYEEEE 322
Cdd:cd05591  241 CVAsqGGEDAIRQHPFFREIDWEALEQRKVKPPFKPKIKTKRDANNFDqDFTKEE 295
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
29-335 1.45e-85

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: 261.09  E-value: 1.45e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILdkQKVVKLKQIEHTL--NEKRILQAVEFPFLVRLEYSFKDNSNLYM 106
Cdd:cd05601    1 KDFEVKNVIGRGHFGEVQVVKEKATGDIYAMKVL--KKSETLAQEEVSFfeEERDIMAKANSPWITKLQYAFQDSENLYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 107 VMEYVPGGEMFSHL-RRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRV---KGR 182
Cdd:cd05601   79 VMEYHPGGDLLSLLsRYDDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGSAAKLssdKTV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 183 TWTL-CGTPEYLAPEIILSKGYNKA------VDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGK--VRFPSHF--SS 251
Cdd:cd05601  159 TSKMpVGTPDYIAPEVLTSMNGGSKgtygveCDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNIMNFKkfLKFPEDPkvSE 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 252 DLKDLLRNLLQvDLTKRFgnlknGVSDIKTHKWFATTDWIAIyqRKVEAPFIPKFRGSGDTSNFDDYEEE-EIRVSITEK 330
Cdd:cd05601  239 SAVDLIKGLLT-DAKERL-----GYEGLCCHPFFSGIDWNNL--RQTVPPFVPTLTSDDDTSNFDEFEPKkTRPSYENFN 310

                 ....*
gi 255958318 331 CGKEF 335
Cdd:cd05601  311 KSKGF 315
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
35-316 9.06e-83

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


Pssm-ID: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 253.48  E-value: 9.06e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKH---KATEQYYAMKILdKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYV 111
Cdd:cd05582    1 KVLGQGSFGKVFLVRKitgPDAGTLYAMKVL-KKATLKVRDRVRTKMERDILADVNHPFIVKLHYAFQTEGKLYLILDFL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 112 PGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRV---KGRTWTLCG 188
Cdd:cd05582   80 RGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKESidhEKKAYSFCG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 189 TPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKR 268
Cdd:cd05582  160 TVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRALFKRNPANR 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 255958318 269 FGNLKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTSNFD 316
Cdd:cd05582  240 LGAGPDGVEEIKRHPFFATIDWNKLYRKEIKPPFKPAVSRPDDTFYFD 287
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
28-330 2.39e-81

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


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 250.61  E-value: 2.39e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  28 LEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQ-AVEFPFLVRLEYSFKDNSNLYM 106
Cdd:cd05619    4 IEDFVLHKMLGKGSFGKVFLAELKGTNQFFAIKALKKDVVLMDDDVECTMVEKRVLSlAWEHPFLTHLFCTFQTKENLFF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 107 VMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRV---KGRT 183
Cdd:cd05619   84 VMEYLNGGDLMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKENmlgDAKT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 184 WTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQV 263
Cdd:cd05619  164 STFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSIRMDNPFYPRWLEKEAKDILVKLFVR 243
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255958318 264 DLTKRFGnlknGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTSNFD-DYEEEEIRVSITEK 330
Cdd:cd05619  244 EPERRLG----VRGDIRQHPFFREINWEALEEREIEPPFKPKVKSPFDCSNFDkEFLNEKPRLSFADR 307
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
30-290 2.70e-81

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: 248.47  E-value: 2.70e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  30 DFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVME 109
Cdd:cd05609    1 DFETIKLISNGAYGAVYLVRHRETRQRFAMKKINKQNLILRNQIQQVFVERDILTFAENPFVVSMYCSFETKRHLCMVME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 110 YVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAK-RVKGRTWTL-- 186
Cdd:cd05609   81 YVEGGDCATLLKNIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLSKiGLMSLTTNLye 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 187 ---------------CGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSH--- 248
Cdd:cd05609  161 ghiekdtrefldkqvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEIEWPEGdda 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 255958318 249 FSSDLKDLLRNLLQVDLTKRFGNLknGVSDIKTHKWFATTDW 290
Cdd:cd05609  241 LPDDAQDLITRLLQQNPLERLGTG--GAEEVKQHPFFQDLDW 280
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
25-318 3.87e-81

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. The cPKC-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270766 [Multi-domain]  Cd Length: 341  Bit Score: 250.30  E-value: 3.87e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  25 NAGLEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFP-FLVRLEYSFKDNSN 103
Cdd:cd05615    6 RVRLTDFNFLMVLGKGSFGKVMLAERKGSDELYAIKILKKDVVIQDDDVECTMVEKRVLALQDKPpFLTQLHSCFQTVDR 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 104 LYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKR--VKG 181
Cdd:cd05615   86 LYFVMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCKEhmVEG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 182 -RTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNL 260
Cdd:cd05615  166 vTTRTFCGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSICKGL 245
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 255958318 261 LQVDLTKRFGNLKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGdTSNFDDY 318
Cdd:cd05615  246 MTKHPAKRLGCGPEGERDIREHAFFRRIDWDKLENREIQPPFKPKVCGKG-AENFDKF 302
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
35-330 2.13e-80

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. It slows down cell proliferation, inducing cell cycle arrest and enhancing cell differentiation. PKC-delta is also involved in the regulation of transcription as well as immune and inflammatory responses. It plays a central role in the genotoxic stress response that leads to DNA damaged-induced apoptosis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 247.55  E-value: 2.13e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQ-AVEFPFLVRLEYSFKDNSNLYMVMEYVPG 113
Cdd:cd05620    1 KVLGKGSFGKVLLAELKGKGEYFAVKALKKDVVLIDDDVECTMVEKRVLAlAWENPFLTHLYCTFQTKEHLFFVMEFLNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 114 GEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKR-VKG--RTWTLCGTP 190
Cdd:cd05620   81 GDLMFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKEnVFGdnRASTFCGTP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 191 EYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFG 270
Cdd:cd05620  161 DYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTPHYPRWITKESKDILEKLFERDPTRRLG 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255958318 271 NLKNgvsdIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTSNFD-DYEEEEIRVSITEK 330
Cdd:cd05620  241 VVGN----IRGHPFFKTINWTALEKRELDPPFKPKVKSPSDYSNFDrEFLSEKPRLSYSDK 297
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
29-316 3.49e-79

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: 244.95  E-value: 3.49e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVM 108
Cdd:cd05597    1 DDFEILKVIGRGAFGEVAVVKLKSTEKVYAMKILNKWEMLKRAETACFREERDVLVNGDRRWITKLHYAFQDENYLYLVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 109 EYVPGGEMFSHLRRIG-RFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVK--GRTW- 184
Cdd:cd05597   81 DYYCGGDLLTLLSKFEdRLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFGSCLKLRedGTVQs 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 185 -TLCGTPEYLAPEIILS----KG-YNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVS--GKVRFPSH---FSSDL 253
Cdd:cd05597  161 sVAVGTPDYISPEILQAmedgKGrYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNhkEHFSFPDDeddVSEEA 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255958318 254 KDLLRNLLQvDLTKRFGnlKNGVSDIKTHKWFATTDWIAIyqRKVEAPFIPKFRGSGDTSNFD 316
Cdd:cd05597  241 KDLIRRLIC-SRERRLG--QNGIDDFKKHPFFEGIDWDNI--RDSTPPYIPEVTSPTDTSNFD 298
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
30-304 3.96e-79

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: 243.37  E-value: 3.96e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  30 DFERKKTLGTGSFGRVMLVKHKA---TEQYYAMKILDKQKVV-KLKQIEHTLNEKRILQAV-EFPFLVRLEYSFKDNSNL 104
Cdd:cd05613    1 NFELLKVLGTGAYGKVFLVRKVSghdAGKLYAMKVLKKATIVqKAKTAEHTRTERQVLEHIrQSPFLVTLHYAFQTDTKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 105 YMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRV----K 180
Cdd:cd05613   81 HLILDYINGGELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKEFlldeN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 181 GRTWTLCGTPEYLAPEIIL--SKGYNKAVDWWALGVLIYEMAAGYPPFFAD----QPIQIYEKIVSGKVRFPSHFSSDLK 254
Cdd:cd05613  161 ERAYSFCGTIEYMAPEIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTVDgeknSQAEISRRILKSEPPYPQEMSALAK 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 255958318 255 DLLRNLLQVDLTKRFGNLKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIP 304
Cdd:cd05613  241 DIIQRLLMKDPKKRLGCGPNGADEIKKHPFFQKINWDDLAAKKVPAPFKP 290
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
35-290 6.21e-79

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: 242.00  E-value: 6.21e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRIL--QAvEFPFLVRLEYSFKDNSNLYMVMEYVP 112
Cdd:cd05611    2 KPISKGAFGSVYLAKKRSTGDYFAIKVLKKSDMIAKNQVTNVKAERAIMmiQG-ESPYVAKLYYSFQSKDYLYLVMEYLN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 113 GGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAK--RVKGRTWTLCGTP 190
Cdd:cd05611   81 GGDCASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSRngLEKRHNKKFVGTP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 191 EYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSH----FSSDLKDLLRNLLQVDLT 266
Cdd:cd05611  161 DYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNILSRRINWPEEvkefCSPEAVDLINRLLCMDPA 240
                        250       260
                 ....*....|....*....|....
gi 255958318 267 KRFGnlKNGVSDIKTHKWFATTDW 290
Cdd:cd05611  241 KRLG--ANGYQEIKSHPFFKSINW 262
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
35-316 3.24e-78

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 242.33  E-value: 3.24e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRIL-QAVEFPFLVRLEYSFKDNSNLYMVMEYVPG 113
Cdd:cd05588    1 RVIGRGSYAKVLMVELKKTKRIYAMKVIKKELVNDDEDIDWVQTEKHVFeTASNHPFLVGLHSCFQTESRLFFVIEFVNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 114 GEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAK---RVKGRTWTLCGTP 190
Cdd:cd05588   81 GDLMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMCKeglRPGDTTSTFCGTP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 191 EYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPF----FADQPIQ-----IYEKIVSGKVRFPSHFSSDLKDLLRNLL 261
Cdd:cd05588  161 NYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPFdivgSSDNPDQntedyLFQVILEKPIRIPRSLSVKAASVLKGFL 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 255958318 262 QVDLTKRFG-NLKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTSNFD 316
Cdd:cd05588  241 NKNPAERLGcHPQTGFADIQSHPFFRTIDWEQLEQKQVTPPYKPRIESERDLENFD 296
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
29-320 1.73e-76

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: 239.37  E-value: 1.73e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVM 108
Cdd:cd05629    1 EDFHTVKVIGKGAFGEVRLVQKKDTGKIYAMKTLLKSEMFKKDQLAHVKAERDVLAESDSPWVVSLYYSFQDAQYLYLIM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 109 EYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDF----GFAK------- 177
Cdd:cd05629   81 EFLPGGDLMTMLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDFglstGFHKqhdsayy 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 178 ------------------------------RVKGRTW---------TLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYE 218
Cdd:cd05629  161 qkllqgksnknridnrnsvavdsinltmssKDQIATWkknrrlmaySTVGTPDYIAPEIFLQQGYGQECDWWSLGAIMFE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 219 MAAGYPPFFADQPIQIYEKIVSGK--VRFPS--HFSSDLKDLLRNLLqVDLTKRFGnlKNGVSDIKTHKWFATTDWIAIy 294
Cdd:cd05629  241 CLIGWPPFCSENSHETYRKIINWRetLYFPDdiHLSVEAEDLIRRLI-TNAENRLG--RGGAHEIKSHPFFRGVDWDTI- 316
                        330       340
                 ....*....|....*....|....*...
gi 255958318 295 qRKVEAPFIPKFRGSGDTSNF--DDYEE 320
Cdd:cd05629  317 -RQIRAPFIPQLKSITDTSYFptDELEQ 343
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
28-322 5.82e-74

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: 233.39  E-value: 5.82e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  28 LEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMV 107
Cdd:cd05600   10 LSDFQILTQVGQGGYGSVFLARKKDTGEICALKIMKKKVLFKLNEVNHVLTERDILTTTNSPWLVKLLYAFQDPENVYLA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 108 MEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFA----------- 176
Cdd:cd05600   90 MEYVPGGDFRTLLNNSGILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDFGLAsgtlspkkies 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 177 -----------------------------KRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFF 227
Cdd:cd05600  170 mkirleevkntafleltakerrniyramrKEDQNYANSVVGSPDYMAPEVLRGEGYDLTVDYWSLGCILFECLVGFPPFS 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 228 ADQPIQIYEKI----------VSGKVRFPSHFSSDLKDLLRNLLqVDLTKRFGNLKngvsDIKTHKWFATTDWIAIYQRk 297
Cdd:cd05600  250 GSTPNETWANLyhwkktlqrpVYTDPDLEFNLSDEAWDLITKLI-TDPQDRLQSPE----QIKNHPFFKNIDWDRLREG- 323
                        330       340
                 ....*....|....*....|....*
gi 255958318 298 VEAPFIPKFRGSGDTSNFDDYEEEE 322
Cdd:cd05600  324 SKPPFIPELESEIDTSYFDDFNDEA 348
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
23-316 6.92e-74

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


Pssm-ID: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 232.62  E-value: 6.92e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  23 PSNAGLEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRIL-QAVEFPFLVRLEYSFKDN 101
Cdd:cd05618   14 SSSLGLQDFDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDDEDIDWVQTEKHVFeQASNHPFLVGLHSCFQTE 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 102 SNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAK---R 178
Cdd:cd05618   94 SRLFFVIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKeglR 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 179 VKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPF----FADQPIQ-----IYEKIVSGKVRFPSHF 249
Cdd:cd05618  174 PGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFdivgSSDNPDQntedyLFQVILEKQIRIPRSL 253
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255958318 250 SSDLKDLLRNLLQVDLTKRFGNL-KNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTSNFD 316
Cdd:cd05618  254 SVKAASVLKSFLNKDPKERLGCHpQTGFADIQGHPFFRNVDWDLMEQKQVVPPFKPNISGEFGLDNFD 321
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
27-316 5.48e-73

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


Pssm-ID: 270768 [Multi-domain]  Cd Length: 357  Bit Score: 229.91  E-value: 5.48e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  27 GLEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRIL-QAVEFPFLVRLEYSFKDNSNLY 105
Cdd:cd05617   13 GLQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFeQASSNPFLVGLHSCFQTTSRLF 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 106 MVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAK---RVKGR 182
Cdd:cd05617   93 LVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKeglGPGDT 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 183 TWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPF--FADQPIQ-----IYEKIVSGKVRFPSHFSSDLKD 255
Cdd:cd05617  173 TSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFdiITDNPDMntedyLFQVILEKPIRIPRFLSVKASH 252
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255958318 256 LLRNLLQVDLTKRFG-NLKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTSNFD 316
Cdd:cd05617  253 VLKGFLNKDPKERLGcQPQTGFSDIKSHTFFRSIDWDLLEKKQVTPPFKPQITDDYGLENFD 314
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
9-322 7.07e-73

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: 230.27  E-value: 7.07e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318   9 KAKEDFLRKWENPPPSNAGL----EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQ 84
Cdd:cd05621   28 KNIDNFLNRYEKIVNKIRELqmkaEDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSDSAFFWEERDIMA 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  85 AVEFPFLVRLEYSFKDNSNLYMVMEYVPGGEMFShLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDH 164
Cdd:cd05621  108 FANSPWVVQLFCAFQDDKYLYMVMEYMPGGDLVN-LMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDK 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 165 QGYIQVTDFGFAKRVKGRTWTLC----GTPEYLAPEIILSKG----YNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYE 236
Cdd:cd05621  187 YGHLKLADFGTCMKMDETGMVHCdtavGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYS 266
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 237 KIVSGK--VRFPShfSSDLKDLLRNLLQVDLTKRFGNL-KNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTS 313
Cdd:cd05621  267 KIMDHKnsLNFPD--DVEISKHAKNLICAFLTDREVRLgRNGVEEIKQHPFFRNDQWNWDNIRETAAPVVPELSSDIDTS 344

                 ....*....
gi 255958318 314 NFDDYEEEE 322
Cdd:cd05621  345 NFDDIEDDK 353
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
29-316 2.70e-72

Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-beta is expressed ubiquitously in many tissues. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-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. This alignment model includes the dimerization domain.


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 229.90  E-value: 2.70e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVM 108
Cdd:cd05624   72 DDFEIIKVIGRGAFGEVAVVKMKNTERIYAMKILNKWEMLKRAETACFREERNVLVNGDCQWITTLHYAFQDENYLYLVM 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 109 EYVPGGEMFSHLRRI-GRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKG----RT 183
Cdd:cd05624  152 DYYVGGDLLTLLSKFeDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFGSCLKMNDdgtvQS 231
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 184 WTLCGTPEYLAPEII--LSKG---YNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVR--FPSHF---SSDL 253
Cdd:cd05624  232 SVAVGTPDYISPEILqaMEDGmgkYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHEERfqFPSHVtdvSEEA 311
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255958318 254 KDLLRNLLqVDLTKRFGnlKNGVSDIKTHKWFATTDWIAIyqRKVEAPFIPKFRGSGDTSNFD 316
Cdd:cd05624  312 KDLIQRLI-CSRERRLG--QNGIEDFKKHAFFEGLNWENI--RNLEAPYIPDVSSPSDTSNFD 369
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
37-304 4.46e-72

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


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 224.71  E-value: 4.46e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGGEM 116
Cdd:cd05577    1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIKKKKGETMALNEKIILEKVSSPFIVSLAYAFETKDKLCLVLTLMNGGDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 117 FSHLRRIGR--FSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTWT--LCGTPEY 192
Cdd:cd05577   81 KYHIYNVGTrgFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAVEFKGGKKIkgRVGTHGY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 193 LAPEIILSK-GYNKAVDWWALGVLIYEMAAGYPPFFADQPI----QIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTK 267
Cdd:cd05577  161 MAPEVLQKEvAYDFSVDWFALGCMLYEMIAGRSPFRQRKEKvdkeELKRRTLEMAVEYPDSFSPEARSLCEGLLQKDPER 240
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 255958318 268 RFGNLKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIP 304
Cdd:cd05577  241 RLGCRGGSADEVKEHPFFRSLNWQRLEAGMLEPPFVP 277
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
31-321 5.20e-72

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: 227.97  E-value: 5.20e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEY 110
Cdd:cd05626    3 FVKIKTLGIGAFGEVCLACKVDTHALYAMKTLRKKDVLNRNQVAHVKAERDILAEADNEWVVKLYYSFQDKDNLYFVMDY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 111 VPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAkrvKGRTWT----- 185
Cdd:cd05626   83 IPGGDMMSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLC---TGFRWThnsky 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 186 ------------------------------------------------LCGTPEYLAPEIILSKGYNKAVDWWALGVLIY 217
Cdd:cd05626  160 yqkgshirqdsmepsdlwddvsncrcgdrlktleqratkqhqrclahsLVGTPNYIAPEVLLRKGYTQLCDWWSVGVILF 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 218 EMAAGYPPFFADQPIQIYEKIVS--GKVRFPSH--FSSDLKDLLRNLLqVDLTKRFGnlKNGVSDIKTHKWFATTDWiAI 293
Cdd:cd05626  240 EMLVGQPPFLAPTPTETQLKVINweNTLHIPPQvkLSPEAVDLITKLC-CSAEERLG--RNGADDIKAHPFFSEVDF-SS 315
                        330       340
                 ....*....|....*....|....*...
gi 255958318 294 YQRKVEAPFIPKFRGSGDTSNFDDYEEE 321
Cdd:cd05626  316 DIRTQPAPYVPKISHPMDTSNFDPVEEE 343
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
9-322 5.92e-72

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: 228.74  E-value: 5.92e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318   9 KAKEDFLRKWENPPPSNAGL----EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQ 84
Cdd:cd05622   49 KNIDNFLSRYKDTINKIRDLrmkaEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMA 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  85 AVEFPFLVRLEYSFKDNSNLYMVMEYVPGGEMFSHLRRIGrFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDH 164
Cdd:cd05622  129 FANSPWVVQLFYAFQDDRYLYMVMEYMPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDK 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 165 QGYIQVTDFGFAKRVKG----RTWTLCGTPEYLAPEIILSKG----YNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYE 236
Cdd:cd05622  208 SGHLKLADFGTCMKMNKegmvRCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYS 287
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 237 KIVSGK--VRFPShfSSDLKDLLRNLLQVDLTKRFGNL-KNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTS 313
Cdd:cd05622  288 KIMNHKnsLTFPD--DNDISKEAKNLICAFLTDREVRLgRNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTS 365

                 ....*....
gi 255958318 314 NFDDYEEEE 322
Cdd:cd05622  366 NFDDLEEDK 374
Pkinase pfam00069
Protein kinase domain;
31-285 2.43e-71

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 220.96  E-value: 2.43e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318   31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQiEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEY 110
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKD-KNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  111 VPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYlhsldliyrdlkpenllidhqgyiqvtdfgfakrvKGRTWTLCGTP 190
Cdd:pfam00069  80 VEGGSLFDLLSEKGAFSEREAKFIMKQILEGLES-----------------------------------GSSLTTFVGTP 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  191 EYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRF---PSHFSSDLKDLLRNLLQVDLTK 267
Cdd:pfam00069 125 WYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFpelPSNLSEEAKDLLKKLLKKDPSK 204
                         250
                  ....*....|....*...
gi 255958318  268 RFgnlknGVSDIKTHKWF 285
Cdd:pfam00069 205 RL-----TATQALQHPWF 217
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
28-323 3.27e-71

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR2 (also called STK38-like) plays a role in proper centrosome duplication. In addition, it is involved in regulating neuronal growth and differentiation, as well as in facilitating neurite outgrowth. NDR2 is also implicated in fear conditioning as it contributes to the coupling of neuronal morphological changes with fear-memory consolidation. 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 NDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 225.71  E-value: 3.27e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  28 LEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMV 107
Cdd:cd05627    1 LDDFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEQVAHIRAERDILVEADGAWVVKMFYSFQDKRNLYLI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 108 MEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFA----------- 176
Cdd:cd05627   81 MEFLPGGDMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLCtglkkahrtef 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 177 ------------------KRVKGRTW---------TLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFAD 229
Cdd:cd05627  161 yrnlthnppsdfsfqnmnSKRKAETWkknrrqlaySTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 230 QPIQIYEKIVSGK--VRFPSH--FSSDLKDLLRNLLqVDLTKRFGNlkNGVSDIKTHKWFATTDWIAIYQRKVEAPFipK 305
Cdd:cd05627  241 TPQETYRKVMNWKetLVFPPEvpISEKAKDLILRFC-TDAENRIGS--NGVEEIKSHPFFEGVDWEHIRERPAAIPI--E 315
                        330
                 ....*....|....*...
gi 255958318 306 FRGSGDTSNFDDYEEEEI 323
Cdd:cd05627  316 IKSIDDTSNFDDFPESDI 333
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
35-284 2.00e-69

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: 217.19  E-value: 2.00e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVvklKQIEHTL-NEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPG 113
Cdd:cd14095    6 RVIGDGNFAVVKECRDKATDKEYALKIIDKAKC---KGKEHMIeNEVAILRRVKHPNIVQLIEEYDTDTELYLVMELVKG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 114 GEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLI----DHQGYIQVTDFGFAKRVKGRTWTLCGT 189
Cdd:cd14095   83 GDLFDAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVveheDGSKSLKLADFGLATEVKEPLFTVCGT 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 190 PEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQ--IYEKIVSGKVRFPS----HFSSDLKDLLRNLLQV 263
Cdd:cd14095  163 PTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFRSPDRDQeeLFDLILAGEFEFLSpywdNISDSAKDLISRMLVV 242
                        250       260
                 ....*....|....*....|.
gi 255958318 264 DLTKRFgnlknGVSDIKTHKW 284
Cdd:cd14095  243 DPEKRY-----SAGQVLDHPW 258
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
30-268 1.06e-68

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: 215.40  E-value: 1.06e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  30 DFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVvKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVME 109
Cdd:cd08215    1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNM-SEKEREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIVME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 110 YVPGGEMFSHLRR----IGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKrVKGRTW- 184
Cdd:cd08215   80 YADGGDLAQKIKKqkkkGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISK-VLESTTd 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 185 ---TLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVR-FPSHFSSDLKDLLRNL 260
Cdd:cd08215  159 lakTVVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQYPpIPSQYSSELRDLVNSM 238

                 ....*...
gi 255958318 261 LQVDLTKR 268
Cdd:cd08215  239 LQKDPEKR 246
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
4-316 2.45e-68

Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-alpha is expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 219.50  E-value: 2.45e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318   4 KEFLAKAKEDFLRKwenpppsnaglEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRIL 83
Cdd:cd05623   58 KPFTSKVKQMRLHK-----------EDFEILKVIGRGAFGEVAVVKLKNADKVFAMKILNKWEMLKRAETACFREERDVL 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  84 QAVEFPFLVRLEYSFKDNSNLYMVMEYVPGGEMFSHLRRI-GRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLI 162
Cdd:cd05623  127 VNGDSQWITTLHYAFQDDNNLYLVMDYYVGGDLLTLLSKFeDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILM 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 163 DHQGYIQVTDFGFAKRVKG----RTWTLCGTPEYLAPEIILS----KG-YNKAVDWWALGVLIYEMAAGYPPFFADQPIQ 233
Cdd:cd05623  207 DMNGHIRLADFGSCLKLMEdgtvQSSVAVGTPDYISPEILQAmedgKGkYGPECDWWSLGVCMYEMLYGETPFYAESLVE 286
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 234 IYEKIVSGKVR--FPSHF---SSDLKDLLRNLLqVDLTKRFGnlKNGVSDIKTHKWFATTDWIAIyqRKVEAPFIPKFRG 308
Cdd:cd05623  287 TYGKIMNHKERfqFPTQVtdvSENAKDLIRRLI-CSREHRLG--QNGIEDFKNHPFFVGIDWDNI--RNCEAPYIPEVSS 361

                 ....*...
gi 255958318 309 SGDTSNFD 316
Cdd:cd05623  362 PTDTSNFD 369
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
31-304 7.09e-68

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


Pssm-ID: 270756 [Multi-domain]  Cd Length: 285  Bit Score: 214.14  E-value: 7.09e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEY 110
Cdd:cd05605    2 FRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 111 VPGGEMFSHLRRIGR--FSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFA------KRVKGR 182
Cdd:cd05605   82 MNGGDLKFHIYNMGNpgFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAveipegETIRGR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 183 TwtlcGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQpiqiyEKI----VSGKVR-----FPSHFSSDL 253
Cdd:cd05605  162 V----GTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFRARK-----EKVkreeVDRRVKedqeeYSEKFSEEA 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 255958318 254 KDLLRNLLQVDLTKRFGNLKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIP 304
Cdd:cd05605  233 KSICSQLLQKDPKTRLGCRGEGAEDVKSHPFFKSINFKRLEAGLLEPPFVP 283
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
30-284 4.43e-67

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: 211.49  E-value: 4.43e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  30 DFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVME 109
Cdd:cd14663    1 RYELGRTLGEGTFAKVKFARNTKTGESVAIKIIDKEQVAREGMVEQIKREIAIMKLLRHPNIVELHEVMATKTKIFFVME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 110 YVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGF-----AKRVKGRTW 184
Cdd:cd14663   81 LVTGGELFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLsalseQFRQDGLLH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 185 TLCGTPEYLAPEIILSKGYNKA-VDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQV 263
Cdd:cd14663  161 TTCGTPNYVAPEVLARRGYDGAkADIWSCGVILFVLLAGYLPFDDENLMALYRKIMKGEFEYPRWFSPGAKSLIKRILDP 240
                        250       260
                 ....*....|....*....|.
gi 255958318 264 DLTKRFgnlknGVSDIKTHKW 284
Cdd:cd14663  241 NPSTRI-----TVEQIMASPW 256
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
31-323 5.31e-67

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS1 functions as a tumor suppressor and is implicated in cell cycle regulation. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. Promoter methylation, loss of heterozygosity, and missense mutations targeting the LATS1 gene have also been found in human sarcomas and ovarian cancers. In addition, decreased expression of LATS1 is associated with an aggressive phenotype and poor prognosis. LATS1 induces G2 arrest and promotes cytokinesis. It may be a component of the mitotic exit network in higher eukaryotes. The LATS1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270775 [Multi-domain]  Cd Length: 382  Bit Score: 215.30  E-value: 5.31e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEY 110
Cdd:cd05625    3 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 111 VPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGF--------------- 175
Cdd:cd05625   83 IPGGDMMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdskyyqs 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 176 -----------------------AKRVKGRTW------------TLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMA 220
Cdd:cd05625  163 gdhlrqdsmdfsnewgdpencrcGDRLKPLERraarqhqrclahSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEML 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 221 AGYPPFFADQPIQIYEKIVSGKVRF----PSHFSSDLKDLLRNLLQvDLTKRFGnlKNGVSDIKTHKWFATTDWIAIYqR 296
Cdd:cd05625  243 VGQPPFLAQTPLETQMKVINWQTSLhippQAKLSPEASDLIIKLCR-GPEDRLG--KNGADEIKAHPFFKTIDFSSDL-R 318
                        330       340
                 ....*....|....*....|....*..
gi 255958318 297 KVEAPFIPKFRGSGDTSNFDDYEEEEI 323
Cdd:cd05625  319 QQSAPYIPKITHPTDTSNFDPVDPDKL 345
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
29-323 9.41e-67

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: 214.52  E-value: 9.41e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVM 108
Cdd:cd05628    1 EDFESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEQVGHIRAERDILVEADSLWVVKMFYSFQDKLNLYLIM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 109 EYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFA------------ 176
Cdd:cd05628   81 EFLPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLCtglkkahrtefy 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 177 -----------------KRVKGRTW---------TLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQ 230
Cdd:cd05628  161 rnlnhslpsdftfqnmnSKRKAETWkrnrrqlafSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSET 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 231 PIQIYEKIVSGK--VRFPSH--FSSDLKDLLRNLLqVDLTKRFGnlKNGVSDIKTHKWFATTDWIAIYQRKVEAPFipKF 306
Cdd:cd05628  241 PQETYKKVMNWKetLIFPPEvpISEKAKDLILRFC-CEWEHRIG--APGVEEIKTNPFFEGVDWEHIRERPAAIPI--EI 315
                        330
                 ....*....|....*..
gi 255958318 307 RGSGDTSNFDDYEEEEI 323
Cdd:cd05628  316 KSIDDTSNFDEFPDSDI 332
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
35-285 9.23e-66

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: 207.88  E-value: 9.23e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGG 114
Cdd:cd14081    7 KTLGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSKESVLMKVEREIAIMKLIEHPNVLKLYDVYENKKYLYLVLEYVSGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 115 EMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTW--TLCGTPEY 192
Cdd:cd14081   87 ELFDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMASLQPEGSLleTSCGSPHY 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 193 LAPEIILSKGYN-KAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFgn 271
Cdd:cd14081  167 ACPEVIKGEKYDgRKADIWSCGVILYALLVGALPFDDDNLRQLLEKVKRGVFHIPHFISPDAQDLLRRMLEVNPEKRI-- 244
                        250
                 ....*....|....
gi 255958318 272 lknGVSDIKTHKWF 285
Cdd:cd14081  245 ---TIEEIKKHPWF 255
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
29-285 8.36e-65

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: 205.48  E-value: 8.36e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVM 108
Cdd:cd14099    1 KRYRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSSLTKPKQREKLKSEIKIHRSLKHPNIVKFHDCFEDEENVYILL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 109 EYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKG---RTWT 185
Cdd:cd14099   81 ELCSNGSLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAARLEYdgeRKKT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 186 LCGTPEYLAPEIIL-SKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSH--FSSDLKDLLRNLLQ 262
Cdd:cd14099  161 LCGTPNYIAPEVLEkKKGHSFEVDIWSLGVILYTLLVGKPPFETSDVKETYKRIKKNEYSFPSHlsISDEAKDLIRSMLQ 240
                        250       260
                 ....*....|....*....|...
gi 255958318 263 VDLTKRfgnlkNGVSDIKTHKWF 285
Cdd:cd14099  241 PDPTKR-----PSLDEILSHPFF 258
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
31-269 1.27e-63

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: 202.60  E-value: 1.27e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKvvkLKQIEHTL-NEKRILQAVEFPFLVRLEYSFKDNSNLYMVME 109
Cdd:cd14083    5 YEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKA---LKGKEDSLeNEIAVLRKIKHPNIVQLLDIYESKSHLYLVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 110 YVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLI---DHQGYIQVTDFGFAK-RVKGRTWT 185
Cdd:cd14083   82 LVTGGELFDRIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYyspDEDSKIMISDFGLSKmEDSGVMST 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 186 LCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDL----KDLLRNLL 261
Cdd:cd14083  162 ACGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILKAEYEFDSPYWDDIsdsaKDFIRHLM 241

                 ....*...
gi 255958318 262 QVDLTKRF 269
Cdd:cd14083  242 EKDPNKRY 249
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
37-304 1.49e-63

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: 203.05  E-value: 1.49e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKqKVVKLKQIEH-TLNEKRILQAV----EFPFLVRLEYSFKDNSNLYMVMEYV 111
Cdd:cd05606    2 IGRGGFGEVYGCRKADTGKMYAMKCLDK-KRIKMKQGETlALNERIMLSLVstggDCPFIVCMTYAFQTPDKLCFILDLM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 112 PGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTWTLC-GTP 190
Cdd:cd05606   81 NGGDLHYHLSQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLACDFSKKKPHASvGTH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 191 EYLAPEiILSKG--YNKAVDWWALGVLIYEMAAGYPPFF---ADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDL 265
Cdd:cd05606  161 GYMAPE-VLQKGvaYDSSADWFSLGCMLYKLLKGHSPFRqhkTKDKHEIDRMTLTMNVELPDSFSPELKSLLEGLLQRDV 239
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 255958318 266 TKRFGNLKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIP 304
Cdd:cd05606  240 SKRLGCLGRGATEVKEHPFFKGVDWQQVYLQKYPPPLIP 278
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
35-284 3.56e-62

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: 199.54  E-value: 3.56e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYYAMKILDKQK--VVKLKQIEHT---LNEKRILQAVEFPFLVRLEYSFKDNSNLYMVME 109
Cdd:cd14084   12 RTLGSGACGEVKLAYDKSTCKKVAIKIINKRKftIGSRREINKPrniETEIEILKKLSHPCIIKIEDFFDAEDDYYIVLE 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 110 YVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLI---DHQGYIQVTDFGFAKRVKGRTW-- 184
Cdd:cd14084   92 LMEGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLssqEEECLIKITDFGLSKILGETSLmk 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 185 TLCGTPEYLAPEIILSKG---YNKAVDWWALGVLIYEMAAGYPPFFADQP-IQIYEKIVSGKVRF-PSHF---SSDLKDL 256
Cdd:cd14084  172 TLCGTPTYLAPEVLRSFGtegYTRAVDCWSLGVILFICLSGYPPFSEEYTqMSLKEQILSGKYTFiPKAWknvSEEAKDL 251
                        250       260
                 ....*....|....*....|....*...
gi 255958318 257 LRNLLQVDLTKRFgnlknGVSDIKTHKW 284
Cdd:cd14084  252 VKKMLVVDPSRRP-----SIEEALEHPW 274
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
37-285 1.78e-61

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: 197.39  E-value: 1.78e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLK-----------QIEHTLNEKRILQAVEFPFLVRL----EYSFKDN 101
Cdd:cd14008    1 LGRGSFGKVKLALDTETGQLYAIKIFNKSRLRKRRegkndrgkiknALDDVRREIAIMKKLDHPNIVRLyeviDDPESDK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 102 snLYMVMEYVPGGEMFS--HLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRV 179
Cdd:cd14008   81 --LYLVLEYCEGGPVMEldSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFGVSEMF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 180 KGRTWTL---CGTPEYLAPEI--ILSKGYN-KAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRF--PSHFSS 251
Cdd:cd14008  159 EDGNDTLqktAGTPAFLAPELcdGDSKTYSgKAADIWALGVTLYCLVFGRLPFNGDNILELYEAIQNQNDEFpiPPELSP 238
                        250       260       270
                 ....*....|....*....|....*....|....
gi 255958318 252 DLKDLLRNLLQVDLTKRFgnlknGVSDIKTHKWF 285
Cdd:cd14008  239 ELKDLLRRMLEKDPEKRI-----TLKEIKEHPWV 267
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
28-316 2.05e-61

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: 199.72  E-value: 2.05e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  28 LEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMV 107
Cdd:cd05610    3 IEEFVIVKPISRGAFGKVYLGRKKNNSKLYAVKVVKKADMINKNMVHQVQAERDALALSKSPFIVHLYYSLQSANNVYLV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 108 MEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAK---------- 177
Cdd:cd05610   83 MEYLIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKvtlnrelnmm 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 178 ----------------RVKGRTWTLC------------------------------GTPEYLAPEIILSKGYNKAVDWWA 211
Cdd:cd05610  163 dilttpsmakpkndysRTPGQVLSLIsslgfntptpyrtpksvrrgaarvegerilGTPDYLAPELLLGKPHGPAVDWWA 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 212 LGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFP---SHFSSDLKDLLRNLLQVDLTKRfgnlkNGVSDIKTHKWFATT 288
Cdd:cd05610  243 LGVCLFEFLTGIPPFNDETPQQVFQNILNRDIPWPegeEELSVNAQNAIEILLTMDPTKR-----AGLKELKQHPLFHGV 317
                        330       340
                 ....*....|....*....|....*...
gi 255958318 289 DWIAIYQRkvEAPFIPKFRGSGDTSNFD 316
Cdd:cd05610  318 DWENLQNQ--TMPFIPQPDDETDTSYFE 343
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
31-304 3.44e-61

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


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 197.14  E-value: 3.44e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEY 110
Cdd:cd05631    2 FRHYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKRILEKVNSRFVVSLAYAYETKDALCLVLTI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 111 VPGGEMFSHLRRIGR--FSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFA------KRVKGR 182
Cdd:cd05631   82 MNGGDLKFHIYNMGNpgFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAvqipegETVRGR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 183 TwtlcGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPI----QIYEKIVSGKVRFPSHFSSDLKDLLR 258
Cdd:cd05631  162 V----GTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRKERvkreEVDRRVKEDQEEYSEKFSEDAKSICR 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 255958318 259 NLLQVDLTKRFGNLKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIP 304
Cdd:cd05631  238 MLLTKNPKERLGCRGNGAAGVKQHPIFKNINFKRLEANMLEPPFCP 283
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
30-268 5.58e-61

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: 195.82  E-value: 5.58e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  30 DFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVvKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVME 109
Cdd:cd06606    1 RWKKGELLGKGSFGSVYLALNLDTGELMAVKEVELSGD-SEEELEALEREIRILSSLKHPNIVRYLGTERTENTLNIFLE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 110 YVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTW----- 184
Cdd:cd06606   80 YVPGGSLASLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKRLAEIATgegtk 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 185 TLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFA-DQPIQIYEKIVSGKV--RFPSHFSSDLKDLLRNLL 261
Cdd:cd06606  160 SLRGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWSElGNPVAALFKIGSSGEppPIPEHLSEEAKDFLRKCL 239

                 ....*..
gi 255958318 262 QVDLTKR 268
Cdd:cd06606  240 QRDPKKR 246
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
37-268 1.89e-60

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: 192.87  E-value: 1.89e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKQKVvkLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGGEM 116
Cdd:cd00180    1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKL--KKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 117 FSHLR-RIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTWTL-----CGTP 190
Cdd:cd00180   79 KDLLKeNKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLLkttggTTPP 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255958318 191 EYLAPEIILSKGYNKAVDWWALGVLIYEMaagyppffadqpiqiyekivsgkvrfpshfsSDLKDLLRNLLQVDLTKR 268
Cdd:cd00180  159 YYAPPELLGGRYYGPKVDIWSLGVILYEL-------------------------------EELKDLIRRMLQYDPKKR 205
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
35-304 2.32e-60

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: 195.10  E-value: 2.32e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGG 114
Cdd:cd05608    7 RVLGKGGFGEVSACQMRATGKLYACKKLNKKRLKKRKGYEGAMVEKRILAKVHSRFIVSLAYAFQTKTDLCLVMTIMNGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 115 EMFSHLRRIGR----FSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFA---KRVKGRTWTLC 187
Cdd:cd05608   87 DLRYHIYNVDEenpgFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAvelKDGQTKTKGYA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 188 GTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFAD----QPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQV 263
Cdd:cd05608  167 GTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFRARgekvENKELKQRILNDSVTYSEKFSPASKSICEALLAK 246
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 255958318 264 DLTKRFGnLKNGVSD-IKTHKWFATTDWIAIYQRKVEAPFIP 304
Cdd:cd05608  247 DPEKRLG-FRDGNCDgLRTHPFFRDINWRKLEAGILPPPFVP 287
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
37-270 2.69e-60

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: 193.59  E-value: 2.69e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKlKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGGEM 116
Cdd:cd14009    1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKLNK-KLQENLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAGGDL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 117 FSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLI---DHQGYIQVTDFGFAKRVkgRTW----TLCGT 189
Cdd:cd14009   80 SQYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLstsGDDPVLKIADFGFARSL--QPAsmaeTLCGS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 190 PEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFP----SHFSSDLKDLLRNLLQVDL 265
Cdd:cd14009  158 PLYMAPEILQFQKYDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIERSDAVIPfpiaAQLSPDCKDLLRRLLRRDP 237

                 ....*
gi 255958318 266 TKRFG 270
Cdd:cd14009  238 AERIS 242
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
31-304 4.97e-60

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK6 is widely expressed in many tissues and is expressed as multiple splice variants with different domain architectures. It is post-translationally palmitoylated and localized in the membrane. GRK6 plays important roles in the regulation of dopamine, M3 muscarinic, opioid, and chemokine receptor signaling. It also plays maladaptive roles in addiction and Parkinson's disease. GRK6-deficient mice exhibit altered dopamine receptor regulation, decreased lymphocyte chemotaxis, and increased acute inflammation and neutrophil chemotaxis. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 194.09  E-value: 4.97e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEY 110
Cdd:cd05630    2 FRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 111 VPGGEMFSHLRRIGR--FSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFA------KRVKGR 182
Cdd:cd05630   82 MNGGDLKFHIYHMGQagFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAvhvpegQTIKGR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 183 TwtlcGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPfFADQPIQI----YEKIV-SGKVRFPSHFSSDLKDLL 257
Cdd:cd05630  162 V----GTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSP-FQQRKKKIkreeVERLVkEVPEEYSEKFSPQARSLC 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 255958318 258 RNLLQVDLTKRFGNLKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIP 304
Cdd:cd05630  237 SMLLCKDPAERLGCRGGGAREVKEHPLFKKLNFKRLGAGMLEPPFKP 283
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
29-269 5.53e-60

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: 194.06  E-value: 5.53e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEhtlNEKRILQAVEFPFLVRLEYSFKDNSNLYMVM 108
Cdd:cd14166    3 ETFIFMEVLGSGAFSEVYLVKQRSTGKLYALKCIKKSPLSRDSSLE---NEIAVLKRIKHENIVTLEDIYESTTHYYLVM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 109 EYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLI---DHQGYIQVTDFGFAKRVK-GRTW 184
Cdd:cd14166   80 QLVSGGELFDRILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYltpDENSKIMITDFGLSKMEQnGIMS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 185 TLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDL----KDLLRNL 260
Cdd:cd14166  160 TACGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEETESRLFEKIKEGYYEFESPFWDDIsesaKDFIRHL 239

                 ....*....
gi 255958318 261 LQVDLTKRF 269
Cdd:cd14166  240 LEKNPSKRY 248
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
35-285 8.34e-60

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: 192.48  E-value: 8.34e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGG 114
Cdd:cd14079    8 KTLGVGSFGKVKLAEHELTGHKVAVKILNRQKIKSLDMEEKIRREIQILKLFRHPHIIRLYEVIETPTDIFMVMEYVSGG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 115 EMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVK-GRTW-TLCGTPEY 192
Cdd:cd14079   88 ELFDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLSNIMRdGEFLkTSCGSPNY 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 193 LAPEIILSKGY-NKAVDWWALGVLIYEMAAGYPPfFADQPIQ-IYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFg 270
Cdd:cd14079  168 AAPEVISGKLYaGPEVDVWSCGVILYALLCGSLP-FDDEHIPnLFKKIKSGIYTIPSHLSPGARDLIKRMLVVDPLKRI- 245
                        250
                 ....*....|....*
gi 255958318 271 nlknGVSDIKTHKWF 285
Cdd:cd14079  246 ----TIPEIRQHPWF 256
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
37-269 2.00e-59

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: 191.65  E-value: 2.00e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGGEM 116
Cdd:cd14014    8 LGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVMEYVEGGSL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 117 FSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTWT----LCGTPEY 192
Cdd:cd14014   88 ADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGLTqtgsVLGTPAY 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 193 LAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPS----HFSSDLKDLLRNLLQVDLTKR 268
Cdd:cd14014  168 MAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSplnpDVPPALDAIILRALAKDPEER 247

                 .
gi 255958318 269 F 269
Cdd:cd14014  248 P 248
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
28-284 8.22e-59

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: 190.29  E-value: 8.22e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  28 LEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKqkvvklKQIEHTL----NEKRILQAVEFPFLVRLEYSFKDNSN 103
Cdd:cd14078    2 LKYYELHETIGSGGFAKVKLATHILTGEKVAIKIMDK------KALGDDLprvkTEIEALKNLSHQHICRLYHVIETDNK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 104 LYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKG-- 181
Cdd:cd14078   76 IFMVLEYCPGGELFDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLCAKPKGgm 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 182 --RTWTLCGTPEYLAPEIILSKGY--NKAvDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLL 257
Cdd:cd14078  156 dhHLETCCGSPAYAAPELIQGKPYigSEA-DVWSMGVLLYALLCGFLPFDDDNVMALYRKIQSGKYEEPEWLSPSSKLLL 234
                        250       260
                 ....*....|....*....|....*..
gi 255958318 258 RNLLQVDLTKRFgnlknGVSDIKTHKW 284
Cdd:cd14078  235 DQMLQVDPKKRI-----TVKELLNHPW 256
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
31-284 2.46e-58

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: 188.90  E-value: 2.46e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKqkvvKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEY 110
Cdd:cd14087    3 YDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIET----KCRGREVCESELNVLRRVRHTNIIQLIEVFETKERVYMVMEL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 111 VPGGEMFSHLRRIGRFSEPHARfYAAQIVLT-FEYLHSLDLIYRDLKPENLLIDHQGY---IQVTDFGFAKRVKGR---- 182
Cdd:cd14087   79 ATGGELFDRIIAKGSFTERDAT-RVLQMVLDgVKYLHGLGITHRDLKPENLLYYHPGPdskIMITDFGLASTRKKGpncl 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 183 TWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDL----KDLLR 258
Cdd:cd14087  158 MKTTCGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRAKYSYSGEPWPSVsnlaKDFID 237
                        250       260
                 ....*....|....*....|....*.
gi 255958318 259 NLLQVDLTKRFgnlknGVSDIKTHKW 284
Cdd:cd14087  238 RLLTVNPGERL-----SATQALKHPW 258
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
37-271 1.16e-57

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 193.69  E-value: 1.16e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGGEM 116
Cdd:COG0515   15 LGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLVMEYVEGESL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 117 FSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKG----RTWTLCGTPEY 192
Cdd:COG0515   95 ADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGatltQTGTVVGTPGY 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 193 LAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHF----SSDLKDLLRNLLQVDLTKR 268
Cdd:COG0515  175 MAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELrpdlPPALDAIVLRALAKDPEER 254

                 ...
gi 255958318 269 FGN 271
Cdd:COG0515  255 YQS 257
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
31-285 2.47e-57

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: 186.06  E-value: 2.47e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKV--VKLKQIehtLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVM 108
Cdd:cd14071    2 YDIERTIGKGNFAVVKLARHRITKTEVAIKIIDKSQLdeENLKKI---YREVQIMKMLNHPHIIKLYQVMETKDMLYLVT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 109 EYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKG----RTW 184
Cdd:cd14071   79 EYASNGEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFSNFFKPgellKTW 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 185 tlCGTPEYLAPEIILSKGYN-KAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQV 263
Cdd:cd14071  159 --CGSPPYAAPEVFEGKEYEgPQLDIWSLGVVLYVLVCGALPFDGSTLQTLRDRVLSGRFRIPFFMSTDCEHLIRRMLVL 236
                        250       260
                 ....*....|....*....|..
gi 255958318 264 DLTKRFgnlknGVSDIKTHKWF 285
Cdd:cd14071  237 DPSKRL-----TIEQIKKHKWM 253
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
26-284 2.62e-57

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: 186.08  E-value: 2.62e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  26 AGLEDFErkKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQiEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLY 105
Cdd:cd14074    2 AGLYDLE--ETLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDDVSK-AHLFQEVRCMKLVQHPNVVRLYEVIDTQTKLY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 106 MVMEYVPGGEMFSHLRRIGR-FSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLI-DHQGYIQVTDFGFAKRVK--G 181
Cdd:cd14074   79 LILELGDGGDMYDYIMKHENgLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQpgE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 182 RTWTLCGTPEYLAPEIILSKGYNK-AVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNL 260
Cdd:cd14074  159 KLETSCGSLAYSAPEILLGDEYDApAVDIWSLGVILYMLVCGQPPFQEANDSETLTMIMDCKYTVPAHVSPECKDLIRRM 238
                        250       260
                 ....*....|....*....|....
gi 255958318 261 LQVDLTKRFgnlknGVSDIKTHKW 284
Cdd:cd14074  239 LIRDPKKRA-----SLEEIENHPW 257
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
29-269 5.51e-57

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: 186.02  E-value: 5.51e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILD----KQKVVKLKQI-EHTLNEKRILQAVE-FPFLVRLEYSFKDNS 102
Cdd:cd14093    3 AKYEPKEILGRGVSSTVRRCIEKETGQEFAVKIIDitgeKSSENEAEELrEATRREIEILRQVSgHPNIIELHDVFESPT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 103 NLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVK-G 181
Cdd:cd14093   83 FIFLVFELCRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFATRLDeG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 182 RTWT-LCGTPEYLAPEIIL------SKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPS----HFS 250
Cdd:cd14093  163 EKLReLCGTPGYLAPEVLKcsmydnAPGYGKEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNIMEGKYEFGSpewdDIS 242
                        250
                 ....*....|....*....
gi 255958318 251 SDLKDLLRNLLQVDLTKRF 269
Cdd:cd14093  243 DTAKDLISKLLVVDPKKRL 261
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
30-324 9.92e-57

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: 186.79  E-value: 9.92e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  30 DFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVvKLKQIEH-TLNEKRILQAV---EFPFLVRLEYSFKDNSNLY 105
Cdd:cd14223    1 DFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRI-KMKQGETlALNERIMLSLVstgDCPFIVCMSYAFHTPDKLS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 106 MVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFA-KRVKGRTW 184
Cdd:cd14223   80 FILDLMNGGDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLAcDFSKKKPH 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 185 TLCGTPEYLAPEiILSKG--YNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYE---KIVSGKVRFPSHFSSDLKDLLRN 259
Cdd:cd14223  160 ASVGTHGYMAPE-VLQKGvaYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEidrMTLTMAVELPDSFSPELRSLLEG 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255958318 260 LLQVDLTKRFGNLKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKfRG---SGDTSNFDDYEEEEIR 324
Cdd:cd14223  239 LLQRDVNRRLGCMGRGAQEVKEEPFFRGLDWQMVFLQKYPPPLIPP-RGevnAADAFDIGSFDEEDTK 305
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
29-269 1.65e-56

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: 184.46  E-value: 1.65e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKqKVVKLKQ--IEhtlNEKRILQAVEFPFLVRLEYSFKDNSNLYM 106
Cdd:cd14167    3 DIYDFREVLGTGAFSEVVLAEEKRTQKLVAIKCIAK-KALEGKEtsIE---NEIAVLHKIKHPNIVALDDIYESGGHLYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 107 VMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLL---IDHQGYIQVTDFGFAKrVKGR- 182
Cdd:cd14167   79 IMQLVSGGELFDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGLSK-IEGSg 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 183 --TWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDL----KDL 256
Cdd:cd14167  158 svMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAEYEFDSPYWDDIsdsaKDF 237
                        250
                 ....*....|...
gi 255958318 257 LRNLLQVDLTKRF 269
Cdd:cd14167  238 IQHLMEKDPEKRF 250
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
28-335 2.11e-56

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: 186.81  E-value: 2.11e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  28 LEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVvKLKQIEH-TLNEKRILQAV---EFPFLVRLEYSFKDNSN 103
Cdd:cd05633    4 MNDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRI-KMKQGETlALNERIMLSLVstgDCPFIVCMTYAFHTPDK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 104 LYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFA-KRVKGR 182
Cdd:cd05633   83 LCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLAcDFSKKK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 183 TWTLCGTPEYLAPEiILSKG--YNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYE---KIVSGKVRFPSHFSSDLKDLL 257
Cdd:cd05633  163 PHASVGTHGYMAPE-VLQKGtaYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEidrMTLTVNVELPDSFSPELKSLL 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 258 RNLLQVDLTKRFGNLKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKfRG---SGDTSNFDDYEEEEIRVSITEKCGKE 334
Cdd:cd05633  242 EGLLQRDVSKRLGCHGRGAQEVKEHSFFKGIDWQQVYLQKYPPPLIPP-RGevnAADAFDIGSFDEEDTKGIKLLDSDQE 320

                 .
gi 255958318 335 F 335
Cdd:cd05633  321 L 321
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
31-269 2.49e-56

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: 183.61  E-value: 2.49e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKvvkLKQIEHTL-NEKRILQAVEFPFLVRLEYSFKDNSNLYMVME 109
Cdd:cd14185    2 YEIGRTIGDGNFAVVKECRHWNENQEYAMKIIDKSK---LKGKEDMIeSEILIIKSLSHPNIVKLFEVYETEKEIYLILE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 110 YVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQG----YIQVTDFGFAKRVKGRTWT 185
Cdd:cd14185   79 YVRGGDLFDAIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQHNPdkstTLKLADFGLAKYVTGPIFT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 186 LCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQ--IYEKIVSGKVRFPS----HFSSDLKDLLRN 259
Cdd:cd14185  159 VCGTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFRSPERDQeeLFQIIQLGHYEFLPpywdNISEAAKDLISR 238
                        250
                 ....*....|
gi 255958318 260 LLQVDLTKRF 269
Cdd:cd14185  239 LLVVDPEKRY 248
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
31-305 1.94e-55

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


Pssm-ID: 270758 [Multi-domain]  Cd Length: 286  Bit Score: 182.41  E-value: 1.94e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEY 110
Cdd:cd05607    4 FYEFRVLGKGGFGEVCAVQVKNTGQMYACKKLDKKRLKKKSGEKMALLEKEILEKVNSPFIVSLAYAFETKTHLCLVMSL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 111 VPGGEMFSHLRRIGRFSEPHAR--FYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVK-GRTWTL- 186
Cdd:cd05607   84 MNGGDLKYHIYNVGERGIEMERviFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVEVKeGKPITQr 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 187 CGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPF--FADQPI--QIYEKIVSGKVRFP-SHFSSDLKDLLRNLL 261
Cdd:cd05607  164 AGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFrdHKEKVSkeELKRRTLEDEVKFEhQNFTEEAKDICRLFL 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 255958318 262 QVDLTKRFGNLKNGvSDIKTHKWFATTDWIAIYQRKVEAPFIPK 305
Cdd:cd05607  244 AKKPENRLGSRTND-DDPRKHEFFKSINFPRLEAGLIDPPFVPD 286
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
28-284 3.16e-55

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: 180.92  E-value: 3.16e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  28 LEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKlKQIEHTLN-EKRILQAVEFPFLVRLEYSFKDNSNLYM 106
Cdd:cd14116    4 LEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEK-AGVEHQLRrEVEIQSHLRHPNILRLYGYFHDATRVYL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 107 VMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRV-KGRTWT 185
Cdd:cd14116   83 ILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHApSSRRTT 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 186 LCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDL 265
Cdd:cd14116  163 LCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLLKHNP 242
                        250
                 ....*....|....*....
gi 255958318 266 TKRFgnlknGVSDIKTHKW 284
Cdd:cd14116  243 SQRP-----MLREVLEHPW 256
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
31-269 3.51e-54

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: 178.93  E-value: 3.51e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKvvkLKQIEHTL-NEKRILQAVEFPFLVRLEYSFKDNSNLYMVME 109
Cdd:cd14169    5 YELKEKLGEGAFSEVVLAQERGSQRLVALKCIPKKA---LRGKEAMVeNEIAVLRRINHENIVSLEDIYESPTHLYLAME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 110 YVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLID---HQGYIQVTDFGFAK-RVKGRTWT 185
Cdd:cd14169   82 LVTGGELFDRIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYAtpfEDSKIMISDFGLSKiEAQGMLST 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 186 LCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDL----KDLLRNLL 261
Cdd:cd14169  162 ACGTPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDENDSELFNQILKAEYEFDSPYWDDIsesaKDFIRHLL 241

                 ....*...
gi 255958318 262 QVDLTKRF 269
Cdd:cd14169  242 ERDPEKRF 249
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
37-284 5.22e-54

Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIM1 is a widely-expressed kinase belonging to the AMP-activated protein kinase (AMPK) subfamily. Although present in most tissues, NIM1 kinase activity is only observed in the brain and testis. NIM1 is capable of autophosphorylating and activating itself, but may be present in other tissues in the inactive form. The physiological function of NIM1 has yet to be elucidated. The NIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270977 [Multi-domain]  Cd Length: 255  Bit Score: 177.53  E-value: 5.22e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKQKvvkLKQIEHTLNEKRI--LQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGG 114
Cdd:cd14075   10 LGSGNFSQVKLGIHQLTKEKVAIKILDKTK---LDQKTQRLLSREIssMEKLHHPNIIRLYEVVETLSKLHLVMEYASGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 115 EMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVK-GRTW-TLCGTPEY 192
Cdd:cd14075   87 ELYTKISTEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGFSTHAKrGETLnTFCGSPPY 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 193 LAPEIILSKGY-NKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFgn 271
Cdd:cd14075  167 AAPELFKDEHYiGIYVDIWALGVLLYFMVTGVMPFRAETVAKLKKCILEGTYTIPSYVSEPCQELIRGILQPVPSDRY-- 244
                        250
                 ....*....|...
gi 255958318 272 lknGVSDIKTHKW 284
Cdd:cd14075  245 ---SIDEIKNSEW 254
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
30-268 9.44e-54

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: 177.20  E-value: 9.44e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  30 DFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKlKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVME 109
Cdd:cd08530    1 DFKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNLGSLSQ-KEREDSVNEIRLLASVNHPNIIRYKEAFLDGNRLCIVME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 110 YVPGGEMFSHLRRIGR----FSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGR-TW 184
Cdd:cd08530   80 YAPFGDLSKLISKRKKkrrlFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGISKVLKKNlAK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 185 TLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKV-RFPSHFSSDLKDLLRNLLQV 263
Cdd:cd08530  160 TQIGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFEARTMQELRYKVCRGKFpPIPPVYSQDLQQIIRSLLQV 239

                 ....*
gi 255958318 264 DLTKR 268
Cdd:cd08530  240 NPKKR 244
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
30-304 1.15e-53

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: 177.83  E-value: 1.15e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  30 DFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLnekRILQaveFPFLVRLEYSFKDNSNLYMVME 109
Cdd:cd14091    1 EYEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIDKSKRDPSEEIEILL---RYGQ---HPNIITLRDVYDDGNSVYLVTE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 110 YVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLL-IDHQG---YIQVTDFGFAKRVK---GR 182
Cdd:cd14091   75 LLRGGELLDRILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILyADESGdpeSLRICDFGFAKQLRaenGL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 183 TWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFA---DQPIQIYEKIVSGKVRFPS----HFSSDLKD 255
Cdd:cd14091  155 LMTPCYTANFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPFASgpnDTPEVILARIGSGKIDLSGgnwdHVSDSAKD 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 255958318 256 LLRNLLQVDLTKRFgnlknGVSDIKTHKWFATTDwiAIYQRKVEAPFIP 304
Cdd:cd14091  235 LVRKMLHVDPSQRP-----TAAQVLQHPWIRNRD--SLPQRQLTDPQDA 276
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
31-308 1.34e-53

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK5 is widely expressed in many tissues. It associates with the membrane though an N-terminal PIP2 binding domain and also binds phospholipids via its C-terminus. GRK5 deficiency is associated with early Alzheimer's disease in humans and mouse models. GRK5 also plays a crucial role in the pathogenesis of sporadic Parkinson's disease. It participates in the regulation and desensitization of PDGFRbeta, a receptor tyrosine kinase involved in a variety of downstream cellular effects including cell growth, chemotaxis, apoptosis, and angiogenesis. GRK5 also regulates Toll-like receptor 4, which is involved in innate and adaptive immunity. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 178.63  E-value: 1.34e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEY 110
Cdd:cd05632    4 FRQYRVLGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKGESMALNEKQILEKVNSQFVVNLAYAYETKDALCLVLTI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 111 VPGGEMFSHLRRIGR--FSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKR------VKGR 182
Cdd:cd05632   84 MNGGDLKFHIYNMGNpgFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVKipegesIRGR 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 183 TwtlcGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPI----QIYEKIVSGKVRFPSHFSSDLKDLLR 258
Cdd:cd05632  164 V----GTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEKvkreEVDRRVLETEEVYSAKFSEEAKSICK 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 255958318 259 NLLQVDLTKRFGNLKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRG 308
Cdd:cd05632  240 MLLTKDPKQRLGCQEEGAGEVKRHPFFRNMNFKRLEAGMLDPPFVPDPRA 289
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
29-284 5.29e-53

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: 175.22  E-value: 5.29e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVvklKQIEHTL-NEKRILQAVEFPFLVRLEYSFKDNSNLYMV 107
Cdd:cd14184    1 EKYKIGKVIGDGNFAVVKECVERSTGKEFALKIIDKAKC---CGKEHLIeNEVSILRRVKHPNIIMLIEEMDTPAELYLV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 108 MEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLI----DHQGYIQVTDFGFAKRVKGRT 183
Cdd:cd14184   78 MELVKGGDLFDAITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVceypDGTKSLKLGDFGLATVVEGPL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 184 WTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQ--IYEKIVSGKVRFPSHF----SSDLKDLL 257
Cdd:cd14184  158 YTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSENNLQedLFDQILLGKLEFPSPYwdniTDSAKELI 237
                        250       260
                 ....*....|....*....|....*..
gi 255958318 258 RNLLQVDLTKRFgnlknGVSDIKTHKW 284
Cdd:cd14184  238 SHMLQVNVEARY-----TAEQILSHPW 259
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
35-268 7.12e-53

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: 174.90  E-value: 7.12e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYYAMKIL-----DKQKVVKLKQIEHTLNekrILQAVEFPFLVRLEYSFKDNSNLYMVME 109
Cdd:cd06632    6 QLLGSGSFGSVYEGFNGDTGDFFAVKEVslvddDKKSRESVKQLEQEIA---LLSKLRHPNIVQYYGTEREEDNLYIFLE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 110 YVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTWTLC-- 187
Cdd:cd06632   83 YVPGGSIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKHVEAFSFAKSfk 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 188 GTPEYLAPEIILSK--GYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKV--RFPSHFSSDLKDLLRNLLQV 263
Cdd:cd06632  163 GSPYWMAPEVIMQKnsGYGLAVDIWSLGCTVLEMATGKPPWSQYEGVAAIFKIGNSGElpPIPDHLSPDAKDFIRLCLQR 242

                 ....*
gi 255958318 264 DLTKR 268
Cdd:cd06632  243 DPEDR 247
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
29-268 2.22e-52

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: 173.55  E-value: 2.22e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMK-ILDKQKVVKLKQIehtLNEKRILQAVEFPFLVRLEYSFKDNSNLYMV 107
Cdd:cd06623    1 SDLERVKVLGQGSSGVVYKVRHKPTGKIYALKkIHVDGDEEFRKQL---LRELKTLRSCESPYVVKCYGAFYKEGEISIV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 108 MEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHS-LDLIYRDLKPENLLIDHQGYIQVTDFGFAK---RVKGRT 183
Cdd:cd06623   78 LEYMDGGSLADLLKKVGKIPEPVLAYIARQILKGLDYLHTkRHIIHRDIKPSNLLINSKGEVKIADFGISKvleNTLDQC 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 184 WTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAG-YPPFFADQP--IQIYEKIVSGKVRF--PSHFSSDLKDLLR 258
Cdd:cd06623  158 NTFVGTVTYMSPERIQGESYSYAADIWSLGLTLLECALGkFPFLPPGQPsfFELMQAICDGPPPSlpAEEFSPEFRDFIS 237
                        250
                 ....*....|
gi 255958318 259 NLLQVDLTKR 268
Cdd:cd06623  238 ACLQKDPKKR 247
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
30-268 5.73e-52

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: 172.39  E-value: 5.73e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  30 DFERKKTLGTGSFGRVMLVKHKATEQYYAMKILdkqKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVME 109
Cdd:cd05122    1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKI---NLESKEKKESILNEIAILKKCKHPNIVKYYGSYLKKDELWIVME 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 110 YVPGGEMFSHLR-RIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTW--TL 186
Cdd:cd05122   78 FCSGGSLKDLLKnTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQLSDGKTrnTF 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 187 CGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSG---KVRFPSHFSSDLKDLLRNLLQV 263
Cdd:cd05122  158 VGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSELPPMKALFLIATNgppGLRNPKKWSKEFKDFLKKCLQK 237

                 ....*
gi 255958318 264 DLTKR 268
Cdd:cd05122  238 DPEKR 242
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
35-284 7.81e-52

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: 171.93  E-value: 7.81e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVvKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGG 114
Cdd:cd14072    6 KTIGKGNFAKVKLARHVLTGREVAIKIIDKTQL-NPSSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEYASGG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 115 EMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAK--RVKGRTWTLCGTPEY 192
Cdd:cd14072   85 EVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNefTPGNKLDTFCGSPPY 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 193 LAPEIILSKGYN-KAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRfGN 271
Cdd:cd14072  165 AAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLVLNPSKR-GT 243
                        250
                 ....*....|...
gi 255958318 272 LKNgvsdIKTHKW 284
Cdd:cd14072  244 LEQ----IMKDRW 252
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
30-268 1.22e-51

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: 171.89  E-value: 1.22e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  30 DFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQ-IEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVM 108
Cdd:cd14098    1 KYQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKRKVAGNDKnLQLFQREINILKSLEHPGIVRLIDWYEDDQHIYLVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 109 EYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQG--YIQVTDFGFAKRVKGRTW-- 184
Cdd:cd14098   81 EYVEGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDpvIVKISDFGLAKVIHTGTFlv 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 185 TLCGTPEYLAPEIILSK------GYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGkvRFPS------HFSSD 252
Cdd:cd14098  161 TFCGTMAYLAPEILMSKeqnlqgGYSNLVDMWSVGCLVYVMLTGALPFDGSSQLPVEKRIRKG--RYTQpplvdfNISEE 238
                        250
                 ....*....|....*.
gi 255958318 253 LKDLLRNLLQVDLTKR 268
Cdd:cd14098  239 AIDFILRLLDVDPEKR 254
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
35-285 3.21e-51

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: 170.44  E-value: 3.21e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHK--ATEQYYAMKILDKQKVVKlKQIEHTL-NEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYV 111
Cdd:cd14080    6 KTIGEGSYSKVKLAEYTksGLKEKVACKIIDKKKAPK-DFLEKFLpRELEILRKLRHPNIIQVYSIFERGSKVFIFMEYA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 112 PGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTW-----TL 186
Cdd:cd14080   85 EHGDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGFARLCPDDDGdvlskTF 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 187 CGTPEYLAPEIILSKGYN-KAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPS---HFSSDLKDLLRNLLQ 262
Cdd:cd14080  165 CGSAAYAAPEILQGIPYDpKKYDIWSLGVILYIMLCGSMPFDDSNIKKMLKDQQNRKVRFPSsvkKLSPECKDLIDQLLE 244
                        250       260
                 ....*....|....*....|...
gi 255958318 263 VDLTKRFgnlknGVSDIKTHKWF 285
Cdd:cd14080  245 PDPTKRA-----TIEEILNHPWL 262
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
29-270 1.52e-50

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: 168.58  E-value: 1.52e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKlKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVM 108
Cdd:cd14002    1 ENYHVLELIGEGSFGKVYKGRRKYTGQVVALKFIPKRGKSE-KELRNLRQEIEILRKLNHPNIIEMLDSFETKKEFVVVT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 109 EYVPGgEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTWTLC- 187
Cdd:cd14002   80 EYAQG-ELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFARAMSCNTLVLTs 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 188 --GTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDL 265
Cdd:cd14002  159 ikGTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYTNSIYQLVQMIVKDPVKWPSNMSPEFKSFLQGLLNKDP 238

                 ....*
gi 255958318 266 TKRFG 270
Cdd:cd14002  239 SKRLS 243
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
34-284 1.93e-50

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated 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 MAPK-activated protein kinases MK2, MK3, MK5 (also called PRAK for p38-regulated/activated protein kinase), and related proteins. These proteins contain a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. In addition, MK2 and MK3 contain an N-terminal proline-rich region that can bind to SH3 domains. MK2 and MK3 are bonafide substrates for the MAPK p38, while MK5 plays a functional role in the p38 MAPK pathway although their direct interaction has been difficult to detect. MK2 and MK3 are closely related and show, thus far, indistinguishable substrate specificity, while MK5 shows a distinct spectrum of substrates. MK2 and MK3 are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270991 [Multi-domain]  Cd Length: 263  Bit Score: 168.62  E-value: 1.93e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  34 KKTLGTGSFGRVMLVKHKATEQYYAMKIL-DKQKV---VKLkqieHtlnekriLQAVEFPFLVRL----EYSFKDNSNLY 105
Cdd:cd14089    6 KQVLGLGINGKVLECFHKKTGEKFALKVLrDNPKArreVEL----H-------WRASGCPHIVRIidvyENTYQGRKCLL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 106 MVMEYVPGGEMFSHL--RRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLI---DHQGYIQVTDFGFAKRVK 180
Cdd:cd14089   75 VVMECMEGGELFSRIqeRADSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYsskGPNAILKLTDFGFAKETT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 181 GRTW--TLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFAD--QPIQ--IYEKIVSGKVRFP----SHFS 250
Cdd:cd14089  155 TKKSlqTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNhgLAISpgMKKRIRNGQYEFPnpewSNVS 234
                        250       260       270
                 ....*....|....*....|....*....|....
gi 255958318 251 SDLKDLLRNLLQVDLTKRFgnlknGVSDIKTHKW 284
Cdd:cd14089  235 EEAKDLIRGLLKTDPSERL-----TIEEVMNHPW 263
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
33-285 3.12e-50

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


Pssm-ID: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 169.79  E-value: 3.12e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  33 RKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQkvvklkqIEHTLnEKRILQAVE-FPFLVRLEYSFKDNSNLYMVMEYV 111
Cdd:cd14092   10 REEALGDGSFSVCRKCVHKKTGQEFAVKIVSRR-------LDTSR-EVQLLRLCQgHPNIVKLHEVFQDELHTYLVMELL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 112 PGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLL---IDHQGYIQVTDFGFAkRVKG---RTWT 185
Cdd:cd14092   82 RGGELLERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLftdEDDDAEIKIVDFGFA-RLKPenqPLKT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 186 LCGTPEYLAPEIIL----SKGYNKAVDWWALGVLIYEMAAGYPPFFA----DQPIQIYEKIVSGKVRFPS----HFSSDL 253
Cdd:cd14092  161 PCFTLPYAAPEVLKqalsTQGYDESCDLWSLGVILYTMLSGQVPFQSpsrnESAAEIMKRIKSGDFSFDGeewkNVSSEA 240
                        250       260       270
                 ....*....|....*....|....*....|..
gi 255958318 254 KDLLRNLLQVDLTKRFgnlknGVSDIKTHKWF 285
Cdd:cd14092  241 KSLIQGLLTVDPSKRL-----TMSELRNHPWL 267
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
29-284 9.34e-50

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: 167.09  E-value: 9.34e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVvklKQIEHTL-NEKRILQAVEFPFLVRLEYSFKDNSNLYMV 107
Cdd:cd14183    6 ERYKVGRTIGDGNFAVVKECVERSTGREYALKIINKSKC---RGKEHMIqNEVSILRRVKHPNIVLLIEEMDMPTELYLV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 108 MEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLI-DHQG---YIQVTDFGFAKRVKGRT 183
Cdd:cd14183   83 MELVKGGDLFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVyEHQDgskSLKLGDFGLATVVDGPL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 184 WTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQ--IYEKIVSGKVRFPSHF----SSDLKDLL 257
Cdd:cd14183  163 YTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGSGDDQevLFDQILMGQVDFPSPYwdnvSDSAKELI 242
                        250       260
                 ....*....|....*....|....*..
gi 255958318 258 RNLLQVDLTKRFGNLKngvsdIKTHKW 284
Cdd:cd14183  243 TMMLQVDVDQRYSALQ-----VLEHPW 264
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
30-268 2.19e-49

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: 165.79  E-value: 2.19e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  30 DFERKKTLGTGSFGRVMLVKHKATEQYYAMKILD------KQKvvklKQIehtLNEKRILQAVEFPFLVRLEYSF--KDN 101
Cdd:cd08217    1 DYEVLETIGKGSFGTVRKVRRKSDGKILVWKEIDygkmseKEK----QQL---VSEVNILRELKHPNIVRYYDRIvdRAN 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 102 SNLYMVMEYVPGGEMFSHLRRI----GRFSEPHARFYAAQIVLTFEYLHSLD-----LIYRDLKPENLLIDHQGYIQVTD 172
Cdd:cd08217   74 TTLYIVMEYCEGGDLAQLIKKCkkenQYIPEEFIWKIFTQLLLALYECHNRSvgggkILHRDLKPANIFLDSDNNVKLGD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 173 FGFAKRVKGRTW---TLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKV-RFPSH 248
Cdd:cd08217  154 FGLARVLSHDSSfakTYVGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPPFQAANQLELAKKIKEGKFpRIPSR 233
                        250       260
                 ....*....|....*....|
gi 255958318 249 FSSDLKDLLRNLLQVDLTKR 268
Cdd:cd08217  234 YSSELNEVIKSMLNVDPDKR 253
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
28-284 3.85e-49

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: 165.42  E-value: 3.85e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  28 LEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKlKQIEHTLNEKRILQA-VEFPFLVRLEYSFKDNSNLYM 106
Cdd:cd14117    5 IDDFDIGRPLGKGKFGNVYLAREKQSKFIVALKVLFKSQIEK-EGVEHQLRREIEIQShLRHPNILRLYNYFHDRKRIYL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 107 VMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKG-RTWT 185
Cdd:cd14117   84 ILEYAPRGELYKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWSVHAPSlRRRT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 186 LCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDL 265
Cdd:cd14117  164 MCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKVDLKFPPFLSDGSRDLISKLLRYHP 243
                        250
                 ....*....|....*....
gi 255958318 266 TKRFgnlknGVSDIKTHKW 284
Cdd:cd14117  244 SERL-----PLKGVMEHPW 257
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
37-284 4.59e-49

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: 166.07  E-value: 4.59e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVM-LVKHKATEQYYAMKILDK----QKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYV 111
Cdd:cd14096    9 IGEGAFSNVYkAVPLRNTGKPVAIKVVRKadlsSDNLKGSSRANILKEVQIMKRLSHPNIVKLLDFQESDEYYYIVLELA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 112 PGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLID--------HQ------------------ 165
Cdd:cd14096   89 DGGEIFHQIVRLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFEpipfipsiVKlrkadddetkvdegefip 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 166 -------GYIQVTDFGFAKRVK-GRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEK 237
Cdd:cd14096  169 gvggggiGIVKLADFGLSKQVWdSNTKTPCGTVGYTAPEVVKDERYSKKVDMWALGCVLYTLLCGFPPFYDESIETLTEK 248
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 255958318 238 IVSGKVRFPS----HFSSDLKDLLRNLLQVDLTKRFgnlknGVSDIKTHKW 284
Cdd:cd14096  249 ISRGDYTFLSpwwdEISKSAKDLISHLLTVDPAKRY-----DIDEFLAHPW 294
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
30-268 7.08e-49

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: 164.51  E-value: 7.08e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  30 DFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQiEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVME 109
Cdd:cd08529    1 DFEILNKLGKGSFGVVYKVVRKVDGRVYALKQIDISRMSRKMR-EEAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIVME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 110 YVPGGEMFSHLRR-IGR-FSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRT---W 184
Cdd:cd08529   80 YAENGDLHSLIKSqRGRpLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAKILSDTTnfaQ 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 185 TLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVR-FPSHFSSDLKDLLRNLLQV 263
Cdd:cd08529  160 TIVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIVRGKYPpISASYSQDLSQLIDSCLTK 239

                 ....*
gi 255958318 264 DLTKR 268
Cdd:cd08529  240 DYRQR 244
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
35-284 1.13e-48

Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They contain N-terminal cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. The PKD subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 164.12  E-value: 1.13e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKlKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGG 114
Cdd:cd14082    9 EVLGSGQFGIVYGGKHRKTGRDVAIKVIDKLRFPT-KQESQLRNEVAILQQLSHPGVVNLECMFETPERVFVVMEKLHGD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 115 --EM-FSHLRriGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPEN-LLIDHQGYIQVT--DFGFAKRVKGRTW--TL 186
Cdd:cd14082   88 mlEMiLSSEK--GRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENvLLASAEPFPQVKlcDFGFARIIGEKSFrrSV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 187 CGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQiyEKIVSGKVRFP----SHFSSDLKDLLRNLLQ 262
Cdd:cd14082  166 VGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIN--DQIQNAAFMYPpnpwKEISPDAIDLINNLLQ 243
                        250       260
                 ....*....|....*....|..
gi 255958318 263 VDLTKRFgnlknGVSDIKTHKW 284
Cdd:cd14082  244 VKMRKRY-----SVDKSLSHPW 260
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
29-286 2.18e-48

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: 164.45  E-value: 2.18e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKvvkLKQIEHTL-NEKRILQAVEFPFLVRLEYSFKDNSNLYMV 107
Cdd:cd14168   10 KIFEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKA---LKGKESSIeNEIAVLRKIKHENIVALEDIYESPNHLYLV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 108 MEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLI---DHQGYIQVTDFGFAKrVKGR-- 182
Cdd:cd14168   87 MQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYfsqDEESKIMISDFGLSK-MEGKgd 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 183 -TWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDL----KDLL 257
Cdd:cd14168  166 vMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKADYEFDSPYWDDIsdsaKDFI 245
                        250       260
                 ....*....|....*....|....*....
gi 255958318 258 RNLLQVDLTKRfgnlkNGVSDIKTHKWFA 286
Cdd:cd14168  246 RNLMEKDPNKR-----YTCEQALRHPWIA 269
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
29-292 6.48e-48

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: 162.98  E-value: 6.48e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVV--KLKQIEHtlnEKRILQAVEFPFLVRLEYSFKDNSNLYM 106
Cdd:cd14086    1 DEYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSarDHQKLER---EARICRLLKHPNIVRLHDSISEEGFHYL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 107 VMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLI---DHQGYIQVTDFGFAKRVKG-- 181
Cdd:cd14086   78 VFDLVTGGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLaskSKGAAVKLADFGLAIEVQGdq 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 182 RTW-TLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSH----FSSDLKDL 256
Cdd:cd14086  158 QAWfGFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPSPewdtVTPEAKDL 237
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 255958318 257 LRNLLQVDLTKRFgnlknGVSDIKTHKWFATTDWIA 292
Cdd:cd14086  238 INQMLTVNPAKRI-----TAAEALKHPWICQRDRVA 268
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
37-268 2.47e-47

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: 160.13  E-value: 2.47e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKlkqiEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGGEM 116
Cdd:cd14006    1 LGRGRFGVVKRCIEKATGREFAAKFIPKRDKKK----EAVLREISILNQLQHPRIIQLHEAYESPTELVLILELCSGGEL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 117 FSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQV--TDFGFAKRVKGR--TWTLCGTPEY 192
Cdd:cd14006   77 LDRLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPSPQIkiIDFGLARKLNPGeeLKEIFGTPEF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 193 LAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRF----PSHFSSDLKDLLRNLLQVDLTKR 268
Cdd:cd14006  157 VAPEIVNGEPVSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISACRVDFseeyFSSVSQEAKDFIRKLLVKEPRKR 236
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
34-289 8.18e-47

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: 160.19  E-value: 8.18e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  34 KKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEhtlnekRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPG 113
Cdd:cd14175    6 KETIGVGSYSVCKRCVHKATNMEYAVKVIDKSKRDPSEEIE------ILLRYGQHPNIITLKDVYDDGKHVYLVTELMRG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 114 GEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLL-IDHQG---YIQVTDFGFAKRVK---GRTWTL 186
Cdd:cd14175   80 GELLDKILRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILyVDESGnpeSLRICDFGFAKQLRaenGLLMTP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 187 CGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPF---FADQPIQIYEKIVSGKVRFP----SHFSSDLKDLLRN 259
Cdd:cd14175  160 CYTANFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFangPSDTPEEILTRIGSGKFTLSggnwNTVSDAAKDLVSK 239
                        250       260       270
                 ....*....|....*....|....*....|
gi 255958318 260 LLQVDLTKRFgnlknGVSDIKTHKWFATTD 289
Cdd:cd14175  240 MLHVDPHQRL-----TAKQVLQHPWITQKD 264
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
30-284 9.13e-47

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: 159.15  E-value: 9.13e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  30 DFERKKTLGTGSFGRVMLVKHKATEQYYAMKILD-------KQKVVKLKQIE-----HTLNEKRILQAVEFPFLVRLEYS 97
Cdd:cd14077    2 NWEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIPrasnaglKKEREKRLEKEisrdiRTIREAALSSLLNHPHICRLRDF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  98 FKDNSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFG--- 174
Cdd:cd14077   82 LRTPNHYYMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFGlsn 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 175 -FAKRVKGRTWtlCGTPEYLAPEIILSKGY-NKAVDWWALGVLIYEMAAGYPPfFADQPIQI-YEKIVSGKVRFPSHFSS 251
Cdd:cd14077  162 lYDPRRLLRTF--CGSLYFAAPELLQAQPYtGPEVDVWSFGVVLYVLVCGKVP-FDDENMPAlHAKIKKGKVEYPSYLSS 238
                        250       260       270
                 ....*....|....*....|....*....|...
gi 255958318 252 DLKDLLRNLLQVDLTKRFGnLKNGVSdiktHKW 284
Cdd:cd14077  239 ECKSLISRMLVVDPKKRAT-LEQVLN----HPW 266
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
31-305 1.37e-46

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: 160.96  E-value: 1.37e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEhtlnekRILQAVEFPFLVRLEYSFKDNSNLYMVMEY 110
Cdd:cd14176   21 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIE------ILLRYGQHPNIITLKDVYDDGKYVYVVTEL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 111 VPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLL-IDHQG---YIQVTDFGFAKRVK---GRT 183
Cdd:cd14176   95 MKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGnpeSIRICDFGFAKQLRaenGLL 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 184 WTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFF---ADQPIQIYEKIVSGKVRFPSHF----SSDLKDL 256
Cdd:cd14176  175 MTPCYTANFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFSLSGGYwnsvSDTAKDL 254
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 255958318 257 LRNLLQVDLTKRFgnlknGVSDIKTHKWFATTDWIAIYQ-RKVEAPFIPK 305
Cdd:cd14176  255 VSKMLHVDPHQRL-----TAALVLRHPWIVHWDQLPQYQlNRQDAPHLVK 299
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
37-284 4.66e-46

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: 157.52  E-value: 4.66e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKQKVVK----------------LKQIEHTLN----EKRILQAVEFPFLVRLEY 96
Cdd:cd14118    2 IGKGSYGIVKLAYNEEDNTLYAMKILSKKKLLKqagffrrppprrkpgaLGKPLDPLDrvyrEIAILKKLDHPNVVKLVE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  97 SFKD--NSNLYMVMEYVPGGEMfshLRRIGR--FSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTD 172
Cdd:cd14118   82 VLDDpnEDNLYMVFELVDKGAV---MEVPTDnpLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIAD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 173 FGFAKRVKGRTWTL---CGTPEYLAPEIILSKGYN---KAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFP 246
Cdd:cd14118  159 FGVSNEFEGDDALLsstAGTPAFMAPEALSESRKKfsgKALDIWAMGVTLYCFVFGRCPFEDDHILGLHEKIKTDPVVFP 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 255958318 247 SHF--SSDLKDLLRNLLQVDLTKRFgnlknGVSDIKTHKW 284
Cdd:cd14118  239 DDPvvSEQLKDLILRMLDKNPSERI-----TLPEIKEHPW 273
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
31-295 5.41e-46

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: 158.25  E-value: 5.41e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEhtlnekRILQAVEFPFLVRLEYSFKDNSNLYMVMEY 110
Cdd:cd14178    5 YEIKEDIGIGSYSVCKRCVHKATSTEYAVKIIDKSKRDPSEEIE------ILLRYGQHPNIITLKDVYDDGKFVYLVMEL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 111 VPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLL-IDHQG---YIQVTDFGFAKRVK---GRT 183
Cdd:cd14178   79 MRGGELLDRILRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILyMDESGnpeSIRICDFGFAKQLRaenGLL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 184 WTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFF---ADQPIQIYEKIVSGKVRFP----SHFSSDLKDL 256
Cdd:cd14178  159 MTPCYTANFVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPFAngpDDTPEEILARIGSGKYALSggnwDSISDAAKDI 238
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 255958318 257 LRNLLQVDLTKRFGNLKngvsdIKTHKWFATTDWIAIYQ 295
Cdd:cd14178  239 VSKMLHVDPHQRLTAPQ-----VLRHPWIVNREYLSQNQ 272
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
31-284 7.03e-46

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: 156.39  E-value: 7.03e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEY 110
Cdd:cd14073    3 YELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKIEDEQDMVRIRREIEIMSSLNHPHIIRIYEVFENKDKIVIVMEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 111 VPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTW--TLCG 188
Cdd:cd14073   83 ASGGELYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLSNLYSKDKLlqTFCG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 189 TPEYLAPEIILSKGY-NKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHfSSDLKDLLRNLLQVDLTK 267
Cdd:cd14073  163 SPLYASPEIVNGTPYqGPEVDCWSLGVLLYTLVYGTMPFDGSDFKRLVKQISSGDYREPTQ-PSDASGLIRWMLTVNPKR 241
                        250
                 ....*....|....*..
gi 255958318 268 RfgnlkNGVSDIKTHKW 284
Cdd:cd14073  242 R-----ATIEDIANHWW 253
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
29-269 1.12e-45

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: 157.05  E-value: 1.12e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILD----KQKVVKLKQI-EHTLNEKRILQAVE-FPFLVRLEYSFKDNS 102
Cdd:cd14181   10 QKYDPKEVIGRGVSSVVRRCVHRHTGQEFAVKIIEvtaeRLSPEQLEEVrSSTLKEIHILRQVSgHPSIITLIDSYESST 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 103 NLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVK-- 180
Cdd:cd14181   90 FIFLVFDLMRRGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGFSCHLEpg 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 181 GRTWTLCGTPEYLAPEII------LSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPS----HFS 250
Cdd:cd14181  170 EKLRELCGTPGYLAPEILkcsmdeTHPGYGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMIMEGRYQFSSpewdDRS 249
                        250
                 ....*....|....*....
gi 255958318 251 SDLKDLLRNLLQVDLTKRF 269
Cdd:cd14181  250 STVKDLISRLLVVDPEIRL 268
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
28-268 1.42e-45

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: 155.83  E-value: 1.42e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  28 LEDFERkktLGTGSFGRVMLVKHKATEQYYAMKILDKQKvvklKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMV 107
Cdd:cd06614    2 YKNLEK---IGEGASGEVYKATDRATGKEVAIKKMRLRK----QNKELIINEILIMKECKHPNIVDYYDSYLVGDELWVV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 108 MEYVPGGEMFSHLRR-IGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFA----KRVKGR 182
Cdd:cd06614   75 MEYMDGGSLTDIITQnPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAaqltKEKSKR 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 183 TwTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSG---KVRFPSHFSSDLKDLLRN 259
Cdd:cd06614  155 N-SVVGTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPYLEEPPLRALFLITTKgipPLKNPEKWSPEFKDFLNK 233

                 ....*....
gi 255958318 260 LLQVDLTKR 268
Cdd:cd06614  234 CLVKDPEKR 242
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
31-305 7.28e-45

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: 155.17  E-value: 7.28e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEhtlnekRILQAVEFPFLVRLEYSFKDNSNLYMVMEY 110
Cdd:cd14177    6 YELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDKSKRDPSEEIE------ILMRYGQHPNIITLKDVYDDGRYVYLVTEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 111 VPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLL-IDHQG---YIQVTDFGFAKRVKGRTWTL 186
Cdd:cd14177   80 MKGGELLDRILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILyMDDSAnadSIRICDFGFAKQLRGENGLL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 187 ---CGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFF---ADQPIQIYEKIVSGKVRFP----SHFSSDLKDL 256
Cdd:cd14177  160 ltpCYTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPFAngpNDTPEEILLRIGSGKFSLSggnwDTVSDAAKDL 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 255958318 257 LRNLLQVDLTKRFgnlknGVSDIKTHKWFATTDWIAIYQ-RKVEAPFIPK 305
Cdd:cd14177  240 LSHMLHVDPHQRY-----TAEQVLKHSWIACRDQLPHYQlNRQDAPHLVK 284
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
29-269 7.52e-45

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: 154.69  E-value: 7.52e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILD--------KQKVVKLKqiEHTLNEKRILQAVE-FPFLVRLEYSFK 99
Cdd:cd14182    3 EKYEPKEILGRGVSSVVRRCIHKPTRQEYAVKIIDitgggsfsPEEVQELR--EATLKEIDILRKVSgHPNIIQLKDTYE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 100 DNSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRV 179
Cdd:cd14182   81 TNTFFFLVFDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFSCQL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 180 K--GRTWTLCGTPEYLAPEIIL------SKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPS---- 247
Cdd:cd14182  161 DpgEKLREVCGTPGYLAPEIIEcsmddnHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMSGNYQFGSpewd 240
                        250       260
                 ....*....|....*....|..
gi 255958318 248 HFSSDLKDLLRNLLQVDLTKRF 269
Cdd:cd14182  241 DRSDTVKDLISRFLVVQPQKRY 262
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
30-268 5.27e-44

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: 152.09  E-value: 5.27e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  30 DFERKKTLGTGSFGRVMLVKHKATEQY-YAMKILDKQKVVKlkqiEHTL--NEKRILQAVEFPFLVRLeYSFKDNSN-LY 105
Cdd:cd14202    3 EFSRKDLIGHGAFAVVFKGRHKEKHDLeVAVKCINKKNLAK----SQTLlgKEIKILKELKHENIVAL-YDFQEIANsVY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 106 MVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQG---------YIQVTDFGFA 176
Cdd:cd14202   78 LVMEYCNGGDLADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGgrksnpnniRIKIADFGFA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 177 KRVKGRTW--TLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPI---QIYEKIVSGKVRFPSHFSS 251
Cdd:cd14202  158 RYLQNNMMaaTLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQdlrLFYEKNKSLSPNIPRETSS 237
                        250
                 ....*....|....*..
gi 255958318 252 DLKDLLRNLLQVDLTKR 268
Cdd:cd14202  238 HLRQLLLGLLQRNQKDR 254
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
37-262 6.96e-44

Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. ULK2 is ubiquitously expressed and is essential in autophagy induction. ULK1 and ULK2 have unique and cell-type specific roles, but also display partially redundant roles in starvation-induced autophagy. They both display neuron-specific functions: ULK1 is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, and axon branching; ULK2 plays a role in axon development. The ULK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271022 [Multi-domain]  Cd Length: 256  Bit Score: 151.37  E-value: 6.96e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKA-TEQYYAMKILDKQKVVKLKqiehTLNEK--RILQAVEFPFLVRLeYSFKDNSN-LYMVMEYVP 112
Cdd:cd14120    1 IGHGAFAVVFKGRHRKkPDLPVAIKCITKKNLSKSQ----NLLGKeiKILKELSHENVVAL-LDCQETSSsVYLVMEYCN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 113 GGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQG---------YIQVTDFGFAKRVKGRT 183
Cdd:cd14120   76 GGDLADYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSgrkpspndiRLKIADFGFARFLQDGM 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 184 W--TLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQ---IYEKIVSGKVRFPSHFSSDLKDLLR 258
Cdd:cd14120  156 MaaTLCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFQAQTPQElkaFYEKNANLRPNIPSGTSPALKDLLL 235

                 ....
gi 255958318 259 NLLQ 262
Cdd:cd14120  236 GLLK 239
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
28-284 3.44e-43

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 5 (MAPKAP5 or MK5) is also called PRAK (p38-regulated/activated protein kinase). It contains a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271073 [Multi-domain]  Cd Length: 289  Bit Score: 150.69  E-value: 3.44e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  28 LEDFER--KKTLGTGSFGRVMLVKHKATEQYYAMKIL-DKQKVvklkQIEHTL--------NEKRILQ----AVEFPflv 92
Cdd:cd14171    3 LEEYEVnwTQKLGTGISGPVRVCVKKSTGERFALKILlDRPKA----RTEVRLhmmcsghpNIVQIYDvyanSVQFP--- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  93 RLEYSfkdNSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGY---IQ 169
Cdd:cd14171   76 GESSP---RARLLIVMELMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNSEdapIK 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 170 VTDFGFAKRVKGRTWTLCGTPEYLAPEIILSK-----------------GYNKAVDWWALGVLIYEMAAGYPPFFADQPI 232
Cdd:cd14171  153 LCDFGFAKVDQGDLMTPQFTPYYVAPQVLEAQrrhrkersgiptsptpyTYDKSCDMWSLGVIIYIMLCGYPPFYSEHPS 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255958318 233 Q-----IYEKIVSGKVRFP----SHFSSDLKDLLRNLLQVDLTKRFgnlknGVSDIKTHKW 284
Cdd:cd14171  233 RtitkdMKRKIMTGSYEFPeeewSQISEMAKDIVRKLLCVDPEERM-----TIEEVLHHPW 288
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
29-285 6.16e-43

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: 149.02  E-value: 6.16e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLkQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVM 108
Cdd:cd14069    1 EDWDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMKRAPGD-CPENIKKEVCIQKMLSHKNVVRFYGHRREGEFQYLFL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 109 EYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAK--RVKGRTWTL 186
Cdd:cd14069   80 EYASGGELFDKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLATvfRYKGKERLL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 187 ---CGTPEYLAPEIILSKGYN-KAVDWWALGVLIYEMAAGYPPFfaDQPI---QIYEKIVSGKVRF--P-SHFSSDLKDL 256
Cdd:cd14069  160 nkmCGTLPYVAPELLAKKKYRaEPVDVWSCGIVLFAMLAGELPW--DQPSdscQEYSDWKENKKTYltPwKKIDTAALSL 237
                        250       260
                 ....*....|....*....|....*....
gi 255958318 257 LRNLLQVDLTKRFgnlknGVSDIKTHKWF 285
Cdd:cd14069  238 LRKILTENPNKRI-----TIEDIKKHPWY 261
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
29-262 1.29e-42

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: 148.09  E-value: 1.29e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVM 108
Cdd:cd14186    1 EDFKVLNLLGKGSFACVYRARSLHTGLEVAIKMIDKKAMQKAGMVQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 109 EYVPGGEMFSHLRRIGR-FSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVK---GRTW 184
Cdd:cd14186   81 EMCHNGEMSRYLKNRKKpFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLKmphEKHF 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255958318 185 TLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQ 262
Cdd:cd14186  161 TMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVLADYEMPAFLSREAQDLIHQLLR 238
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
31-269 2.33e-42

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: 147.70  E-value: 2.33e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKktLGTGSFGRVMLVKHKATEQYYAMKILDKQKV--VKLKQIEHTLNekrILQAVEFPFLVRLEYSFKDNSNLYMVM 108
Cdd:cd14097    5 FGRK--LGQGSFGVVIEATHKETQTKWAIKKINREKAgsSAVKLLEREVD---ILKHVNHAHIIHLEEVFETPKRMYLVM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 109 EYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGY-------IQVTDFGFAKRVKG 181
Cdd:cd14097   80 ELCEDGELKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSIIdnndklnIKVTDFGLSVQKYG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 182 RTWTL----CGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFP----SHFSSDL 253
Cdd:cd14097  160 LGEDMlqetCGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRKGDLTFTqsvwQSVSDAA 239
                        250
                 ....*....|....*.
gi 255958318 254 KDLLRNLLQVDLTKRF 269
Cdd:cd14097  240 KNVLQQLLKVDPAHRM 255
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
31-284 6.66e-42

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: 146.25  E-value: 6.66e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYyAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEY 110
Cdd:cd14161    5 YEFLETLGKGTYGRVKKARDSSGRLV-AIKSIRKDRIKDEQDLLHIRREIEIMSSLNHPHIISVYEVFENSSKIVIVMEY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 111 VPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTW--TLCG 188
Cdd:cd14161   84 ASRGDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLSNLYNQDKFlqTYCG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 189 TPEYLAPEIILSKGY-NKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHfSSDLKDLLRNLLQVDLTK 267
Cdd:cd14161  164 SPLYASPEIVNGRPYiGPEVDSWSLGVLLYILVHGTMPFDGHDYKILVKQISSGAYREPTK-PSDACGLIRWLLMVNPER 242
                        250
                 ....*....|....*..
gi 255958318 268 RfgnlkNGVSDIKTHKW 284
Cdd:cd14161  243 R-----ATLEDVASHWW 254
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
37-285 9.01e-42

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: 145.86  E-value: 9.01e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKQKvvkLKQI----EHTLNEKRILQAVEFPFLVRLEYSFKDNSN--LYMVMEY 110
Cdd:cd14119    1 LGEGSYGKVKEVLDTETLCRRAVKILKKRK---LRRIpngeANVKREIQILRRLNHRNVIKLVDVLYNEEKqkLYMVMEY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 111 VPGG--EMFShLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVK-----GRT 183
Cdd:cd14119   78 CVGGlqEMLD-SAPDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVAEALDlfaedDTC 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 184 WTLCGTPEYLAPEIILSKGY--NKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLL 261
Cdd:cd14119  157 TTSQGSPAFQPPEIANGQDSfsGFKVDIWSAGVTLYNMTTGKYPFEGDNIYKLFENIGKGEYTIPDDVDPDLQDLLRGML 236
                        250       260
                 ....*....|....*....|....
gi 255958318 262 QVDLTKRFgnlknGVSDIKTHKWF 285
Cdd:cd14119  237 EKDPEKRF-----TIEQIRQHPWF 255
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
35-268 1.30e-41

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: 145.73  E-value: 1.30e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLN-EKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPG 113
Cdd:cd14070    8 RKLGEGSFAKVREGLHAVTGEKVAIKVIDKKKAKKDSYVTKNLRrEGRIQQMIRHPNITQLLDILETENSYYLVMELCPG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 114 GEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAK--RVKGRT---WTLCG 188
Cdd:cd14070   88 GNLMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSNcaGILGYSdpfSTQCG 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 189 TPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADqPI---QIYEKIVSGKVR-FPSHFSSDLKDLLRNLLQVD 264
Cdd:cd14070  168 SPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPFTVE-PFslrALHQKMVDKEMNpLPTDLSPGAISFLRSLLEPD 246

                 ....
gi 255958318 265 LTKR 268
Cdd:cd14070  247 PLKR 250
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
37-268 1.56e-41

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: 144.99  E-value: 1.56e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEqyYAMKILDKQKVVKlKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGGEM 116
Cdd:cd13999    1 IGSGSFGEVYKGKWRGTD--VAIKKLKVEDDND-ELLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 117 FSHLRRI-GRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRV---KGRTWTLCGTPEY 192
Cdd:cd13999   78 YDLLHKKkIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKnstTEKMTGVVGTPRW 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255958318 193 LAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVR--FPSHFSSDLKDLLRNLLQVDLTKR 268
Cdd:cd13999  158 MAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFKELSPIQIAAAVVQKGLRppIPPDCPPELSKLIKRCWNEDPEKR 235
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
29-268 2.52e-41

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: 145.18  E-value: 2.52e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMK-ILDKQKVVKLKQIehtLNEKRILQAVEFPFLVRLEYSFKDNSNLYMV 107
Cdd:cd06605    1 DDLEYLGELGEGNGGVVSKVRHRPSGQIMAVKvIRLEIDEALQKQI---LRELDVLHKCNSPYIVGFYGAFYSEGDISIC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 108 MEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHS-LDLIYRDLKPENLLIDHQGYIQVTDFGFAKR-VKGRTWT 185
Cdd:cd06605   78 MEYMDGGSLDKILKEVGRIPERILGKIAVAVVKGLIYLHEkHKIIHRDVKPSNILVNSRGQVKLCDFGVSGQlVDSLAKT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 186 LCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAG---YPPFFADQPIQIYE---KIVSGKV-RFPSH-FSSDLKDLL 257
Cdd:cd06605  158 FVGTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGrfpYPPPNAKPSMMIFEllsYIVDEPPpLLPSGkFSPDFQDFV 237
                        250
                 ....*....|.
gi 255958318 258 RNLLQVDLTKR 268
Cdd:cd06605  238 SQCLQKDPTER 248
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
31-268 2.96e-41

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: 145.74  E-value: 2.96e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILdkQKVVKLKQIEhtlNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEY 110
Cdd:cd14085    5 FEIESELGRGATSVVYRCRQKGTQKPYAVKKL--KKTVDKKIVR---TEIGVLLRLSHPNIIKLKEIFETPTEISLVLEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 111 VPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGY---IQVTDFGFAKRVKGR--TWT 185
Cdd:cd14085   80 VTGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPdapLKIADFGLSKIVDQQvtMKT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 186 LCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQ-IYEKIVSGKVRFPSHF----SSDLKDLLRNL 260
Cdd:cd14085  160 VCGTPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEPFYDERGDQyMFKRILNCDYDFVSPWwddvSLNAKDLVKKL 239

                 ....*...
gi 255958318 261 LQVDLTKR 268
Cdd:cd14085  240 IVLDPKKR 247
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
28-284 3.47e-41

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: 145.49  E-value: 3.47e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  28 LEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVK-----------------------LKQIEHTLNEKRILQ 84
Cdd:cd14199    1 LNQYKLKDEIGKGSYGVVKLAYNEDDNTYYAMKVLSKKKLMRqagfprrppprgaraapegctqpRGPIERVYQEIAILK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  85 AVEFPFLVRLEYSFKDNS--NLYMVMEYVPGGEMFShLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLI 162
Cdd:cd14199   81 KLDHPNVVKLVEVLDDPSedHLYMVFELVKQGPVME-VPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 163 DHQGYIQVTDFGFAKRVKGRTWTL---CGTPEYLAPEIILSKGYN---KAVDWWALGVLIYEMAAGYPPFFADQPIQIYE 236
Cdd:cd14199  160 GEDGHIKIADFGVSNEFEGSDALLtntVGTPAFMAPETLSETRKIfsgKALDVWAMGVTLYCFVFGQCPFMDERILSLHS 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 255958318 237 KIVSGKVRFPSH--FSSDLKDLLRNLLQVDLTKRFgnlknGVSDIKTHKW 284
Cdd:cd14199  240 KIKTQPLEFPDQpdISDDLKDLLFRMLDKNPESRI-----SVPEIKLHPW 284
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
37-284 3.82e-41

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: 145.25  E-value: 3.82e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKQ------KVvkLKQIE---HTLNEKRILQAVEFpflvrleysFKDNSNLYMV 107
Cdd:cd14090   10 LGEGAYASVQTCINLYTGKEYAVKIIEKHpghsrsRV--FREVEtlhQCQGHPNILQLIEY---------FEDDERFYLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 108 MEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYI---QVTDFGFAKRVKGRTW 184
Cdd:cd14090   79 FEKMRGGPLLSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKVspvKICDFDLGSGIKLSST 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 185 -----------TLCGTPEYLAPEII-----LSKGYNKAVDWWALGVLIYEMAAGYPPFF-------------ADQPIQ-- 233
Cdd:cd14090  159 smtpvttpellTPVGSAEYMAPEVVdafvgEALSYDKRCDLWSLGVILYIMLCGYPPFYgrcgedcgwdrgeACQDCQel 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 255958318 234 IYEKIVSGKVRFP----SHFSSDLKDLLRNLLQVDLTKRFgnlknGVSDIKTHKW 284
Cdd:cd14090  239 LFHSIQEGEYEFPekewSHISAEAKDLISHLLVRDASQRY-----TAEQVLQHPW 288
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
35-284 6.41e-41

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: 144.16  E-value: 6.41e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYY-----AMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVME 109
Cdd:cd14076    7 RTLGEGEFGKVKLGWPLPKANHRsgvqvAIKLIRRDTQQENCQTSKIMREINILKGLTHPNIVRLLDVLKTKKYIGIVLE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 110 YVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRV---KGRTW-T 185
Cdd:cd14076   87 FVSGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANTFdhfNGDLMsT 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 186 LCGTPEYLAPEIILSKG--YNKAVDWWALGVLIYEMAAGYPPF-------FADQPIQIYEKIVSGKVRFPSHFSSDLKDL 256
Cdd:cd14076  167 SCGSPCYAAPELVVSDSmyAGRKADIWSCGVILYAMLAGYLPFdddphnpNGDNVPRLYRYICNTPLIFPEYVTPKARDL 246
                        250       260
                 ....*....|....*....|....*...
gi 255958318 257 LRNLLQVDLTKRFgnlknGVSDIKTHKW 284
Cdd:cd14076  247 LRRILVPNPRKRI-----RLSAIMRHAW 269
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
51-270 9.59e-41

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: 143.59  E-value: 9.59e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  51 KATEQYYAMKILDKqkvvklKQIEHTLNEKRILQAVEFPFLVRLeYSFKDNSN-LYMVMEYVPGGEMFSHLRRIGRFSEP 129
Cdd:cd14010   22 KGTIEFVAIKCVDK------SKRPEVLNEVRLTHELKHPNVLKF-YEWYETSNhLWLVVEYCTGGDLETLLRQDGNLPES 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 130 HARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRV-------------------KGRTWTLCGTP 190
Cdd:cd14010   95 SVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLARREgeilkelfgqfsdegnvnkVSKKQAKRGTP 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 191 EYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSG-----KVRFPSHFSSDLKDLLRNLLQVDL 265
Cdd:cd14010  175 YYMAPELFQGGVHSFASDLWALGCVLYEMFTGKPPFVAESFTELVEKILNEdppppPPKVSSKPSPDFKSLLKGLLEKDP 254

                 ....*
gi 255958318 266 TKRFG 270
Cdd:cd14010  255 AKRLS 259
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
31-285 1.02e-40

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: 143.21  E-value: 1.02e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEY 110
Cdd:cd14162    2 YIVGKTLGHGSYAVVKKAYSTKHKCKVAIKIVSKKKAPEDYLQKFLPREIEVIKGLKHPNLICFYEAIETTSRVYIIMEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 111 VPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRV----KGRT--- 183
Cdd:cd14162   82 AENGDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFARGVmktkDGKPkls 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 184 WTLCGTPEYLAPEIILSKGYN-KAVDWWALGVLIYEMAAGYPPfFADQPIQIYEKIVSGKVRFPSH--FSSDLKDLLRNL 260
Cdd:cd14162  162 ETYCGSYAYASPEILRGIPYDpFLSDIWSMGVVLYTMVYGRLP-FDDSNLKVLLKQVQRRVVFPKNptVSEECKDLILRM 240
                        250       260
                 ....*....|....*....|....*
gi 255958318 261 LqVDLTKRFgnlknGVSDIKTHKWF 285
Cdd:cd14162  241 L-SPVKKRI-----TIEEIKRDPWF 259
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
37-268 1.46e-40

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: 142.81  E-value: 1.46e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKA-TEQYYAMKILDKQKVVKLkQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGGE 115
Cdd:cd14121    3 LGSGTYATVYKAYRKSgAREVVAVKCVSKSSLNKA-STENLLTEIELLKKLKHPHIVELKDFQWDEEHIYLIMEYCSGGD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 116 MFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLID--HQGYIQVTDFGFAKRVKGR--TWTLCGTPE 191
Cdd:cd14121   82 LSRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSsrYNPVLKLADFGFAQHLKPNdeAHSLRGSPL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 192 YLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGK-VRFPS--HFSSDLKDLLRNLLQVDLTKR 268
Cdd:cd14121  162 YMAPEMILKKKYDARVDLWSVGVILYECLFGRAPFASRSFEELEEKIRSSKpIEIPTrpELSADCRDLLLRLLQRDPDRR 241
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
33-268 1.72e-40

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: 142.88  E-value: 1.72e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  33 RKKTLGTGSFGRVMLVKHKATEQYYAMKildkqkVVKLKQIE-HTLNEKRILQaVEFPFLVRLEY--------SFKDNSN 103
Cdd:cd06625    4 QGKLLGQGAFGQVYLCYDADTGRELAVK------QVEIDPINtEASKEVKALE-CEIQLLKNLQHerivqyygCLQDEKS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 104 LYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRV---- 179
Cdd:cd06625   77 LSIFMEYMPGGSVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGASKRLqtic 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 180 -KGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRF--PSHFSSDLKDL 256
Cdd:cd06625  157 sSTGMKSVTGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPWAEFEPMAAIFKIATQPTNPqlPPHVSEDARDF 236
                        250
                 ....*....|..
gi 255958318 257 LRNLLQVDLTKR 268
Cdd:cd06625  237 LSLIFVRNKKQR 248
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
31-284 2.10e-40

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: 143.17  E-value: 2.10e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVK-----------------------LKQIEHTLNEKRILQAVE 87
Cdd:cd14200    2 YKLQSEIGKGSYGVVKLAYNESDDKYYAMKVLSKKKLLKqygfprrppprgskaaqgeqakpLAPLERVYQEIAILKKLD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  88 FPFLVRLEYSFKD--NSNLYMVMEYVPGGEMFsHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQ 165
Cdd:cd14200   82 HVNIVKLIEVLDDpaEDNLYMVFDLLRKGPVM-EVPSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGDD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 166 GYIQVTDFGFAKRVKGRTWTL---CGTPEYLAPEIILSKGYN---KAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIV 239
Cdd:cd14200  161 GHVKIADFGVSNQFEGNDALLsstAGTPAFMAPETLSDSGQSfsgKALDVWAMGVTLYCFVYGKCPFIDEFILALHNKIK 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 255958318 240 SGKVRFPS--HFSSDLKDLLRNLLQVDLTKRFgnlknGVSDIKTHKW 284
Cdd:cd14200  241 NKPVEFPEepEISEELKDLILKMLDKNPETRI-----TVPEIKVHPW 282
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
37-268 2.43e-40

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: 2.43e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVmlvkHKA----TEQYYAMKILDKQKVVKlKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVP 112
Cdd:cd06627    8 IGRGAFGSV----YKGlnlnTGEFVAIKQISLEKIPK-SDLKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYIILEYVE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 113 GGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFA---KRVKGRTWTLCGT 189
Cdd:cd06627   83 NGSLASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVAtklNEVEKDENSVVGT 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 190 PEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGK-VRFPSHFSSDLKDLLRNLLQVDLTKR 268
Cdd:cd06627  163 PYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPYYDLQPMAALFRIVQDDhPPLPENISPELRDFLLQCFQKDPTLR 242
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
36-285 3.86e-40

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: 141.84  E-value: 3.86e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  36 TLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKlKQIEHTL-NEKRILQAVEFPFLVRLEYSFKDNSN-LYMVMEYVPG 113
Cdd:cd14165    8 NLGEGSYAKVKSAYSERLKCNVAIKIIDKKKAPD-DFVEKFLpRELEILARLNHKSIIKTYEIFETSDGkVYIVMELGVQ 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 114 GEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRV----KGRTW---TL 186
Cdd:cd14165   87 GDLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRClrdeNGRIVlskTF 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 187 CGTPEYLAPEIILSKGYN-KAVDWWALGVLIYEMAAGYPPfFADQPIQIYEKI-VSGKVRFPS--HFSSDLKDLLRNLLQ 262
Cdd:cd14165  167 CGSAAYAAPEVLQGIPYDpRIYDIWSLGVILYIMVCGSMP-YDDSNVKKMLKIqKEHRVRFPRskNLTSECKDLIYRLLQ 245
                        250       260
                 ....*....|....*....|...
gi 255958318 263 VDLTKRFgnlknGVSDIKTHKWF 285
Cdd:cd14165  246 PDVSQRL-----CIDEVLSHPWL 263
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
31-268 3.90e-40

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: 141.99  E-value: 3.90e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEY 110
Cdd:cd14187    9 YVRGRFLGKGGFAKCYEITDADTKEVFAGKIVPKSLLLKPHQKEKMSMEIAIHRSLAHQHVVGFHGFFEDNDFVYVVLEL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 111 VPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVK---GRTWTLC 187
Cdd:cd14187   89 CRRRSLLELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLATKVEydgERKKTLC 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 188 GTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTK 267
Cdd:cd14187  169 GTPNYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTA 248

                 .
gi 255958318 268 R 268
Cdd:cd14187  249 R 249
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
29-268 6.87e-40

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: 140.86  E-value: 6.87e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKIL----DKQKVVKlkqiehtlnEKRILQAVEFPFLVRLEYSFKDNSNL 104
Cdd:cd06612    3 EVFDILEKLGEGSYGSVYKAIHKETGQVVAIKVVpveeDLQEIIK---------EISILKQCDSPYIVKYYGSYFKNTDL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 105 YMVMEYVPGGEMFSHLRRIGR-FSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRT 183
Cdd:cd06612   74 WIVMEYCGAGSVSDIMKITNKtLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQLTDTM 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 184 W---TLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIV---SGKVRFPSHFSSDLKDLL 257
Cdd:cd06612  154 AkrnTVIGTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPYSDIHPMRAIFMIPnkpPPTLSDPEKWSPEFNDFV 233
                        250
                 ....*....|.
gi 255958318 258 RNLLQVDLTKR 268
Cdd:cd06612  234 KKCLVKDPEER 244
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
30-268 1.04e-39

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: 140.64  E-value: 1.04e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  30 DFERKKTLGTGSFGRVMLVKHKateqyyamkilDKQKVVKLKQI----------EHTLNEKRILQAVEFPFLVRLEYSFK 99
Cdd:cd08220    1 KYEKIRVVGRGAYGTVYLCRRK-----------DDNKLVIIKQIpveqmtkeerQAALNEVKVLSMLHHPNIIEYYESFL 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 100 DNSNLYMVMEYVPGGEMFSHLRRIGR--FSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLID-HQGYIQVTDFGFA 176
Cdd:cd08220   70 EDKALMIVMEYAPGGTLFEYIQQRKGslLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNkKRTVVKIGDFGIS 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 177 KRV--KGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPS-HFSSDL 253
Cdd:cd08220  150 KILssKSKAYTVVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAFEAANLPALVLKIMRGTFAPISdRYSEEL 229
                        250
                 ....*....|....*
gi 255958318 254 KDLLRNLLQVDLTKR 268
Cdd:cd08220  230 RHLILSMLHLDPNKR 244
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
33-261 1.06e-39

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: 140.53  E-value: 1.06e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  33 RKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVP 112
Cdd:cd14188    5 RGKVLGKGGFAKCYEMTDLTTNKVYAAKIIPHSRVSKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 113 GGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVK---GRTWTLCGT 189
Cdd:cd14188   85 RRSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAARLEpleHRRRTICGT 164
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255958318 190 PEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLL 261
Cdd:cd14188  165 PNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYSLPSSLLAPAKHLIASML 236
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
30-269 1.44e-39

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: 140.53  E-value: 1.44e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  30 DFE--RKKTLGTGSFGRVMLVKH-KATEQYYAMKILDKQKVVKLKQIehTLNEKRILQAVEFPFLVRLeYSFKDNSN-LY 105
Cdd:cd14201    5 DFEysRKDLVGHGAFAVVFKGRHrKKTDWEVAIKSINKKNLSKSQIL--LGKEIKILKELQHENIVAL-YDVQEMPNsVF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 106 MVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGY---------IQVTDFGFA 176
Cdd:cd14201   82 LVMEYCNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASRkkssvsgirIKIADFGFA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 177 KRVKGRTW--TLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQI---YEKIVSGKVRFPSHFSS 251
Cdd:cd14201  162 RYLQSNMMaaTLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQDLrmfYEKNKNLQPSIPRETSP 241
                        250
                 ....*....|....*...
gi 255958318 252 DLKDLLRNLLQVDLTKRF 269
Cdd:cd14201  242 YLADLLLGLLQRNQKDRM 259
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
31-268 1.70e-39

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: 139.95  E-value: 1.70e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVvKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEY 110
Cdd:cd08218    2 YVRIKKIGEGSFGKALLVKSKEDGKQYVIKEINISKM-SPKEREESRKEVAVLSKMKHPNIVQYQESFEENGNLYIVMDY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 111 VPGGEMFSHL--RRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAkRVKGRTWTLC- 187
Cdd:cd08218   81 CDGGDLYKRInaQRGVLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIA-RVLNSTVELAr 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 188 ---GTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKV-RFPSHFSSDLKDLLRNLLQV 263
Cdd:cd08218  160 tciGTPYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFEAGNMKNLVLKIIRGSYpPVPSRYSYDLRSLVSQLFKR 239

                 ....*
gi 255958318 264 DLTKR 268
Cdd:cd08218  240 NPRDR 244
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
33-268 2.23e-39

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: 141.33  E-value: 2.23e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  33 RKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKvvklkqiehTLNEKRILQAVEF----PFLVRLEYSFKDNSNLYMVM 108
Cdd:cd14179   11 KDKPLGEGSFSICRKCLHKKTNQEYAVKIVSKRM---------EANTQREIAALKLceghPNIVKLHEVYHDQLHTFLVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 109 EYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQG---YIQVTDFGFAkRVK----G 181
Cdd:cd14179   82 ELLKGGELLERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDESdnsEIKIIDFGFA-RLKppdnQ 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 182 RTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPF-------FADQPIQIYEKIVSGKVRFP----SHFS 250
Cdd:cd14179  161 PLKTPCFTLHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFqchdkslTCTSAEEIMKKIKQGDFSFEgeawKNVS 240
                        250
                 ....*....|....*...
gi 255958318 251 SDLKDLLRNLLQVDLTKR 268
Cdd:cd14179  241 QEAKDLIQGLLTVDPNKR 258
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
33-285 2.50e-39

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: 141.16  E-value: 2.50e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  33 RKKTLGTGSFGRVMLVKHKATEQYYAMKILDKqkvvklKQIEHTLNEKRILQAVE-FPFLVRLEYSFKDNSNLYMVMEYV 111
Cdd:cd14180   10 EEPALGEGSFSVCRKCRHRQSGQEYAVKIISR------RMEANTQREVAALRLCQsHPNIVALHEVLHDQYHTYLVMELL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 112 PGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQG---YIQVTDFGFAK-RVKGRT--WT 185
Cdd:cd14180   84 RGGELLDRIKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESdgaVLKVIDFGFARlRPQGSRplQT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 186 LCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPF-------FADQPIQIYEKIVSGKVRFP----SHFSSDLK 254
Cdd:cd14180  164 PCFTLQYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFqskrgkmFHNHAADIMHKIKEGDFSLEgeawKGVSEEAK 243
                        250       260       270
                 ....*....|....*....|....*....|.
gi 255958318 255 DLLRNLLQVDLTKRfgnLKngVSDIKTHKWF 285
Cdd:cd14180  244 DLVRGLLTVDPAKR---LK--LSELRESDWL 269
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
31-268 3.37e-39

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: 139.32  E-value: 3.37e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVvKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEY 110
Cdd:cd08225    2 YEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKM-PVKEKEASKKEVILLAKMKHPNIVTFFASFQENGRLFIVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 111 VPGGEMfshLRRIGR-----FSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYI-QVTDFGFAKRVKGRT- 183
Cdd:cd08225   81 CDGGDL---MKRINRqrgvlFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVaKLGDFGIARQLNDSMe 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 184 --WTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPS-HFSSDLKDLLRNL 260
Cdd:cd08225  158 laYTCVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFEGNNLHQLVLKICQGYFAPISpNFSRDLRSLISQL 237

                 ....*...
gi 255958318 261 LQVDLTKR 268
Cdd:cd08225  238 FKVSPRDR 245
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
29-284 3.41e-39

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


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 139.74  E-value: 3.41e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFE-RKKTLGTGSFGRVMLVKHKATEQYYAMKIL-DKQKVvkLKQIEHTLnekrilQAVEFPFLVRL----EYSFKDNS 102
Cdd:cd14172    3 DDYKlSKQVLGLGVNGKVLECFHRRTGQKCALKLLyDSPKA--RREVEHHW------RASGGPHIVHIldvyENMHHGKR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 103 NLYMVMEYVPGGEMFSHLRRIG--RFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLI---DHQGYIQVTDFGFAK 177
Cdd:cd14172   75 CLLIIMECMEGGELFSRIQERGdqAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYtskEKDAVLKLTDFGFAK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 178 R--VKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFAD--QPIQ--IYEKIVSGKVRFP----S 247
Cdd:cd14172  155 EttVQNALQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYSNtgQAISpgMKRRIRMGQYGFPnpewA 234
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 255958318 248 HFSSDLKDLLRNLLQVDLTKRFgnlknGVSDIKTHKW 284
Cdd:cd14172  235 EVSEEAKQLIRHLLKTDPTERM-----TITQFMNHPW 266
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
31-284 3.91e-39

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: 138.96  E-value: 3.91e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILDK-QKV---VKLKQIEHtlnekrilQAVEFPFLVRLEYSFKDNSNLYM 106
Cdd:cd14665    2 YELVKDIGSGNFGVARLMRDKQTKELVAVKYIERgEKIdenVQREIINH--------RSLRHPNIVRFKEVILTPTHLAI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 107 VMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQG--YIQVTDFGFAKR--VKGR 182
Cdd:cd14665   74 VMEYAAGGELFERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPapRLKICDFGYSKSsvLHSQ 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 183 TWTLCGTPEYLAPEIILSKGYN-KAVDWWALGVLIYEMAAGYPPFFADQPIQIYEK----IVSGKVRFPS--HFSSDLKD 255
Cdd:cd14665  154 PKSTVGTPAYIAPEVLLKKEYDgKIADVWSCGVTLYVMLVGAYPFEDPEEPRNFRKtiqrILSVQYSIPDyvHISPECRH 233
                        250       260
                 ....*....|....*....|....*....
gi 255958318 256 LLRNLLQVDLTKRFgnlknGVSDIKTHKW 284
Cdd:cd14665  234 LISRIFVADPATRI-----TIPEIRNHEW 257
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
32-268 1.19e-38

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: 137.82  E-value: 1.19e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  32 ERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVvKLKQIEHTLNEKRILQAVEFPFLVRLeYSFKDNSN-LYMVMEY 110
Cdd:cd06626    3 QRGNKIGEGTFGKVYTAVNLDTGELMAMKEIRFQDN-DPKTIKEIADEMKVLEGLDHPNLVRY-YGVEVHREeVYIFMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 111 VPGGEMFsHLRRIGRFsEPHA--RFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTWT--- 185
Cdd:cd06626   81 CQEGTLE-ELLRHGRI-LDEAviRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAVKLKNNTTTmap 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 186 -----LCGTPEYLAPEIILS---KGYNKAVDWWALGVLIYEMAAGYPPF-FADQPIQIYEKIVSG-KVRFPSH--FSSDL 253
Cdd:cd06626  159 gevnsLVGTPAYMAPEVITGnkgEGHGRAADIWSLGCVVLEMATGKRPWsELDNEWAIMYHVGMGhKPPIPDSlqLSPEG 238
                        250
                 ....*....|....*
gi 255958318 254 KDLLRNLLQVDLTKR 268
Cdd:cd06626  239 KDFLSRCLESDPKKR 253
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
31-284 2.17e-38

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: 137.21  E-value: 2.17e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKvvklKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEY 110
Cdd:cd14662    2 YELVKDIGSGNFGVARLMRNKETKELVAVKYIERGL----KIDENVQREIINHRSLRHPNIIRFKEVVLTPTHLAIVMEY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 111 VPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQ--GYIQVTDFGFAKR--VKGRTWTL 186
Cdd:cd14662   78 AAGGELFERICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGSpaPRLKICDFGYSKSsvLHSQPKST 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 187 CGTPEYLAPEIILSKGYN-KAVDWWALGVLIYEMAAGYPPFF-ADQPIQI---YEKIVSGKVRFPS--HFSSDLKDLLRN 259
Cdd:cd14662  158 VGTPAYIAPEVLSRKEYDgKVADVWSCGVTLYVMLVGAYPFEdPDDPKNFrktIQRIMSVQYKIPDyvRVSQDCRHLLSR 237
                        250       260
                 ....*....|....*....|....*
gi 255958318 260 LLQVDLTKRFgnlknGVSDIKTHKW 284
Cdd:cd14662  238 IFVANPAKRI-----TIPEIKNHPW 257
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
29-268 2.97e-38

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: 136.80  E-value: 2.97e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDkqkVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVM 108
Cdd:cd06648    7 SDLDNFVKIGEGSTGIVCIATDKSTGRQVAVKKMD---LRKQQRRELLFNEVVIMRDYQHPNIVEMYSSYLVGDELWVVM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 109 EYVPGG---EMFSHlrriGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKG---R 182
Cdd:cd06648   84 EFLEGGaltDIVTH----TRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFCAQVSKevpR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 183 TWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSG---KVRFPSHFSSDLKDLLRN 259
Cdd:cd06648  160 RKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIRDNeppKLKNLHKVSPRLRSFLDR 239

                 ....*....
gi 255958318 260 LLQVDLTKR 268
Cdd:cd06648  240 MLVRDPAQR 248
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
37-268 5.50e-38

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: 136.80  E-value: 5.50e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKQKVvklKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGGEM 116
Cdd:cd06611   13 LGDGAFGKVYKAQHKETGLFAAAKIIQIESE---EELEDFMVEIDILSECKHPNIVGLYEAYFYENKLWILIEFCDGGAL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 117 FSHLRRIGR-FSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFA---KRVKGRTWTLCGTPEY 192
Cdd:cd06611   90 DSIMLELERgLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSaknKSTLQKRDTFIGTPYW 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 193 LAPEIIL-----SKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSG---KVRFPSHFSSDLKDLLRNLLQVD 264
Cdd:cd06611  170 MAPEVVAcetfkDNPYDYKADIWSLGITLIELAQMEPPHHELNPMRVLLKILKSeppTLDQPSKWSSSFNDFLKSCLVKD 249

                 ....
gi 255958318 265 LTKR 268
Cdd:cd06611  250 PDDR 253
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
33-262 6.35e-38

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: 135.83  E-value: 6.35e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  33 RKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVP 112
Cdd:cd14189    5 KGRLLGKGGFARCYEMTDLATNKTYAVKVIPHSRVAKPHQREKIVNEIELHRDLHHKHVVKFSHHFEDAENIYIFLELCS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 113 GGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKR---VKGRTWTLCGT 189
Cdd:cd14189   85 RKSLAHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAARlepPEQRKKTICGT 164
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255958318 190 PEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQ 262
Cdd:cd14189  165 PNYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFETLDLKETYRCIKQVKYTLPASLSLPARHLLAGILK 237
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
29-292 8.47e-38

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: 136.90  E-value: 8.47e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDkqkVVKLKQ-----IEHTLNEKRILQAVEFPFLVRLEYSFKDNSN 103
Cdd:cd14094    3 DVYELCEVIGKGPFSVVRRCIHRETGQQFAVKIVD---VAKFTSspglsTEDLKREASICHMLKHPHIVELLETYSSDGM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 104 LYMVMEYVPGGEM-FSHLRRIGR---FSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLI---DHQGYIQVTDFGFA 176
Cdd:cd14094   80 LYMVFEFMDGADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 177 KRVKGRTWTLCG---TPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQpIQIYEKIVSGKVRFP----SHF 249
Cdd:cd14094  160 IQLGESGLVAGGrvgTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKGKYKMNprqwSHI 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 255958318 250 SSDLKDLLRNLLQVDLTKRFgnlknGVSDIKTHKWFATTDWIA 292
Cdd:cd14094  239 SESAKDLVRRMLMLDPAERI-----TVYEALNHPWIKERDRYA 276
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
37-284 1.14e-37

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module. MLCK2, MLCK3, and MLCK4 share a simpler domain architecture of a single kinase domain near the C-terminus and the absence of Ig-like or FN3 domains. The MLCK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271005 [Multi-domain]  Cd Length: 250  Bit Score: 135.05  E-value: 1.14e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILdkqKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGGEM 116
Cdd:cd14103    1 LGRGKFGTVYRCVEKATGKELAAKFI---KCRKAKDREDVRNEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAGGEL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 117 F-------SHLrrigrfSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLL-IDHQGY-IQVTDFGFAKRVKGRTWT-- 185
Cdd:cd14103   78 FervvdddFEL------TERDCILFMRQICEGVQYMHKQGILHLDLKPENILcVSRTGNqIKIIDFGLARKYDPDKKLkv 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 186 LCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFP-SHF---SSDLKDLLRNLL 261
Cdd:cd14103  152 LFGTPEFVAPEVVNYEPISYATDMWSVGVICYVLLSGLSPFMGDNDAETLANVTRAKWDFDdEAFddiSDEAKDFISKLL 231
                        250       260
                 ....*....|....*....|...
gi 255958318 262 QVDLTKRFgnlknGVSDIKTHKW 284
Cdd:cd14103  232 VKDPRKRM-----SAAQCLQHPW 249
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
29-268 1.24e-37

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: 135.91  E-value: 1.24e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYA---MKILDKQKVVKlkqiEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLY 105
Cdd:cd07833    1 NKYEVLGVVGEGAYGVVLKCRNKATGEIVAikkFKESEDDEDVK----KTALREVKVLRQLRHENIVNLKEAFRRKGRLY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 106 MVMEYVPGgEMFSHLRRIGRFSEPHA-RFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTW 184
Cdd:cd07833   77 LVFEYVER-TLLELLEASPGGLPPDAvRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFARALTARPA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 185 TLC----GTPEYLAPEIILSKG-YNKAVDWWALGVLIYEMAAGYPPFFADQPI-QIY----------------------- 235
Cdd:cd07833  156 SPLtdyvATRWYRAPELLVGDTnYGKPVDVWAIGCIMAELLDGEPLFPGDSDIdQLYliqkclgplppshqelfssnprf 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 255958318 236 --------EKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKR 268
Cdd:cd07833  236 agvafpepSQPESLERRYPGKVSSPALDFLKACLRMDPKER 276
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
35-285 1.37e-37

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: 134.67  E-value: 1.37e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYYAMKILdKQKVVKLKQiehTLNEKRILQ----AVEFPFLVRLEYSFKDN--SNLYMVM 108
Cdd:cd05118    5 RKIGEGAFGTVWLARDKVTGEKVAIKKI-KNDFRHPKA---ALREIKLLKhlndVEGHPNIVKLLDVFEHRggNHLCLVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 109 EYVpgGEMFSHL--RRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQ-GYIQVTDFGFAKRVKGRTWT 185
Cdd:cd05118   81 ELM--GMNLYELikDYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLElGQLKLADFGLARSFTSPPYT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 186 -LCGTPEYLAPEIIL-SKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVS--GKvrfpshfsSDLKDLLRNLL 261
Cdd:cd05118  159 pYVATRWYRAPEVLLgAKPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIVRllGT--------PEALDLLSKML 230
                        250       260
                 ....*....|....*....|....
gi 255958318 262 QVDLTKRFgnlknGVSDIKTHKWF 285
Cdd:cd05118  231 KYDPAKRI-----TASQALAHPYF 249
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
35-284 1.65e-37

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 2 (MAPKAP2 or MK2) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK2 is a bonafide substrate for the MAPK p38. It is closely related to MK3 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. The MK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 136.32  E-value: 1.65e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYYAMKILdkQKVVKLKQiEHTLNekriLQAVEFPFLVRL----EYSFKDNSNLYMVMEY 110
Cdd:cd14170    8 QVLGLGINGKVLQIFNKRTQEKFALKML--QDCPKARR-EVELH----WRASQCPHIVRIvdvyENLYAGRKCLLIVMEC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 111 VPGGEMFSHLRRIG--RFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQ---GYIQVTDFGFAKRVKGRT-- 183
Cdd:cd14170   81 LDGGELFSRIQDRGdqAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKrpnAILKLTDFGFAKETTSHNsl 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 184 WTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIY----EKIVSGKVRFP----SHFSSDLKD 255
Cdd:cd14170  161 TTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAISpgmkTRIRMGQYEFPnpewSEVSEEVKM 240
                        250       260
                 ....*....|....*....|....*....
gi 255958318 256 LLRNLLQVDLTKRFgnlknGVSDIKTHKW 284
Cdd:cd14170  241 LIRNLLKTEPTQRM-----TITEFMNHPW 264
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
30-285 1.88e-37

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: 134.44  E-value: 1.88e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  30 DFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVV--------KLK------QIEHTLNEKRilqaveFPFLVRLE 95
Cdd:cd14004    1 DYTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFKERILvdtwvrdrKLGtvpleiHILDTLNKRS------HPNIVKLL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  96 YSFKDNSNLYMVME-YVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFG 174
Cdd:cd14004   75 DFFEDDEFYYLVMEkHGSGMDLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 175 FAKRVK-GRTWTLCGTPEYLAPEIILSKGY-NKAVDWWALGVLIYEMAAGYPPFFAdqpiqiYEKIVSGKVRFPSHFSSD 252
Cdd:cd14004  155 SAAYIKsGPFDTFVGTIDYAAPEVLRGNPYgGKEQDIWALGVLLYTLVFKENPFYN------IEEILEADLRIPYAVSED 228
                        250       260       270
                 ....*....|....*....|....*....|...
gi 255958318 253 LKDLLRNLLQVDLTKRfgnlkNGVSDIKTHKWF 285
Cdd:cd14004  229 LIDLISRMLNRDVGDR-----PTIEELLTDPWL 256
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
34-285 2.98e-37

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


Pssm-ID: 271008 [Multi-domain]  Cd Length: 268  Bit Score: 134.40  E-value: 2.98e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  34 KKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVK--LKQIEHtlnEKRIL-QAVEFPFLVRLEYSFKDNSNLYMVMEY 110
Cdd:cd14106   13 STPLGRGKFAVVRKCIHKETGKEYAAKFLRKRRRGQdcRNEILH---EIAVLeLCKDCPRVVNLHEVYETRSELILILEL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 111 VPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDH---QGYIQVTDFGFAKRVKGRT--WT 185
Cdd:cd14106   90 AAGGELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSefpLGDIKLCDFGISRVIGEGEeiRE 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 186 LCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPS-HF---SSDLKDLLRNLL 261
Cdd:cd14106  170 ILGTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNISQCNLDFPEeLFkdvSPLAIDFIKRLL 249
                        250       260
                 ....*....|....*....|....
gi 255958318 262 QVDLTKRFgnlknGVSDIKTHKWF 285
Cdd:cd14106  250 VKDPEKRL-----TAKECLEHPWL 268
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
29-268 3.04e-37

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: 134.68  E-value: 3.04e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKvvKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVM 108
Cdd:cd06609    1 ELFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDLEE--AEDEIEDIQQEIQFLSQCDSPYITKYYGSFLKGSKLWIIM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 109 EYVPGGEMfSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKG---RTWT 185
Cdd:cd06609   79 EYCGGGSV-LDLLKPGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSGQLTStmsKRNT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 186 LCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSgkvRFP-----SHFSSDLKDLLRNL 260
Cdd:cd06609  158 FVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPLSDLHPMRVLFLIPK---NNPpslegNKFSKPFKDFVELC 234

                 ....*...
gi 255958318 261 LQVDLTKR 268
Cdd:cd06609  235 LNKDPKER 242
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
30-268 9.24e-37

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: 132.79  E-value: 9.24e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  30 DFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKvvKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVME 109
Cdd:cd08219    1 QYNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIRLPK--SSSAVEDSRKEAVLLAKMKHPNIVAFKESFEADGHLYIVME 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 110 YVPGGEMFSHLR-RIGR-FSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTWTLC 187
Cdd:cd08219   79 YCDGGDLMQKIKlQRGKlFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLTSPGAYAC 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 188 ---GTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVR-FPSHFSSDLKDLLRNLLQV 263
Cdd:cd08219  159 tyvGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGSYKpLPSHYSYELRSLIKQMFKR 238

                 ....*
gi 255958318 264 DLTKR 268
Cdd:cd08219  239 NPRSR 243
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
33-268 1.70e-36

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: 132.27  E-value: 1.70e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  33 RKKTLGTGSFGRVMLVKHKATEQYYAMK--ILD----KQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYM 106
Cdd:cd06628    4 KGALIGSGSFGSVYLGMNASSGELMAVKqvELPsvsaENKDRKKSMLDALQREIALLRELQHENIVQYLGSSSDANHLNI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 107 VMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVK------ 180
Cdd:cd06628   84 FLEYVPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISKKLEanslst 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 181 ---GRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKI-VSGKVRFPSHFSSDLKDL 256
Cdd:cd06628  164 knnGARPSLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPFPDCTQMQAIFKIgENASPTIPSNISSEARDF 243
                        250
                 ....*....|..
gi 255958318 257 LRNLLQVDLTKR 268
Cdd:cd06628  244 LEKTFEIDHNKR 255
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
37-268 4.28e-36

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


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 131.25  E-value: 4.28e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKqKVVKLKQIEHTLNekrILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGGEM 116
Cdd:cd14113   15 LGRGRFSVVKKCDQRGTKRAVATKFVNK-KLMKRDQVTHELG---VLQSLQHPQLVGLLDTFETPTSYILVLEMADQGRL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 117 FSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDH---QGYIQVTDFGFAKRVKGRTWT--LCGTPE 191
Cdd:cd14113   91 LDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQslsKPTIKLADFGDAVQLNTTYYIhqLLGSPE 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 192 YLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHF----SSDLKDLLRNLLQVDLTK 267
Cdd:cd14113  171 FAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFLDESVEETCLNICRLDFSFPDDYfkgvSQKAKDFVCFLLQMDPAK 250

                 .
gi 255958318 268 R 268
Cdd:cd14113  251 R 251
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
31-284 4.44e-36

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: 131.30  E-value: 4.44e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHtlNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEY 110
Cdd:cd14088    3 YDLGQVIKTEEFCEIFRAKDKTTGKLYTCKKFLKRDGRKVRKAAK--NEINILKMVKHPNILQLVDVFETRKEYFIFLEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 111 VPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQ---GYIQVTDFGFAKRVKGRTWTLC 187
Cdd:cd14088   81 ATGREVFDWILDQGYYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYYNRlknSKIVISDFHLAKLENGLIKEPC 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 188 GTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYE--------KIVSGKVRFPSHFSSDL----KD 255
Cdd:cd14088  161 GTPEYLAPEVVGRQRYGRPVDCWAIGVIMYILLSGNPPFYDEAEEDDYEnhdknlfrKILAGDYEFDSPYWDDIsqaaKD 240
                        250       260
                 ....*....|....*....|....*....
gi 255958318 256 LLRNLLQVDLTKRFgnlknGVSDIKTHKW 284
Cdd:cd14088  241 LVTRLMEVEQDQRI-----TAEEAISHEW 264
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
28-284 4.85e-36

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. DAPK2 is also called DAPK-related protein 1 (DRP-1), while DAPK3 has also been named DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk). These proteins are ubiquitously expressed in adult tissues, are capable of cross talk with each other, and may act synergistically in regulating cell death. The DAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 131.46  E-value: 4.85e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  28 LEDF-ERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKV------VKLKQIEHtlnEKRILQAVEFPFLVRLEYSFKD 100
Cdd:cd14105    3 VEDFyDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSkasrrgVSREDIER---EVSILRQVLHPNIITLHDVFEN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 101 NSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQG----YIQVTDFGFA 176
Cdd:cd14105   80 KTDVVLILELVAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNvpipRIKLIDFGLA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 177 KRVK-GRTW-TLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHF---SS 251
Cdd:cd14105  160 HKIEdGNEFkNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVNYDFDDEYfsnTS 239
                        250       260       270
                 ....*....|....*....|....*....|....
gi 255958318 252 DL-KDLLRNLLQVDLTKRFgnlknGVSDIKTHKW 284
Cdd:cd14105  240 ELaKDFIRQLLVKDPRKRM-----TIQESLRHPW 268
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
30-268 6.72e-36

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: 130.85  E-value: 6.72e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  30 DFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVME 109
Cdd:cd08224    1 NYEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQIFEMMDAKARQDCLKEIDLLQQLNHPNIIKYLASFIENNELNIVLE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 110 YVPGGE---MFSHLRRIGR-FSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRT-- 183
Cdd:cd08224   81 LADAGDlsrLIKHFKKQKRlIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGLGRFFSSKTta 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 184 -WTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQpIQIY---EKIVSGKvrFP----SHFSSDLKD 255
Cdd:cd08224  161 aHSLVGTPYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFYGEK-MNLYslcKKIEKCE--YPplpaDLYSQELRD 237
                        250
                 ....*....|...
gi 255958318 256 LLRNLLQVDLTKR 268
Cdd:cd08224  238 LVAACIQPDPEKR 250
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
37-268 7.13e-36

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: 130.50  E-value: 7.13e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHK--ATEQYYAMKILDKQKVVKLKQ--IEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLY-MVMEYV 111
Cdd:cd13994    1 IGKGATSVVRIVTKKnpRSGVLYAVKEYRRRDDESKRKdyVKRLTSEYIISSKLHHPNIVKVLDLCQDLHGKWcLVMEYC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 112 PGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKG-------RTW 184
Cdd:cd13994   81 PGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTAEVFGMpaekespMSA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 185 TLCGTPEYLAPEIILSKGYN-KAVDWWALGVLIYEMAAGYPPF----FADQPIQIYEKIVSGKVRFPSH----FSSDLKD 255
Cdd:cd13994  161 GLCGSEPYMAPEVFTSGSYDgRAVDVWSCGIVLFALFTGRFPWrsakKSDSAYKAYEKSGDFTNGPYEPienlLPSECRR 240
                        250
                 ....*....|...
gi 255958318 256 LLRNLLQVDLTKR 268
Cdd:cd13994  241 LIYRMLHPDPEKR 253
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
33-284 1.12e-35

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: 130.92  E-value: 1.12e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  33 RKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQ------KVVK-LKQIEHTLNEKRILQAVEFpflvrleysFKDNSNLY 105
Cdd:cd14173    6 QEEVLGEGAYARVQTCINLITNKEYAVKIIEKRpghsrsRVFReVEMLYQCQGHRNVLELIEF---------FEEEDKFY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 106 MVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYI---QVTDFGFAKRVKGR 182
Cdd:cd14173   77 LVFEKMRGGSILSHIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQVspvKICDFDLGSGIKLN 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 183 T----------WTLCGTPEYLAPEIILSKG-----YNKAVDWWALGVLIYEMAAGYPPFFA----------DQPIQ---- 233
Cdd:cd14173  157 SdcspistpelLTPCGSAEYMAPEVVEAFNeeasiYDKRCDLWSLGVILYIMLSGYPPFVGrcgsdcgwdrGEACPacqn 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 255958318 234 -IYEKIVSGKVRFP----SHFSSDLKDLLRNLLQVDLTKRFgnlknGVSDIKTHKW 284
Cdd:cd14173  237 mLFESIQEGKYEFPekdwAHISCAAKDLISKLLVRDAKQRL-----SAAQVLQHPW 287
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
37-284 2.50e-35

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


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 130.15  E-value: 2.50e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKQ----KVVKLKQIEhTLNE----KRILQAVEFpflvrleysFKDNSNLYMVM 108
Cdd:cd14174   10 LGEGAYAKVQGCVSLQNGKEYAVKIIEKNaghsRSRVFREVE-TLYQcqgnKNILELIEF---------FEDDTRFYLVF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 109 EYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLI---DHQGYIQVTDFGFAKRVKGRT-- 183
Cdd:cd14174   80 EKLRGGSILAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCespDKVSPVKICDFDLGSGVKLNSac 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 184 --------WTLCGTPEYLAPEII-----LSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPI---------------QIY 235
Cdd:cd14174  160 tpittpelTTPCGSAEYMAPEVVevftdEATFYDKRCDLWSLGVILYIMLSGYPPFVGHCGTdcgwdrgevcrvcqnKLF 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 255958318 236 EKIVSGKVRFP----SHFSSDLKDLLRNLLQVDLTKRFgnlknGVSDIKTHKW 284
Cdd:cd14174  240 ESIQEGKYEFPdkdwSHISSEAKDLISKLLVRDAKERL-----SAAQVLQHPW 287
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
30-268 2.97e-35

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: 128.71  E-value: 2.97e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  30 DFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKlKQIEHTLNEKRILQAVEFPFLVRLEYSFKD-NSNLYMVM 108
Cdd:cd08223    1 EYQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASK-RERKAAEQEAKLLSKLKHPNIVSYKESFEGeDGFLYIVM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 109 EYVPGGEMFSHLR-RIGR-FSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAkRVKGRTW-- 184
Cdd:cd08223   80 GFCEGGDLYTRLKeQKGVlLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIA-RVLESSSdm 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 185 --TLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKV-RFPSHFSSDLKDLLRNLL 261
Cdd:cd08223  159 atTLIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAFNAKDMNSLVYKILEGKLpPMPKQYSPELGELIKAML 238

                 ....*..
gi 255958318 262 QVDLTKR 268
Cdd:cd08223  239 HQDPEKR 245
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
31-268 3.08e-35

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: 129.52  E-value: 3.08e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKildkqkVVKLKQIEH-----TLNEKRILQAVEFPFLVRLEYSFKDNSNLY 105
Cdd:cd07829    1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALK------KIRLDNEEEgipstALREISLLKELKHPNIVKLLDVIHTENKLY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 106 MVMEYVpggEM--FSHLRRIGR-FSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAK--RVK 180
Cdd:cd07829   75 LVFEYC---DQdlKKYLDKRPGpLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGLARafGIP 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 181 GRTWtlcgTPE-----YLAPEIIL-SKGYNKAVDWWALGVLIYEMAAGYPPFFA----DQPIQIYE-------------- 236
Cdd:cd07829  152 LRTY----THEvvtlwYRAPEILLgSKHYSTAVDIWSVGCIFAELITGKPLFPGdseiDQLFKIFQilgtpteeswpgvt 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 255958318 237 KIVSGKVRFPSH-----------FSSDLKDLLRNLLQVDLTKR 268
Cdd:cd07829  228 KLPDYKPTFPKWpkndlekvlprLDPEGIDLLSKMLQYNPAKR 270
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
37-268 4.59e-35

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: 128.77  E-value: 4.59e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLV-KHKATEQYYAMK-------ILDKQKVVKLKQIEHTLNEKRIL-QAVEFPFLVRLEYSFKDNSNLYMV 107
Cdd:cd08528    8 LGSGAFGCVYKVrKKSNGQTLLALKeinmtnpAFGRTEQERDKSVGDIISEVNIIkEQLRHPNIVRYYKTFLENDRLYIV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 108 MEYVPG---GEMFSHLR-RIGRFSEPHARFYAAQIVLTFEYLH-SLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRvKGR 182
Cdd:cd08528   88 MELIEGaplGEHFSSLKeKNEHFTEDRIWNIFVQMVLALRYLHkEKQIVHRDLKPNNIMLGEDDKVTITDFGLAKQ-KGP 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 183 TW----TLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVR-FPSH-FSSDLKDL 256
Cdd:cd08528  167 ESskmtSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPFYSTNMLTLATKIVEAEYEpLPEGmYSDDITFV 246
                        250
                 ....*....|..
gi 255958318 257 LRNLLQVDLTKR 268
Cdd:cd08528  247 IRSCLTPDPEAR 258
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
31-285 5.71e-35

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: 128.08  E-value: 5.71e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEhtlnEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEY 110
Cdd:cd14107    4 YEVKEEIGRGTFGFVKRVTHKGNGECCAAKFIPLRSSTRARAFQ----ERDILARLSHRRLTCLLDQFETRKTLILILEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 111 VPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGY--IQVTDFGFAKRVKG--RTWTL 186
Cdd:cd14107   80 CSSEELLDRLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVSPTRedIKICDFGFAQEITPseHQFSK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 187 CGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPS----HFSSDLKDLLRNLLQ 262
Cdd:cd14107  160 YGSPEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEGVVSWDTpeitHLSEDAKDFIKRVLQ 239
                        250       260
                 ....*....|....*....|...
gi 255958318 263 VDLTKRfgnlkNGVSDIKTHKWF 285
Cdd:cd14107  240 PDPEKR-----PSASECLSHEWF 257
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
29-273 1.14e-34

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: 128.22  E-value: 1.14e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDF-ERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVvklKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMV 107
Cdd:cd06643    4 EDFwEIVGELGDGAFGKVYKAQNKETGILAAAKVIDTKSE---EELEDYMVEIDILASCDHPNIVKLLDAFYYENNLWIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 108 MEYVPGGEMFSHLRRIGR-FSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFA---KRVKGRT 183
Cdd:cd06643   81 IEFCAGGAVDAVMLELERpLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSaknTRTLQRR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 184 WTLCGTPEYLAPEIIL-----SKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGK---VRFPSHFSSDLKD 255
Cdd:cd06643  161 DSFIGTPYWMAPEVVMcetskDRPYDYKADVWSLGVTLIEMAQIEPPHHELNPMRVLLKIAKSEpptLAQPSRWSPEFKD 240
                        250
                 ....*....|....*...
gi 255958318 256 LLRNLLQVDLTKRFGNLK 273
Cdd:cd06643  241 FLRKCLEKNVDARWTTSQ 258
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
31-269 1.15e-34

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: 127.43  E-value: 1.15e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILdkqKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEY 110
Cdd:cd14191    4 YDIEERLGSGKFGQVFRLVEKKTKKVWAGKFF---KAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 111 VPGGEMFSHL-RRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLL-IDHQGY-IQVTDFGFAKRVK--GRTWT 185
Cdd:cd14191   81 VSGGELFERIiDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTkIKLIDFGLARRLEnaGSLKV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 186 LCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFP----SHFSSDLKDLLRNLL 261
Cdd:cd14191  161 LFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDdeafDEISDDAKDFISNLL 240

                 ....*...
gi 255958318 262 QVDLTKRF 269
Cdd:cd14191  241 KKDMKARL 248
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
29-284 1.38e-34

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. It is Ca2+/calmodulin (CaM)-regulated and actin-associated protein that contains an N-terminal kinase domain followed by an autoinhibitory CaM binding region and a large C-terminal extension with multiple functional domains including ankyrin (ANK) repeats, a cytoskeletal binding domain, a Death domain, and a serine-rich tail. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. The DAPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 127.44  E-value: 1.38e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKV------VKLKQIEHtlnEKRILQAVEFPFLVRLEYSFKDNS 102
Cdd:cd14194    5 DYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTkssrrgVSREDIER---EVSILKEIQHPNVITLHEVYENKT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 103 NLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGY----IQVTDFGFAKR 178
Cdd:cd14194   82 DVILILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVpkprIKIIDFGLAHK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 179 VK-GRTW-TLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFP----SHFSSD 252
Cdd:cd14194  162 IDfGNEFkNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEdeyfSNTSAL 241
                        250       260       270
                 ....*....|....*....|....*....|..
gi 255958318 253 LKDLLRNLLQVDLTKRFgnlknGVSDIKTHKW 284
Cdd:cd14194  242 AKDFIRRLLVKDPKKRM-----TIQDSLQHPW 268
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
37-284 2.21e-34

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: 126.73  E-value: 2.21e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMK-------ILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVR-LEYSFKDNSnLYMVM 108
Cdd:cd06629    9 IGKGTYGRVYLAMNATTGEMLAVKqvelpktSSDRADSRQKTVVDALKSEIDTLKDLDHPNIVQyLGFEETEDY-FSIFL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 109 EYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKG-----RT 183
Cdd:cd06629   88 EYVPGGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGISKKSDDiygnnGA 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 184 WTLCGTPEYLAPEIILS--KGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFP----SHFSSDLKDLL 257
Cdd:cd06629  168 TSMQGSVFWMAPEVIHSqgQGYSAKVDIWSLGCVVLEMLAGRRPWSDDEAIAAMFKLGNKRSAPPvpedVNLSPEALDFL 247
                        250       260
                 ....*....|....*....|....*..
gi 255958318 258 RNLLQVDLTKRfgnlkNGVSDIKTHKW 284
Cdd:cd06629  248 NACFAIDPRDR-----PTAAELLSHPF 269
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
37-274 4.03e-34

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: 126.79  E-value: 4.03e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMK-------ILDKQKVV-KLK-QIEHTLNEKRILQAVEFPflvrlEYSFKDNSNL--Y 105
Cdd:cd13989    1 LGSGGFGYVTLWKHQDTGEYVAIKkcrqelsPSDKNRERwCLEvQIMKKLNHPNVVSARDVP-----PELEKLSPNDlpL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 106 MVMEYVPGGEMFSHLRRIGRFS---EPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQG---YIQVTDFGFAKRV 179
Cdd:cd13989   76 LAMEYCSGGDLRKVLNQPENCCglkESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGgrvIYKLIDLGYAKEL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 180 -KGRTWT-LCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFAD-QPIQIYEKI-------------VSGKV 243
Cdd:cd13989  156 dQGSLCTsFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPFLPNwQPVQWHGKVkqkkpehicayedLTGEV 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 255958318 244 RF------PSHFSSDLKD----LLRNLLQVDLTKRFGNLKN 274
Cdd:cd13989  236 KFsselpsPNHLSSILKEylesWLQLMLRWDPRQRGGGPQN 276
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
37-261 5.51e-34

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: 126.68  E-value: 5.51e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKQKVvklKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGGEM 116
Cdd:cd06644   20 LGDGAFGKVYKAKNKETGALAAAKVIETKSE---EELEDYMVEIEILATCNHPYIVKLLGAFYWDGKLWIMIEFCPGGAV 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 117 FSHLRRIGR-FSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGF-AKRVKG--RTWTLCGTPEY 192
Cdd:cd06644   97 DAIMLELDRgLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVsAKNVKTlqRRDSFIGTPYW 176
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255958318 193 LAPEIILSKG-----YNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGK---VRFPSHFSSDLKDLLRNLL 261
Cdd:cd06644  177 MAPEVVMCETmkdtpYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSEpptLSQPSKWSMEFRDFLKTAL 253
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
31-268 6.12e-34

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: 126.05  E-value: 6.12e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILD-----------KQKVVKLKQIEHTlnekrilqavEFPFLVRLEYSFK 99
Cdd:cd06917    3 YRRLELVGRGSYGAVYRGYHVKTGRVVALKVLNldtddddvsdiQKEVALLSQLKLG----------QPKNIIKYYGSYL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 100 DNSNLYMVMEYVPGGEMFShLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRV 179
Cdd:cd06917   73 KGPSLWIIMDYCEGGSIRT-LMRAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 180 ---KGRTWTLCGTPEYLAPEIILS-KGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKV-RFP-SHFSSDL 253
Cdd:cd06917  152 nqnSSKRSTFVGTPYWMAPEVITEgKYYDTKADIWSLGITTYEMATGNPPYSDVDALRAVMLIPKSKPpRLEgNGYSPLL 231
                        250
                 ....*....|....*
gi 255958318 254 KDLLRNLLQVDLTKR 268
Cdd:cd06917  232 KEFVAACLDEEPKDR 246
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
28-285 1.16e-33

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 124.97  E-value: 1.16e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  28 LEDFERKKTLGT--GSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRilqavefPFLVRLEYSFKDNSNLY 105
Cdd:PHA03390  13 LKNCEIVKKLKLidGKFGKVSVLKHKPTQKLFVQKIIKAKNFNAIEPMVHQLMKDN-------PNFIKLYYSVTTLKGHV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 106 MVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLID-HQGYIQVTDFGFAKRVkGRTW 184
Cdd:PHA03390  86 LIMDYIKDGDLFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDrAKDRIYLCDYGLCKII-GTPS 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 185 TLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQ----PIQIYEKIVSGKVRFPSHFSSDLKDLLRNL 260
Cdd:PHA03390 165 CYDGTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFKEDEdeelDLESLLKRQQKKLPFIKNVSKNANDFVQSM 244
                        250       260
                 ....*....|....*....|....*
gi 255958318 261 LQVDLTKRFGNLKngvsDIKTHKWF 285
Cdd:PHA03390 245 LKYNINYRLTNYN----EIIKHPFL 265
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
28-268 1.29e-33

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: 125.48  E-value: 1.29e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  28 LEDFERkktLGTGSFGRVMLVKHKATEQYYAMKILDKQKvvkLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMV 107
Cdd:cd06659   23 LENYVK---IGEGSTGVVCIAREKHSGRQVAVKMMDLRK---QQRRELLFNEVVIMRDYQHPNVVEMYKSYLVGEELWVL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 108 MEYVPGGEMFSHLRRIgRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGF----AKRVKGRT 183
Cdd:cd06659   97 MEYLQGGALTDIVSQT-RLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGFcaqiSKDVPKRK 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 184 wTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSG---KVRFPSHFSSDLKDLLRNL 260
Cdd:cd06659  176 -SLVGTPYWMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLRDSpppKLKNSHKASPVLRDFLERM 254

                 ....*...
gi 255958318 261 LQVDLTKR 268
Cdd:cd06659  255 LVRDPQER 262
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
31-268 1.71e-33

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: 124.27  E-value: 1.71e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIehtLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEY 110
Cdd:cd06647    9 YTRFEKIGQGASGTVYTAIDVATGQEVAIKQMNLQQQPKKELI---INEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 111 VPGGEMFSHLRRIgRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRV---KGRTWTLC 187
Cdd:cd06647   86 LAGGSLTDVVTET-CMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQItpeQSKRSTMV 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 188 GTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQ-IYEKIVSGKVRF--PSHFSSDLKDLLRNLLQVD 264
Cdd:cd06647  165 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRaLYLIATNGTPELqnPEKLSAIFRDFLNRCLEMD 244

                 ....
gi 255958318 265 LTKR 268
Cdd:cd06647  245 VEKR 248
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
35-269 2.24e-33

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: 124.07  E-value: 2.24e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIE--HTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVP 112
Cdd:cd08222    6 RKLGSGNFGTVYLVSDLKATADEELKVLKEISVGELQPDEtvDANREAKLLSKLDHPAIVKFHDSFVEKESFCIVTEYCE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 113 GGEM---FSHLRRIGR-FSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIdHQGYIQVTDFGFAKRVKGRT---WT 185
Cdd:cd08222   86 GGDLddkISEYKKSGTtIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFL-KNNVIKVGDFGISRILMGTSdlaTT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 186 LCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKV-RFPSHFSSDLKDLLRNLLQVD 264
Cdd:cd08222  165 FTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAFDGQNLLSVMYKIVEGETpSLPDKYSKELNAIYSRMLNKD 244

                 ....*
gi 255958318 265 LTKRF 269
Cdd:cd08222  245 PALRP 249
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
29-268 2.66e-33

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: 124.84  E-value: 2.66e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIehtLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVM 108
Cdd:cd06655   19 KKYTRYEKIGQGASGTVFTAIDVATGQEVAIKQINLQKQPKKELI---INEILVMKELKNPNIVNFLDSFLVGDELFVVM 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 109 EYVPGGEMFSHLRRIGrFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRV---KGRTWT 185
Cdd:cd06655   96 EYLAGGSLTDVVTETC-MDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCAQItpeQSKRST 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 186 LCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSG---KVRFPSHFSSDLKDLLRNLLQ 262
Cdd:cd06655  175 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNgtpELQNPEKLSPIFRDFLNRCLE 254

                 ....*.
gi 255958318 263 VDLTKR 268
Cdd:cd06655  255 MDVEKR 260
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
30-268 3.42e-33

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: 123.26  E-value: 3.42e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  30 DFERKKTLGTGSFGRVMLVKHKATEQYYAMKILdKQKVVKLKQIEHTLNEKRILQAVEF-PFLVRLEYSFKDNSNLYMVM 108
Cdd:cd13997    1 HFHELEQIGSGSFSEVFKVRSKVDGCLYAVKKS-KKPFRGPKERARALREVEAHAALGQhPNIVRYYSSWEEGGHLYIQM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 109 EYVPGGEMFSHLRR---IGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTWT 185
Cdd:cd13997   80 ELCENGSLQDALEElspISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLATRLETSGDV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 186 LCGTPEYLAPEII-LSKGYNKAVDWWALGVLIYEMAAGYP-PFFADQpiqiYEKIVSGKVRFP--SHFSSDLKDLLRNLL 261
Cdd:cd13997  160 EEGDSRYLAPELLnENYTHLPKADIFSLGVTVYEAATGEPlPRNGQQ----WQQLRQGKLPLPpgLVLSQELTRLLKVML 235

                 ....*..
gi 255958318 262 QVDLTKR 268
Cdd:cd13997  236 DPDPTRR 242
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
37-285 4.28e-33

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: 123.98  E-value: 4.28e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEqyyamkildkqKVVKLKQI----------EHTLNEKRILQAVEF-PFLVRLEYSFKDNSNLY 105
Cdd:cd07832    8 IGEGAHGIVFKAKDRETG-----------ETVALKKValrkleggipNQALREIKALQACQGhPYVVKLRDVFPHGTGFV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 106 MVMEYVPGGeMFSHLRRIGR-FSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTW 184
Cdd:cd07832   77 LVFEYMLSS-LSEVLRDEERpLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLARLFSEEDP 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 185 TL----CGTPEYLAPEIIL-SKGYNKAVDWWALGVLIYEMAAGYPPFFADQPI---------------QIYEKIVS---- 240
Cdd:cd07832  156 RLyshqVATRWYRAPELLYgSRKYDEGVDLWAVGCIFAELLNGSPLFPGENDIeqlaivlrtlgtpneKTWPELTSlpdy 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 255958318 241 GKVRFPSHFSSDLK-----------DLLRNLLQVDLTKRFgnlknGVSDIKTHKWF 285
Cdd:cd07832  236 NKITFPESKGIRLEeifpdcspeaiDLLKGLLVYNPKKRL-----SAEEALRHPYF 286
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
34-272 5.67e-33

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: 122.66  E-value: 5.67e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318    34 KKTLGTGSFGRVmlvkHKATeqYYAMKILDKQKV-VK-LK------QIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLY 105
Cdd:smart00221   4 GKKLGEGAFGEV----YKGT--LKGKGDGKEVEVaVKtLKedaseqQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLM 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318   106 MVMEYVPGGEMFSHLRRIGRFSEPHARF--YAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRT 183
Cdd:smart00221  78 IVMEYMPGGDLLDYLRKNRPKELSLSDLlsFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDD 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318   184 WTLCGTPE----YLAPEIILSKGYNKAVDWWALGVLIYEMAA-GYPPFFADQPIQIYEKIVSGKVR-FPSHFSSDLKDLL 257
Cdd:smart00221 158 YYKVKGGKlpirWMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEEPYPGMSNAEVLEYLKKGYRLpKPPNCPPELYKLM 237
                          250
                   ....*....|....*..
gi 255958318   258 RNLLQVDLTKR--FGNL 272
Cdd:smart00221 238 LQCWAEDPEDRptFSEL 254
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
28-284 7.40e-33

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK2, also called DAPK-related protein 1 (DRP-1), is a Ca2+/calmodulin (CaM)-regulated protein containing an N-terminal kinase domain, a CaM autoinhibitory site and a dimerization module. It lacks the cytoskeletal binding regions of DAPK1 and the exogenous protein has been shown to be soluble and cytoplasmic. FLAG-tagged DAPK2, however, accumulated within membrane-enclosed autophagic vesicles. It is unclear where endogenous DAPK2 is localized. DAPK2 participates in TNF-alpha and FAS-receptor induced cell death and enhances neutrophilic maturation in myeloid leukemic cells. It contributes to the induction of anoikis and its down-regulation is implicated in the beta-catenin induced resistance of malignant epithelial cells to anoikis. The DAPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 122.76  E-value: 7.40e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  28 LEDF-ERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKV------VKLKQIEHTLNekrILQAVEFPFLVRLEYSFKD 100
Cdd:cd14196    3 VEDFyDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSrasrrgVSREEIEREVS---ILRQVLHPNIITLHDVYEN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 101 NSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPEN-LLIDHQG---YIQVTDFGFA 176
Cdd:cd14196   80 RTDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENiMLLDKNIpipHIKLIDFGLA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 177 KRVK-GRTW-TLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHF---SS 251
Cdd:cd14196  160 HEIEdGVEFkNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFfshTS 239
                        250       260       270
                 ....*....|....*....|....*....|....
gi 255958318 252 DL-KDLLRNLLQVDLTKRFgnlknGVSDIKTHKW 284
Cdd:cd14196  240 ELaKDFIRKLLVKETRKRL-----TIQEALRHPW 268
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
35-226 7.62e-33

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: 123.03  E-value: 7.62e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYYAMKILDKqkvvKLKQIEH--TLNEKRILQAV-EFPFLVRLEYSFKDNSNLYMVMEYV 111
Cdd:cd07830    5 KQLGDGTFGSVYLARNKETGELVAIKKMKK----KFYSWEEcmNLREVKSLRKLnEHPNIVKLKEVFRENDELYFVFEYM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 112 PGG--EMFSHlRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGR---TwTL 186
Cdd:cd07830   81 EGNlyQLMKD-RKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLAREIRSRppyT-DY 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 255958318 187 CGTPEYLAPEIIL-SKGYNKAVDWWALGVLIYEMAAGYPPF 226
Cdd:cd07830  159 VSTRWYRAPEILLrSTSYSSPVDIWALGCIMAELYTLRPLF 199
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
31-285 2.90e-32

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: 120.80  E-value: 2.90e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQI--------EHTLNEKriLQAVEFPFLVRLEySFKDNS 102
Cdd:cd14005    2 YEVGDLLGKGGFGTVYSGVRIRDGLPVAVKFVPKSRVTEWAMIngpvpvplEIALLLK--ASKPGVPGVIRLL-DWYERP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 103 NLY-MVMEY-VPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLID-HQGYIQVTDFGFAKRV 179
Cdd:cd14005   79 DGFlLIMERpEPCQDLFDFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINlRTGEVKLIDFGCGALL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 180 KGRTWT-LCGTPEYLAPEIILSKGYN-KAVDWWALGVLIYEMAAGYPPFFADqpiqiyEKIVSGKVRFPSHFSSDLKDLL 257
Cdd:cd14005  159 KDSVYTdFDGTRVYSPPEWIRHGRYHgRPATVWSLGILLYDMLCGDIPFEND------EQILRGNVLFRPRLSKECCDLI 232
                        250       260
                 ....*....|....*....|....*...
gi 255958318 258 RNLLQVDLTKRFgNLKngvsDIKTHKWF 285
Cdd:cd14005  233 SRCLQFDPSKRP-SLE----QILSHPWF 255
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
34-268 6.06e-32

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: 120.41  E-value: 6.06e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  34 KKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVvklKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPG 113
Cdd:cd14190    9 KEVLGGGKFGKVHTCTEKRTGLKLAAKVINKQNS---KDKEMVLLEIQVMNQLNHRNLIQLYEAIETPNEIVLFMEYVEG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 114 GEMF-------SHLrrigrfSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPEN-LLIDHQGY-IQVTDFGFAKRVKGRTW 184
Cdd:cd14190   86 GELFerivdedYHL------TEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENiLCVNRTGHqVKIIDFGLARRYNPREK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 185 TLC--GTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFP----SHFSSDLKDLLR 258
Cdd:cd14190  160 LKVnfGTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETLNNVLMGNWYFDeetfEHVSDEAKDFVS 239
                        250
                 ....*....|
gi 255958318 259 NLLQVDLTKR 268
Cdd:cd14190  240 NLIIKERSAR 249
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
34-273 6.73e-32

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 119.94  E-value: 6.73e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318    34 KKTLGTGSFGRVML----VKHKATEQYYAMKILDKQKvvKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVME 109
Cdd:smart00219   4 GKKLGEGAFGEVYKgklkGKGGKKKVEVAVKTLKEDA--SEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYIVME 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318   110 YVPGGEMFSHLR-RIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAK--------RVK 180
Cdd:smart00219  82 YMEGGDLLSYLRkNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRdlydddyyRKR 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318   181 GRTWTLcgtpEYLAPEIILSKGYNKAVDWWALGVLIYEMAA-GYPPFFADQPIQIYEKIVSGKVR-FPSHFSSDLKDLLR 258
Cdd:smart00219 162 GGKLPI----RWMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEEVLEYLKNGYRLpQPPNCPPELYDLML 237
                          250
                   ....*....|....*..
gi 255958318   259 NLLQVDLTKR--FGNLK 273
Cdd:smart00219 238 QCWAEDPEDRptFSELV 254
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
35-261 7.18e-32

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK3 (or MYLK3) phosphorylates myosin regulatory light chain 2 and controls the contraction of cardiac muscles. It is expressed specifically in both the atrium and ventricle of the heart and its expression is regulated by the cardiac protein Nkx2-5. MLCK3 plays an important role in cardiogenesis by regulating the assembly of cardiac sarcomeres, the repeating contractile unit of striated muscle. MLCK3 contains a single kinase domain near the C-terminus and a unique N-terminal half, and unlike MLCK1/2, it does not appear to be regulated by Ca2+/calmodulin. The MLCK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 120.07  E-value: 7.18e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYYAMKILdkqKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGG 114
Cdd:cd14192   10 EVLGGGRFGQVHKCTELSTGLTLAAKII---KVKGAKEREEVKNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVDGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 115 EMFSHLRRIG-RFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLL-IDHQGY-IQVTDFGFAKRVKGRTWTLC--GT 189
Cdd:cd14192   87 ELFDRITDESyQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILcVNSTGNqIKIIDFGLARRYKPREKLKVnfGT 166
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255958318 190 PEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPS----HFSSDLKDLLRNLL 261
Cdd:cd14192  167 PEFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNNIVNCKWDFDAeafeNLSEEAKDFISRLL 242
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
29-268 7.85e-32

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: 120.98  E-value: 7.85e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIehtLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVM 108
Cdd:cd06654   20 KKYTRFEKIGQGASGTVYTAMDVATGQEVAIRQMNLQQQPKKELI---INEILVMRENKNPNIVNYLDSYLVGDELWVVM 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 109 EYVPGGEMFSHLRRIGrFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRV---KGRTWT 185
Cdd:cd06654   97 EYLAGGSLTDVVTETC-MDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQItpeQSKRST 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 186 LCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSG---KVRFPSHFSSDLKDLLRNLLQ 262
Cdd:cd06654  176 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNgtpELQNPEKLSAIFRDFLNRCLE 255

                 ....*.
gi 255958318 263 VDLTKR 268
Cdd:cd06654  256 MDVEKR 261
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
30-268 8.03e-32

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: 119.72  E-value: 8.03e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  30 DFERKKTLGTGSFGRVMLVKHKATEQYYAMKildkqkVVKLKQ---IEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYM 106
Cdd:cd06613    1 DYELIQRIGSGTYGDVYKARNIATGELAAVK------VIKLEPgddFEIIQQEISMLKECRHPNIVAYFGSYLRRDKLWI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 107 VMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVK---GRT 183
Cdd:cd06613   75 VMEYCGGGSLQDIYQVTGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSAQLTatiAKR 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 184 WTLCGTPEYLAPEIILSK---GYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIvsGKVRFP-------SHFSSDL 253
Cdd:cd06613  155 KSFIGTPYWMAPEVAAVErkgGYDGKCDIWALGITAIELAELQPPMFDLHPMRALFLI--PKSNFDppklkdkEKWSPDF 232
                        250
                 ....*....|....*
gi 255958318 254 KDLLRNLLQVDLTKR 268
Cdd:cd06613  233 HDFIKKCLTKNPKKR 247
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
29-268 1.51e-31

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: 120.21  E-value: 1.51e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIehtLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVM 108
Cdd:cd06656   19 KKYTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKKELI---INEILVMRENKNPNIVNYLDSYLVGDELWVVM 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 109 EYVPGGEMFSHLRRIGrFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRV---KGRTWT 185
Cdd:cd06656   96 EYLAGGSLTDVVTETC-MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQItpeQSKRST 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 186 LCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSG---KVRFPSHFSSDLKDLLRNLLQ 262
Cdd:cd06656  175 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNgtpELQNPERLSAVFRDFLNRCLE 254

                 ....*.
gi 255958318 263 VDLTKR 268
Cdd:cd06656  255 MDVDRR 260
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
37-268 3.51e-31

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: 118.31  E-value: 3.51e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLvKHKATEQYYAMK--ILDKQKVVKL-KQIEHTLNEKRILQAVEFPFLVR-LEYSFKDNSnLYMVMEYVP 112
Cdd:cd06631    9 LGKGAYGTVYC-GLTSTGQLIAVKqvELDTSDKEKAeKEYEKLQEEVDLLKTLKHVNIVGyLGTCLEDNV-VSIFMEFVP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 113 GGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVkgrTWTLC----- 187
Cdd:cd06631   87 GGSIASILARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGCAKRL---CINLSsgsqs 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 188 -------GTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGK---VRFPSHFSSDLKDLL 257
Cdd:cd06631  164 qllksmrGTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGKPPWADMNPMAAIFAIGSGRkpvPRLPDKFSPEARDFV 243
                        250
                 ....*....|.
gi 255958318 258 RNLLQVDLTKR 268
Cdd:cd06631  244 HACLTRDQDER 254
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
31-285 5.83e-31

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: 117.40  E-value: 5.83e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILDK--------QKVVKLK-QIEHTLNEKRILQAVEFpflvrLEYSfkdN 101
Cdd:cd14163    2 YQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIIDKsggpeefiQRFLPRElQIVERLDHKNIIHVYEM-----LESA---D 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 102 SNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIdhQGY-IQVTDFGFAKRV- 179
Cdd:cd14163   74 GKIYLVMELAEDGDVFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALL--QGFtLKLTDFGFAKQLp 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 180 KGR---TWTLCGTPEYLAPEIILSKGYN-KAVDWWALGVLIYEMAAGYPPF-FADQPIQIYEKivSGKVRFPSHF--SSD 252
Cdd:cd14163  152 KGGrelSQTFCGSTAYAAPEVLQGVPHDsRKGDIWSMGVVLYVMLCAQLPFdDTDIPKMLCQQ--QKGVSLPGHLgvSRT 229
                        250       260       270
                 ....*....|....*....|....*....|...
gi 255958318 253 LKDLLRNLLQVDLTkrfgnLKNGVSDIKTHKWF 285
Cdd:cd14163  230 CQDLLKRLLEPDMV-----LRPSIEEVSWHPWL 257
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
28-268 7.47e-31

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: 117.39  E-value: 7.47e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  28 LEDFERKKTLGTGSFGRVMLVKHKATEQYYAMK-ILDKQKVVKLKQIehtLNEKRILQAVEFPFLVRLEYSFKDNSNLYM 106
Cdd:cd13996    5 LNDFEEIELLGSGGFGSVYKVRNKVDGVTYAIKkIRLTEKSSASEKV---LREVKALAKLNHPNIVRYYTAWVEEPPLYI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 107 VMEYVPGGEMFSHLRRIGRFS---EPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGY-IQVTDFGFAKRVKGR 182
Cdd:cd13996   82 QMELCEGGTLRDWIDRRNSSSkndRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDDLqVKIGDFGLATSIGNQ 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 183 TWTL-----------------CGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAagYPPFFADQPIQIYEKIVSGKvrF 245
Cdd:cd13996  162 KRELnnlnnnnngntsnnsvgIGTPLYASPEQLDGENYNEKADIYSLGIILFEML--HPFKTAMERSTILTDLRNGI--L 237
                        250       260
                 ....*....|....*....|....*.
gi 255958318 246 PSHFSSDL---KDLLRNLLQVDLTKR 268
Cdd:cd13996  238 PESFKAKHpkeADLIQSLLSKNPEER 263
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
31-268 1.33e-30

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK3, also called DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk), contains an N-terminal kinase domain and a C-terminal region with nuclear localization signals (NLS) and a leucine zipper motif that mediates homodimerization and interaction with other leucine zipper proteins. It interacts with Par-4, a protein that contains a death domain and interacts with actin filaments. DAPK3 is present in both the cytoplasm and nucleus. Its co-expression with Par-4 results in the co-localization of the two proteins to actin filaments. In addition to cell death, DAPK3 is also implicated in mediating cell motility and the contraction of smooth muscles. The DAPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271097 [Multi-domain]  Cd Length: 271  Bit Score: 117.03  E-value: 1.33e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKV------VKLKQIEHTLNekrILQAVEFPFLVRLEYSFKDNSNL 104
Cdd:cd14195    7 YEMGEELGSGQFAIVRKCREKGTGKEYAAKFIKKRRLsssrrgVSREEIEREVN---ILREIQHPNIITLHDIFENKTDV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 105 YMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGY----IQVTDFGFAKRVK 180
Cdd:cd14195   84 VLILELVSGGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNVpnprIKLIDFGIAHKIE 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 181 -GRTW-TLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDL----K 254
Cdd:cd14195  164 aGNEFkNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDEEYFSNTselaK 243
                        250
                 ....*....|....
gi 255958318 255 DLLRNLLQVDLTKR 268
Cdd:cd14195  244 DFIRRLLVKDPKKR 257
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
37-291 1.73e-30

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKalpha is involved in the non-canonical or alternative pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The non-canonical pathway functions in cells lacking NEMO (NF-kB Essential MOdulator) and IKKbeta. It is induced by a subset of TNFR family members including CD40, RANK, and B cell-activating factor receptor. IKKalpha processes the Inhibitor of NF-kB (IkB)-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus. This pathway is dependent on NIK (NF-kB Inducing Kinase) which phosphorylates and activates IKKalpha. The IKKalpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 116.94  E-value: 1.73e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLK-------QIEHTLNEKRILQAVEFPflvrLEYSFKDNSNLYMVME 109
Cdd:cd14039    1 LGTGGFGNVCLYQNQETGEKIAIKSCRLELSVKNKdrwcheiQIMKKLNHPNVVKACDVP----EEMNFLVNDVPLLAME 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 110 YVPGGEmfshLRRIGRFSEPHARFYAAQIVLTF-------EYLHSLDLIYRDLKPENLLI-DHQGYI--QVTDFGFAKRV 179
Cdd:cd14039   77 YCSGGD----LRKLLNKPENCCGLKESQVLSLLsdigsgiQYLHENKIIHRDLKPENIVLqEINGKIvhKIIDLGYAKDL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 180 KgrTWTLC----GTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFAD-QPIQIYEKI-------------VSG 241
Cdd:cd14039  153 D--QGSLCtsfvGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFRPFLHNlQPFTWHEKIkkkdpkhifaveeMNG 230
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 242 KVRFPSHF------SSDLKDLLRNLLQV----DLTKRFGNLKngvSDIKTHKWFATTDWI 291
Cdd:cd14039  231 EVRFSTHLpqpnnlCSLIVEPMEGWLQLmlnwDPVQRGGGLD---TDSKQPRCFVLMDQI 287
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
31-269 2.78e-30

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: 116.45  E-value: 2.78e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKildkqKVVKLKQIEHtlNEKRILQAVEFPFLVRLEYSF------KDNSNL 104
Cdd:cd14137    6 YTIEKVIGSGSFGVVYQAKLLETGEVVAIK-----KVLQDKRYKN--RELQIMRRLKHPNIVKLKYFFyssgekKDEVYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 105 YMVMEYVPG---GEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQ-GYIQVTDFGFAKRVK 180
Cdd:cd14137   79 NLVMEYMPEtlyRVIRHYSKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDPEtGVLKLCDFGSAKRLV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 181 GrtwtlcGTPE--------YLAPEIIL-SKGYNKAVDWWALGVLIYEMAAGYpPFFA-----DQ------------PIQI 234
Cdd:cd14137  159 P------GEPNvsyicsryYRAPELIFgATDYTTAIDIWSAGCVLAELLLGQ-PLFPgessvDQlveiikvlgtptREQI 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 255958318 235 YE-------------KIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRF 269
Cdd:cd14137  232 KAmnpnytefkfpqiKPHPWEKVFPKRTPPDAIDLLSKILVYNPSKRL 279
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
37-268 3.29e-30

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: 115.50  E-value: 3.29e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKQKVvKLKQIEHTLNEKRILQAveFPFLVR-LEYSFKDNSNLYMVMEYVPGGE 115
Cdd:cd13987    1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPST-KLKDFLREYNISLELSV--HPHIIKtYDVAFETEDYYVFAQEYAPYGD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 116 MFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGY--IQVTDFGFAKRVKGRTWTLCGTPEYL 193
Cdd:cd13987   78 LFSIIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDCrrVKLCDFGLTRRVGSTVKRVSGTIPYT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 194 APE---IILSKGY--NKAVDWWALGVLIYEMAAGYPPF----FADQPIQIYEKIVSGKVR-FPSH---FSSDLKDLLRNL 260
Cdd:cd13987  158 APEvceAKKNEGFvvDPSIDVWAFGVLLFCCLTGNFPWekadSDDQFYEEFVRWQKRKNTaVPSQwrrFTPKALRMFKKL 237

                 ....*...
gi 255958318 261 LQVDLTKR 268
Cdd:cd13987  238 LAPEPERR 245
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
28-268 4.86e-30

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: 115.20  E-value: 4.86e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  28 LEDFERKKTLGTGSFGRVmlvkhkateqyYAMKILDKQKVVKLKQI-EHTLNEKRILQAvEFPFLVRLEY--------SF 98
Cdd:cd06624    7 YDESGERVVLGKGTFGVV-----------YAARDLSTQVRIAIKEIpERDSREVQPLHE-EIALHSRLSHknivqylgSV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  99 KDNSNLYMVMEYVPGGEMFSHLR-RIG--RFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLID-HQGYIQVTDFG 174
Cdd:cd06624   75 SEDGFFKIFMEQVPGGSLSALLRsKWGplKDNENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNtYSGVVKISDFG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 175 FAKRVKG---RTWTLCGTPEYLAPEIILS--KGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQ--IYekivsgKVRF-- 245
Cdd:cd06624  155 TSKRLAGinpCTETFTGTLQYMAPEVIDKgqRGYGPPADIWSLGCTIIEMATGKPPFIELGEPQaaMF------KVGMfk 228
                        250       260
                 ....*....|....*....|....*...
gi 255958318 246 -----PSHFSSDLKDLLRNLLQVDLTKR 268
Cdd:cd06624  229 ihpeiPESLSEEAKSFILRCFEPDPDKR 256
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
48-268 4.87e-30

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: 115.15  E-value: 4.87e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  48 VKHKATEQYYAMKILDKQKVVKLKQI---------EHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGGEMFS 118
Cdd:cd06610    9 IGSGATAVVYAAYCLPKKEKVAIKRIdlekcqtsmDELRKEIQAMSQCNHPNVVSYYTSFVVGDELWLVMPLLSGGSLLD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 119 HLRRI---GRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFA-------KRVKGRTWTLCG 188
Cdd:cd06610   89 IMKSSyprGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVSaslatggDRTRKVRKTFVG 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 189 TPEYLAPEIILS-KGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKvrFPS--------HFSSDLKDLLRN 259
Cdd:cd06610  169 TPCWMAPEVMEQvRGYDFKADIWSFGITAIELATGAAPYSKYPPMKVLMLTLQND--PPSletgadykKYSKSFRKMISL 246

                 ....*....
gi 255958318 260 LLQVDLTKR 268
Cdd:cd06610  247 CLQKDPSKR 255
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
37-268 6.51e-30

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: 114.67  E-value: 6.51e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKqkvvKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGGEM 116
Cdd:cd14115    1 IGRGRFSIVKKCLHKATRKDVAVKFVSK----KMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDGRL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 117 FSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQ---GYIQVTDFGFAKRVKG--RTWTLCGTPE 191
Cdd:cd14115   77 LDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGhrHVHHLLGNPE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 192 YLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDL----KDLLRNLLQVDLTK 267
Cdd:cd14115  157 FAAPEVIQGTPVSLATDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPDEYFGDVsqaaRDFINVILQEDPRR 236

                 .
gi 255958318 268 R 268
Cdd:cd14115  237 R 237
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
21-284 1.21e-29

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: 114.72  E-value: 1.21e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  21 PPPSNAgledFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKlKQIEHTLNekrILQAV-EFPFLVRL--EYS 97
Cdd:cd06638   14 PDPSDT----WEIIETIGKGTYGKVFKVLNKKNGSKAAVKILDPIHDID-EEIEAEYN---ILKALsDHPNVVKFygMYY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  98 FKDNSN---LYMVMEYVPGGEMFS----HLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQV 170
Cdd:cd06638   86 KKDVKNgdqLWLVLELCNGGSVTDlvkgFLKRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 171 TDFGFAKRV---KGRTWTLCGTPEYLAPEII-----LSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSG- 241
Cdd:cd06638  166 VDFGVSAQLtstRLRRNTSVGTPFWMAPEVIaceqqLDSTYDARCDVWSLGITAIELGDGDPPLADLHPMRALFKIPRNp 245
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 255958318 242 --KVRFPSHFSSDLKDLLRNLLQVDLTKRfgnlkNGVSDIKTHKW 284
Cdd:cd06638  246 ppTLHQPELWSNEFNDFIRKCLTKDYEKR-----PTVSDLLQHVF 285
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
35-226 1.51e-29

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: 113.80  E-value: 1.51e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLvkhkATEQYY----AMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRL-EYSFKDNSNLYMVME 109
Cdd:cd14164    6 TTIGEGSFSKVKL----ATSQKYcckvAIKIVDRRRASPDFVQKFLPRELSILRRVNHPNIVQMfECIEVANGRLYIVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 110 yVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQG-YIQVTDFGFAKRVKGR---TWT 185
Cdd:cd14164   82 -AAATDLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDrKIKIADFGFARFVEDYpelSTT 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 255958318 186 LCGTPEYLAPEIILSKGYN-KAVDWWALGVLIYEMAAGYPPF 226
Cdd:cd14164  161 FCGSRAYTPPEVILGTPYDpKKYDVWSLGVVLYVMVTGTMPF 202
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
31-285 2.01e-29

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: 114.20  E-value: 2.01e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKildkqkvvKLKqIEH--------TLNEKRILQAVEFPFLVRL------EY 96
Cdd:cd07840    1 YEKIAQIGEGTYGQVYKARNKKTGELVALK--------KIR-MENekegfpitAIREIKLLQKLDHPNVVRLkeivtsKG 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  97 SFKDNSNLYMVMEYvpggemFSH-----LRRIG-RFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQV 170
Cdd:cd07840   72 SAKYKGSIYMVFEY------MDHdltglLDNPEvKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKL 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 171 TDFGFAkrvkgRTWTLCGTPE---------YLAPEIIL-SKGYNKAVDWWALGVLIYEMAAGYPPFF----ADQPIQIYE 236
Cdd:cd07840  146 ADFGLA-----RPYTKENNADytnrvitlwYRPPELLLgATRYGPEVDMWSVGCILAELFTGKPIFQgkteLEQLEKIFE 220
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255958318 237 -------------------KIVSGKVRFPSHF--------SSDLKDLLRNLLQVDLTKRFgnlknGVSDIKTHKWF 285
Cdd:cd07840  221 lcgspteenwpgvsdlpwfENLKPKKPYKRRLrevfknviDPSALDLLDKLLTLDPKKRI-----SADQALQHEYF 291
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
30-261 2.06e-29

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: 113.64  E-value: 2.06e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  30 DFERKKTLGTGSFGRVMLVKHKATEQYYAMKIL--DKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNS--NLY 105
Cdd:cd06651    8 NWRRGKLLGQGAFGRVYLCYDVDTGRELAAKQVqfDPESPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAekTLT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 106 MVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKgrtwT 185
Cdd:cd06651   88 IFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQ----T 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 186 LC----------GTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKV--RFPSHFSSDL 253
Cdd:cd06651  164 ICmsgtgirsvtGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTnpQLPSHISEHA 243

                 ....*...
gi 255958318 254 KDLLRNLL 261
Cdd:cd06651  244 RDFLGCIF 251
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
31-269 5.75e-29

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: 112.78  E-value: 5.75e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKIL-DKQKVVKLKqiEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVME 109
Cdd:cd07848    3 FEVLGVVGEGAYGVVLKCRHKETKEIVAIKKFkDSEENEEVK--ETTLRELKMLRTLKQENIVELKEAFRRRGKLYLVFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 110 YVPGgEMFSHLRRIGRFSEPH-ARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRT---WT 185
Cdd:cd07848   81 YVEK-NMLELLEEMPNGVPPEkVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNLSEGSnanYT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 186 -LCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYP-------------------PFFADQPIQIYEKIVSGKVRF 245
Cdd:cd07848  160 eYVATRWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQPlfpgeseidqlftiqkvlgPLPAEQMKLFYSNPRFHGLRF 239
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 255958318 246 PS--H-----------FSSDLKDLLRNLLQVDLTKRF 269
Cdd:cd07848  240 PAvnHpqslerrylgiLSGVLLDLMKNLLKLNPTDRY 276
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
35-261 7.43e-29

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: 112.06  E-value: 7.43e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYYAMKIL--DKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKD--NSNLYMVMEY 110
Cdd:cd06652    8 KLLGQGAFGRVYLCYDADTGRELAVKQVqfDPESPETSKEVNALECEIQLLKNLLHERIVQYYGCLRDpqERTLSIFMEY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 111 VPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKgrtwTLC--- 187
Cdd:cd06652   88 MPGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGASKRLQ----TIClsg 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 188 -------GTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKV--RFPSHFSSDLKDLLR 258
Cdd:cd06652  164 tgmksvtGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPWAEFEAMAAIFKIATQPTnpQLPAHVSDHCRDFLK 243

                 ...
gi 255958318 259 NLL 261
Cdd:cd06652  244 RIF 246
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
28-268 9.87e-29

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: 112.04  E-value: 9.87e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  28 LEDFERKKTLGTGSFgrvmlvkhkaTEQYYAMKILDKQKV-VKLKQIEHTLNEKR---------ILQAVEFPFLVRLEYS 97
Cdd:cd08228    1 LANFQIEKKIGRGQF----------SEVYRATCLLDRKPVaLKKVQIFEMMDAKArqdcvkeidLLKQLNHPNVIKYLDS 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  98 FKDNSNLYMVMEYVPGG---EMFSHLRRIGRF-SEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDF 173
Cdd:cd08228   71 FIEDNELNIVLELADAGdlsQMIKYFKKQKRLiPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 174 GFAKRVKGRT---WTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQP--IQIYEKIvsGKVRFP-- 246
Cdd:cd08228  151 GLGRFFSSKTtaaHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMnlFSLCQKI--EQCDYPpl 228
                        250       260
                 ....*....|....*....|....
gi 255958318 247 --SHFSSDLKDLLRNLLQVDLTKR 268
Cdd:cd08228  229 ptEHYSEKLRELVSMCIYPDPDQR 252
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
37-268 1.00e-28

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: 112.25  E-value: 1.00e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMK----ILDKQKvvkLKQIehtLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVP 112
Cdd:cd06622    9 LGKGNYGSVYKVLHRPTGVTMAMKeirlELDESK---FNQI---IMELDILHKAVSPYIVDFYGAFFIEGAVYMCMEYMD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 113 GGEM---FSHLRRIGRFSEPHARFYAAQIVLTFEYL-HSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKR-VKGRTWTLC 187
Cdd:cd06622   83 AGSLdklYAGGVATEGIPEDVLRRITYAVVKGLKFLkEEHNIIHRDVKPTNVLVNGNGQVKLCDFGVSGNlVASLAKTNI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 188 GTPEYLAPEIILSKG------YNKAVDWWALGVLIYEMAAG---YPPFFADQPIQIYEKIVSGK-VRFPSHFSSDLKDLL 257
Cdd:cd06622  163 GCQSYMAPERIKSGGpnqnptYTVQSDVWSLGLSILEMALGrypYPPETYANIFAQLSAIVDGDpPTLPSGYSDDAQDFV 242
                        250
                 ....*....|.
gi 255958318 258 RNLLQVDLTKR 268
Cdd:cd06622  243 AKCLNKIPNRR 253
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
28-268 1.01e-28

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: 112.08  E-value: 1.01e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  28 LEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKildkqkvvKLKQIEHTLNEKRILQAVEF------PFLVRLEYSFKDN 101
Cdd:cd14046    5 LTDFEELQVLGKGAFGQVVKVRNKLDGRYYAIK--------KIKLRSESKNNSRILREVMLlsrlnhQHVVRYYQAWIER 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 102 SNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKG 181
Cdd:cd14046   77 ANLYIQMEYCEKSTLRDLIDSGLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLATSNKL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 182 RTWTL---------------------CGTPEYLAPEIILSKG--YNKAVDWWALGVLIYEMAagYPPFFADQPIQIYEKI 238
Cdd:cd14046  157 NVELAtqdinkstsaalgssgdltgnVGTALYVAPEVQSGTKstYNEKVDMYSLGIIFFEMC--YPFSTGMERVQILTAL 234
                        250       260       270
                 ....*....|....*....|....*....|....
gi 255958318 239 VSGKVRFPSHFSSDLK----DLLRNLLQVDLTKR 268
Cdd:cd14046  235 RSVSIEFPPDFDDNKHskqaKLIRWLLNHDPAKR 268
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
37-284 1.66e-28

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: 111.75  E-value: 1.66e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKIL--DKQKVVKlKQIehtLNEKRILQAVEFPFLVRLEYSFKDN--SNLYMVMEYVP 112
Cdd:cd06621    9 LGEGAGGSVTKCRLRNTKTIFALKTIttDPNPDVQ-KQI---LRELEINKSCASPYIVKYYGAFLDEqdSSIGIAMEYCE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 113 GGEMFSHLRRI----GRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFA-KRVKGRTWTLC 187
Cdd:cd06621   85 GGSLDSIYKKVkkkgGRIGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGVSgELVNSLAGTFT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 188 GTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQ-----PIQIYEKIVSGKVRF----PSH---FSSDLKD 255
Cdd:cd06621  165 GTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPFPPEGepplgPIELLSYIVNMPNPElkdePENgikWSESFKD 244
                        250       260
                 ....*....|....*....|....*....
gi 255958318 256 LLRNLLQVDLTKRfgnlkNGVSDIKTHKW 284
Cdd:cd06621  245 FIEKCLEKDGTRR-----PGPWQMLAHPW 268
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
34-285 1.67e-28

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: 111.17  E-value: 1.67e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  34 KKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEhTLNEKRILQAVEF-PFLVRLEYSFKDNSNLYMVMEYVP 112
Cdd:cd14198   13 SKELGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQDCRAE-ILHEIAVLELAKSnPRVVNLHEVYETTSEIILILEYAA 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 113 GGEMFSHL--RRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLL---IDHQGYIQVTDFGFAKRV--KGRTWT 185
Cdd:cd14198   92 GGEIFNLCvpDLAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILlssIYPLGDIKIVDFGMSRKIghACELRE 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 186 LCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFP----SHFSSDLKDLLRNLL 261
Cdd:cd14198  172 IMGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFVGEDNQETFLNISQVNVDYSeetfSSVSQLATDFIQKLL 251
                        250       260
                 ....*....|....*....|....
gi 255958318 262 QVDLTKRfgnlkNGVSDIKTHKWF 285
Cdd:cd14198  252 VKNPEKR-----PTAEICLSHSWL 270
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
49-268 1.71e-28

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 114.73  E-value: 1.71e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  49 KHKATEQYYAMKILD-KQKVVKL-------KQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGGEMFSHL 120
Cdd:PTZ00267  77 RNPTTAAFVATRGSDpKEKVVAKfvmlndeRQAAYARSELHCLAACDHFGIVKHFDDFKSDDKLLLIMEYGSGGDLNKQI 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 121 RRIGR----FSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTW-----TLCGTPE 191
Cdd:PTZ00267 157 KQRLKehlpFQEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQYSDSVSldvasSFCGTPY 236
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255958318 192 YLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVR-FPSHFSSDLKDLLRNLLQVDLTKR 268
Cdd:PTZ00267 237 YLAPELWERKRYSKKADMWSLGVILYELLTLHRPFKGPSQREIMQQVLYGKYDpFPCPVSSGMKALLDPLLSKNPALR 314
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
31-268 2.16e-28

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: 110.66  E-value: 2.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318   31 FERKKTLGTGSFGRVmlvkHKATeqYYAMKILDKQKV-VK-LK------QIEHTLNEKRILQAVEFPFLVRLEYSFKDNS 102
Cdd:pfam07714   1 LTLGEKLGEGAFGEV----YKGT--LKGEGENTKIKVaVKtLKegadeeEREDFLEEASIMKKLDHPNIVKLLGVCTQGE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  103 NLYMVMEYVPGGEMFSHLRR-IGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKG 181
Cdd:pfam07714  75 PLYIVTEYMPGGDLLDFLRKhKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDIYD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  182 RTWTLCGTPEYL-----APEIILSKGYNKAVDWWALGVLIYEMAA-GYPPFFADQPIQIYEKIVSGKV-RFPSHFSSDLK 254
Cdd:pfam07714 155 DDYYRKRGGGKLpikwmAPESLKDGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEEVLEFLEDGYRlPQPENCPDELY 234
                         250
                  ....*....|....
gi 255958318  255 DLLRNLLQVDLTKR 268
Cdd:pfam07714 235 DLMKQCWAYDPEDR 248
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
29-239 3.58e-28

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: 110.59  E-value: 3.58e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKIL---DKQKVVKlkqiEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLY 105
Cdd:cd07846    1 EKYENLGLVGEGSYGMVMKCRHKETGQIVAIKKFlesEDDKMVK----KIAMREIKMLKQLRHENLVNLIEVFRRKKRWY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 106 MVMEYV-----------PGGEMFSHLRRigrfsepharfYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFG 174
Cdd:cd07846   77 LVFEFVdhtvlddlekyPNGLDESRVRK-----------YLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFG 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255958318 175 FAKRVK--GRTWT-LCGTPEYLAPEIILSK-GYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIV 239
Cdd:cd07846  146 FARTLAapGEVYTdYVATRWYRAPELLVGDtKYGKAVDVWAVGCLVTEMLTGEPLFPGDSDIDQLYHII 214
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
40-285 3.79e-28

Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RPK118 contains an N-terminal Phox homology (PX) domain, a Microtubule Interacting and Trafficking (MIT) domain, and a kinase domain containing a long uncharacterized insert. Also included in the family is human RPK60 (or ribosomal protein S6 kinase-like 1), which also contains MIT and kinase domains but lacks a PX domain. RPK118 binds sphingosine kinase, a key enzyme in the synthesis of sphingosine 1-phosphate (SPP), a lipid messenger involved in many cellular events. RPK118 may be involved in transmitting SPP-mediated signaling. RPK118 also binds the antioxidant peroxiredoxin-3. RPK118 may be involved in the transport of PRDX3 from the cytoplasm to its site of function in the mitochondria. The RPK118-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: 270728 [Multi-domain]  Cd Length: 265  Bit Score: 110.33  E-value: 3.79e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  40 GSFGRVMLVKHKATEQYYAMKILDKQKvvklkqiEHTLNEKRIL-QAVefPFLVRLEYSFKDNSNLYMVMEYVPGGEMFS 118
Cdd:cd05576   10 GVIDKVLLVMDTRTQETFILKGLRKSS-------EYSRERKTIIpRCV--PNMVCLRKYIISEESVFLVLQHAEGGKLWS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 119 HLRRIGRFSEPH-------------ARFY---------AAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFA 176
Cdd:cd05576   81 YLSKFLNDKEIHqlfadlderlaaaSRFYipeeciqrwAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRW 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 177 KRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGyPPFFADQPIQIYEKIvsgKVRFPSHFSSDLKDL 256
Cdd:cd05576  161 SEVEDSCDSDAIENMYCAPEVGGISEETEACDWWSLGALLFELLTG-KALVECHPAGINTHT---TLNIPEWVSEEARSL 236
                        250       260
                 ....*....|....*....|....*....
gi 255958318 257 LRNLLQVDLTKRFGNLKNGVSDIKTHKWF 285
Cdd:cd05576  237 LQQLLQFNPTERLGAGVAGVEDIKSHPFF 265
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
21-284 5.26e-28

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: 110.08  E-value: 5.26e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  21 PPPSNagleDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDkqkvVKLKQIEHTLNEKRILQA-------VEFPFLVR 93
Cdd:cd06608    2 PDPAG----IFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMD----IIEDEEEEIKLEINILRKfsnhpniATFYGAFI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  94 LEYSFKDNSNLYMVMEYVPGG---EMFSHLRRIG-RFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQ 169
Cdd:cd06608   74 KKDPPGGDDQLWLVMEYCGGGsvtDLVKGLRKKGkRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAEVK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 170 VTDFGFA---KRVKGRTWTLCGTPEYLAPEIILSK-----GYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSG 241
Cdd:cd06608  154 LVDFGVSaqlDSTLGRRNTFIGTPYWMAPEVIACDqqpdaSYDARCDVWSLGITAIELADGKPPLCDMHPMRALFKIPRN 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 255958318 242 ---KVRFPSHFSSDLKDLLRNLLQVDLTKRfgnlkNGVSDIKTHKW 284
Cdd:cd06608  234 pppTLKSPEKWSKEFNDFISECLIKNYEQR-----PFTEELLEHPF 274
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
37-264 5.47e-28

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270892 [Multi-domain]  Cd Length: 279  Bit Score: 110.10  E-value: 5.47e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVmlvkHKA----TEQYYAMKI--LDKQ--KVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFK-DNSNLYMV 107
Cdd:cd13990    8 LGKGGFSEV----YKAfdlvEQRYVACKIhqLNKDwsEEKKQNYIKHALREYEIHKSLDHPRIVKLYDVFEiDTDSFCTV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 108 MEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLD--LIYRDLKPENLLIDHQ---GYIQVTDFGFAKRVKGR 182
Cdd:cd13990   84 LEYCDGNDLDFYLKQHKSIPEREARSIIMQVVSALKYLNEIKppIIHYDLKPGNILLHSGnvsGEIKITDFGLSKIMDDE 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 183 TWTL---------CGTPEYLAPEIILS-----KGYNKaVDWWALGVLIYEMAAGYPPFFADQP-IQIYEK---IVSGKVR 244
Cdd:cd13990  164 SYNSdgmeltsqgAGTYWYLPPECFVVgktppKISSK-VDVWSVGVIFYQMLYGRKPFGHNQSqEAILEEntiLKATEVE 242
                        250       260
                 ....*....|....*....|..
gi 255958318 245 FPS--HFSSDLKDLLRNLLQVD 264
Cdd:cd13990  243 FPSkpVVSSEAKDFIRRCLTYR 264
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
29-234 5.84e-28

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: 110.14  E-value: 5.84e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKlkQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVM 108
Cdd:cd06640    4 ELFTKLERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEEAED--EIEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 109 EYVPGGEMFShLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKG---RTWT 185
Cdd:cd06640   82 EYLGGGSALD-LLRAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDtqiKRNT 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 255958318 186 LCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQI 234
Cdd:cd06640  161 FVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPPNSDMHPMRV 209
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
37-265 1.62e-27

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: 109.28  E-value: 1.62e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLK-------QIEHTLNEKRILQAVEFPFLVRleySFKDNSNLYMVME 109
Cdd:cd14038    2 LGTGGFGNVLRWINQETGEQVAIKQCRQELSPKNRerwcleiQIMKRLNHPNVVAARDVPEGLQ---KLAPNDLPLLAME 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 110 YVPGGEMFSHLRRIGR---FSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDH--QGYI-QVTDFGFAKRVKgrT 183
Cdd:cd14038   79 YCQGGDLRKYLNQFENccgLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQgeQRLIhKIIDLGYAKELD--Q 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 184 WTLC----GTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFAD-QPIQIYEKI-------------VSGKVRF 245
Cdd:cd14038  157 GSLCtsfvGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPFLPNwQPVQWHGKVrqksnedivvyedLTGAVKF 236
                        250       260
                 ....*....|....*....|....*.
gi 255958318 246 ------PSHFSSDLKDLLRNLLQVDL 265
Cdd:cd14038  237 ssvlptPNNLNGILAGKLERWLQCML 262
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
32-261 1.70e-27

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: 108.46  E-value: 1.70e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  32 ERKKTLGTGSFGRVMLVKHKATEQYYAMKILdkqKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYV 111
Cdd:cd14193    7 NKEEILGGGRFGQVHKCEEKSSGLKLAAKII---KARSQKEKEEVKNEIEVMNQLNHANLIQLYDAFESRNDIVLVMEYV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 112 PGGEMFSH-LRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLL-IDHQGY-IQVTDFGFAKRVKGRTWTLC- 187
Cdd:cd14193   84 DGGELFDRiIDENYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILcVSREANqVKIIDFGLARRYKPREKLRVn 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255958318 188 -GTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFP----SHFSSDLKDLLRNLL 261
Cdd:cd14193  164 fGTPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILACQWDFEdeefADISEEAKDFISKLL 242
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
29-261 1.98e-27

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: 108.19  E-value: 1.98e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKIL----DKQKVVKlkQIEHTLNEKRILQAVEFPFLVRLEYSFKDNS-- 102
Cdd:cd06653    2 VNWRLGKLLGRGAFGEVYLCYDADTGRELAVKQVpfdpDSQETSK--EVNALECEIQLLKNLRHDRIVQYYGCLRDPEek 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 103 NLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKgr 182
Cdd:cd06653   80 KLSIFVEYMPGGSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRIQ-- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 183 twTLC----------GTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVS--GKVRFPSHFS 250
Cdd:cd06653  158 --TICmsgtgiksvtGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPWAEYEAMAAIFKIATqpTKPQLPDGVS 235
                        250
                 ....*....|.
gi 255958318 251 SDLKDLLRNLL 261
Cdd:cd06653  236 DACRDFLRQIF 246
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
38-242 2.22e-27

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: 107.99  E-value: 2.22e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  38 GTGSFGRVMLVKHKATEQYYAMKIL-----DKQKVVKLKQIEHTLNEKRILQavefpflvrLEYSFKDNSNLYMVMEYVP 112
Cdd:cd14111   12 ARGRFGVIRRCRENATGKNFPAKIVpyqaeEKQGVLQEYEILKSLHHERIMA---------LHEAYITPRYLVLIAEFCS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 113 GGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTWTLC----G 188
Cdd:cd14111   83 GKELLHSLIDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGSAQSFNPLSLRQLgrrtG 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 255958318 189 TPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGK 242
Cdd:cd14111  163 TLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFEDQDPQETEAKILVAK 216
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
35-261 2.70e-27

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


Pssm-ID: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 108.10  E-value: 2.70e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEhTLNEKRILQ-AVEFPFLVRLEYSFKDNSNLYMVMEYVPG 113
Cdd:cd14197   15 RELGRGKFAVVRKCVEKDSGKEFAAKFMRKRRKGQDCRME-IIHEIAVLElAQANPWVINLHEVYETASEMILVLEYAAG 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 114 GEMFSHL--RRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQ---GYIQVTDFGFAKRVKG--RTWTL 186
Cdd:cd14197   94 GEIFNQCvaDREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSEsplGDIKIVDFGLSRILKNseELREI 173
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255958318 187 CGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPS----HFSSDLKDLLRNLL 261
Cdd:cd14197  174 MGTPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQMNVSYSEeefeHLSESAIDFIKTLL 252
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
37-285 3.51e-27

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: 107.28  E-value: 3.51e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEhtlNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGGEM 116
Cdd:cd14114   10 LGTGAFGVVHRCTERATGNNFAAKFIMTPHESDKETVR---KEIQIMNQLHHPKLINLHDAFEDDNEMVLILEFLSGGEL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 117 FSHLRRIG-RFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQ--GYIQVTDFGFAKR------VKGRTwtlc 187
Cdd:cd14114   87 FERIAAEHyKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTKrsNEVKLIDFGLATHldpkesVKVTT---- 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 188 GTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFP----SHFSSDLKDLLRNLLQV 263
Cdd:cd14114  163 GTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVKSCDWNFDdsafSGISEEAKDFIRKLLLA 242
                        250       260
                 ....*....|....*....|..
gi 255958318 264 DLTKRFgnlknGVSDIKTHKWF 285
Cdd:cd14114  243 DPNKRM-----TIHQALEHPWL 259
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
33-268 4.67e-27

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: 107.13  E-value: 4.67e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  33 RKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQ---IEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVME 109
Cdd:cd06630    4 KGPLLGTGAFSSCYQARDVKTGTLMAVKQVSFCRNSSSEQeevVEAIREEIRMMARLNHPNIVRMLGATQHKSHFNIFVE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 110 YVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQG-YIQVTDFGFAKRVKGRTW---- 184
Cdd:cd06630   84 WMAGGSVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGqRLRIADFGAAARLASKGTgage 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 185 ---TLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQpIQ-----IYeKIVS--GKVRFPSHFSSDLK 254
Cdd:cd06630  164 fqgQLLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPWNAEK-ISnhlalIF-KIASatTPPPIPEHLSPGLR 241
                        250
                 ....*....|....
gi 255958318 255 DLLRNLLQVDLTKR 268
Cdd:cd06630  242 DVTLRCLELQPEDR 255
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
35-268 4.93e-27

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: 106.85  E-value: 4.93e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVmlvkHKATeqyyaMKILDKQKV---VK-------LKQIEHTLNEKRILQAVEFPFLVRLeYSF-KDNSN 103
Cdd:cd00192    1 KKLGEGAFGEV----YKGK-----LKGGDGKTVdvaVKtlkedasESERKDFLKEARVMKKLGHPNVVRL-LGVcTEEEP 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 104 LYMVMEYVPGGEMFSHLR--RIGRFSEPHARF-------YAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFG 174
Cdd:cd00192   71 LYLVMEYMEGGDLLDFLRksRPVFPSPEPSTLslkdllsFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFG 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 175 FAKRV----KGRTWTLCGTP-EYLAPEIILSKGYNKAVDWWALGVLIYEMAA-GYPPFFADQPIQIYEKIVSGKV-RFPS 247
Cdd:cd00192  151 LSRDIydddYYRKKTGGKLPiRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTlGATPYPGLSNEEVLEYLRKGYRlPKPE 230
                        250       260
                 ....*....|....*....|.
gi 255958318 248 HFSSDLKDLLRNLLQVDLTKR 268
Cdd:cd00192  231 NCPDELYELMLSCWQLDPEDR 251
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
31-234 5.23e-27

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: 107.45  E-value: 5.23e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKlkQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEY 110
Cdd:cd06642    6 FTKLERIGKGSFGEVYKGIDNRTKEVVAIKIIDLEEAED--EIEDIQQEITVLSQCDSPYITRYYGSYLKGTKLWIIMEY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 111 VPGGEMFSHLRRiGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKG---RTWTLC 187
Cdd:cd06642   84 LGGGSALDLLKP-GPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDtqiKRNTFV 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 255958318 188 GTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQI 234
Cdd:cd06642  163 GTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNSDLHPMRV 209
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
30-221 9.69e-27

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: 106.74  E-value: 9.69e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  30 DFERKKTLGTGSFGRVMLVKHK-ATEQYYAMKILdKQKVVKLKQIEHTLNEKRILQAVEF---PFLVRLEYSFKDNSNLY 105
Cdd:cd14052    1 RFANVELIGSGEFSQVYKVSERvPTGKVYAVKKL-KPNYAGAKDRLRRLEEVSILRELTLdghDNIVQLIDSWEYHGHLY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 106 MVMEYVPGGEM---FSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVK-G 181
Cdd:cd14052   80 IQTELCENGSLdvfLSELGLLGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMATVWPlI 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 255958318 182 RTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAA 221
Cdd:cd14052  160 RGIEREGDREYIAPEILSEHMYDKPADIFSLGLILLEAAA 199
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
34-268 1.80e-26

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 109.19  E-value: 1.80e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  34 KKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKlKQIEHTLNEKRILQAVEFPFLVRL--EYSFKDNSN------LY 105
Cdd:PTZ00283  37 SRVLGSGATGTVLCAKRVSDGEPFAVKVVDMEGMSE-ADKNRAQAEVCCLLNCDFFSIVKCheDFAKKDPRNpenvlmIA 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 106 MVMEYVPGGEMFSHLR---RIGR-FSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVK- 180
Cdd:PTZ00283 116 LVLDYANAGDLRQEIKsraKTNRtFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLGDFGFSKMYAa 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 181 ------GRTWtlCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGkvRF---PSHFSS 251
Cdd:PTZ00283 196 tvsddvGRTF--CGTPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPFDGENMEEVMHKTLAG--RYdplPPSISP 271
                        250
                 ....*....|....*..
gi 255958318 252 DLKDLLRNLLQVDLTKR 268
Cdd:PTZ00283 272 EMQEIVTALLSSDPKRR 288
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
20-238 2.52e-26

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: 105.89  E-value: 2.52e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  20 NPPPSNAGLEDFERkktLGTGSFGRVMLVKHKATEQYYAMKILDKQKvvkLKQIEHTLNEKRILQAVEFPFLVRLEYSFK 99
Cdd:cd06658   16 SPGDPREYLDSFIK---IGEGSTGIVCIATEKHTGKQVAVKKMDLRK---QQRRELLFNEVVIMRDYHHENVVDMYNSYL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 100 DNSNLYMVMEYVPGGEMfSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRV 179
Cdd:cd06658   90 VGDELWVVMEFLEGGAL-TDIVTHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQV 168
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255958318 180 KG---RTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKI 238
Cdd:cd06658  169 SKevpKRKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRI 230
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
31-287 2.54e-26

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: 106.12  E-value: 2.54e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKildKQKVVKLKQIEHTLN-----EKRILQAVEFPFLVRLEYSFKDNSNLY 105
Cdd:cd07841    2 YEKGKKLGEGTYAVVYKARDKETGRIVAIK---KIKLGERKEAKDGINftalrEIKLLQELKHPNIIGLLDVFGHKSNIN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 106 MVMEYvpggeMFSHLR-----RIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRvk 180
Cdd:cd07841   79 LVFEF-----METDLEkvikdKSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLARS-- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 181 grtwtlCGTPE-----------YLAPEIIL-SKGYNKAVDWWALGVLIYEMAAGYpPFFA-----DQPIQIYEKI----- 238
Cdd:cd07841  152 ------FGSPNrkmthqvvtrwYRAPELLFgARHYGVGVDMWSVGCIFAELLLRV-PFLPgdsdiDQLGKIFEALgtpte 224
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255958318 239 --------------------VSGKVRFPsHFSSDLKDLLRNLLQVDLTKRFgnlknGVSDIKTHKWFAT 287
Cdd:cd07841  225 enwpgvtslpdyvefkpfppTPLKQIFP-AASDDALDLLQRLLTLNPNKRI-----TARQALEHPYFSN 287
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
28-268 3.15e-26

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 109.83  E-value: 3.15e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318   28 LEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKvVKLKQIEHTLNEKRILQAVEFPFLVRLEYSF--KDNSNLY 105
Cdd:PTZ00266   12 LNEYEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAISYRG-LKEREKSQLVIEVNVMRELKHKNIVRYIDRFlnKANQKLY 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  106 MVMEYVPGGEMFSHLRR----IGRFSEPHARFYAAQIVLTFEYLHSLD-------LIYRDLKPENLL----IDHQGYI-- 168
Cdd:PTZ00266   91 ILMEFCDAGDLSRNIQKcykmFGKIEEHAIVDITRQLLHALAYCHNLKdgpngerVLHRDLKPQNIFlstgIRHIGKIta 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  169 -----------QVTDFGFAKR--VKGRTWTLCGTPEYLAPEIIL--SKGYNKAVDWWALGVLIYEMAAGYPPFF-ADQPI 232
Cdd:PTZ00266  171 qannlngrpiaKIGDFGLSKNigIESMAHSCVGTPYYWSPELLLheTKSYDDKSDMWALGCIIYELCSGKTPFHkANNFS 250
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 255958318  233 QIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKR 268
Cdd:PTZ00266  251 QLISELKRGPDLPIKGKSKELNILIKNLLNLSAKER 286
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
29-234 3.17e-26

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: 105.15  E-value: 3.17e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKlkQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVM 108
Cdd:cd06641    4 ELFTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEAED--EIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 109 EYVPGGEMFSHLRRiGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKG---RTWT 185
Cdd:cd06641   82 EYLGGGSALDLLEP-GPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDtqiKRN* 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 255958318 186 LCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQI 234
Cdd:cd06641  161 FVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSELHPMKV 209
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
37-268 5.24e-26

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: 105.10  E-value: 5.24e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKQKvvkLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGGEM 116
Cdd:cd06657   28 IGEGSTGIVCIATVKSSGKLVAVKKMDLRK---QQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGAL 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 117 fSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKG---RTWTLCGTPEYL 193
Cdd:cd06657  105 -TDIVTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKevpRRKSLVGTPYWM 183
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255958318 194 APEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKI---VSGKVRFPSHFSSDLKDLLRNLLQVDLTKR 268
Cdd:cd06657  184 APELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIrdnLPPKLKNLHKVSPSLKGFLDRLLVRDPAQR 261
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
37-241 6.02e-26

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: 104.07  E-value: 6.02e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKQKVVkLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGGEM 116
Cdd:cd13978    1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNC-IEERKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGSL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 117 FSHLRRIGRFSEPHARF-YAAQIVLTFEYLHSLD--LIYRDLKPENLLIDHQGYIQVTDFGFAKRV--------KGRTWT 185
Cdd:cd13978   80 KSLLEREIQDVPWSLRFrIIHEIALGMNFLHNMDppLLHHDLKPENILLDNHFHVKISDFGLSKLGmksisanrRRGTEN 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 255958318 186 LCGTPEYLAPEII--LSKGYNKAVDWWALGVLIYEMAAGYPPFF-ADQPIQIYEKIVSG 241
Cdd:cd13978  160 LGGTPIYMAPEAFddFNKKPTSKSDVYSFAIVIWAVLTRKEPFEnAINPLLIMQIVSKG 218
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
31-268 8.84e-26

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: 103.50  E-value: 8.84e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKvvklKQIEHTLNEKRILQ------AVEFPFLVRLEYSFKDNSNL 104
Cdd:cd14133    1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKIIKNNK----DYLDQSLDEIRLLEllnkkdKADKYHIVRLKDVFYFKNHL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 105 YMVMEYVpGGEMFSHLR--RIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLI-DHQGY-IQVTDFGFAKRVK 180
Cdd:cd14133   77 CIVFELL-SQNLYEFLKqnKFQYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLaSYSRCqIKIIDFGSSCFLT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 181 GRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHF-------SSDL 253
Cdd:cd14133  156 QRLYSYIQSRYYRAPEVILGLPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIIGTIGIPPAHMldqgkadDELF 235
                        250
                 ....*....|....*
gi 255958318 254 KDLLRNLLQVDLTKR 268
Cdd:cd14133  236 VDFLKKLLEIDPKER 250
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
35-264 1.23e-25

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


Pssm-ID: 270887 [Multi-domain]  Cd Length: 272  Bit Score: 103.57  E-value: 1.23e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIehtLNEKRILQAVE-FPFLVRL----EYSFKDNSNLYMVME 109
Cdd:cd13985    6 KQLGEGGFSYVYLAHDVNTGRRYALKRMYFNDEEQLRVA---IKEIEIMKRLCgHPNIVQYydsaILSSEGRKEVLLLME 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 110 YVPGgEMFSHLRRI--GRFSEPHARFYAAQIVLTFEYLHSLD--LIYRDLKPENLLIDHQGYIQVTDFGFAKR--VKGRT 183
Cdd:cd13985   83 YCPG-SLVDILEKSppSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFGSATTehYPLER 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 184 WTLCG----------TPEYLAPEII---LSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIqiyeKIVSGKVRFPSH-- 248
Cdd:cd13985  162 AEEVNiieeeiqkntTPMYRAPEMIdlySKKPIGEKADIWALGCLLYKLCFFKLPFDESSKL----AIVAGKYSIPEQpr 237
                        250
                 ....*....|....*.
gi 255958318 249 FSSDLKDLLRNLLQVD 264
Cdd:cd13985  238 YSPELHDLIRHMLTPD 253
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
28-268 2.34e-25

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: 103.29  E-value: 2.34e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  28 LEDFERKKTLGTGSFGRVMLVKHKATEQYYAMK-ILDKQKVVKLKQIehtLNEKRILQAVEFPFLVRLEYSF-KDNSNLY 105
Cdd:cd06620    4 NQDLETLKDLGAGNGGSVSKVLHIPTGTIMAKKvIHIDAKSSVRKQI---LRELQILHECHSPYIVSFYGAFlNENNNII 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 106 MVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHS-LDLIYRDLKPENLLIDHQGYIQVTDFGFAKR-VKGRT 183
Cdd:cd06620   81 ICMEYMDCGSLDKILKKKGPFPEEVLGKIAVAVLEGLTYLYNvHRIIHRDIKPSNILVNSKGQIKLCDFGVSGElINSIA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 184 WTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFA--------DQPIQIYE---KIVSGKV-RFPS--HF 249
Cdd:cd06620  161 DTFVGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPFAGsnddddgyNGPMGILDllqRIVNEPPpRLPKdrIF 240
                        250
                 ....*....|....*....
gi 255958318 250 SSDLKDLLRNLLQVDLTKR 268
Cdd:cd06620  241 PKDLRDFVDRCLLKDPRER 259
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
35-268 2.84e-25

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: 102.12  E-value: 2.84e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKlKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGG 114
Cdd:cd08221    6 RVLGRGAFGEAVLYRKTEDNSLVVWKEVNLSRLSE-KERRDALNEIDILSLLNHDNIITYYNHFLDGESLFIEMEYCNGG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 115 EMFSHLRRIGR--FSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTW---TLCGT 189
Cdd:cd08221   85 NLHDKIAQQKNqlFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKVLDSESSmaeSIVGT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 190 PEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVR-FPSHFSSDLKDLLRNLLQVDLTKR 268
Cdd:cd08221  165 PYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRTFDATNPLRLAVKIVQGEYEdIDEQYSEEIIQLVHDCLHQDPEDR 244
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
37-268 4.07e-25

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: 102.04  E-value: 4.07e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDK----QKVVKLKQIEHTLNEKRI-LQAVEFPFLVRLEYSFKDNSNLYMVMEYV 111
Cdd:cd13993    8 IGEGAYGVVYLAVDLRTGRKYAIKCLYKsgpnSKDGNDFQKLPQLREIDLhRRVSRHPNIITLHDVFETEVAIYIVLEYC 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 112 PGGEMFS--HLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGY-IQVTDFGFAKRVKGRTWTLCG 188
Cdd:cd13993   88 PNGDLFEaiTENRIYVGKTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDEGtVKLCDFGLATTEKISMDFGVG 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 189 TPEYLAPEII-----LSKGYN-KAVDWWALGVLIYEMAAGYPPF-------------FADQPIqIYEKIVSgkvrfpshF 249
Cdd:cd13993  168 SEFYMAPECFdevgrSLKGYPcAAGDIWSLGIILLNLTFGRNPWkiasesdpifydyYLNSPN-LFDVILP--------M 238
                        250
                 ....*....|....*....
gi 255958318 250 SSDLKDLLRNLLQVDLTKR 268
Cdd:cd13993  239 SDDFYNLLRQIFTVNPNNR 257
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
20-226 5.16e-25

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 103.36  E-value: 5.16e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  20 NPPPSNAGLEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKIL--DKQKVVKlKQIehtLNEKRILQAVEFPFLVRLEYS 97
Cdd:PLN00034  65 SAPSAAKSLSELERVNRIGSGAGGTVYKVIHRPTGRLYALKVIygNHEDTVR-RQI---CREIEILRDVNHPNVVKCHDM 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  98 FKDNSNLYMVMEYVPGGEMFSHlrRIGrfSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAk 177
Cdd:PLN00034 141 FDHNGEIQVLLEFMDGGSLEGT--HIA--DEQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVS- 215
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 255958318 178 RVKGRTWTLC----GTPEYLAPEII---LSKG-YNK-AVDWWALGVLIYEMAAGYPPF 226
Cdd:PLN00034 216 RILAQTMDPCnssvGTIAYMSPERIntdLNHGaYDGyAGDIWSLGVSILEFYLGRFPF 273
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
35-285 1.16e-24

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: 100.66  E-value: 1.16e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYYAMKILDKQkvvklkqiEHTLNEKRILQAVEFPFLVRLEYSFKDNS-NLYMVMEYVPG 113
Cdd:cd14109   10 EDEKRAAQGAPFHVTERSTGRNFLAQLRYGD--------PFLMREVDIHNSLDHPNIVQMHDAYDDEKlAVTVIDNLAST 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 114 GEMFSH--LRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLI--DHqgyIQVTDFGFAKR-VKGRTWTLC- 187
Cdd:cd14109   82 IELVRDnlLPGKDYYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILLqdDK---LKLADFGQSRRlLRGKLTTLIy 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 188 GTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFP----SHFSSDLKDLLRNLLQV 263
Cdd:cd14109  159 GSPEFVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISPFLGDNDRETLTNVRSGKWSFDssplGNISDDARDFIKKLLVY 238
                        250       260
                 ....*....|....*....|....*
gi 255958318 264 DLTKRFgnlkngvsDIKT---HKWF 285
Cdd:cd14109  239 IPESRL--------TVDEalnHPWF 255
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
28-268 1.17e-24

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: 101.26  E-value: 1.17e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  28 LEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMV 107
Cdd:cd08229   23 LANFRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQIFDLMDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIV 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 108 MEYVPGGE---MFSHLRRIGRF-SEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRT 183
Cdd:cd08229  103 LELADAGDlsrMIKHFKKQKRLiPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKT 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 184 ---WTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQpIQIYEkiVSGKVR------FPS-HFSSDL 253
Cdd:cd08229  183 taaHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDK-MNLYS--LCKKIEqcdyppLPSdHYSEEL 259
                        250
                 ....*....|....*
gi 255958318 254 KDLLRNLLQVDLTKR 268
Cdd:cd08229  260 RQLVNMCINPDPEKR 274
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
30-268 2.29e-24

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: 99.98  E-value: 2.29e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  30 DFERKKTLGTGSFGRVMLVKhKATEQYYAMKildkqkVVKLKQIEHT-----LNEKRILQAVEF-PFLVRL---EYSFKD 100
Cdd:cd14131    2 PYEILKQLGKGGSSKVYKVL-NPKKKIYALK------RVDLEGADEQtlqsyKNEIELLKKLKGsDRIIQLydyEVTDED 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 101 nSNLYMVMEYvpgGEM-FSHL---RRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIdHQGYIQVTDFGFA 176
Cdd:cd14131   75 -DYLYMVMEC---GEIdLATIlkkKRPKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLL-VKGRLKLIDFGIA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 177 KRVKGRTWTL-----CGTPEYLAPEIIL---SKGYNKAV-------DWWALGVLIYEMAAGYPPFFADQ-PIQIYEKIV- 239
Cdd:cd14131  150 KAIQNDTTSIvrdsqVGTLNYMSPEAIKdtsASGEGKPKskigrpsDVWSLGCILYQMVYGKTPFQHITnPIAKLQAIId 229
                        250       260       270
                 ....*....|....*....|....*....|
gi 255958318 240 -SGKVRFPSHFSSDLKDLLRNLLQVDLTKR 268
Cdd:cd14131  230 pNHEIEFPDIPNPDLIDVMKRCLQRDPKKR 259
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
29-224 3.36e-24

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: 100.20  E-value: 3.36e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILD---KQKVvkLKQIehtLNEKRILQAVEFPFLVRLEYSFKDNSNLY 105
Cdd:cd06615    1 DDFEKLGELGAGNGGVVTKVLHRPSGLIMARKLIHleiKPAI--RNQI---IRELKVLHECNSPYIVGFYGAFYSDGEIS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 106 MVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHS-LDLIYRDLKPENLLIDHQGYIQVTDFGfakrVKGR-- 182
Cdd:cd06615   76 ICMEHMDGGSLDQVLKKAGRIPENILGKISIAVLRGLTYLREkHKIMHRDVKPSNILVNSRGEIKLCDFG----VSGQli 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 255958318 183 ---TWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAG-YP 224
Cdd:cd06615  152 dsmANSFVGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGrYP 197
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
31-226 3.53e-24

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: 100.31  E-value: 3.53e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVK-HKaTEQYYAMKILDKQKvvKLKQieHTLNEKRILQAV------EFPFLVRLEYSFKDNSN 103
Cdd:cd14210   15 YEVLSVLGKGSFGQVVKCLdHK-TGQLVAIKIIRNKK--RFHQ--QALVEVKILKHLndndpdDKHNIVRYKDSFIFRGH 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 104 LYMVMEyVPGGEMFSHLRRIG--RFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGY--IQVTDFGFAKRV 179
Cdd:cd14210   90 LCIVFE-LLSINLYELLKSNNfqGLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPSKssIKVIDFGSSCFE 168
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 255958318 180 KGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPF 226
Cdd:cd14210  169 GEKVYTYIQSRFYRAPEVILGLPYDTAIDMWSLGCILAELYTGYPLF 215
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
37-268 4.61e-24

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: 99.66  E-value: 4.61e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATeqyyamkildkQKVVKLKQIEHTLNEK-------------RILQAVEFPFLVRLE--YSFKDN 101
Cdd:cd07838    7 IGEGAYGTVYKARDLQD-----------GRFVALKKVRVPLSEEgiplstireiallKQLESFEHPNVVRLLdvCHGPRT 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 102 SN---LYMVMEYV-------------PGgemfshlrrigrFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQ 165
Cdd:cd07838   76 DRelkLTLVFEHVdqdlatyldkcpkPG------------LPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSD 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 166 GYIQVTDFGFAkRVKGRTWTLCG---TPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFF----ADQPIQIYEKI 238
Cdd:cd07838  144 GQVKLADFGLA-RIYSFEMALTSvvvTLWYRAPEVLLQSSYATPVDMWSVGCIFAELFNRRPLFRgsseADQLGKIFDVI 222
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 255958318 239 ------------VSGKVRFPSHFSSDLK-----------DLLRNLLQVDLTKR 268
Cdd:cd07838  223 glpseeewprnsALPRSSFPSYTPRPFKsfvpeideeglDLLKKMLTFNPHKR 275
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
31-238 9.45e-24

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: 98.52  E-value: 9.45e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKildkqkVVKLKQIEH-----TLNEKRILQAVEFPFLVRLEYSFKDNSNLY 105
Cdd:cd07835    1 YQKLEKIGEGTYGVVYKARDKLTGEIVALK------KIRLETEDEgvpstAIREISLLKELNHPNIVRLLDVVHSENKLY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 106 MVMEYVpGGEMFSHLRRIGRFSEPHARF--YAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKR--VKG 181
Cdd:cd07835   75 LVFEFL-DLDLKKYMDSSPLTGLDPPLIksYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLARAfgVPV 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 182 RTWTL-CGTPEYLAPEIIL-SKGYNKAVDWWALGVLIYEMAAGYPPFFADQPI-QIYeKI 238
Cdd:cd07835  154 RTYTHeVVTLWYRAPEILLgSKHYSTPVDIWSVGCIFAEMVTRRPLFPGDSEIdQLF-RI 212
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
37-240 3.35e-23

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: 98.13  E-value: 3.35e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDK--QKVVKLKQiehTLNEKRILQAVEFPFLVRLEYSFKDNSNL------YMVM 108
Cdd:cd07851   23 VGSGAYGQVCSAFDTKTGRKVAIKKLSRpfQSAIHAKR---TYRELRLLKHMKHENVIGLLDVFTPASSLedfqdvYLVT 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 109 EYVpgGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTWTLCG 188
Cdd:cd07851  100 HLM--GADLNNIVKCQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLARHTDDEMTGYVA 177
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 255958318 189 TPEYLAPEIILSKG-YNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVS 240
Cdd:cd07851  178 TRWYRAPEIMLNWMhYNQTVDIWSVGCIMAELLTGKTLFPGSDHIDQLKRIMN 230
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
31-268 4.69e-23

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are three PIM2 isoforms resulting from alternative translation initiation sites. PIM2 is highly expressed in leukemia and lymphomas and has been shown to promote the survival and proliferation of tumor cells. The PIM2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 96.07  E-value: 4.69e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVV---KLKQIEHTLNEKRILQAV----EFPFLVRLEYSFKDNSN 103
Cdd:cd14101    2 YTMGNLLGKGGFGTVYAGHRISDGLQVAIKQISRNRVQqwsKLPGVNPVPNEVALLQSVgggpGHRGVIRLLDWFEIPEG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 104 LYMVMEY-VPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLID-HQGYIQVTDFGFAKRVKG 181
Cdd:cd14101   82 FLLVLERpQHCQDLFDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDlRTGDIKLIDFGSGATLKD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 182 RTWT-LCGTPEYLAPEIILSKGYNK-AVDWWALGVLIYEMAAGYPPFFADQpiqiyeKIVSGKVRFPSHFSSDLKDLLRN 259
Cdd:cd14101  162 SMYTdFDGTRVYSPPEWILYHQYHAlPATVWSLGILLYDMVCGDIPFERDT------DILKAKPSFNKRVSNDCRSLIRS 235

                 ....*....
gi 255958318 260 LLQVDLTKR 268
Cdd:cd14101  236 CLAYNPSDR 244
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
31-269 5.23e-23

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: 96.47  E-value: 5.23e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKIL-----DKQKVVKLKQIEHTLNEKRILqavefpflvRLEYSFKDNSNLY 105
Cdd:cd14104    2 YMIAEELGRGQFGIVHRCVETSSKKTYMAKFVkvkgaDQVLVKKEISILNIARHRNIL---------RLHESFESHEELV 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 106 MVMEYVPGGEMFshlRRIG----RFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLL-IDHQGY-IQVTDFGFAKRV 179
Cdd:cd14104   73 MIFEFISGVDIF---ERITtarfELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIyCTRRGSyIKIIEFGQSRQL 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 180 K-GRTWTLCGT-PEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPS----HFSSDL 253
Cdd:cd14104  150 KpGDKFRLQYTsAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNAEYAFDDeafkNISIEA 229
                        250
                 ....*....|....*.
gi 255958318 254 KDLLRNLLQVDLTKRF 269
Cdd:cd14104  230 LDFVDRLLVKERKSRM 245
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
37-242 5.37e-23

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: 96.14  E-value: 5.37e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVmlvkHKATEQYYAMKILDKQ-KVVKLKQIEHT--LNEKRILQAVEFPFLVRLEYSFKDNSNLYMVM--EYV 111
Cdd:cd13983    9 LGRGSFKTV----YRAFDTEEGIEVAWNEiKLRKLPKAERQrfKQEIEILKSLKHPNIIKFYDSWESKSKKEVIFitELM 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 112 PGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLD--LIYRDLKPENLLID-HQGYIQVTDFGFAK-RVKGRTWTLC 187
Cdd:cd13983   85 TSGTLKQYLKRFKRLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFINgNTGEVKIGDLGLATlLRQSFAKSVI 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 255958318 188 GTPEYLAPEiILSKGYNKAVDWWALGVLIYEMAAG-YPPFFADQPIQIYEKIVSGK 242
Cdd:cd13983  165 GTPEFMAPE-MYEEHYDEKVDIYAFGMCLLEMATGeYPYSECTNAAQIYKKVTSGI 219
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
18-268 6.50e-23

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: 97.43  E-value: 6.50e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  18 WENPppsnaglEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDK--QKVVKLKQiehTLNEKRILQAVEFPFLVRL- 94
Cdd:cd07878   11 WEVP-------ERYQNLTPVGSGAYGSVCSAYDTRLRQKVAVKKLSRpfQSLIHARR---TYRELRLLKHMKHENVIGLl 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  95 -----EYSFKDNSNLYMVMEYVpgGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQ 169
Cdd:cd07878   81 dvftpATSIENFNEVYLVTNLM--GADLNNIVKCQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 170 VTDFGFAKRVKGRTWTLCGTPEYLAPEIILS-KGYNKAVDWWALGVLIYEMAAGYPPF----FADQPIQIYE-------- 236
Cdd:cd07878  159 ILDFGLARQADDEMTGYVATRWYRAPEIMLNwMHYNQTVDIWSVGCIMAELLKGKALFpgndYIDQLKRIMEvvgtpspe 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 255958318 237 ---KIVSGKVR-----FPSHFSSDLKDLLR--NLLQVDLTKR 268
Cdd:cd07878  239 vlkKISSEHARkyiqsLPHMPQQDLKKIFRgaNPLAIDLLEK 280
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
35-285 6.65e-23

Catalytic kinase domain, first 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: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 95.74  E-value: 6.65e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYYAMKILDkqkvVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGG 114
Cdd:cd14108    8 KEIGRGAFSYLRRVKEKSSDLSFAAKFIP----VRAKKKTSARRELALLAELDHKSIVRFHDAFEKRRVVIIVTELCHEE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 115 EMfshLRRIGRFS--EPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQG--YIQVTDFGFAKRVKGRTWTLC--G 188
Cdd:cd14108   84 LL---ERITKRPTvcESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKtdQVRICDFGNAQELTPNEPQYCkyG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 189 TPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPshfSSDLKDLLRN----LLQVD 264
Cdd:cd14108  161 TPEFVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPFVGENDRTTLMNIRNYNVAFE---ESMFKDLCREakgfIIKVL 237
                        250       260
                 ....*....|....*....|.
gi 255958318 265 LTKRfgnLKNGVSDIKTHKWF 285
Cdd:cd14108  238 VSDR---LRPDAEETLEHPWF 255
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
29-239 6.68e-23

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: 96.10  E-value: 6.68e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKL-KQIehtLNEKRILQAVEFPFLVRLEYSFKDNSNLYMV 107
Cdd:cd06619    1 QDIQYQEILGHGNGGTVYKAYHLLTRRILAVKVIPLDITVELqKQI---MSELEILYKCDSPYIIGFYGAFFVENRISIC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 108 MEYVPGGEmfshLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKR-VKGRTWTL 186
Cdd:cd06619   78 TEFMDGGS----LDVYRKIPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQlVNSIAKTY 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 187 CGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAG---YPPFFADQ----PIQIYEKIV 239
Cdd:cd06619  154 VGTNAYMAPERISGEQYGIHSDVWSLGISFMELALGrfpYPQIQKNQgslmPLQLLQCIV 213
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
28-285 1.36e-22

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


Pssm-ID: 270849 [Multi-domain]  Cd Length: 311  Bit Score: 95.84  E-value: 1.36e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  28 LEDFERKKTLGTGSFGRVMLVKHKATEQYYAMK--ILDKQK----VVKLKQIE--HTLNEKRILQAVEFpFLVRLEYSFK 99
Cdd:cd07866    7 LRDYEILGKLGEGTFGEVYKARQIKTGRVVALKkiLMHNEKdgfpITALREIKilKKLKHPNVVPLIDM-AVERPDKSKR 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 100 DNSNLYMVMEYvpggeMFSHL------RRIgRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDF 173
Cdd:cd07866   86 KRGSVYMVTPY-----MDHDLsgllenPSV-KLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 174 GFAKRVKG-------------RTWTLC-GTPEYLAPEIILS-KGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKI 238
Cdd:cd07866  160 GLARPYDGpppnpkggggggtRKYTNLvVTRWYRPPELLLGeRRYTTAVDIWGIGCVFAEMFTRRPILQGKSDIDQLHLI 239
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255958318 239 --------------------VSGKVRFPSH----------FSSDLKDLLRNLLQVDLTKRFgnlknGVSDIKTHKWF 285
Cdd:cd07866  240 fklcgtpteetwpgwrslpgCEGVHSFTNYprtleerfgkLGPEGLDLLSKLLSLDPYKRL-----TASDALEHPYF 311
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
31-226 1.41e-22

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: 96.06  E-value: 1.41e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILDK--QKVVKLKQIehtLNEKRILQAVEFPFLVRLE--------YSFKD 100
Cdd:cd07834    2 YELLKPIGSGAYGVVCSAYDKRTGRKVAIKKISNvfDDLIDAKRI---LREIKILRHLKHENIIGLLdilrppspEEFND 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 101 nsnLYMVMEYvpggeMFSHLRRIGRFSEP----HARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFA 176
Cdd:cd07834   79 ---VYIVTEL-----METDLHKVIKSPQPltddHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFGLA 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255958318 177 KRV----KGRTWTlcgtpEYL------APEIILS-KGYNKAVDWWALGVLIYEMAAGYPPF 226
Cdd:cd07834  151 RGVdpdeDKGFLT-----EYVvtrwyrAPELLLSsKKYTKAIDIWSVGCIFAELLTRKPLF 206
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
31-270 1.54e-22

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: 96.32  E-value: 1.54e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQ-----------YYAMKILDKQKVVKLKQIEHTLNEKRILQavefpfLVRLEYSFK 99
Cdd:cd07857    2 YELIKELGQGAYGIVCSARNAETSEeetvaikkitnVFSKKILAKRALRELKLLRHFRGHKNITC------LYDMDIVFP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 100 DNSN---LYM-VMEYvpggEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGF 175
Cdd:cd07857   76 GNFNelyLYEeLMEA----DLHQIIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 176 A-------KRVKGRTWTLCGTPEYLAPEIILS-KGYNKAVDWWALGVLIYEMAAGYPPF----FADQPIQIYE------- 236
Cdd:cd07857  152 ArgfsenpGENAGFMTEYVATRWYRAPEIMLSfQSYTKAIDVWSVGCILAELLGRKPVFkgkdYVDQLNQILQvlgtpde 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 255958318 237 ----KIVSGK-------------VRFPSHF---SSDLKDLLRNLLQVDLTKRFG 270
Cdd:cd07857  232 etlsRIGSPKaqnyirslpnipkKPFESIFpnaNPLALDLLEKLLAFDPTKRIS 285
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
100-234 2.63e-22

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 97.56  E-value: 2.63e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 100 DNSNLYMVMEYVPGgemfSHLRRI----GRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGF 175
Cdd:NF033483  78 DGGIPYIVMEYVDG----RTLKDYirehGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGI 153
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255958318 176 AKRVKGRTWT----LCGTPEYLAPEIIlsKGynKAV----DWWALGVLIYEMAAGYPPFFADQPIQI 234
Cdd:NF033483 154 ARALSSTTMTqtnsVLGTVHYLSPEQA--RG--GTVdarsDIYSLGIVLYEMLTGRPPFDGDSPVSV 216
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
29-219 3.07e-22

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: 94.09  E-value: 3.07e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKildkqkVVKLKQiEHTLNEKRILQAVEFPFLVRLEYSFKDNSN----- 103
Cdd:cd14047    6 QDFKEIELIGSGGFGQVFKAKHRIDGKTYAIK------RVKLNN-EKAEREVKALAKLDHPNIVRYNGCWDGFDYdpets 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 104 -----------LYMVMEYVPGGEMFSHL-RRIGRFSEP---HARFYaaQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYI 168
Cdd:cd14047   79 ssnssrsktkcLFIQMEFCEKGTLESWIeKRNGEKLDKvlaLEIFE--QITKGVEYIHSKKLIHRDLKPSNIFLVDTGKV 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 255958318 169 QVTDFGFA-------KRVKGRtwtlcGTPEYLAPEIILSKGYNKAVDWWALGVLIYEM 219
Cdd:cd14047  157 KIGDFGLVtslkndgKRTKSK-----GTLSYMSPEQISSQDYGKEVDIYALGLILFEL 209
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
23-268 3.45e-22

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: 94.67  E-value: 3.45e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  23 PSNAGLED-------FERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKlKQIEHTLNekrILQAV-EFPFLVRL 94
Cdd:cd06639    9 SSMLGLESladpsdtWDIIETIGKGTYGKVYKVTNKKDGSLAAVKILDPISDVD-EEIEAEYN---ILRSLpNHPNVVKF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  95 EYSFKD-----NSNLYMVMEYVPGG---EMFSHLRRIG-RFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQ 165
Cdd:cd06639   85 YGMFYKadqyvGGQLWLVLELCNGGsvtELVKGLLKCGqRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTE 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 166 GYIQVTDFGFAKRVKG---RTWTLCGTPEYLAPEIILSK-----GYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEK 237
Cdd:cd06639  165 GGVKLVDFGVSAQLTSarlRRNTSVGTPFWMAPEVIACEqqydySYDARCDVWSLGITAIELADGDPPLFDMHPVKALFK 244
                        250       260       270
                 ....*....|....*....|....*....|....
gi 255958318 238 I---VSGKVRFPSHFSSDLKDLLRNLLQVDLTKR 268
Cdd:cd06639  245 IprnPPPTLLNPEKWCRGFSHFISQCLIKDFEKR 278
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
28-268 4.53e-22

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: 94.93  E-value: 4.53e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  28 LEDFERKKTLGTGSFGRVMlvkhkateqyyamKILDKQ--KVVKLKQI----------EHTLNEKRILQAV-EFPFLVRL 94
Cdd:cd07852    6 LRRYEILKKLGKGAYGIVW-------------KAIDKKtgEVVALKKIfdafrnatdaQRTFREIMFLQELnDHPNIIKL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  95 EYSFK--DNSNLYMVMEYvpggeMFSHLR---RIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQ 169
Cdd:cd07852   73 LNVIRaeNDKDIYLVFEY-----METDLHaviRANILEDIHKQYIMYQLLKALKYLHSGGVIHRDLKPSNILLNSDCRVK 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 170 VTDFGFAKRVKGRTWTLCG--------TPEYLAPEIIL-SKGYNKAVDWWALGVLIYEMAAGYPPFFADQPI-QIyEKIV 239
Cdd:cd07852  148 LADFGLARSLSQLEEDDENpvltdyvaTRWYRAPEILLgSTRYTKGVDMWSVGCILGEMLLGKPLFPGTSTLnQL-EKII 226
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 240 ----------------------------SGKVRFPSHF---SSDLKDLLRNLLQVDLTKR 268
Cdd:cd07852  227 evigrpsaediesiqspfaatmleslppSRPKSLDELFpkaSPDALDLLKKLLVFNPNKR 286
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
31-227 5.59e-22

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: 93.28  E-value: 5.59e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILD---KQKVVKLKQIehtLNEKRILQAVEFPFLVRLEYSFKDNSNLYMV 107
Cdd:cd06607    3 FEDLREIGHGSFGAVYYARNKRTSEVVAIKKMSysgKQSTEKWQDI---IKEVKFLRQLRHPNTIEYKGCYLREHTAWLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 108 MEYVPG--GEMFSHLRRIGRFSEPHArfYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTwT 185
Cdd:cd06607   80 MEYCLGsaSDIVEVHKKPLQEVEIAA--ICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFGSASLVCPAN-S 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 255958318 186 LCGTPEYLAPEIILS--KG-YNKAVDWWALGVLIYEMAAGYPPFF 227
Cdd:cd06607  157 FVGTPYWMAPEVILAmdEGqYDGKVDVWSLGITCIELAERKPPLF 201
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
35-226 6.18e-22

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


Pssm-ID: 143359 [Multi-domain]  Cd Length: 342  Bit Score: 94.85  E-value: 6.18e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMlvkhKATEQYYAMKILDKQKVVKLKQ-IEHTLNEKRILQAVEFPFLVRL-EYSFKDNSNL-------- 104
Cdd:cd07854   11 RPLGCGSNGLVF----SAVDSDCDKRVAVKKIVLTDPQsVKHALREIKIIRRLDHDNIVKVyEVLGPSGSDLtedvgslt 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 105 -----YMVMEYvpggeMFSHLRRI---GRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYI-QVTDFGF 175
Cdd:cd07854   87 elnsvYIVQEY-----METDLANVleqGPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTEDLVlKIGDFGL 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 255958318 176 AKRV------KGRTWTLCGTPEYLAPEIILS-KGYNKAVDWWALGVLIYEMAAGYPPF 226
Cdd:cd07854  162 ARIVdphyshKGYLSEGLVTKWYRSPRLLLSpNNYTKAIDMWAAGCIFAEMLTGKPLF 219
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
29-307 7.43e-22

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: 94.35  E-value: 7.43e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKildkqKVVK----LKQIEHTLNEKRILQAVEFPFLVRLEYSFK----- 99
Cdd:cd07855    5 DRYEPIETIGSGAYGVVCSAIDTKSGQKVAIK-----KIPNafdvVTTAKRTLRELKILRHFKHDNIIAIRDILRpkvpy 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 100 -DNSNLYMVMEYvpggeMFSHLRRIGRFSEP----HARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFG 174
Cdd:cd07855   80 aDFKDVYVVLDL-----MESDLHHIIHSDQPltleHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 175 FAKrvkgrtwTLCGTPE--------------YLAPEIILS-KGYNKAVDWWALGVLIYEMAAGYPPF----FADQ----- 230
Cdd:cd07855  155 MAR-------GLCTSPEehkyfmteyvatrwYRAPELMLSlPEYTQAIDMWSVGCIFAEMLGRRQLFpgknYVHQlqlil 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 231 ------PIQIYEKIVSGKVR-----FPSHFSSDLK-----------DLLRNLLQVDLTKRFgnlknGVSDIKTHKWFATt 288
Cdd:cd07855  228 tvlgtpSQAVINAIGADRVRryiqnLPNKQPVPWEtlypkadqqalDLLSQMLRFDPSERI-----TVAEALQHPFLAK- 301
                        330       340
                 ....*....|....*....|
gi 255958318 289 dwiaiYQRKVEAPF-IPKFR 307
Cdd:cd07855  302 -----YHDPDDEPDcAPPFD 316
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
37-226 1.52e-21

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


Pssm-ID: 270825 [Multi-domain]  Cd Length: 282  Bit Score: 92.33  E-value: 1.52e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILdKQKVVKLKQIEHtLNEKRILQAVE-FPFLVRLEYSFKDNSN--LYMVMEYVPG 113
Cdd:cd07831    7 IGEGTFSEVLKAQSRKTGKYYAIKCM-KKHFKSLEQVNN-LREIQALRRLSpHPNILRLIEVLFDRKTgrLALVFELMDM 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 114 gEMFSHLR-RIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDhQGYIQVTDFGFAKrvkgrtwTLCGTP-- 190
Cdd:cd07831   85 -NLYELIKgRKRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIK-DDILKLADFGSCR-------GIYSKPpy 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 255958318 191 -EYL------APEIILSKG-YNKAVDWWALGVLIYEMAAGYPPF 226
Cdd:cd07831  156 tEYIstrwyrAPECLLTDGyYGPKMDIWAVGCVFFEILSLFPLF 199
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
30-232 1.53e-21

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: 92.48  E-value: 1.53e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  30 DFERKKTLGTGSFGRVMLVKHKATEQYYAMKildkqkVVKLKQIEH-----TLNEKRILQAVEFPFLVRLEYSFKDNSNL 104
Cdd:cd07861    1 DYTKIEKIGEGTYGVVYKGRNKKTGQIVAMK------KIRLESEEEgvpstAIREISLLKELQHPNIVCLEDVLMQENRL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 105 YMVMEYVpGGEMFSHLRRI--GRFSEPH-ARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKR--V 179
Cdd:cd07861   75 YLVFEFL-SMDLKKYLDSLpkGKYMDAElVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLARAfgI 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 255958318 180 KGRTWTL-CGTPEYLAPEIIL-SKGYNKAVDWWALGVLIYEMAAGYPPFFADQPI 232
Cdd:cd07861  154 PVRVYTHeVVTLWYRAPEVLLgSPRYSTPVDIWSIGTIFAEMATKKPLFHGDSEI 208
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
37-268 1.75e-21

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: 92.36  E-value: 1.75e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKildKQKVVKLKQIEHTLNEKRILQAVEFPFLVRL-EYSFK----DNSNLYMVMEYV 111
Cdd:cd13986    8 LGEGGFSFVYLVEDLSTGRLYALK---KILCHSKEDVKEAMREIENYRLFNHPNILRLlDSQIVkeagGKKEVYLLLPYY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 112 PGGEMFSHLRRIgrfSEPHARFYAAQIVLTF-------EYLHSLDLI---YRDLKPENLLIDHQGYIQVTDFGFA----K 177
Cdd:cd13986   85 KRGSLQDEIERR---LVKGTFFPEDRILHIFlgicrglKAMHEPELVpyaHRDIKPGNVLLSEDDEPILMDLGSMnparI 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 178 RVKGRTWTLC--------GTPEYLAPE--------IILSKgynkaVDWWALGVLIYEMAAGYPPFFAD----QPIQIyeK 237
Cdd:cd13986  162 EIEGRREALAlqdwaaehCTMPYRAPElfdvkshcTIDEK-----TDIWSLGCTLYALMYGESPFERIfqkgDSLAL--A 234
                        250       260       270
                 ....*....|....*....|....*....|...
gi 255958318 238 IVSGKVRFP--SHFSSDLKDLLRNLLQVDLTKR 268
Cdd:cd13986  235 VLSGNYSFPdnSRYSEELHQLVKSMLVVNPAER 267
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
29-233 1.81e-21

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: 92.03  E-value: 1.81e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILD----------KQKVVKLKQIEHtlnekrilqavefPFLVRLEYSF 98
Cdd:cd06645   11 EDFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKlepgedfavvQQEIIMMKDCKH-------------SNIVAYFGSY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  99 KDNSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKR 178
Cdd:cd06645   78 LRRDKLWICMEFCGGGSLQDIYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQ 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255958318 179 VK---GRTWTLCGTPEYLAPEIILSK---GYNKAVDWWALGVLIYEMAAGYPPFFADQPIQ 233
Cdd:cd06645  158 ITatiAKRKSFIGTPYWMAPEVAAVErkgGYNQLCDIWAVGITAIELAELQPPMFDLHPMR 218
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
29-269 1.84e-21

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: 92.43  E-value: 1.84e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMK-ILDKQKVVKLKQIehTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMV 107
Cdd:cd07847    1 EKYEKLSKIGEGSYGVVFKCRNRETGQIVAIKkFVESEDDPVIKKI--ALREIRMLKQLKHPNLVNLIEVFRRKRKLHLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 108 MEYVPG---GEMFSHLRRIgrfSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKG--R 182
Cdd:cd07847   79 FEYCDHtvlNELEKNPRGV---PEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFARILTGpgD 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 183 TWTLC-GTPEYLAPEIILSK-GYNKAVDWWALGVLIYEMAAGYP--P------------------------------FFA 228
Cdd:cd07847  156 DYTDYvATRWYRAPELLVGDtQYGPPVDVWAIGCVFAELLTGQPlwPgksdvdqlylirktlgdliprhqqifstnqFFK 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 255958318 229 DQPIQIYEKIVSGKVRFPSHfSSDLKDLLRNLLQVDLTKRF 269
Cdd:cd07847  236 GLSIPEPETREPLESKFPNI-SSPALSFLKGCLQMDPTERL 275
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
29-268 2.13e-21

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: 92.10  E-value: 2.13e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQyyamkildkqkVVKLKQIEHTLN---EKRIL-------QAVEFPFLVRLEYSF 98
Cdd:cd06617    1 DDLEVIEELGRGAYGVVDKMRHVPTGT-----------IMAVKRIRATVNsqeQKRLLmdldismRSVDCPYTVTFYGAL 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  99 KDNSNLYMVMEYVPGG------EMFSHLRRIGrfsEPHARFYAAQIVLTFEYLHS-LDLIYRDLKPENLLIDHQGYIQVT 171
Cdd:cd06617   70 FREGDVWICMEVMDTSldkfykKVYDKGLTIP---EDILGKIAVSIVKALEYLHSkLSVIHRDVKPSNVLINRNGQVKLC 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 172 DFG--------FAKRVKGrtwtlcGTPEYLAPEII----LSKGYNKAVDWWALGVLIYEMAAGYPPFfaDQ---PIQIYE 236
Cdd:cd06617  147 DFGisgylvdsVAKTIDA------GCKPYMAPERInpelNQKGYDVKSDVWSLGITMIELATGRFPY--DSwktPFQQLK 218
                        250       260       270
                 ....*....|....*....|....*....|....
gi 255958318 237 KIVSGKV-RFPSH-FSSDLKDLLRNLLQVDLTKR 268
Cdd:cd06617  219 QVVEEPSpQLPAEkFSPEFQDFVNKCLKKNYKER 252
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
31-268 2.13e-21

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: 92.18  E-value: 2.13e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKI--LDKQKvvklKQIEHT-LNEKRILQAVEFPFLVRLEYSFKDNSNLYMV 107
Cdd:cd07860    2 FQKVEKIGEGTYGVVYKARNKLTGEVVALKKirLDTET----EGVPSTaIREISLLKELNHPNIVKLLDVIHTENKLYLV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 108 MEYVPGG-EMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKR--VKGRTW 184
Cdd:cd07860   78 FEFLHQDlKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAfgVPVRTY 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 185 TL-CGTPEYLAPEIIL-SKGYNKAVDWWALGVLIYEMAAGYPPFFADQPI-QIY----------EKIVSGKVRFPSHFSS 251
Cdd:cd07860  158 THeVVTLWYRAPEILLgCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIdQLFrifrtlgtpdEVVWPGVTSMPDYKPS 237
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 255958318 252 ------------------DLKDLLRNLLQVDLTKR 268
Cdd:cd07860  238 fpkwarqdfskvvppldeDGRDLLSQMLHYDPNKR 272
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
31-233 3.03e-21

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: 91.61  E-value: 3.03e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILD---------KQKVVKLKQIEHTLNekrilQAVEFPFLVRLEYSFKDN 101
Cdd:cd06636   18 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDvtedeeeeiKLEINMLKKYSHHRN-----IATYYGAFIKKSPPGHDD 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 102 sNLYMVMEYVPGGEMFSHLRRI--GRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFA--- 176
Cdd:cd06636   93 -QLWLVMEFCGAGSVTDLVKNTkgNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSaql 171
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255958318 177 KRVKGRTWTLCGTPEYLAPEIIL-----SKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQ 233
Cdd:cd06636  172 DRTVGRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMR 233
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
37-226 4.81e-21

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: 90.53  E-value: 4.81e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVM-------LVKHKATEQYyamkiLDKQKVVKLKQIehtLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVME 109
Cdd:cd14061    2 IGVGGFGKVYrgiwrgeEVAVKAARQD-----PDEDISVTLENV---RQEARLFWMLRHPNIIALRGVCLQPPNLCLVME 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 110 YVPGGEMFSHLrrIGRFSEPHARF-YAAQIVLTFEYLHS---LDLIYRDLKPENLLIDH--------QGYIQVTDFGFAK 177
Cdd:cd14061   74 YARGGALNRVL--AGRKIPPHVLVdWAIQIARGMNYLHNeapVPIIHRDLKSSNILILEaienedleNKTLKITDFGLAR 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 255958318 178 RVKGRT-WTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPF 226
Cdd:cd14061  152 EWHKTTrMSAAGTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPY 201
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
40-245 4.82e-21

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: 90.75  E-value: 4.82e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  40 GSFGRVMLVKHKATEQYYAMKIL-----DKQKVvklkqiehtLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGG 114
Cdd:cd14110   14 GRFSVVRQCEEKRSGQMLAAKIIpykpeDKQLV---------LREYQVLRRLSHPRIAQLHSAYLSPRHLVLIEELCSGP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 115 EMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRV-KGRTWTLCGTPEYL 193
Cdd:cd14110   85 ELLYNLAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLGNAQPFnQGKVLMTDKKGDYV 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 255958318 194 ---APEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRF 245
Cdd:cd14110  165 etmAPELLEGQGAGPQTDIWAIGVTAFIMLSADYPVSSDLNWERDRNIRKGKVQL 219
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
37-227 5.44e-21

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: 91.64  E-value: 5.44e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILD---KQKVVKLKQIehtLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPG 113
Cdd:cd06633   29 IGHGSFGAVYFATNSHTNEVVAIKKMSysgKQTNEKWQDI---IKEVKFLQQLKHPNTIEYKGCYLKDHTAWLVMEYCLG 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 114 GEmfSHLRRIGRfsEPHARFYAAQI----VLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTwTLCGT 189
Cdd:cd06633  106 SA--SDLLEVHK--KPLQEVEIAAIthgaLQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIASPAN-SFVGT 180
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 255958318 190 PEYLAPEIILSKG---YNKAVDWWALGVLIYEMAAGYPPFF 227
Cdd:cd06633  181 PYWMAPEVILAMDegqYDGKVDIWSLGITCIELAERKPPLF 221
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
18-226 6.20e-21

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: 92.02  E-value: 6.20e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  18 WENPppsnaglEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDK--QKVVKLKQiehTLNEKRILQAVEFPFLVRL- 94
Cdd:cd07877   13 WEVP-------ERYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSRpfQSIIHAKR---TYRELRLLKHMKHENVIGLl 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  95 -----EYSFKDNSNLYMVMEYVpgGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQ 169
Cdd:cd07877   83 dvftpARSLEEFNDVYLVTHLM--GADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELK 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 255958318 170 VTDFGFAKRVKGRTWTLCGTPEYLAPEIILS-KGYNKAVDWWALGVLIYEMAAGYPPF 226
Cdd:cd07877  161 ILDFGLARHTDDEMTGYVATRWYRAPEIMLNwMHYNQTVDIWSVGCIMAELLTGRTLF 218
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
29-241 9.95e-21

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: 90.88  E-value: 9.95e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQkvVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVM 108
Cdd:cd06650    5 DDFEKISELGAGNGGVVFKVSHKPSGLVMARKLIHLE--IKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 109 EYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSL-DLIYRDLKPENLLIDHQGYIQVTDFGFAKR-VKGRTWTL 186
Cdd:cd06650   83 EHMDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYLREKhKIMHRDVKPSNILVNSRGEIKLCDFGVSGQlIDSMANSF 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 255958318 187 CGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAG---YPPFFADQPIQIYEKIVSG 241
Cdd:cd06650  163 VGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGrypIPPPDAKELELMFGCQVEG 220
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
13-267 1.18e-20

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: 89.70  E-value: 1.18e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  13 DFLRKweNPPpsnaglEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKIldkqkvVKLKQ-IEHTLNEKRILQAVEFPFL 91
Cdd:cd06646    1 DILRR--NPQ------HDYELIQRVGSGTYGDVYKARNLHTGELAAVKI------IKLEPgDDFSLIQQEIFMVKECKHC 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  92 VRLEY--SFKDNSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQ 169
Cdd:cd06646   67 NIVAYfgSYLSREKLWICMEYCGGGSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVK 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 170 VTDFGFAKRVK---GRTWTLCGTPEYLAPEIILSK---GYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKV 243
Cdd:cd06646  147 LADFGVAAKITatiAKRKSFIGTPYWMAPEVAAVEkngGYNQLCDIWAVGITAIELAELQPPMFDLHPMRALFLMSKSNF 226
                        250       260       270
                 ....*....|....*....|....*....|
gi 255958318 244 RFPShfssdLKDLLR------NLLQVDLTK 267
Cdd:cd06646  227 QPPK-----LKDKTKwsstfhNFVKISLTK 251
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
37-254 1.82e-20

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 91.64  E-value: 1.82e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVM-LVKHKATEQYYAMKIL-DKQKVVKLKQIEHTLNEKRILqavefpFLVRLEY--SFKDNS-NLYM--VME 109
Cdd:PTZ00036  74 IGNGSFGVVYeAICIDTSEKVAIKKVLqDPQYKNRELLIMKNLNHINII------FLKDYYYteCFKKNEkNIFLnvVME 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 110 YVPGgEMFSHLRRIGRFSEPH----ARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGY-IQVTDFGFAKRVKG--R 182
Cdd:PTZ00036 148 FIPQ-TVHKYMKHYARNNHALplflVKLYSYQLCRALAYIHSKFICHRDLKPQNLLIDPNTHtLKLCDFGSAKNLLAgqR 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 183 TWTLCGTPEYLAPEIIL-SKGYNKAVDWWALGVLIYEMAAGYPPFFA----DQPIQIYE----------KIVS---GKVR 244
Cdd:PTZ00036 227 SVSYICSRFYRAPELMLgATNYTTHIDLWSLGCIIAEMILGYPIFSGqssvDQLVRIIQvlgtptedqlKEMNpnyADIK 306
                        250
                 ....*....|
gi 255958318 245 FPSHFSSDLK 254
Cdd:PTZ00036 307 FPDVKPKDLK 316
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
37-219 2.70e-20

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: 88.85  E-value: 2.70e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKQKvvklKQIEHT-LNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGGE 115
Cdd:cd14222    1 LGKGFFGQAIKVTHKATGKVMVMKELIRCD----EETQKTfLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 116 MFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRV--------------KG 181
Cdd:cd14222   77 LKDFLRADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveekkkpppdkpttKK 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 255958318 182 RT---------WTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEM 219
Cdd:cd14222  157 RTlrkndrkkrYTVVGNPYWMAPEMLNGKSYDEKVDIFSFGIVLCEI 203
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
29-268 3.71e-20

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: 89.67  E-value: 3.71e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKildkqkvvKLKQIEHTLNEKRILQavEFPFLVRLEY------------ 96
Cdd:cd07849    5 PRYQNLSYIGEGAYGMVCSAVHKPTGQKVAIK--------KISPFEHQTYCLRTLR--EIKILLRFKHeniigildiqrp 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  97 -SFKDNSNLYMVMEYvpggeMFSHLRRIGR---FSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTD 172
Cdd:cd07849   75 pTFESFKDVYIVQEL-----METDLYKLIKtqhLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICD 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 173 FGFAkRV-------KGRTWTLCGTPEYLAPEIIL-SKGYNKAVDWWALGVLIYEMAAGYPPF----FADQPIQI------ 234
Cdd:cd07849  150 FGLA-RIadpehdhTGFLTEYVATRWYRAPEIMLnSKGYTKAIDIWSVGCILAEMLSNRPLFpgkdYLHQLNLIlgilgt 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 255958318 235 -----YEKIVSGKVR-----------------FPSHFSSDLkDLLRNLLQVDLTKR 268
Cdd:cd07849  229 psqedLNCIISLKARnyikslpfkpkvpwnklFPNADPKAL-DLLDKMLTFNPHKR 283
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
31-267 3.78e-20

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: 89.34  E-value: 3.78e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEY 110
Cdd:cd06635   27 FSDLREIGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQRIKHPNSIEYKGCYLREHTAWLVMEY 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 111 VPGGEmfSHLRRIGRfsEPHARFYAAQI----VLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTwTL 186
Cdd:cd06635  107 CLGSA--SDLLEVHK--KPLQEIEIAAIthgaLQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIASPAN-SF 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 187 CGTPEYLAPEIILSKG---YNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVrfPSHFSSDLKDLLRNLLQV 263
Cdd:cd06635  182 VGTPYWMAPEVILAMDegqYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNES--PTLQSNEWSDYFRNFVDS 259

                 ....
gi 255958318 264 DLTK 267
Cdd:cd06635  260 CLQK 263
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
22-260 4.49e-20

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 89.55  E-value: 4.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  22 PPSNAGLE-----DFERKKTLGTGSFGRVMLVKHKATEQyyamkildkQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEY 96
Cdd:PHA03209  54 PTKQKAREvvaslGYTVIKTLTPGSEGRVFVATKPGQPD---------PVVLKIGQKGTTLIEAMLLQNVNHPSVIRMKD 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  97 SFKDNSNLYMVMEYVpGGEMFSHL-RRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGF 175
Cdd:PHA03209 125 TLVSGAITCMVLPHY-SSDLYTYLtKRSRPLPIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIFINDVDQVCIGDLGA 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 176 AK--RVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAgYP-PFFADQPIQIYEKIVSGKvrfpshfsSD 252
Cdd:PHA03209 204 AQfpVVAPAFLGLAGTVETNAPEVLARDKYNSKADIWSAGIVLFEMLA-YPsTIFEDPPSTPEEYVKSCH--------SH 274

                 ....*...
gi 255958318 253 LKDLLRNL 260
Cdd:PHA03209 275 LLKIISTL 282
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
37-219 4.66e-20

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: 88.09  E-value: 4.66e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKQKvvklKQIEHT-LNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGGE 115
Cdd:cd14221    1 LGKGCFGQAIKVTHRETGEVMVMKELIRFD----EETQRTfLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 116 mfshLRRIGRFSEPHARF-----YAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFA-------------- 176
Cdd:cd14221   77 ----LRGIIKSMDSHYPWsqrvsFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLArlmvdektqpeglr 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 255958318 177 ---KRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEM 219
Cdd:cd14221  153 slkKPDRKKRYTVVGNPYWMAPEMINGRSYDEKVDVFSFGIVLCEI 198
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
37-284 5.36e-20

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 3; 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). PIM3 can inhibit apoptosis and promote cell survival and protein translation, therefore, it can enhance the proliferation of normal and cancer cells. Mice deficient with PIM3 show minimal effects, suggesting that PIM3 msy not be essential. Since its expression is enhanced in several cancers, it may make a good molecular target for cancer drugs. The PIM3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 87.70  E-value: 5.36e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLN--EKRILQAVEFPF--LVRLEYSFKDNSNLYMVMEYV- 111
Cdd:cd14102    8 LGSGGFGTVYAGSRIADGLPVAVKHVVKERVTEWGTLNGVMVplEIVLLKKVGSGFrgVIKLLDWYERPDGFLIVMERPe 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 112 PGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLID-HQGYIQVTDFGFAKRVKGRTWT-LCGT 189
Cdd:cd14102   88 PVKDLFDFITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDlRTGELKLIDFGSGALLKDTVYTdFDGT 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 190 PEYLAPEIILSKGYN-KAVDWWALGVLIYEMAAGYPPFFADqpiqiyEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKR 268
Cdd:cd14102  168 RVYSPPEWIRYHRYHgRSATVWSLGVLLYDMVCGDIPFEQD------EEILRGRLYFRRRVSPECQQLIKWCLSLRPSDR 241
                        250
                 ....*....|....*.
gi 255958318 269 fgnlkNGVSDIKTHKW 284
Cdd:cd14102  242 -----PTLEQIFDHPW 252
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
31-233 7.12e-20

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: 88.24  E-value: 7.12e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILD---------KQKVVKLKQIEHTLNEKRILQAvefpFLVRLEYSFKDN 101
Cdd:cd06637    8 FELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDvtgdeeeeiKQEINMLKKYSHHRNIATYYGA----FIKKNPPGMDDQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 102 snLYMVMEYVPGGEMFSHLRRI--GRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFA--- 176
Cdd:cd06637   84 --LWLVMEFCGAGSVTDLIKNTkgNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSaql 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255958318 177 KRVKGRTWTLCGTPEYLAPEIIL-----SKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQ 233
Cdd:cd06637  162 DRTVGRRNTFIGTPYWMAPEVIAcdenpDATYDFKSDLWSLGITAIEMAEGAPPLCDMHPMR 223
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
37-219 9.91e-20

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: 87.64  E-value: 9.91e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHK----ATEQYYAMKILDKQKVVKLKQIEHtlnEKRILQAVEFPFLVRLE---YSfKDNSNLYMVME 109
Cdd:cd05081   12 LGKGNFGSVELCRYDplgdNTGALVAVKQLQHSGPDQQRDFQR---EIQILKALHSDFIVKYRgvsYG-PGRRSLRLVME 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 110 YVPGGEMFSHLRR-IGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAK----------- 177
Cdd:cd05081   88 YLPSGCLRDFLQRhRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKllpldkdyyvv 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 255958318 178 RVKGRTWTLCGTPEYLAPEIilskgYNKAVDWWALGVLIYEM 219
Cdd:cd05081  168 REPGQSPIFWYAPESLSDNI-----FSRQSDVWSFGVVLYEL 204
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
28-226 1.06e-19

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: 87.76  E-value: 1.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  28 LEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILdkqkvvklkQIEH-------TLNEKRILQAVEFPFLVRLEYSFKD 100
Cdd:cd07871    4 LETYVKLDKLGEGTYATVFKGRSKLTENLVALKEI---------RLEHeegapctAIREVSLLKNLKHANIVTLHDIIHT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 101 NSNLYMVMEYVPGgEMFSHLRRIGRFSEPH-ARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGF--AK 177
Cdd:cd07871   75 ERCLTLVFEYLDS-DLKQYLDNCGNLMSMHnVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLarAK 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 255958318 178 RVKGRTWT-LCGTPEYLAPEIIL-SKGYNKAVDWWALGVLIYEMAAGYPPF 226
Cdd:cd07871  154 SVPTKTYSnEVVTLWYRPPDVLLgSTEYSTPIDMWGVGCILYEMATGRPMF 204
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
18-234 1.15e-19

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: 88.42  E-value: 1.15e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  18 WENPppsnaglEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDK------------QKVVKLKQIEHTlNEKRILQa 85
Cdd:cd07879   11 WELP-------ERYTSLKQVGSGAYGSVCSAIDKRTGEKVAIKKLSRpfqseifakrayRELTLLKHMQHE-NVIGLLD- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  86 VEFPflvrlEYSFKDNSNLYMVMEYvpggeMFSHLRRI--GRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLID 163
Cdd:cd07879   82 VFTS-----AVSGDEFQDFYLVMPY-----MQTDLQKImgHPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVN 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255958318 164 HQGYIQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILS-KGYNKAVDWWALGVLIYEMAAGYPPF----FADQPIQI 234
Cdd:cd07879  152 EDCELKILDFGLARHADAEMTGYVVTRWYRAPEVILNwMHYNQTVDIWSVGCIMAEMLTGKTLFkgkdYLDQLTQI 227
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
30-239 1.45e-19

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: 87.42  E-value: 1.45e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  30 DFERKKTLGTGSFGRVmlvkhkateqyYAMKILDKQKVVKLKQIE----------HTLNEKRILQAVEFPFLVRLEYSFK 99
Cdd:cd07845    8 EFEKLNRIGEGTYGIV-----------YRARDTTSGEIVALKKVRmdnerdgipiSSLREITLLLNLRHPNIVELKEVVV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 100 DNS--NLYMVMEYVPGgEMFSHLRRIGR-FSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFA 176
Cdd:cd07845   77 GKHldSIFLVMEYCEQ-DLASLLDNMPTpFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGLA 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255958318 177 KR----VKGRTWTLCgTPEYLAPEIIL-SKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIV 239
Cdd:cd07845  156 RTyglpAKPMTPKVV-TLWYRAPELLLgCTTYTTAIDMWAVGCILAELLAHKPLLPGKSEIEQLDLII 222
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
37-285 1.64e-19

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: 86.60  E-value: 1.64e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTlNEKRILQAVEFPFLVRLEYSFKDNSN----LYMVMEYVP 112
Cdd:cd14033    9 IGRGSFKTVYRGLDTETTVEVAWCELQTRKLSKGERQRFS-EEVEMLKGLQHPNIVRFYDSWKSTVRghkcIILVTELMT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 113 GGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSL--DLIYRDLKPENLLIDH-QGYIQVTDFGFAKRVKGR-TWTLCG 188
Cdd:cd14033   88 SGTLKTYLKRFREMKLKLLQRWSRQILKGLHFLHSRcpPILHRDLKCDNIFITGpTGSVKIGDLGLATLKRASfAKSVIG 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 189 TPEYLAPEIILSKgYNKAVDWWALGVLIYEMAAG-YPPFFADQPIQIYEKIVSG-------KVRFPshfssDLKDLLRNL 260
Cdd:cd14033  168 TPEFMAPEMYEEK-YDEAVDVYAFGMCILEMATSeYPYSECQNAAQIYRKVTSGikpdsfyKVKVP-----ELKEIIEGC 241
                        250       260
                 ....*....|....*....|....*
gi 255958318 261 LQVDLTKRFgnlknGVSDIKTHKWF 285
Cdd:cd14033  242 IRTDKDERF-----TIQDLLEHRFF 261
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
37-284 2.14e-19

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 1; 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 isoforms resulting from alternative translation initiation sites. PIM1 is the founding member of the PIM subfamily. It is involved in regulating cell growth, differentiation, and apoptosis. It promotes cancer development when overexpressed by inhibiting apoptosis, promoting cell proliferation, and promoting genomic instability. The PIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 86.18  E-value: 2.14e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLN---EKRILQAVEFPF--LVRLEYSFKDNSNLYMVMEYV 111
Cdd:cd14100    8 LGSGGFGSVYSGIRVADGAPVAIKHVEKDRVSEWGELPNGTRvpmEIVLLKKVGSGFrgVIRLLDWFERPDSFVLVLERP 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 112 -PGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLID-HQGYIQVTDFGFAKRVKGRTWT-LCG 188
Cdd:cd14100   88 ePVQDLFDFITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDlNTGELKLIDFGSGALLKDTVYTdFDG 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 189 TPEYLAPEIILSKGYN-KAVDWWALGVLIYEMAAGYPPFFADqpiqiyEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTK 267
Cdd:cd14100  168 TRVYSPPEWIRFHRYHgRSAAVWSLGILLYDMVCGDIPFEHD------EEIIRGQVFFRQRVSSECQHLIKWCLALRPSD 241
                        250
                 ....*....|....*..
gi 255958318 268 RfgnlkNGVSDIKTHKW 284
Cdd:cd14100  242 R-----PSFEDIQNHPW 253
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
37-226 3.14e-19

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: 85.86  E-value: 3.14e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKlKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGGEM 116
Cdd:cd14146    2 IGVGGFGKVYRATWKGQEVAVKAARQDPDEDIK-ATAESVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEFARGGTL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 117 FSHL--------RRIGRFSEPHARF-YAAQIVLTFEYLHS---LDLIYRDLKPENLL----IDH----QGYIQVTDFGFA 176
Cdd:cd14146   81 NRALaaanaapgPRRARRIPPHILVnWAVQIARGMLYLHEeavVPILHRDLKSSNILllekIEHddicNKTLKITDFGLA 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 255958318 177 KRVKGRT-WTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPF 226
Cdd:cd14146  161 REWHRTTkMSAAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPY 211
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
28-226 3.30e-19

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK3 is a mitogen-activated protein kinase kinase kinases (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK3 activates multiple MAPK pathways and plays a role in apoptosis, proliferation, migration, and differentiation, depending on the cellular context. It is highly expressed in breast cancer cells and its signaling through c-Jun N-terminal kinase has been implicated in the migration, invasion, and malignancy of cancer cells. MLK3 also functions as a negative regulator of Inhibitor of Nuclear Factor-KappaB Kinase (IKK) and consequently, it also impacts inflammation and immunity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271049 [Multi-domain]  Cd Length: 267  Bit Score: 85.85  E-value: 3.30e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  28 LEDFERKKTLGTGSFGRVM-------LVKHKATEQyyamkilDKQKVVKLKQiEHTLNEKRILQAVEFPFLVRLEYSFKD 100
Cdd:cd14147    2 FQELRLEEVIGIGGFGKVYrgswrgeLVAVKAARQ-------DPDEDISVTA-ESVRQEARLFAMLAHPNIIALKAVCLE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 101 NSNLYMVMEYVPGGEMFSHLrrIGRFSEPHARF-YAAQIVLTFEYLHS---LDLIYRDLKPENLLIDHQGY--------I 168
Cdd:cd14147   74 EPNLCLVMEYAAGGPLSRAL--AGRRVPPHVLVnWAVQIARGMHYLHCealVPVIHRDLKSNNILLLQPIEnddmehktL 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 255958318 169 QVTDFGFAKRVKGRT-WTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPF 226
Cdd:cd14147  152 KITDFGLAREWHKTTqMSAAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPY 210
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
26-268 3.60e-19

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: 86.27  E-value: 3.60e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  26 AGLEDFERKKTLGTGSFGRVmlvkhkateqyYAMKILDKQKVVKLKQIEHTLNE---KRILQAVEF-------PFLVRLE 95
Cdd:cd06618   12 ADLNDLENLGEIGSGTCGQV-----------YKMRHKKTGHVMAVKQMRRSGNKeenKRILMDLDVvlkshdcPYIVKCY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  96 YSFKDNSNLYMVMEYVpgGEMFSHL-RRI-GRFSEPHARFYAAQIVLTFEYL---HSLdlIYRDLKPENLLIDHQGYIQV 170
Cdd:cd06618   81 GYFITDSDVFICMELM--STCLDKLlKRIqGPIPEDILGKMTVSIVKALHYLkekHGV--IHRDVKPSNILLDESGNVKL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 171 TDFGFAKRV---KGRTWTlCGTPEYLAPEIILSKG---YNKAVDWWALGVLIYEMAAG-YPPFFADQPIQIYEKIVSGKV 243
Cdd:cd06618  157 CDFGISGRLvdsKAKTRS-AGCAAYMAPERIDPPDnpkYDIRADVWSLGISLVELATGqFPYRNCKTEFEVLTKILNEEP 235
                        250       260
                 ....*....|....*....|....*...
gi 255958318 244 RFPSH---FSSDLKDLLRNLLQVDLTKR 268
Cdd:cd06618  236 PSLPPnegFSPDFCSFVDLCLTKDHRYR 263
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
37-219 7.72e-19

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: 84.87  E-value: 7.72e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILdkqkvvkLKQIEHT----LNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVP 112
Cdd:cd14154    1 LGKGFFGQAIKVTHRETGEVMVMKEL-------IRFDEEAqrnfLKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIP 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 113 GGEMFSHLRRIGR-FSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFA--------------- 176
Cdd:cd14154   74 GGTLKDVLKDMARpLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLArliveerlpsgnmsp 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 255958318 177 --------KRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEM 219
Cdd:cd14154  154 setlrhlkSPDRKKRYTVVGNPYWMAPEMLNGRSYDEKVDIFSFGIVLCEI 204
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
38-268 1.07e-18

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: 83.85  E-value: 1.07e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  38 GTGSFGRVMLVKHKATEQYYAMKildkqkvvKLKQIEhtlNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGGEMF 117
Cdd:cd14060    2 GGGSFGSVYRAIWVSQDKEVAVK--------KLLKIE---KEAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGSLF 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 118 SHL--RRIGRFSEPHARFYAAQIVLTFEYLHS---LDLIYRDLKPENLLIDHQGYIQVTDFGfAKRVKGRT--WTLCGTP 190
Cdd:cd14060   71 DYLnsNESEEMDMDQIMTWATDIAKGMHYLHMeapVKVIHRDLKSRNVVIAADGVLKICDFG-ASRFHSHTthMSLVGTF 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 191 EYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVR--FPSHFSSDLKDLLRNLLQVDLTKR 268
Cdd:cd14060  150 PWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPFKGLEGLQVAWLVVEKNERptIPSSCPRSFAELMRRCWEADVKER 229
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
37-226 1.24e-18

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: 83.88  E-value: 1.24e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQiEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGGEM 116
Cdd:cd14148    2 IGVGGFGKVYKGLWRGEEVAVKAARQDPDEDIAVTA-ENVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVMEYARGGAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 117 FSHLrrIGRFSEPHARF-YAAQIVLTFEYLHS---LDLIYRDLKPENLLI-------DHQG-YIQVTDFGFAKRVKGRT- 183
Cdd:cd14148   81 NRAL--AGKKVPPHVLVnWAVQIARGMNYLHNeaiVPIIHRDLKSSNILIlepiendDLSGkTLKITDFGLAREWHKTTk 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 255958318 184 WTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPF 226
Cdd:cd14148  159 MSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPY 201
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
35-268 1.39e-18

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: 84.26  E-value: 1.39e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYYAMK---ILDKQKVVKLKQiEHTL-----NEKRILQAVEFPFLvrleYSFKDNSNLYM 106
Cdd:cd14037    9 KYLAEGGFAHVYLVKTSNGGNRAALKrvyVNDEHDLNVCKR-EIEImkrlsGHKNIVGYIDSSAN----RSGNGVYEVLL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 107 VMEYVPGGE----MFSHLRRigRFSEPHARFYAAQIVLTFEYLHSLD--LIYRDLKPENLLIDHQGYIQVTDFGFAKRVK 180
Cdd:cd14037   84 LMEYCKGGGvidlMNQRLQT--GLTESEILKIFCDVCEAVAAMHYLKppLIHRDLKVENVLISDSGNYKLCDFGSATTKI 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 181 GRTWTLCG------------TPEYLAPEII---LSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIqiyeKIVSGKVRF 245
Cdd:cd14037  162 LPPQTKQGvtyveedikkytTLQYRAPEMIdlyRGKPITEKSDIWALGCLLYKLCFYTTPFEESGQL----AILNGNFTF 237
                        250       260
                 ....*....|....*....|....*
gi 255958318 246 P--SHFSSDLKDLLRNLLQVDLTKR 268
Cdd:cd14037  238 PdnSRYSKRLHKLIRYMLEEDPEKR 262
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
37-226 1.40e-18

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: 83.31  E-value: 1.40e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEqyYAMKILDKQKVVKLKQiehtlnekriLQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGGEM 116
Cdd:cd14059    1 LGSGAQGAVFLGKFRGEE--VAVKKVRDEKETDIKH----------LRKLNHPNIIKFKGVCTQAPCYCILMEYCPYGQL 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 117 FSHLRRiGRFSEPHARF-YAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAK--RVKGRTWTLCGTPEYL 193
Cdd:cd14059   69 YEVLRA-GREITPSLLVdWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKelSEKSTKMSFAGTVAWM 147
                        170       180       190
                 ....*....|....*....|....*....|...
gi 255958318 194 APEIILSKGYNKAVDWWALGVLIYEMAAGYPPF 226
Cdd:cd14059  148 APEVIRNEPCSEKVDIWSFGVVLWELLTGEIPY 180
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
31-226 1.58e-18

Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and -Regulated Kinases 2 and 3; 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 DYRK2 and DYRK3, and similar proteins. Drosophila DYRK2 interacts and phosphorylates the chromatin remodelling factor, SNR1 (Snf5-related 1), and also interacts with the essential chromatin component, trithorax. It may play a role in chromatin remodelling. Vertebrate DYRK2 phosphorylates and regulates the tumor suppressor p53 to induce apoptosis in response to DNA damage. It can also phosphorylate the transcription factor, nuclear factor of activated T cells (NFAT). DYRK2 is overexpressed in lung adenocarcinoma and esophageal carcinomas, and is a predictor for favorable prognosis in lung adenocarcinoma. DYRK3, also called regulatory erythroid kinase (REDK), is highly expressed in erythroid cells and the testis, and is also present in adult kidney and liver. It promotes cell survival by phosphorylating and activating SIRT1, an NAD(+)-dependent protein deacetylase, which promotes p53 deacetylation, resulting in the inhibition of apoptosis. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other S/T kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 85.57  E-value: 1.58e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEhtlnEKRILQAvefpflvrLEYSFKDNS-NLYMVME 109
Cdd:cd14224   67 YEVLKVIGKGSFGQVVKAYDHKTHQHVALKMVRNEKRFHRQAAE----EIRILEH--------LKKQDKDNTmNVIHMLE 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 110 YVP-------GGEMFS-------HLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGY--IQVTDF 173
Cdd:cd14224  135 SFTfrnhicmTFELLSmnlyeliKKNKFQGFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGRsgIKVIDF 214
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 255958318 174 GFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPF 226
Cdd:cd14224  215 GSSCYEHQRIYTYIQSRFYRAPEVILGARYGMPIDMWSFGCILAELLTGYPLF 267
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
29-224 1.64e-18

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: 84.72  E-value: 1.64e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQkvVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVM 108
Cdd:cd06649    5 DDFERISELGAGNGGVVTKVQHKPSGLIMARKLIHLE--IKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 109 EYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSL-DLIYRDLKPENLLIDHQGYIQVTDFGFAKR-VKGRTWTL 186
Cdd:cd06649   83 EHMDGGSLDQVLKEAKRIPEEILGKVSIAVLRGLAYLREKhQIMHRDVKPSNILVNSRGEIKLCDFGVSGQlIDSMANSF 162
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 255958318 187 CGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAG-YP 224
Cdd:cd06649  163 VGTRSYMSPERLQGTHYSVQSDIWSMGLSLVELAIGrYP 201
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
37-224 1.68e-18

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: 83.31  E-value: 1.68e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKIL---DKQKvvklkqieHTLNEKRILQAVEFPFLVR-LEYSFKDNsNLYMVMEYVP 112
Cdd:cd14065    1 LGKGFFGEVYKVTHRETGKVMVMKELkrfDEQR--------SFLKEVKLMRRLSHPNILRfIGVCVKDN-KLNFITEYVN 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 113 GGEMFSHLRRIG-RFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLI---DHQGYIQVTDFGFAKRV--------- 179
Cdd:cd14065   72 GGTLEELLKSMDeQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVreaNRGRNAVVADFGLAREMpdektkkpd 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 255958318 180 KGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYP 224
Cdd:cd14065  152 RKKRLTVVGSPYWMAPEMLRGESYDEKVDVFSFGIVLCEIIGRVP 196
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
31-285 2.01e-18

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Pho85 is a multifunctional CDK in yeast. It is regulated by 10 different cyclins (Pcls) and plays a role in G1 progression, cell polarity, phosphate and glycogen metabolism, gene expression, and in signaling changes in the environment. It is not essential for yeast viability and is the functional homolog of mammalian CDK5, which plays a role in central nervous system development. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The Pho85 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143341 [Multi-domain]  Cd Length: 284  Bit Score: 83.68  E-value: 2.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKildkqkVVKLKQIEHT----LNEKRILQAVEFPFLVRLEYSFKDNSNLYM 106
Cdd:cd07836    2 FKQLEKLGEGTYATVYKGRNRTTGEIVALK------EIHLDAEEGTpstaIREISLMKELKHENIVRLHDVIHTENKLML 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 107 VMEYVPGG---EMFSHLRRiGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRT 183
Cdd:cd07836   76 VFEYMDKDlkkYMDTHGVR-GALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLARAFGIPV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 184 WTLCG---TPEYLAPEIIL-SKGYNKAVDWWALGVLIYEMAAGYPPFF----ADQPIQIY-------EKIVSGKVRFPS- 247
Cdd:cd07836  155 NTFSNevvTLWYRAPDVLLgSRTYSTSIDIWSVGCIMAEMITGRPLFPgtnnEDQLLKIFrimgtptESTWPGISQLPEy 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 255958318 248 -----------------HFSSDLKDLLRNLLQVDLTKRFgnlknGVSDIKTHKWF 285
Cdd:cd07836  235 kptfpryppqdlqqlfpHADPLGIDLLHRLLQLNPELRI-----SAHDALQHPWF 284
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
29-269 2.15e-18

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


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 83.04  E-value: 2.15e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVmlvkHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVR-------LEYSFKDN 101
Cdd:cd14019    1 NKYRIIEKIGEGTFSSV----YKAEDKLHDLYDRNKGRLVALKHIYPTSSPSRILNELECLERLGgsnnvsgLITAFRNE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 102 SNLYMVMEYVPGGEmFSHLrrIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLID-HQGYIQVTDFGFAKRV- 179
Cdd:cd14019   77 DQVVAVLPYIEHDD-FRDF--YRKMSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNrETGKGVLVDFGLAQREe 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 180 --KGRTWTLCGTPEYLAPEIILSkgYNK---AVDWWALGV-LIYEMAAGYPPFFADQPIQIYEKIVS--GkvrfpshfSS 251
Cdd:cd14019  154 drPEQRAPRAGTRGFRAPEVLFK--CPHqttAIDIWSAGViLLSILSGRFPFFFSSDDIDALAEIATifG--------SD 223
                        250
                 ....*....|....*...
gi 255958318 252 DLKDLLRNLLQVDLTKRF 269
Cdd:cd14019  224 EAYDLLDKLLELDPSKRI 241
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
114-285 2.77e-18

Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Tribbles Homolog (TRB) proteins interact with many proteins involved in signaling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, differentiation, and gene expression. TRB proteins bind to the middle kinase in mitogen activated protein kinase (MAPK) signaling cascades, MAPK kinases. They regulate the activity of MAPK kinases, and thus, affect MAPK signaling. In Drosophila, Tribbles regulates String, the ortholog of mammalian Cdc25, during morphogenesis. String is implicated in the progression of mitosis during embryonic development. Vertebrates contain three TRB proteins encoded by three separate genes: Tribbles-1 (TRB1 or TRIB1), Tribbles-2 (TRB2 or TRIB2), and Tribbles-3 (TRB3 or TRIB3). The TRB 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: 270878 [Multi-domain]  Cd Length: 242  Bit Score: 82.48  E-value: 2.77e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 114 GEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLL-IDHQ-GYIQVTDFGFAKRVKGRTWTLC---G 188
Cdd:cd13976   69 GDLHSYVRSRKRLREPEAARLFRQIASAVAHCHRNGIVLRDLKLRKFVfADEErTKLRLESLEDAVILEGEDDSLSdkhG 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 189 TPEYLAPEIILSKG-YN-KAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLT 266
Cdd:cd13976  149 CPAYVSPEILNSGAtYSgKAADVWSLGVILYTMLVGRYPFHDSEPASLFAKIRRGQFAIPETLSPRARCLIRSLLRREPS 228
                        170
                 ....*....|....*....
gi 255958318 267 KRFgnlknGVSDIKTHKWF 285
Cdd:cd13976  229 ERL-----TAEDILLHPWL 242
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
28-226 3.86e-18

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: 83.13  E-value: 3.86e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  28 LEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILdkqkvvklkQIEH-------TLNEKRILQAVEFPFLVRLEYSFKD 100
Cdd:cd07873    1 LETYIKLDKLGEGTYATVYKGRSKLTDNLVALKEI---------RLEHeegapctAIREVSLLKDLKHANIVTLHDIIHT 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 101 NSNLYMVMEYVpGGEMFSHLRRIGRFSEPH-ARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGF--AK 177
Cdd:cd07873   72 EKSLTLVFEYL-DKDLKQYLDDCGNSINMHnVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLarAK 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 255958318 178 RVKGRTWT-LCGTPEYLAPEIIL-SKGYNKAVDWWALGVLIYEMAAGYPPF 226
Cdd:cd07873  151 SIPTKTYSnEVVTLWYRPPDILLgSTDYSTQIDMWGVGCIFYEMSTGRPLF 201
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
37-226 4.33e-18

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: 82.48  E-value: 4.33e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVmlvkHKAT--EQYYAMKILDKQKVVKLKQIEhtlneKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGG 114
Cdd:cd14058    1 VGRGSFGVV----CKARwrNQIVAVKIIESESEKKAFEVE-----VRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGG 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 115 EMFSHLRriGRFSEP-----HARFYAAQIVLTFEYLHSLD---LIYRDLKPENLLIDHQG-YIQVTDFGFAKRVKGRTWT 185
Cdd:cd14058   72 SLYNVLH--GKEPKPiytaaHAMSWALQCAKGVAYLHSMKpkaLIHRDLKPPNLLLTNGGtVLKICDFGTACDISTHMTN 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 255958318 186 LCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPF 226
Cdd:cd14058  150 NKGSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPF 190
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
28-268 4.47e-18

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


Pssm-ID: 270950 [Multi-domain]  Cd Length: 281  Bit Score: 83.00  E-value: 4.47e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  28 LEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKqiEHTLNEKRILQAVEFPFLVRLEYSF--------- 98
Cdd:cd14048    5 LTDFEPIQCLGRGGFGVVFEAKNKVDDCNYAVKRIRLPNNELAR--EKVLREVRALAKLDHPGIVRYFNAWlerppegwq 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  99 --KDNSNLYMVMEYVPGGEMFSHLRRiGRFSEPHARFYA----AQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTD 172
Cdd:cd14048   83 ekMDEVYLYIQMQLCRKENLKDWMNR-RCTMESRELFVClnifKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKVGD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 173 FGFAKRVK---------------GRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAagYPpfFADQPIQIYEK 237
Cdd:cd14048  162 FGLVTAMDqgepeqtvltpmpayAKHTGQVGTRLYMSPEQIHGNQYSEKVDIFALGLILFELI--YS--FSTQMERIRTL 237
                        250       260       270
                 ....*....|....*....|....*....|....
gi 255958318 238 IVSGKVRFPSHFSSDL---KDLLRNLLQVDLTKR 268
Cdd:cd14048  238 TDVRKLKFPALFTNKYpeeRDMVQQMLSPSPSER 271
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
34-246 6.56e-18

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: 82.40  E-value: 6.56e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  34 KKTLGTGSFGRVmlvkHKA--TEQYYAMKILDKQKVVKLKQ-IEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEY 110
Cdd:cd14145   11 EEIIGIGGFGKV----YRAiwIGDEVAVKAARHDPDEDISQtIENVRQEAKLFAMLKHPNIIALRGVCLKEPNLCLVMEF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 111 VPGGEMFSHLRriGRFSEPHARF-YAAQIVLTFEYLHS---LDLIYRDLKPENLLIDHQ--------GYIQVTDFGFAKR 178
Cdd:cd14145   87 ARGGPLNRVLS--GKRIPPDILVnWAVQIARGMNYLHCeaiVPVIHRDLKSSNILILEKvengdlsnKILKITDFGLARE 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255958318 179 VKGRT-WTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFP 246
Cdd:cd14145  165 WHRTTkMSAAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPFRGIDGLAVAYGVAMNKLSLP 233
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
31-226 7.17e-18

Catalytic domain of the Dual-specificity protein kinases, CDC-like 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. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on S/T residues. In Drosophila, the CLK homolog DOA (Darkener of apricot) is essential for embryogenesis and its mutation leads to defects in sexual differentiation, eye formation, and neuronal development. In fission yeast, the CLK homolog Lkh1 is a negative regulator of filamentous growth and asexual flocculation, and is also involved in oxidative stress response. Vertebrates contain mutliple CLK proteins and mammals have four (CLK1-4). The CLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 83.00  E-value: 7.17e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKvvklKQIEHTLNEKRILQ------AVEFPFLVRLEYSFKDNSNL 104
Cdd:cd14134   14 YKILRLLGEGTFGKVLECWDRKRKRYVAVKIIRNVE----KYREAAKIEIDVLEtlaekdPNGKSHCVQLRDWFDYRGHM 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 105 YMVMEyVPGGEMFSHLR--RIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDF---GFAKRV 179
Cdd:cd14134   90 CIVFE-LLGPSLYDFLKknNYGPFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLVDSDYVKVYNPkkkRQIRVP 168
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255958318 180 KGRTWTLC----------------GTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPF 226
Cdd:cd14134  169 KSTDIKLIdfgsatfddeyhssivSTRHYRAPEVILGLGWSYPCDVWSIGCILVELYTGELLF 231
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
35-285 7.49e-18

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 82.89  E-value: 7.49e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYYAMKildKQKVVKLKQIEH--------------TLNEKRILQAVEFPFLVRLEYSFKD 100
Cdd:PTZ00024  15 AHLGEGTYGKVEKAYDTLTGKIVAIK---KVKIIEISNDVTkdrqlvgmcgihftTLRELKIMNEIKHENIMGLVDVYVE 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 101 NSNLYMVMEYvpggeMFSHLRRI----GRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFA 176
Cdd:PTZ00024  92 GDFINLVMDI-----MASDLKKVvdrkIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGLA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 177 KR------------VKGRTWTLCGTPE-----YLAPEIIL-SKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKI 238
Cdd:PTZ00024 167 RRygyppysdtlskDETMQRREEMTSKvvtlwYRAPELLMgAEKYHFAVDMWSVGCIFAELLTGKPLFPGENEIDQLGRI 246
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255958318 239 V-------------------------SGKVRFPSHF---SSDLKDLLRNLLQVDLTKRFgnlknGVSDIKTHKWF 285
Cdd:PTZ00024 247 FellgtpnednwpqakklplyteftpRKPKDLKTIFpnaSDDAIDLLQSLLKLNPLERI-----SAKEALKHEYF 316
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
28-238 7.59e-18

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 82.56  E-value: 7.59e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  28 LEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKildkqkVVKLKQIEH-----TLNEKRILQAVEFPFLVRLEYSFKDNS 102
Cdd:PLN00009   1 MDQYEKVEKIGEGTYGVVYKARDRVTNETIALK------KIRLEQEDEgvpstAIREISLLKEMQHGNIVRLQDVVHSEK 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 103 NLYMVMEYVpGGEMFSHLRRIGRFSEPH--ARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQ-GYIQVTDFGFAKR- 178
Cdd:PLN00009  75 RLYLVFEYL-DLDLKKHMDSSPDFAKNPrlIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRtNALKLADFGLARAf 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255958318 179 -VKGRTWTL-CGTPEYLAPEIIL-SKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKI 238
Cdd:PLN00009 154 gIPVRTFTHeVVTLWYRAPEILLgSRHYSTPVDIWSVGCIFAEMVNQKPLFPGDSEIDELFKI 216
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
29-226 8.96e-18

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: 82.27  E-value: 8.96e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMK--ILDKQK----VVKLKQIEhtlnekrILQAVEFPFLVRL-EYSFKDN 101
Cdd:cd07843    5 DEYEKLNRIEEGTYGVVYRARDKKTGEIVALKklKMEKEKegfpITSLREIN-------ILLKLQHPNIVTVkEVVVGSN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 102 SN-LYMVMEYVPGgEMFSHLRRI-GRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRV 179
Cdd:cd07843   78 LDkIYMVMEYVEH-DLKSLMETMkQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGLAREY 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 255958318 180 KG--RTWT-LCGTPEYLAPEIILS-KGYNKAVDWWALGVLIYEMAAGYPPF 226
Cdd:cd07843  157 GSplKPYTqLVVTLWYRAPELLLGaKEYSTAIDMWSVGCIFAELLTKKPLF 207
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
28-279 9.96e-18

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: 81.57  E-value: 9.96e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  28 LEDFERKKTLGTGSFGRVMLVKHKATEqyyamkildkqkvVKLKQIEHT------LNEKRILQAVEFPFLVRL-EYSFKD 100
Cdd:cd05082    5 MKELKLLQTIGKGEFGDVMLGDYRGNK-------------VAVKCIKNDataqafLAEASVMTQLRHSNLVQLlGVIVEE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 101 NSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARF--YAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKR 178
Cdd:cd05082   72 KGGLYIVTEYMAKGSLVDYLRSRGRSVLGGDCLlkFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTKE 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 179 VKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAA-GYPPFFADQPIQIYEKIVSG-KVRFPSHFSSDLKDL 256
Cdd:cd05082  152 ASSTQDTGKLPVKWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPYPRIPLKDVVPRVEKGyKMDAPDGCPPAVYDV 231
                        250       260
                 ....*....|....*....|....*
gi 255958318 257 LRNLLQVDLTKR--FGNLKNGVSDI 279
Cdd:cd05082  232 MKNCWHLDAAMRpsFLQLREQLEHI 256
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
18-226 1.27e-17

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: 82.31  E-value: 1.27e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  18 WENPppsnaglEDFERKKTLGTGSFGRVMLVKHKATEQYYAMK---------ILDKQKVVKLKQIEHTLNEKRI-LQAVE 87
Cdd:cd07880   11 WEVP-------DRYRDLKQVGSGAYGTVCSALDRRTGAKVAIKklyrpfqseLFAKRAYRELRLLKHMKHENVIgLLDVF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  88 FPflvrlEYSFKDNSNLYMVMEYVpgGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGY 167
Cdd:cd07880   84 TP-----DLSLDRFHDFYLVMPFM--GTDLGKLMKHEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCE 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 168 IQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILS-KGYNKAVDWWALGVLIYEMAAGYPPF 226
Cdd:cd07880  157 LKILDFGLARQTDSEMTGYVVTRWYRAPEVILNwMHYTQTVDIWSVGCIMAEMLTGKPLF 216
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
37-286 1.34e-17

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: 81.31  E-value: 1.34e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQiEHTLNEKRILQAVEFPFLVRL----EYSFKDNSNLYMVMEYVP 112
Cdd:cd14031   18 LGRGAFKTVYKGLDTETWVEVAWCELQDRKLTKAEQ-QRFKEEAEMLKGLQHPNIVRFydswESVLKGKKCIVLVTELMT 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 113 GGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLD--LIYRDLKPENLLIDH-QGYIQVTDFGFAKRVKGR-TWTLCG 188
Cdd:cd14031   97 SGTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGpTGSVKIGDLGLATLMRTSfAKSVIG 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 189 TPEYLAPEIiLSKGYNKAVDWWALGVLIYEMAAG-YPPFFADQPIQIYEKIVSG--KVRFPSHFSSDLKDLLRNLLQVDL 265
Cdd:cd14031  177 TPEFMAPEM-YEEHYDESVDVYAFGMCMLEMATSeYPYSECQNAAQIYRKVTSGikPASFNKVTDPEVKEIIEGCIRQNK 255
                        250       260
                 ....*....|....*....|.
gi 255958318 266 TKRFgnlknGVSDIKTHKWFA 286
Cdd:cd14031  256 SERL-----SIKDLLNHAFFA 271
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
31-268 1.48e-17

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


Pssm-ID: 270952 [Multi-domain]  Cd Length: 249  Bit Score: 80.82  E-value: 1.48e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKIlDKQKVVKLKQIEHTLNE-KRILQAVEFPFLVRLEYSFKDNSNLYMVME 109
Cdd:cd14050    3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKR-SRSRFRGEKDRKRKLEEvERHEKLGEHPNCVRFIKAWEEKGILYIQTE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 110 YVpGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRV--KGRTWTLC 187
Cdd:cd14050   82 LC-DTSLQQYCEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLVVELdkEDIHDAQE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 188 GTPEYLAPEiILSKGYNKAVDWWALGVLIYEMAAGYP-PFFAD--QPI---QIYEKIVSGkvrfpshFSSDLKDLLRNLL 261
Cdd:cd14050  161 GDPRYMAPE-LLQGSFTKAADIFSLGITILELACNLElPSGGDgwHQLrqgYLPEEFTAG-------LSPELRSIIKLMM 232

                 ....*..
gi 255958318 262 QVDLTKR 268
Cdd:cd14050  233 DPDPERR 239
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
28-219 1.49e-17

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: 80.86  E-value: 1.49e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  28 LEDFERKKTLGTGSFGRVMLVKHKatEQYYAMKILDKQkvvkLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMV 107
Cdd:cd05039    5 KKDLKLGELIGKGEFGDVMLGDYR--GQKVAVKCLKDD----STAAQAFLAEASVMTTLRHPNLVQLLGVVLEGNGLYIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 108 MEYVPGGEMFSHLRRIGRfsepHARFYAAQIVLTF------EYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVK- 180
Cdd:cd05039   79 TEYMAKGSLVDYLRSRGR----AVITRKDQLGFALdvcegmEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAKEASs 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 255958318 181 ----GR---TWTlcgtpeylAPEIILSKGYNKAVDWWALGVLIYEM 219
Cdd:cd05039  155 nqdgGKlpiKWT--------APEALREKKFSTKSDVWSFGILLWEI 192
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
34-178 1.54e-17

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. Some isoforms have several splice variants such as the long (L) and short (S) variants of CK1alpha. CK1 proteins are involved in the regulation of many cellular processes including membrane transport processes, circadian rhythm, cell division, apoptosis, and the development of cancer and neurodegenerative diseases. The CK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 80.96  E-value: 1.54e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  34 KKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKvvKLKQIEHtlnEKRILQAVE----FPflvRLEYSFKDNSNLYMVME 109
Cdd:cd14016    5 VKKIGSGSFGEVYLGIDLKTGEEVAIKIEKKDS--KHPQLEY---EAKVYKLLQggpgIP---RLYWFGQEGDYNVMVMD 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255958318 110 YVpgGEMFSHLRRI--GRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLI---DHQGYIQVTDFGFAKR 178
Cdd:cd14016   77 LL--GPSLEDLFNKcgRKFSLKTVLMLADQMISRLEYLHSKGYIHRDIKPENFLMglgKNSNKVYLIDFGLAKK 148
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
35-259 2.28e-17

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. They are also essential regulators of physiological and pathological processes and are involved in the pathogenesis of several diseases such as diabetes, atherosclerosis, stroke, Parkinson's and Alzheimer's. Vetebrates harbor three different JNK genes (Jnk1, Jnk2, and Jnk3) that are alternatively spliced to produce at least 10 isoforms. JNKs are specifically activated by the MAPK kinases MKK4 and MKK7, which are in turn activated by upstream MAPK kinase kinases as a result of different stimuli including stresses such as ultraviolet (UV) irradiation, hyperosmolarity, heat shock, or cytokines. JNKs activate a large number of different substrates based on specific stimulus, cell type, and cellular condition, and may be implicated in seemingly contradictory functions. The JNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 81.69  E-value: 2.28e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYYAMKILDK--QKVVKLKQiehTLNEKRILQAVEFPFLVRL------EYSFKDNSNLYM 106
Cdd:cd07850    6 KPIGSGAQGIVCAAYDTVTGQNVAIKKLSRpfQNVTHAKR---AYRELVLMKLVNHKNIIGLlnvftpQKSLEEFQDVYL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 107 VMEYvpggeMFSHLRRIGRFSEPHAR--FYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAkRVKGRTW 184
Cdd:cd07850   83 VMEL-----MDANLCQVIQMDLDHERmsYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLA-RTAGTSF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 185 TLcgTPE-----YLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRN 259
Cdd:cd07850  157 MM--TPYvvtryYRAPEVILGMGYKENVDIWSVGCIMGEMIRGTVLFPGTDHIDQWNKIIEQLGTPSDEFMSRLQPTVRN 234
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
31-267 3.88e-17

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: 80.45  E-value: 3.88e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEY 110
Cdd:cd06634   17 FSDLREIGHGSFGAVYFARDVRNNEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQKLRHPNTIEYRGCYLREHTAWLVMEY 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 111 VPGGEmfSHLRRIGRfsEPHARFYAAQI----VLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTwTL 186
Cdd:cd06634   97 CLGSA--SDLLEVHK--KPLQEVEIAAIthgaLQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFGSASIMAPAN-SF 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 187 CGTPEYLAPEIILSKG---YNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVrfPSHFSSDLKDLLRNLLQV 263
Cdd:cd06634  172 VGTPYWMAPEVILAMDegqYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNES--PALQSGHWSEYFRNFVDS 249

                 ....
gi 255958318 264 DLTK 267
Cdd:cd06634  250 CLQK 253
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
28-226 3.93e-17

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: 80.81  E-value: 3.93e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  28 LEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILdkqkvvklkQIEH-------TLNEKRILQAVEFPFLVRLEYSFKD 100
Cdd:cd07872    5 METYIKLEKLGEGTYATVFKGRSKLTENLVALKEI---------RLEHeegapctAIREVSLLKDLKHANIVTLHDIVHT 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 101 NSNLYMVMEYVpGGEMFSHLRRIGRFSEPH-ARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGF--AK 177
Cdd:cd07872   76 DKSLTLVFEYL-DKDLKQYMDDCGNIMSMHnVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLarAK 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 255958318 178 RVKGRTWT-LCGTPEYLAPEIIL-SKGYNKAVDWWALGVLIYEMAAGYPPF 226
Cdd:cd07872  155 SVPTKTYSnEVVTLWYRPPDVLLgSSEYSTQIDMWGVGCIFFEMASGRPLF 205
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
35-273 5.08e-17

Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes Ack1, thirty-eight-negative kinase 1 (Tnk1), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal catalytic domain, an SH3 domain, a Cdc42-binding CRIB domain, and a proline-rich region. They are mainly expressed in brain and skeletal tissues and are involved in the regulation of cell adhesion and growth, receptor degradation, and axonal guidance. Ack1 is also associated with androgen-independent prostate cancer progression. Tnk1 regulates TNFalpha signaling and may play an important role in cell death. The Ack-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 79.31  E-value: 5.08e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYY---AMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLeYSFKDNSNLYMVMEYV 111
Cdd:cd05040    1 EKLGDGSFGVVRRGEWTTPSGKViqvAVKCLKSDVLSQPNAMDDFLKEVNAMHSLDHPNLIRL-YGVVLSSPLMMVTELA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 112 PGGEMFSHLRrigrfsEPHARF-------YAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFG---------- 174
Cdd:cd05040   80 PLGSLLDRLR------KDQGHFlistlcdYAVQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGDFGlmralpqned 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 175 -----FAKRVKgRTWtlCgtpeylAPEIILSKGYNKAVDWWALGVLIYEM-AAGYPPFFADQPIQIYEKIVSGKVRF--P 246
Cdd:cd05040  154 hyvmqEHRKVP-FAW--C------APESLKTRKFSHASDVWMFGVTLWEMfTYGEEPWLGLNGSQILEKIDKEGERLerP 224
                        250       260
                 ....*....|....*....|....*....
gi 255958318 247 SHFSSDLKDLLRNLLQVDLTKR--FGNLK 273
Cdd:cd05040  225 DDCPQDIYNVMLQCWAHKPADRptFVALR 253
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
29-252 6.73e-17

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: 79.15  E-value: 6.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKAteQY-YAMKILDKQKVVKLKQIEhtlnEKRILQAVEFPFLVRLEYSFKDNSNLYMV 107
Cdd:cd05113    4 KDLTFLKELGTGQFGVVKYGKWRG--QYdVAIKMIKEGSMSEDEFIE----EAKVMMNLSHEKLVQLYGVCTKQRPIFII 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 108 MEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVL-TFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTWTL 186
Cdd:cd05113   78 TEYMANGCLLNYLREMRKRFQTQQLLEMCKDVCeAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYVLDDEYTS 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255958318 187 C-GTP---EYLAPEIILSKGYNKAVDWWALGVLIYEM-AAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSD 252
Cdd:cd05113  158 SvGSKfpvRWSPPEVLMYSKFSSKSDVWAFGVLMWEVySLGKMPYERFTNSETVEHVSQGLRLYRPHLASE 228
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
37-226 7.11e-17

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: 79.35  E-value: 7.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKildkqkVVKLKQIEHT----LNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVP 112
Cdd:cd07844    8 LGEGSYATVYKGRSKLTGQLVALK------EIRLEHEEGApftaIREASLLKDLKHANIVTLHDIIHTKKTLTLVFEYLD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 113 GgEMFSHLRRIGRFSEPH-ARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGF--AKRVKGRTW----- 184
Cdd:cd07844   82 T-DLKQYMDDCGGGLSMHnVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLarAKSVPSKTYsnevv 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 255958318 185 TLCgtpeYLAPEIIL-SKGYNKAVDWWALGVLIYEMAAGYPPF 226
Cdd:cd07844  161 TLW----YRPPDVLLgSTEYSTSLDMWGVGCIFYEMATGRPLF 199
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
35-226 7.13e-17

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: 79.92  E-value: 7.13e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYYAMK---------ILDKQKVVKLKQIEHTLNEKRI-LQAVefpFLVRLEysfkdnsNL 104
Cdd:cd07856   16 QPVGMGAFGLVCSARDQLTGQNVAVKkimkpfstpVLAKRTYRELKLLKHLRHENIIsLSDI---FISPLE-------DI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 105 YMVMEYVpgGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTW 184
Cdd:cd07856   86 YFVTELL--GTDLHRLLTSRPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLARIQDPQMT 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 255958318 185 TLCGTPEYLAPEIILS-KGYNKAVDWWALGVLIYEMAAGYPPF 226
Cdd:cd07856  164 GYVSTRYYRAPEIMLTwQKYDVEVDIWSAGCIFAEMLEGKPLF 206
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
37-224 7.50e-17

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


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 80.07  E-value: 7.50e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKQ-KVVKLKQIEHTL-----NEkrilQAVEFPFlVRLEYSFKDNSNLYMVMEY 110
Cdd:cd14229    8 LGRGTFGQVVKCWKRGTNEIVAVKILKNHpSYARQGQIEVGIlarlsNE----NADEFNF-VRAYECFQHRNHTCLVFEM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 111 VPGgEMFSHLRRiGRFSEPHARFYAA---QIVLTFEYLHSLDLIYRDLKPEN-LLID--HQGY-IQVTDFGFAKRVkgrT 183
Cdd:cd14229   83 LEQ-NLYDFLKQ-NKFSPLPLKVIRPilqQVATALKKLKSLGLIHADLKPENiMLVDpvRQPYrVKVIDFGSASHV---S 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 255958318 184 WTLCGT----PEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYP 224
Cdd:cd14229  158 KTVCSTylqsRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWP 202
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
56-285 7.62e-17

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


Pssm-ID: 270925 [Multi-domain]  Cd Length: 242  Bit Score: 78.55  E-value: 7.62e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  56 YYAMKI-LDKQKVVKLKQIEHTlnEKRILQAVEFPFlvrleysfkdNSNLYMVMEYVPG------------GEMFSHLRR 122
Cdd:cd14023   10 YRALQLhSGAELQCKVFPLKHY--QDKIRPYIQLPS----------HRNITGIVEVILGdtkayvffekdfGDMHSYVRS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 123 IGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQV--TDFGFAKRVKGRTWTLC---GTPEYLAPEI 197
Cdd:cd14023   78 CKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSDEERTQLrlESLEDTHIMKGEDDALSdkhGCPAYVSPEI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 198 ILSKGY--NKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFgnlknG 275
Cdd:cd14023  158 LNTTGTysGKSADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPDHVSPKARCLIRSLLRREPSERL-----T 232
                        250
                 ....*....|
gi 255958318 276 VSDIKTHKWF 285
Cdd:cd14023  233 APEILLHPWF 242
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
34-268 1.01e-16

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: 78.62  E-value: 1.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  34 KKTLGTGSFGRVMLVKHKATEQYYAMKILdKQKVVKLKQIehtLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPG 113
Cdd:cd05052   11 KHKLGGGQYGEVYEGVWKKYNLTVAVKTL-KEDTMEVEEF---LKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMPY 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 114 GEMFSHLRRIGRFS-EPHARFY-AAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTWTLCGTPE 191
Cdd:cd05052   87 GNLLDYLRECNREElNAVVLLYmATQIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTYTAHAGAK 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 192 Y----LAPEiilSKGYNK---AVDWWALGVLIYEMAA-GYPPFFADQPIQIYEKIVSG-KVRFPSHFSSDLKDLLRNLLQ 262
Cdd:cd05052  167 FpikwTAPE---SLAYNKfsiKSDVWAFGVLLWEIATyGMSPYPGIDLSQVYELLEKGyRMERPEGCPPKVYELMRACWQ 243

                 ....*.
gi 255958318 263 VDLTKR 268
Cdd:cd05052  244 WNPSDR 249
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
37-218 1.19e-16

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: 78.25  E-value: 1.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQieHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGGEM 116
Cdd:cd05041    3 IGRGNFGDVYRGVLKPDNTEVAVKTCRETLPPDLKR--KFLQEARILKQYDHPNIVKLIGVCVQKQPIMIVMELVPGGSL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 117 FSHLRRigrfsePHARFYAAQIVLT-------FEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTWTLCG- 188
Cdd:cd05041   81 LTFLRK------KGARLTVKQLLQMcldaaagMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSREEEDGEYTVSDg 154
                        170       180       190
                 ....*....|....*....|....*....|....
gi 255958318 189 ---TP-EYLAPEIILSKGYNKAVDWWALGVLIYE 218
Cdd:cd05041  155 lkqIPiKWTAPEALNYGRYTSESDVWSFGILLWE 188
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
119-269 1.36e-16

Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SHIK, also referred to as STK40 or LYK4, is a cytoplasmic and nuclear protein that is involved in the negative regulation of NF-kappaB- and p53-mediated transcription. It was identified as a protein related to SINK, a p65-interacting protein that inhibits p65 phosphorylation by the catalytic subunit of PKA, thereby inhibiting transcriptional competence of NF-kappaB. The SHIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270876 [Multi-domain]  Cd Length: 290  Bit Score: 78.60  E-value: 1.36e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 119 HLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLID-HQGYIQVTDFGFAKRVKGRTWTLC---GTPEYLA 194
Cdd:cd13974  122 YVIREKRLSEREALVIFYDVVRVVEALHKKNIVHRDLKLGNMVLNkRTRKITITNFCLGKHLVSEDDLLKdqrGSPAYIS 201
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255958318 195 PEIILSKGY-NKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPS--HFSSDLKDLLRNLLQVDLTKRF 269
Cdd:cd13974  202 PDVLSGKPYlGKPSDMWALGVVLFTMLYGQFPFYDSIPQELFRKIKAAEYTIPEdgRVSENTVCLIRKLLVLNPQKRL 279
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
37-269 1.43e-16

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A splice variant of TLK1, called TLK1B, is expressed in the presence of double strand breaks (DSBs). It lacks the N-terminal part of TLK1, but is expected to phosphorylate the same substrates. TLK1/1B interacts with Rad9, which is critical in DNA damage-activated checkpoint response, and plays a role in the repair of linearized DNA with incompatible ends. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. The TLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 78.95  E-value: 1.43e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIE----HTLNEKRILQAVEFPFLVRL-EYSFKDNSNLYMVMEYV 111
Cdd:cd14040   14 LGRGGFSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKEnyhkHACREYRIHKELDHPRIVKLyDYFSLDTDTFCTVLEYC 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 112 PGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLD--LIYRDLKPEN-LLIDHQ--GYIQVTDFGFAKRVKGRTWTL 186
Cdd:cd14040   94 EGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNiLLVDGTacGEIKITDFGLSKIMDDDSYGV 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 187 ---------CGTPEYLAPEIIL-----SKGYNKaVDWWALGVLIYEMAAGYPPFFADQPIQ--IYEKIV--SGKVRFPSH 248
Cdd:cd14040  174 dgmdltsqgAGTYWYLPPECFVvgkepPKISNK-VDVWSVGVIFFQCLYGRKPFGHNQSQQdiLQENTIlkATEVQFPVK 252
                        250       260
                 ....*....|....*....|...
gi 255958318 249 --FSSDLKDLLRNLLQVDLTKRF 269
Cdd:cd14040  253 pvVSNEAKAFIRRCLAYRKEDRF 275
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
35-219 2.04e-16

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: 78.19  E-value: 2.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKH-----KATEQYyAMKILdkQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEY-SFKDNSN-LYMV 107
Cdd:cd05038   10 KQLGEGHFGSVELCRYdplgdNTGEQV-AVKSL--QPSGEEQHMSDFKREIEILRTLDHEYIVKYKGvCESPGRRsLRLI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 108 MEYVPGGEMFSHLRRI-GRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRV-KGRTWT 185
Cdd:cd05038   87 MEYLPSGSLRDYLQRHrDQIDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGLAKVLpEDKEYY 166
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 255958318 186 LCGTPE-----YLAPEIILSKGYNKAVDWWALGVLIYEM 219
Cdd:cd05038  167 YVKEPGespifWYAPECLRESRFSSASDVWSFGVTLYEL 205
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
29-233 2.34e-16

Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CdkB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 78.34  E-value: 2.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKildkqkVVKLKQIEH-----TLNEKRILQAV-EFPFLVRL---EYSFK 99
Cdd:cd07837    1 DAYEKLEKIGEGTYGKVYKARDKNTGKLVALK------KTRLEMEEEgvpstALREVSLLQMLsQSIYIVRLldvEHVEE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 100 D-NSNLYMVMEYVpGGEMFSHLRRIGR-----FSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQ-GYIQVTD 172
Cdd:cd07837   75 NgKPLLYLVFEYL-DTDLKKFIDSYGRgphnpLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQkGLLKIAD 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255958318 173 FG----FAKRVKGRTWTLCgTPEYLAPEIIL-SKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQ 233
Cdd:cd07837  154 LGlgraFTIPIKSYTHEIV-TLWYRAPEVLLgSTHYSTPVDMWSVGCIFAEMSRKQPLFPGDSELQ 218
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
67-227 2.60e-16

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 79.27  E-value: 2.60e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  67 VVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGgEMFSHL---RRIgrfsePHARFYAAQ--IVLT 141
Cdd:PHA03212 121 VIKAGQRGGTATEAHILRAINHPSIIQLKGTFTYNKFTCLILPRYKT-DLYCYLaakRNI-----AICDILAIErsVLRA 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 142 FEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFA----KRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIY 217
Cdd:PHA03212 195 IQYLHENRIIHRDIKAENIFINHPGDVCLGDFGAAcfpvDINANKYYGWAGTIATNAPELLARDPYGPAVDIWSAGIVLF 274
                        170
                 ....*....|
gi 255958318 218 EMAAGYPPFF 227
Cdd:PHA03212 275 EMATCHDSLF 284
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
43-284 2.60e-16

Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB3 binds and regulates ATF4, p65/RelA, and PKB (or Akt). It negatively regulates ATF4-mediated gene expression including that of CHOP (C/EBP homologous protein) and HO-1, which are both involved in modulating apoptosis. It also inhibits insulin-mediated phosphorylation of PKB and is a possible determinant of insulin resistance and related disorders. In osteoarthritic chondrocytes where it inhibits insulin-like growth factor 1-mediated cell survival, TRB3 is overexpressed, resulting in increased cell death. TRB3 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB3 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: 270926 [Multi-domain]  Cd Length: 242  Bit Score: 77.23  E-value: 2.60e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  43 GRVMLVKHKATEQYYAMKILDKQKVVK-LKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNlymvmeyvpgGEMFSHLR 121
Cdd:cd14024    7 QELYRAEHYQTEKEYTCKVLSLRSYQEcLAPYDRLGPHEGVCSVLEVVIGQDRAYAFFSRHY----------GDMHSHVR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 122 RIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGR-----TWTLCGTPEYLAPE 196
Cdd:cd14024   77 RRRRLSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTDELRTKLVLVNLEDSCPLNgdddsLTDKHGCPAYVGPE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 197 IILSK-GYN-KAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFgnlkn 274
Cdd:cd14024  157 ILSSRrSYSgKAADVWSLGVCLYTMLLGRYPFQDTEPAALFAKIRRGAFSLPAWLSPGARCLVSCMLRRSPAERL----- 231
                        250
                 ....*....|
gi 255958318 275 GVSDIKTHKW 284
Cdd:cd14024  232 KASEILLHPW 241
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
35-219 2.66e-16

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: 77.75  E-value: 2.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQyyamkilDKQKVVKLKQIEHTLNEK--------RILQAVEFPFLVRLE---YSFKDNsN 103
Cdd:cd14205   10 QQLGKGNFGSVEMCRYDPLQD-------NTGEVVAVKKLQHSTEEHlrdfereiEILKSLQHDNIVKYKgvcYSAGRR-N 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 104 LYMVMEYVPGGEMFSHLRR-IGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRV-KG 181
Cdd:cd14205   82 LRLIMEYLPYGSLRDYLQKhKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLpQD 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 255958318 182 RTWTLCGTPE-----YLAPEIILSKGYNKAVDWWALGVLIYEM 219
Cdd:cd14205  162 KEYYKVKEPGespifWYAPESLTESKFSVASDVWSFGVVLYEL 204
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
114-285 2.86e-16

Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB2 binds and negatively regulates the mitogen activated protein kinase (MAPK) kinases, MKK7 and MEK1, which are activators of the MAPKs, ERK and JNK. It controls the activation of inflammatory monocytes, which is essential in innate immune responses and the pathogenesis of inflammatory diseases such as atherosclerosis. TRB2 expression is down-regulated in human acute myeloid leukaemia (AML), which may lead to enhanced cell survival and pathogenesis of the disease. TRB2 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB2 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: 270924 [Multi-domain]  Cd Length: 242  Bit Score: 77.00  E-value: 2.86e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 114 GEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLI--DHQGYIQVTDFGFAKRVKGRTWTLC---G 188
Cdd:cd14022   69 GDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVFkdEERTRVKLESLEDAYILRGHDDSLSdkhG 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 189 TPEYLAPEIILSKGY--NKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLT 266
Cdd:cd14022  149 CPAYVSPEILNTSGSysGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRREPS 228
                        170
                 ....*....|....*....
gi 255958318 267 KRFGNlkngvSDIKTHKWF 285
Cdd:cd14022  229 ERLTS-----QEILDHPWF 242
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
37-258 3.50e-16

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: 76.97  E-value: 3.50e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVM--LVKHKATEQYYAMKiLDKQKVVKLKqiehTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGG 114
Cdd:cd05085    4 LGKGNFGEVYkgTLKDKTPVAVKTCK-EDLPQELKIK----FLSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVPGG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 115 EMFSHLRR---------IGRFSEPHARFYAaqivltfeYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTWT 185
Cdd:cd05085   79 DFLSFLRKkkdelktkqLVKFSLDAAAGMA--------YLESKNCIHRDLAARNCLVGENNALKISDFGMSRQEDDGVYS 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255958318 186 LCGTPE----YLAPEIILSKGYNKAVDWWALGVLIYE-MAAGYPPFFADQPIQIYEKIVSG-KVRFPSHFSSDLKDLLR 258
Cdd:cd05085  151 SSGLKQipikWTAPEALNYGRYSSESDVWSFGILLWEtFSLGVCPYPGMTNQQAREQVEKGyRMSAPQRCPEDIYKIMQ 229
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
37-227 4.25e-16

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: 76.93  E-value: 4.25e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVmlvkHKAT---EQYYAMKILDKQKVVKLKQieHTLNEKRILQAVEFPFLVRLE-YSFKDNSNLyMVMEYVP 112
Cdd:cd14066    1 IGSGGFGTV----YKGVlenGTVVAVKRLNEMNCAASKK--EFLTELEMLGRLRHPNLVRLLgYCLESDEKL-LVYEYMP 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 113 GGEMFSHLRRiGRFSEPH---ARFYAAQ-IVLTFEYLHS---LDLIYRDLKPENLLIDHQGYIQVTDFGFAK-----RVK 180
Cdd:cd14066   74 NGSLEDRLHC-HKGSPPLpwpQRLKIAKgIARGLEYLHEecpPPIIHGDIKSSNILLDEDFEPKLTDFGLARlippsESV 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 255958318 181 GRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFF 227
Cdd:cd14066  153 SKTSAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVD 199
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
31-224 4.71e-16

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: 77.41  E-value: 4.71e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKildkqKVVKLKQIE----HTLNEKRILQAVEFPFLVRL---------EYS 97
Cdd:cd07865   14 YEKLAKIGQGTFGEVFKARHRKTGQIVALK-----KVLMENEKEgfpiTALREIKILQLLKHENVVNLieicrtkatPYN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  98 fKDNSNLYMVMEyvpggemFSHLRRIGRFSEPHARFYAAQIVLTFE-------YLHSLDLIYRDLKPENLLIDHQGYIQV 170
Cdd:cd07865   89 -RYKGSIYLVFE-------FCEHDLAGLLSNKNVKFTLSEIKKVMKmllnglyYIHRNKILHRDMKAANILITKDGVLKL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255958318 171 TDFGFAK-----------RVKGRTWTLCgtpeYLAPEIILS-KGYNKAVDWWALGVLIYEMAAGYP 224
Cdd:cd07865  161 ADFGLARafslaknsqpnRYTNRVVTLW----YRPPELLLGeRDYGPPIDMWGAGCIMAEMWTRSP 222
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
37-226 5.74e-16

Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TBK1 is also called T2K and NF-kB-activating kinase. It is widely expressed in most cell types and acts as an IkappaB kinase (IKK)-activating kinase responsible for NF-kB activation in response to growth factors. It plays a role in modulating inflammatory responses through the NF-kB pathway. TKB1 is also a major player in innate immune responses since it functions as a virus-activated kinase necessary for establishing an antiviral state. It phosphorylates IRF-3 and IRF-7, which are important transcription factors for inducing type I interferon during viral infection. In addition, TBK1 may also play roles in cell transformation and oncogenesis. The TBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 77.15  E-value: 5.74e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKqkVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNS--NLYMVMEYVPGG 114
Cdd:cd13988    1 LGQGATANVFRGRHKKTGDLYAVKVFNN--LSFMRPLDVQMREFEVLKKLNHKNIVKLFAIEEELTtrHKVLVMELCPCG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 115 EMFSHLRR-IGRFSEPHARFYAA--QIVLTFEYLHSLDLIYRDLKPENLLI----DHQGYIQVTDFGFAKRVKG--RTWT 185
Cdd:cd13988   79 SLYTVLEEpSNAYGLPESEFLIVlrDVVAGMNHLRENGIVHRDIKPGNIMRvigeDGQSVYKLTDFGAARELEDdeQFVS 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 255958318 186 LCGTPEYLAPEI----ILSKGYNKA----VDWWALGVLIYEMAAGYPPF 226
Cdd:cd13988  159 LYGTEEYLHPDMyeraVLRKDHQKKygatVDLWSIGVTFYHAATGSLPF 207
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
40-235 6.37e-16

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: 76.20  E-value: 6.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  40 GSFGRVMLVKHKATEqyyamkildKQKVVKLKQIEHTLNEKRILQA-VEFPFLVRLEYSFKDNSNLYMVMEYVPGGEMFS 118
Cdd:cd13995   15 GAFGKVYLAQDTKTK---------KRMACKLIPVEQFKPSDVEIQAcFRHENIAELYGALLWEETVHLFMEAGEGGSVLE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 119 HLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVtDFGFAKRVKGRTWT---LCGTPEYLAP 195
Cdd:cd13995   86 KLESCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAVLV-DFGLSVQMTEDVYVpkdLRGTEIYMSP 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 255958318 196 EIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIY 235
Cdd:cd13995  165 EVILCRGHNTKADIYSLGATIIHMQTGSPPWVRRYPRSAY 204
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
34-219 8.93e-16

Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR-like proteins are members of the DDR subfamily, which are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 76.55  E-value: 8.93e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  34 KKTLGTGSFGRVMLVKHKATEQYYAM---KILDKQKVVKLKQIEHT---------LNEKRILQAVEFPFLVRLEYSFKDN 101
Cdd:cd05097   10 KEKLGEGQFGEVHLCEAEGLAEFLGEgapEFDGQPVLVAVKMLRADvtktarndfLKEIKIMSRLKNPNIIRLLGVCVSD 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 102 SNLYMVMEYVPGGEM------------FSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQ 169
Cdd:cd05097   90 DPLCMITEYMENGDLnqflsqreiestFTHANNIPSVSIANLLYMAVQIASGMKYLASLNFVHRDLATRNCLVGNHYTIK 169
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 255958318 170 VTDFGFAK--------RVKGRTWtlcgTP-EYLAPEIILSKGYNKAVDWWALGVLIYEM 219
Cdd:cd05097  170 IADFGMSRnlysgdyyRIQGRAV----LPiRWMAWESILLGKFTTASDVWAFGVTLWEM 224
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
37-246 8.98e-16

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK2 subfamily is part of a 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: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 76.64  E-value: 8.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIE----HTLNEKRILQAVEFPFLVRL-EYSFKDNSNLYMVMEYV 111
Cdd:cd14041   14 LGRGGFSEVYKAFDLTEQRYVAVKIHQLNKNWRDEKKEnyhkHACREYRIHKELDHPRIVKLyDYFSLDTDSFCTVLEYC 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 112 PGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLD--LIYRDLKPENLLIDHQ---GYIQVTDFGFAK--------R 178
Cdd:cd14041   94 EGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEIKppIIHYDLKPGNILLVNGtacGEIKITDFGLSKimdddsynS 173
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255958318 179 VKGRTWTL--CGTPEYLAPEIIL-----SKGYNKaVDWWALGVLIYEMAAGYPPFFADQPIQ--IYEKIV--SGKVRFP 246
Cdd:cd14041  174 VDGMELTSqgAGTYWYLPPECFVvgkepPKISNK-VDVWSVGVIFYQCLYGRKPFGHNQSQQdiLQENTIlkATEVQFP 251
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
29-274 9.48e-16

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: 76.25  E-value: 9.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAmkildkqkvvkLKQIEHTLNE---KRILQAVEF-------PFLVRLEYSF 98
Cdd:cd06616    6 EDLKDLGEIGRGAFGTVNKMLHKPSGTIMA-----------VKRIRSTVDEkeqKRLLMDLDVvmrssdcPYIVKFYGAL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  99 KDNSNLYMVME---------YvpggeMFSHLRRIGRFSEPHARFYAAQIVLTFEYL-HSLDLIYRDLKPENLLIDHQGYI 168
Cdd:cd06616   75 FREGDCWICMElmdisldkfY-----KYVYEVLDSVIPEEILGKIAVATVKALNYLkEELKIIHRDVKPSNILLDRNGNI 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 169 QVTDFG--------FAKRVKGrtwtlcGTPEYLAPEIILS----KGYNKAVDWWALGVLIYEMAAG---YPPFfaDQPIQ 233
Cdd:cd06616  150 KLCDFGisgqlvdsIAKTRDA------GCRPYMAPERIDPsasrDGYDVRSDVWSLGITLYEVATGkfpYPKW--NSVFD 221
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 255958318 234 IYEKIVSGKV-RFPS----HFSSDLKDLLRNLLQVDLTKR--FGNLKN 274
Cdd:cd06616  222 QLTQVVKGDPpILSNseerEFSPSFVNFVNLCLIKDESKRpkYKELLK 269
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
37-246 9.94e-16

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: 76.11  E-value: 9.94e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKAteQYYAMKILDKQ------KVVKLKQIEHTL------------NEKRILQAVEFPFLVRL-EYS 97
Cdd:cd14000    2 LGDGGFGSVYRASYKG--EPVAVKIFNKHtssnfaNVPADTMLRHLRatdamknfrllrQELTVLSHLHHPSIVYLlGIG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  98 FKDnsnLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLT----FEYLHSLDLIYRDLKPENLLI-----DHQGYI 168
Cdd:cd14000   80 IHP---LMLVLELAPLGSLDHLLQQDSRSFASLGRTLQQRIALQvadgLRYLHSAMIIYRDLKSHNVLVwtlypNSAIII 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 169 QVTDFGFAKR-VKGRTWTLCGTPEYLAPEII-LSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIyEKIVSGKVRFP 246
Cdd:cd14000  157 KIADYGISRQcCRMGAKGSEGTPGFRAPEIArGNVIYNEKVDVFSFGMLLYEILSGGAPMVGHLKFPN-EFDIHGGLRPP 235
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
37-262 1.04e-15

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: 75.88  E-value: 1.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKAteQYYAMKILDKQKvvKLKQIEHTLNEKRILQAVEFPFLVRL---EYSFKDNSNLYMVMEYVPG 113
Cdd:cd13979   11 LGSGGFGSVYKATYKG--ETVAVKIVRRRR--KNRASRQSFWAELNAARLRHENIVRVlaaETGTDFASLGLIIMEYCGN 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 114 GEMfshLRRIGRFSEP----HARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKG------RT 183
Cdd:cd13979   87 GTL---QQLIYEGSEPlplaHRILISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCSVKLGEgnevgtPR 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 184 WTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEkIVSGKVR--FPSHFSSDLKDLLRNLL 261
Cdd:cd13979  164 SHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPYAGLRQHVLYA-VVAKDLRpdLSGLEDSEFGQRLRSLI 242

                 .
gi 255958318 262 Q 262
Cdd:cd13979  243 S 243
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
37-286 1.16e-15

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


Pssm-ID: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 75.88  E-value: 1.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQiEHTLNEKRILQAVEFPFLVRL----EYSFKDNSNLYMVMEYVP 112
Cdd:cd14032    9 LGRGSFKTVYKGLDTETWVEVAWCELQDRKLTKVER-QRFKEEAEMLKGLQHPNIVRFydfwESCAKGKRCIVLVTELMT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 113 GGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLD--LIYRDLKPENLLIDH-QGYIQVTDFGFAKRVKGR-TWTLCG 188
Cdd:cd14032   88 SGTLKTYLKRFKVMKPKVLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFITGpTGSVKIGDLGLATLKRASfAKSVIG 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 189 TPEYLAPEIiLSKGYNKAVDWWALGVLIYEMAAG-YPPFFADQPIQIYEKIVSG--KVRFPSHFSSDLKDLLRNLLQVDL 265
Cdd:cd14032  168 TPEFMAPEM-YEEHYDESVDVYAFGMCMLEMATSeYPYSECQNAAQIYRKVTCGikPASFEKVTDPEIKEIIGECICKNK 246
                        250       260
                 ....*....|....*....|.
gi 255958318 266 TKRFgnlknGVSDIKTHKWFA 286
Cdd:cd14032  247 EERY-----EIKDLLSHAFFA 262
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
18-253 1.22e-15

Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lyn is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lyn is expressed in B lymphocytes and myeloid cells. It exhibits both positive and negative regulatory roles in B cell receptor (BCR) signaling. Lyn, as well as Fyn and Blk, promotes B cell activation by phosphorylating ITAMs (immunoreceptor tyr activation motifs) in CD19 and in Ig components of BCR. It negatively regulates signaling by its unique ability to phosphorylate ITIMs (immunoreceptor tyr inhibition motifs) in cell surface receptors like CD22 and CD5. Lyn also plays an important role in G-CSF receptor signaling by phosphorylating a variety of adaptor molecules. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lyn subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 75.85  E-value: 1.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  18 WENPPpsnaglEDFERKKTLGTGSFGRV-MLVKHKATEqyYAMKILDKQKVvklkQIEHTLNEKRILQAVEFPFLVRLEY 96
Cdd:cd05072    2 WEIPR------ESIKLVKKLGAGQFGEVwMGYYNNSTK--VAVKTLKPGTM----SVQAFLEEANLMKTLQHDKLVRLYA 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  97 SFKDNSNLYMVMEYVPGGEMFSHLRRI--GRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFG 174
Cdd:cd05072   70 VVTKEEPIYIITEYMAKGSLLDFLKSDegGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 175 FAKRVKGRTWTL---CGTP-EYLAPEIILSKGYNKAVDWWALGVLIYEMaagyppffadqpiqiyekIVSGKVRFPSHFS 250
Cdd:cd05072  150 LARVIEDNEYTAregAKFPiKWTAPEAINFGSFTIKSDVWSFGILLYEI------------------VTYGKIPYPGMSN 211

                 ...
gi 255958318 251 SDL 253
Cdd:cd05072  212 SDV 214
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
35-247 1.25e-15

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


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 75.46  E-value: 1.25e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKH---KATEQYYAMKILDKQKVVKLKQieHTLNEKRILQAVEFPFLVRLEYSFKDNSnLYMVMEYV 111
Cdd:cd05060    1 KELGHGNFGSVRKGVYlmkSGKEVEVAVKTLKQEHEKAGKK--EFLREASVMAQLDHPCIVRLIGVCKGEP-LMLVMELA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 112 PGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVK----------- 180
Cdd:cd05060   78 PLGPLLKYLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMSRALGagsdyyratta 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255958318 181 GRtWTLcgtpEYLAPEIILSKGYNKAVDWWALGVLIYEMAA-GYPPFFADQPIQIYEKIVSGKvRFPS 247
Cdd:cd05060  158 GR-WPL----KWYAPECINYGKFSSKSDVWSYGVTLWEAFSyGAKPYGEMKGPEVIAMLESGE-RLPR 219
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
29-233 1.31e-15

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: 76.27  E-value: 1.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYYAMKildkqkVVKLKQIEHT----LNEKRILQAVEFPFLVRLEYSFKDNSNL 104
Cdd:cd07869    5 DSYEKLEKLGEGSYATVYKGKSKVNGKLVALK------VIRLQEEEGTpftaIREASLLKGLKHANIVLLHDIIHTKETL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 105 YMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGF--AKRVKGR 182
Cdd:cd07869   79 TLVFEYVHTDLCQYMDKHPGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLarAKSVPSH 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 255958318 183 TWT-LCGTPEYLAPEIIL-SKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQ 233
Cdd:cd07869  159 TYSnEVVTLWYRPPDVLLgSTEYSTCLDMWGVGCIFVEMIQGVAAFPGMKDIQ 211
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
16-226 1.52e-15

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 4; 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. DYRK4 is a testis-specific kinase with restricted expression to postmeiotic spermatids. It may function during spermiogenesis, however, it is not required for male fertility. DYRK4 has also been detected in a human teratocarcinoma cell line induced to produce postmitotic neurons. It may have a role in neuronal differentiation. 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. The DYRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 76.28  E-value: 1.52e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  16 RKWENPP--PSNAGLED----------------FERKKTLGTGSFGRVMLVKHKATEQYYAMKIL------DKQKVVKLK 71
Cdd:cd14225   12 KKIEGVPgaPQNNGYDDengsylkvlhdhiayrYEILEVIGKGSFGQVVKALDHKTNEHVAIKIIrnkkrfHHQALVEVK 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  72 QIEHTLNEKR-----ILQAVE-FPFLVRLEYSFKDNS-NLYmvmeyvpggEMFSHLRRIGrFSEPHARFYAAQIVLTFEY 144
Cdd:cd14225   92 ILDALRRKDRdnshnVIHMKEyFYFRNHLCITFELLGmNLY---------ELIKKNNFQG-FSLSLIRRFAISLLQCLRL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 145 LHSLDLIYRDLKPENLLIDHQGY--IQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAG 222
Cdd:cd14225  162 LYRERIIHCDLKPENILLRQRGQssIKVIDFGSSCYEHQRVYTYIQSRFYRSPEVILGLPYSMAIDMWSLGCILAELYTG 241

                 ....
gi 255958318 223 YPPF 226
Cdd:cd14225  242 YPLF 245
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
37-224 1.54e-15

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). They show speckled localization in the nucleus, apart from the nucleoles. They play roles in the regulation of many nuclear pathways including gene transcription, cell survival, proliferation, differentiation, development, and DNA damage response. Vertebrates contain three HIPKs (HIPK1-3) and mammals harbor an additional family member HIPK4, which does not contain a homeobox-interacting domain and is localized in the cytoplasm. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors and it regulates gene transcription during development and in DNA damage response. The HIPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 76.33  E-value: 1.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILdKQKVVKLKQIEhtlNEKRILQ------AVEFPFlVRLEYSFKDNSNLYMVMEY 110
Cdd:cd14211    7 LGRGTFGQVVKCWKRGTNEIVAIKIL-KNHPSYARQGQ---IEVSILSrlsqenADEFNF-VRAYECFQHKNHTCLVFEM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 111 VPGgEMFSHLRRiGRFSE---PHARFYAAQIVLTFEYLHSLDLIYRDLKPEN-LLID--HQGY-IQVTDFGFAKRV-KGR 182
Cdd:cd14211   82 LEQ-NLYDFLKQ-NKFSPlplKYIRPILQQVLTALLKLKSLGLIHADLKPENiMLVDpvRQPYrVKVIDFGSASHVsKAV 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 255958318 183 TWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYP 224
Cdd:cd14211  160 CSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWP 201
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
71-270 1.66e-15

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: 75.09  E-value: 1.66e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  71 KQIEHTLNEKRILQAVEFPFLVRLeYSFK-------DNSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFE 143
Cdd:cd14012   40 KQIQLLEKELESLKKLRHPNLVSY-LAFSierrgrsDGWKVYLLTEYAPGGSLSELLDSVGSVPLDTARRWTLQLLEALE 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 144 YLHSLDLIYRDLKPENLLIDHQ---GYIQVTDFGFAKRVKgrtwTLCGTPE--------YLAPEIIL-SKGYNKAVDWWA 211
Cdd:cd14012  119 YLHRNGVVHKSLHAGNVLLDRDagtGIVKLTDYSLGKTLL----DMCSRGSldefkqtyWLPPELAQgSKSPTRKTDVWD 194
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 255958318 212 LGVLIYEMAAGYPPFfadqpiQIYEKIVSgkVRFPSHFSSDLKDLLRNLLQVDLTKRFG 270
Cdd:cd14012  195 LGLLFLQMLFGLDVL------EKYTSPNP--VLVSLDLSASLQDFLSKCLSLDPKKRPT 245
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
30-233 1.92e-15

Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NLK is an atypical mitogen-activated protein kinase (MAPK) that is not regulated by a MAPK kinase. It functions downstream of the MAPK kinase kinase Tak1, which also plays a role in activating the JNK and p38 MAPKs. The Tak1/NLK pathways are regulated by Wnts, a family of secreted proteins that is critical in the control of asymmetric division and cell polarity. NLK can phosphorylate transcription factors from the TCF/LEF family, inhibiting their ability to activate the transcription of target genes. In prostate cancer cells, NLK is involved in regulating androgen receptor-mediated transcription and its expression is altered during cancer progression. MAPKs are important mediators of cellular responses to extracellular signals. The NLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 76.32  E-value: 1.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  30 DFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDK--QKVVKLKQIEHTL------NEKRILQAVEFPFLVRLEYsFKDn 101
Cdd:cd07853    1 DVEPDRPIGYGAFGVVWSVTDPRDGKRVALKKMPNvfQNLVSCKRVFRELkmlcffKHDNVLSALDILQPPHIDP-FEE- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 102 snLYMVMEYvpggeMFSHLRRI----GRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAk 177
Cdd:cd07853   79 --IYVVTEL-----MQSDLHKIivspQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLA- 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255958318 178 RVKGRTWTLCGTPE-----YLAPEIIL-SKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQ 233
Cdd:cd07853  151 RVEEPDESKHMTQEvvtqyYRAPEILMgSRHYTSAVDIWSVGCIFAELLGRRILFQAQSPIQ 212
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
18-233 2.88e-15

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: 74.69  E-value: 2.88e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  18 WENPPpsnaglEDFERKKTLGTGSFGRVML-----VKHKATEQYYAMKILdkQKVVKLKQIEHTLNEKRILQAVEFPFLV 92
Cdd:cd05032    1 WELPR------EKITLIRELGQGSFGMVYEglakgVVKGEPETRVAIKTV--NENASMRERIEFLNEASVMKEFNCHHVV 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  93 RLEYSFKDNSNLYMVMEYVPGGEMFSHLR-------RIGRFSEPHA-RFY--AAQIVLTFEYLHSLDLIYRDLKPENLLI 162
Cdd:cd05032   73 RLLGVVSTGQPTLVVMELMAKGDLKSYLRsrrpeaeNNPGLGPPTLqKFIqmAAEIADGMAYLAAKKFVHRDLAARNCMV 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255958318 163 DHQGYIQVTDFGFAKRV-------KGRTWTLcgtP-EYLAPEIILSKGYNKAVDWWALGVLIYEMAAgyppfFADQPIQ 233
Cdd:cd05032  153 AEDLTVKIGDFGMTRDIyetdyyrKGGKGLL---PvRWMAPESLKDGVFTTKSDVWSFGVVLWEMAT-----LAEQPYQ 223
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
35-270 4.39e-15

Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Syk is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Syk was first cloned from the spleen, and its function in hematopoietic cells is well-established. It is involved in the signaling downstream of activated receptors (including B-cell and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. More recently, Syk expression has been detected in other cell types (including epithelial cells, vascular endothelial cells, neurons, hepatocytes, and melanocytes), suggesting a variety of biological functions in non-immune cells. Syk plays a critical role in maintaining vascular integrity and in wound healing during embryogenesis. It also regulates Vav3, which is important in osteoclast function including bone development. In breast epithelial cells, where Syk acts as a negative regulator for EGFR signaling, loss of Syk expression is associated with abnormal proliferation during cancer development suggesting a potential role as a tumor suppressor. In mice, Syk has been shown to inhibit malignant transformation of mammary epithelial cells induced with murine mammary tumor virus (MMTV). The Syk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 73.84  E-value: 4.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVM--LVKHKATEQYYAMKIL---DKQKVVKlkqiEHTLNEKRILQAVEFPFLVRLeYSFKDNSNLYMVME 109
Cdd:cd05116    1 GELGSGNFGTVKkgYYQMKKVVKTVAVKILkneANDPALK----DELLREANVMQQLDNPYIVRM-IGICEAESWMLVME 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 110 YVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRV-------KGR 182
Cdd:cd05116   76 MAELGPLNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKALradenyyKAQ 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 183 T---WTLcgtpEYLAPEIILSKGYNKAVDWWALGVLIYE-MAAGYPPFFADQPIQIYEKIVSGK-VRFPSHFSSDLKDLL 257
Cdd:cd05116  156 ThgkWPV----KWYAPECMNYYKFSSKSDVWSFGVLMWEaFSYGQKPYKGMKGNEVTQMIEKGErMECPAGCPPEMYDLM 231
                        250
                 ....*....|...
gi 255958318 258 RNLLQVDLTKRFG 270
Cdd:cd05116  232 KLCWTYDVDERPG 244
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
31-226 4.68e-15

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors including homeodomain proteins (Nkx and HOX families), Smad1-4, Pax6, c-Myb, AML1, the histone acetyltransferase p300, and the tumor repressor p53, among others. It regulates gene transcription during development and in DNA damage response (DDR), and mediates cell processes such as apoptosis, survival, differentiation, and proliferation. HIPK2 mediates apoptosis by phosphorylating and activating p53 during DDR, resulting in the activation of apoptotic genes. In the absence of p53, HIPK2 targets the anti-apoptotic corepressor C-terminal binding protein (CtBP), leading to CtBP's degradation and the promotion of apoptosis. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 75.13  E-value: 4.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQ-KVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVME 109
Cdd:cd14227   17 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHpSYARQGQIEVSILARLSTESADDYNFVRAYECFQHKNHTCLVFE 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 110 YVPGgEMFSHLRRiGRFSE---PHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLI---DHQGY-IQVTDFGFAKRV-KG 181
Cdd:cd14227   97 MLEQ-NLYDFLKQ-NKFSPlplKYIRPILQQVATALMKLKSLGLIHADLKPENIMLvdpSRQPYrVKVIDFGSASHVsKA 174
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 255958318 182 RTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPF 226
Cdd:cd14227  175 VCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLY 219
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
31-226 4.77e-15

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


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 73.99  E-value: 4.77e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVmlvkhkateqYYAMKILDKQKV---VKLKQIEHT---------LNEKRILQAVEFPFLVRLeYSF 98
Cdd:cd05057    9 LEKGKVLGSGAFGTV----------YKGVWIPEGEKVkipVAIKVLREEtgpkaneeiLDEAYVMASVDHPHLVRL-LGI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  99 KDNSNLYMVMEYVPGGEMFSHLRR-IGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAK 177
Cdd:cd05057   78 CLSSQVQLITQLMPLGCLLDYVRNhRDNIGSQLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFGLAK 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 255958318 178 --RVKGRTWTLCG--TP-EYLAPEIILSKGYNKAVDWWALGVLIYE-MAAGYPPF 226
Cdd:cd05057  158 llDVDEKEYHAEGgkVPiKWMALESIQYRIYTHKSDVWSYGVTVWElMTFGAKPY 212
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
29-226 4.85e-15

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK2 plays a role in hepatic insulin signaling and glucose metabolism. It is induced by the insulin/Akt pathway as part of the hepatic refeeding reponse, and it directly phosphorylates the SR domain of PGC-1alpha, which results in decreased gluconeogenic gene expression and glucose output. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK2 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: 271117 [Multi-domain]  Cd Length: 330  Bit Score: 74.67  E-value: 4.85e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVM-LVKHKATEQYYAMKILdkqkvvklKQIEHTLNEKRIlqavEFPFLVRLEYSFKDNSNL--- 104
Cdd:cd14215   12 ERYEIVSTLGEGTFGRVVqCIDHRRGGARVALKII--------KNVEKYKEAARL----EINVLEKINEKDPENKNLcvq 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 105 ---------YMVMEY-VPGGEMFSHLRRIGRFSEP--HARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGY----- 167
Cdd:cd14215   80 mfdwfdyhgHMCISFeLLGLSTFDFLKENNYLPYPihQVRHMAFQVCQAVKFLHDNKLTHTDLKPENILFVNSDYeltyn 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255958318 168 --------------IQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPF 226
Cdd:cd14215  160 lekkrdersvkstaIRVVDFGSATFDHEHHSTIVSTRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLF 232
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
35-273 6.54e-15

Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes (or Fps) is a cytoplasmic (or nonreceptor) PTK containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated PTK activity. Fes kinase is expressed in myeloid, vascular endothelial, epithelial, and neuronal cells. It plays important roles in cell growth and differentiation, angiogenesis, inflammation and immunity, and cytoskeletal regulation. A recent study implicates Fes kinase as a tumor suppressor in colorectal cancer. The Fes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 73.43  E-value: 6.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKqiEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGG 114
Cdd:cd05084    2 ERIGRGNFGEVFSGRLRADNTPVAVKSCRETLPPDLK--AKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 115 EMFSHLRRIGrfsePHARF-----YAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKR----VKGRTWT 185
Cdd:cd05084   80 DFLTFLRTEG----PRLKVkelirMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSREeedgVYAATGG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 186 LCGTP-EYLAPEIILSKGYNKAVDWWALGVLIYE-MAAGYPPFFADQPIQIYEKIVSG-KVRFPSHFSSDLKDLLRNLLQ 262
Cdd:cd05084  156 MKQIPvKWTAPEALNYGRYSSESDVWSFGILLWEtFSLGAVPYANLSNQQTREAVEQGvRLPCPENCPDEVYRLMEQCWE 235
                        250
                 ....*....|...
gi 255958318 263 VDLTKR--FGNLK 273
Cdd:cd05084  236 YDPRKRpsFSTVH 248
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
37-224 6.75e-15

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: 73.32  E-value: 6.75e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILdKQKVVKLKQIEhtlnEKRILQAVEFPFLVR-LEYSFKDNsNLYMVMEYVPGGE 115
Cdd:cd14156    1 IGSGFFSKVYKVTHGATGKVMVVKIY-KNDVDQHKIVR----EISLLQKLSHPNIVRyLGICVKDE-KLHPILEYVSGGC 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 116 MFSHLRRIG-RFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQ---VTDFGFAKRV-------KGRTW 184
Cdd:cd14156   75 LEELLAREElPLSWREKVELACDISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGReavVTDFGLAREVgempandPERKL 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 255958318 185 TLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYP 224
Cdd:cd14156  155 SLVGSAFWMAPEMLRGEPYDRKVDVFSFGIVLCEILARIP 194
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
35-238 8.99e-15

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: 73.46  E-value: 8.99e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYYAMKI--LDKQKVVKLKQIEhtlnEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVP 112
Cdd:cd07870    6 EKLGEGSYATVYKGISRINGQLVALKVisMKTEEGVPFTAIR----EASLLKGLKHANIVLLHDIIHTKETLTFVFEYMH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 113 GGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFA--KRVKGRTWTL-CGT 189
Cdd:cd07870   82 TDLAQYMIQHPGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLAraKSIPSQTYSSeVVT 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 255958318 190 PEYLAPEIIL-SKGYNKAVDWWALGVLIYEMAAGYPPF--FADQPIQIyEKI 238
Cdd:cd07870  162 LWYRPPDVLLgATDYSSALDIWGAGCIFIEMLQGQPAFpgVSDVFEQL-EKI 212
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
30-273 1.06e-14

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: 73.15  E-value: 1.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  30 DFERKKTLGTGSFGRVmlvkHKAteQYYAmkildkQKVVKLKQIEHTLNEKriLQAveFPFLVRleySFK----DNSNLY 105
Cdd:cd14063    1 ELEIKEVIGKGRFGRV----HRG--RWHG------DVAIKLLNIDYLNEEQ--LEA--FKEEVA---AYKntrhDNLVLF 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 106 M-----------VMEYVPGGEMFSHLR-RIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDhQGYIQVTDF 173
Cdd:cd14063   62 MgacmdpphlaiVTSLCKGRTLYSLIHeRKEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLE-NGRVVITDF 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 174 GFAKRVK-------------GRTWtLCgtpeYLAPEII----------LSKGYNKAVDWWALGVLIYEMAAGYPPFFADQ 230
Cdd:cd14063  141 GLFSLSGllqpgrredtlviPNGW-LC----YLAPEIIralspdldfeESLPFTKASDVYAFGTVWYELLAGRWPFKEQP 215
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 255958318 231 PIQIYEKIVSGKVRFPSHFSS--DLKDLLRNLLQVDLTKR--FGNLK 273
Cdd:cd14063  216 AESIIWQVGCGKKQSLSQLDIgrEVKDILMQCWAYDPEKRptFSDLL 262
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
11-268 1.28e-14

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkA is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkA to its ligand, nerve growth factor (NGF), results in receptor oligomerization and activation of the catalytic domain. TrkA is expressed mainly in neural-crest-derived sensory and sympathetic neurons of the peripheral nervous system, and in basal forebrain cholinergic neurons of the central nervous system. It is critical for neuronal growth, differentiation and survival. Alternative TrkA splicing has been implicated as a pivotal regulator of neuroblastoma (NB) behavior. Normal TrkA expression is associated with better NB prognosis, while the hypoxia-regulated TrkAIII splice variant promotes NB pathogenesis and progression. Aberrant TrkA expression has also been demonstrated in non-neural tumors including prostate, breast, lung, and pancreatic cancers. The TrkA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 73.08  E-value: 1.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  11 KEDFLRKWEnpppsnagledferkktLGTGSFGRVMLVK--HKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEF 88
Cdd:cd05092    4 RRDIVLKWE-----------------LGEGAFGKVFLAEchNLLPEQDKMLVAVKALKEATESARQDFQREAELLTVLQH 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  89 PFLVRLEYSFKDNSNLYMVMEYVPGGEMFSHLRR---------------IGRFSEPHARFYAAQIVLTFEYLHSLDLIYR 153
Cdd:cd05092   67 QHIVRFYGVCTEGEPLIMVFEYMRHGDLNRFLRShgpdakildggegqaPGQLTLGQMLQIASQIASGMVYLASLHFVHR 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 154 DLKPENLLIDHQGYIQVTDFGFAK--------RVKGRTWtlcgTP-EYLAPEIILSKGYNKAVDWWALGVLIYEM-AAGY 223
Cdd:cd05092  147 DLATRNCLVGQGLVVKIGDFGMSRdiystdyyRVGGRTM----LPiRWMPPESILYRKFTTESDIWSFGVVLWEIfTYGK 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 255958318 224 PPFFADQPIQIYEKIVSGK-VRFPSHFSSDLKDLLRNLLQVDLTKR 268
Cdd:cd05092  223 QPWYQLSNTEAIECITQGReLERPRTCPPEVYAIMQGCWQREPQQR 268
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
37-249 1.47e-14

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK2 is one of two vertebrate LRRKs which show complementary expression in the brain. Mutations in LRRK2, found in the kinase, ROC-COR, and WD40 domains, are linked to both familial and sporadic forms of Parkinson's disease. The most prevalent mutation, G2019S located in the activation loop of the kinase domain, increases kinase activity. The R1441C/G mutations in the GTPase domain have also been reported to influence kinase activity. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 72.29  E-value: 1.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEqyYAMKILDKQKVVKLKQIEHTlnekrILQAVEFPFLVRLEYSfkDNSNLYMVMEYVPGGEM 116
Cdd:cd14068    2 LGDGGFGSVYRAVYRGED--VAVKIFNKHTSFRLLRQELV-----VLSHLHHPSLVALLAA--GTAPRMLVMELAPKGSL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 117 FSHLRR-IGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLI-----DHQGYIQVTDFGFAK---RVKGRtwTLC 187
Cdd:cd14068   73 DALLQQdNASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLftlypNCAIIAKIADYGIAQyccRMGIK--TSE 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255958318 188 GTPEYLAPEIilSKG---YNKAVDWWALGVLIYEMAAGyppffadqpiqiYEKIVSGkVRFPSHF 249
Cdd:cd14068  151 GTPGFRAPEV--ARGnviYNQQADVYSFGLLLYDILTC------------GERIVEG-LKFPNEF 200
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
28-239 1.50e-14

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: 73.54  E-value: 1.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  28 LEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDK--QKVVKLKQIEHTL------NEKRILQAVEfpfLVRLEYSFK 99
Cdd:cd07875   23 LKRYQNLKPIGSGAQGIVCAAYDAILERNVAIKKLSRpfQNQTHAKRAYRELvlmkcvNHKNIIGLLN---VFTPQKSLE 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 100 DNSNLYMVMEYvpggeMFSHLRRIGRFSEPHAR--FYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAk 177
Cdd:cd07875  100 EFQDVYIVMEL-----MDANLCQVIQMELDHERmsYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLA- 173
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255958318 178 RVKGRTWTLcgTPE-----YLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIV 239
Cdd:cd07875  174 RTAGTSFMM--TPYvvtryYRAPEVILGMGYKENVDIWSVGCIMGEMIKGGVLFPGTDHIDQWNKVI 238
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
29-238 1.81e-14

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: 72.76  E-value: 1.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVmlvkhkateqYYAMKILDKQKVVKLKQIEHTLNEK-------------RILQAVEFPFLVRL- 94
Cdd:cd07862    1 QQYECVAEIGEGAYGKV----------FKARDLKNGGRFVALKRVRVQTGEEgmplstirevavlRHLETFEHPNVVRLf 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  95 ---EYSFKD-NSNLYMVMEYVpGGEMFSHLRRIGRFSEPHARF--YAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYI 168
Cdd:cd07862   71 dvcTVSRTDrETKLTLVFEHV-DQDLTTYLDKVPEPGVPTETIkdMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQI 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255958318 169 QVTDFGFAK--RVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKI 238
Cdd:cd07862  150 KLADFGLARiySFQMALTSVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKPLFRGSSDVDQLGKI 221
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
34-231 2.52e-14

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: 72.33  E-value: 2.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  34 KKTLGTGSFGRVMLVK----HKATEQYYAMKILDKQKV-VKLKQIEHTLN---------EKRILQAVEFPFLVRLEYSFK 99
Cdd:cd05095   10 KEKLGEGQFGEVHLCEaegmEKFMDKDFALEVSENQPVlVAVKMLRADANknarndflkEIKIMSRLKDPNIIRLLAVCI 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 100 DNSNLYMVMEYVPGGEMFSHLRRI---GRFSEPHA---------RFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGY 167
Cdd:cd05095   90 TDDPLCMITEYMENGDLNQFLSRQqpeGQLALPSNaltvsysdlRFMAAQIASGMKYLSSLNFVHRDLATRNCLVGKNYT 169
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255958318 168 IQVTDFGFAK--------RVKGRTWtlcgTP-EYLAPEIILSKGYNKAVDWWALGVLIYEMAAgyppFFADQP 231
Cdd:cd05095  170 IKIADFGMSRnlysgdyyRIQGRAV----LPiRWMSWESILLGKFTTASDVWAFGVTLWETLT----FCREQP 234
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
35-251 2.63e-14

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: 71.82  E-value: 2.63e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYyAMKILDKQKVVKLKQIEhtlnEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGG 114
Cdd:cd05114   10 KELGSGLFGVVRLGKWRAQYKV-AIKAIREGAMSEEDFIE----EAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFMENG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 115 EMFSHLR-RIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTWT-LCGTP-- 190
Cdd:cd05114   85 CLLNYLRqRRGKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTRYVLDDQYTsSSGAKfp 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255958318 191 -EYLAPEIILSKGYNKAVDWWALGVLIYEM-AAGYPPFFADQPIQIYEKIVSGKVRFPSHFSS 251
Cdd:cd05114  165 vKWSPPEVFNYSKFSSKSDVWSFGVLMWEVfTEGKMPFESKSNYEVVEMVSRGHRLYRPKLAS 227
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
35-237 2.68e-14

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: 71.44  E-value: 2.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMlvKHKATEQYYAMKILdKQKVVKlkqiEHTLNEKRILQAVEFPFLVRLEYSFKDNSnLYMVMEYVPGG 114
Cdd:cd05083   12 EIIGEGEFGAVL--QGEYMGQKVAVKNI-KCDVTA----QAFLEETAVMTKLQHKNLVRLLGVILHNG-LYIVMELMSKG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 115 EMFSHLRRIGRFSEPHARF--YAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKrVKGRTWTLCGTP-E 191
Cdd:cd05083   84 NLVNFLRSRGRALVPVIQLlqFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFGLAK-VGSMGVDNSRLPvK 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 255958318 192 YLAPEIILSKGYNKAVDWWALGVLIYEM----AAGYPPFFADQPIQIYEK 237
Cdd:cd05083  163 WTAPEALKNKKFSSKSDVWSYGVLLWEVfsygRAPYPKMSVKEVKEAVEK 212
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
31-226 2.99e-14

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK1 has been implicated in regulating eye size, lens formation, and retinal morphogenesis during late embryogenesis. It also contributes to the regulation of haematopoiesis and leukaemogenesis by phosphorylating and repressing the transcription factor c-Myb, which is crucial in T- and B-cell development. In glucose-deprived conditions, HIPK1 phosphorylates Daxx, leading to its relocalization from the nucleus to the cytoplasm, where it binds and stabilizes ASK1 (apoptosis signal-regulating kinase 1), a mitogen-activated protein kinase (MAPK) kinase kinase that activates the JNK and p38 MAPK pathways. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 72.81  E-value: 2.99e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQ-KVVKLKQIE-HTLNEKRILQAVEFPFlVRLEYSFKDNSNLYMVM 108
Cdd:cd14228   17 YEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNHpSYARQGQIEvSILSRLSSENADEYNF-VRSYECFQHKNHTCLVF 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 109 EYVPGgEMFSHLRRiGRFSE---PHARFYAAQIVLTFEYLHSLDLIYRDLKPEN-LLID--HQGY-IQVTDFGFAKRV-K 180
Cdd:cd14228   96 EMLEQ-NLYDFLKQ-NKFSPlplKYIRPILQQVATALMKLKSLGLIHADLKPENiMLVDpvRQPYrVKVIDFGSASHVsK 173
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 255958318 181 GRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPF 226
Cdd:cd14228  174 AVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLY 219
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
37-226 3.61e-14

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: 71.41  E-value: 3.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHK----ATEQYYAMKILDKQKVvklkqiEHTLNEKRILQAVEFPFLVR-LEYSFKDNSNLYMVMEYV 111
Cdd:cd14064    1 IGSGSFGKVYKGRCRnkivAIKRYRANTYCSKSDV------DMFCREVSILCRLNHPCVIQfVGACLDDPSQFAIVTQYV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 112 PGGEMFSHLRRIGRFSEPHARF-YAAQIVLTFEYLHSLD--LIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGR----TW 184
Cdd:cd14064   75 SGGSLFSLLHEQKRVIDLQSKLiIAVDVAKGMEYLHNLTqpIIHRDLNSHNILLYEDGHAVVADFGESRFLQSLdednMT 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 255958318 185 TLCGTPEYLAPEIILSKG-YNKAVDWWALGVLIYEMAAGYPPF 226
Cdd:cd14064  155 KQPGNLRWMAPEVFTQCTrYSIKADVFSYALCLWELLTGEIPF 197
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
28-238 5.85e-14

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: 71.37  E-value: 5.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  28 LEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKI--LDKQK------VVKLKQIEHTLNEKRILQAVEFPFLVRLEYSF- 98
Cdd:cd07864    6 VDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKvrLDNEKegfpitAIREIKILRQLNHRSVVNLKEIVTDKQDALDFk 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  99 KDNSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAK- 177
Cdd:cd07864   86 KDKGAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLADFGLARl 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255958318 178 --RVKGRTWT-LCGTPEYLAPEIIL-SKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKI 238
Cdd:cd07864  166 ynSEESRPYTnKVITLWYRPPELLLgEERYGPAIDVWSCGCILGELFTKKPIFQANQELAQLELI 230
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
35-226 5.86e-14

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: 70.82  E-value: 5.86e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATeqyYAMKILdKQKVVKLKQIEHTLNEKRILQAVEFPFLVrLEYSFKDNSNLYMVMEYVPGG 114
Cdd:cd14150    6 KRIGTGSFGTVFRGKWHGD---VAVKIL-KVTEPTPEQLQAFKNEMQVLRKTRHVNIL-LFMGFMTRPNFAIITQWCEGS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 115 EMFSHLRRI-GRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIdHQGY-IQVTDFGFAKrVKGRtWT------- 185
Cdd:cd14150   81 SLYRHLHVTeTRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFL-HEGLtVKIGDFGLAT-VKTR-WSgsqqveq 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 255958318 186 LCGTPEYLAPEIILSKG---YNKAVDWWALGVLIYEMAAGYPPF 226
Cdd:cd14150  158 PSGSILWMAPEVIRMQDtnpYSFQSDVYAYGVVLYELMSGTLPY 201
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
17-227 6.41e-14

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: 71.03  E-value: 6.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  17 KWENPppsnaglEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILdkqKVVKLKQIehtLNEKRILQAVE-FPFLVRLE 95
Cdd:cd14132   13 EWGSQ-------DDYEIIRKIGRGKYSEVFEGINIGNNEKVVIKVL---KPVKKKKI---KREIKILQNLRgGPNIVKLL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  96 YSFKD-NSNLY-MVMEYVPGgEMFSHLrrIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGY-IQVTD 172
Cdd:cd14132   80 DVVKDpQSKTPsLIFEYVNN-TDFKTL--YPTLTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMIDHEKRkLRLID 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255958318 173 FGFAK----------RVkgrtwtlcGTPEYLAPEIILS-KGYNKAVDWWALGVLIYEMAAGYPPFF 227
Cdd:cd14132  157 WGLAEfyhpgqeynvRV--------ASRYYKGPELLVDyQYYDYSLDMWSLGCMLASMIFRKEPFF 214
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
35-241 6.52e-14

Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Tec-like subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases form the second largest subfamily of nonreceptor PTKs and are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. Tec kinases play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. Mutations in Btk cause the severe B-cell immunodeficiency, X-linked agammaglobulinaemia (XLA). The Tec-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 70.55  E-value: 6.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYyAMKILDKQKVVKLKQIEhtlnEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGG 114
Cdd:cd05059   10 KELGSGQFGVVHLGKWRGKIDV-AIKMIKEGSMSEDDFIE----EAKVMMKLSHPKLVQLYGVCTKQRPIFIVTEYMANG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 115 EMFSHLR-RIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTWTLC-GTP-- 190
Cdd:cd05059   85 CLLNYLReRRGKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLARYVLDDEYTSSvGTKfp 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 255958318 191 -EYLAPEIILSKGYNKAVDWWALGVLIYEM-AAGYPPFFADQPIQIYEKIVSG 241
Cdd:cd05059  165 vKWSPPEVFMYSKFSSKSDVWSFGVLMWEVfSEGKMPYERFSNSEVVEHISQG 217
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
37-285 8.29e-14

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: 70.85  E-value: 8.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQiEHTLNEKRILQAVEFPFLVRL----EYSFKDNSNLYMVMEYVP 112
Cdd:cd14030   33 IGRGSFKTVYKGLDTETTVEVAWCELQDRKLSKSER-QRFKEEAGMLKGLQHPNIVRFydswESTVKGKKCIVLVTELMT 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 113 GGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLD--LIYRDLKPENLLIDH-QGYIQVTDFGFAKRVKGR-TWTLCG 188
Cdd:cd14030  112 SGTLKTYLKRFKVMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGpTGSVKIGDLGLATLKRASfAKSVIG 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 189 TPEYLAPEIILSKgYNKAVDWWALGVLIYEMAAG-YPPFFADQPIQIYEKIVSG-------KVRFPshfssDLKDLLRNL 260
Cdd:cd14030  192 TPEFMAPEMYEEK-YDESVDVYAFGMCMLEMATSeYPYSECQNAAQIYRRVTSGvkpasfdKVAIP-----EVKEIIEGC 265
                        250       260
                 ....*....|....*....|....*
gi 255958318 261 LQVDLTKRFgnlknGVSDIKTHKWF 285
Cdd:cd14030  266 IRQNKDERY-----AIKDLLNHAFF 285
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
31-238 8.56e-14

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 partners with all three D-type cyclins (D1, D2, and D3) and is also regulated by INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein and plays a role in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the nucleus. CDK4 also shows kinase activity towards Smad3, a signal transducer of TGF-beta signaling which modulates transcription and plays a role in cell proliferation and apoptosis. CDK4 is inhibited by the p21 inhibitor and is specifically mutated in human melanoma. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143368 [Multi-domain]  Cd Length: 288  Bit Score: 70.76  E-value: 8.56e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMK---ILDKQKVVKLKQIEHTLNEKRiLQAVEFPFLVRL-----EYSFKDNS 102
Cdd:cd07863    2 YEPVAEIGVGAYGTVYKARDPHSGHFVALKsvrVQTNEDGLPLSTVREVALLKR-LEAFDHPNIVRLmdvcaTSRTDRET 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 103 NLYMVMEYVpGGEMFSHLRRIGRFSEP--HARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVk 180
Cdd:cd07863   81 KVTLVFEHV-DQDLRTYLDKVPPPGLPaeTIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLARIY- 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255958318 181 grTWTLCGTPE-----YLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFF----ADQPIQIYEKI 238
Cdd:cd07863  159 --SCQMALTPVvvtlwYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCgnseADQLGKIFDLI 223
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
37-241 1.09e-13

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP1 harbors a C-terminal Death domain (DD), which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 can also recruit other kinases including MEKK1, MEKK3, and RIP3 through an intermediate domain (ID) that bears a RIP homotypic interaction motif (RHIM). RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accummulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. RIP kinases serve as essential sensors of cellular stress. The RIP1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 70.22  E-value: 1.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKaTEQYYAMKILDKQKVVKLKQiEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGGEM 116
Cdd:cd14027    1 LDSGGFGKVSLCFHR-TQGLVVLKTVYTGPNCIEHN-EALLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKGNL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 117 FSHLRRIGRFSEPHARFYAaQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFA----------------KRVK 180
Cdd:cd14027   79 MHVLKKVSVPLSVKGRIIL-EIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwskltkeehneqREVD 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255958318 181 GRTWTLCGTPEYLAPEIILS---KGYNKAvDWWALGVLIYEMAAGYPPF-FADQPIQIYEKIVSG 241
Cdd:cd14027  158 GTAKKNAGTLYYMAPEHLNDvnaKPTEKS-DVYSFAIVLWAIFANKEPYeNAINEDQIIMCIKSG 221
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
29-226 1.15e-13

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK3 is predominantly expressed in mature spermatozoa, and might play a role in the fertilization process. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK3 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: 271116 [Multi-domain]  Cd Length: 331  Bit Score: 70.81  E-value: 1.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVM-LVKHKATEQYYAMKILdkQKVVKLKQIEHtlnekrilqaVEFPFLVRLEYSFKDNSNLYMV 107
Cdd:cd14214   13 ERYEIVGDLGEGTFGKVVeCLDHARGKSQVALKII--RNVGKYREAAR----------LEINVLKKIKEKDKENKFLCVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 108 ME--YVPGGEMFSHLRRIGR-------------FSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGY----- 167
Cdd:cd14214   81 MSdwFNFHGHMCIAFELLGKntfeflkennfqpYPLPHIRHMAYQLCHALKFLHENQLTHTDLKPENILFVNSEFdtlyn 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255958318 168 --------------IQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPF 226
Cdd:cd14214  161 esksceeksvkntsIRVADFGSATFDHEHHTTIVATRHYRPPEVILELGWAQPCDVWSLGCILFEYYRGFTLF 233
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
35-226 1.18e-13

Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TEY subtype of plant MAPKs and is further subdivided into three groups (A, B, and C). Group A is represented by AtMPK3, AtMPK6, Nicotiana tabacum BTF4 (NtNTF4), among others. They are mostly involved in environmental and hormonal responses. AtMPK3 and AtMPK6 are also key regulators for stomatal development and patterning. Group B is represented by AtMPK4, AtMPK13, and NtNTF6, among others. They may be involved in both cell division and environmental stress response. AtMPK4 also participates in regulating innate immunity. Group C is represented by AtMPK1, AtMPK2, NtNTF3, Oryza sativa MAPK4 (OsMAPK4), among others. They may also be involved in stress responses. AtMPK1 and AtMPK2 are activated following mechanical injury and in the presence of stress chemicals such as jasmonic acid, hydrogen peroxide and abscisic acid. OsMAPK4 is also called OsMSRMK3 for Multiple Stress-Responsive MAPK3. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20. The TEY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 70.86  E-value: 1.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYYAMK--------ILD-KQKVVKLKQIEHTLNEKRI-LQAVEFPFLVRleySFKDnsnL 104
Cdd:cd07858   11 KPIGRGAYGIVCSAKNSETNEKVAIKkianafdnRIDaKRTLREIKLLRHLDHENVIaIKDIMPPPHRE---AFND---V 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 105 YMVMEYvpggeMFSHLRRIGRFSEP----HARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAkRVK 180
Cdd:cd07858   85 YIVYEL-----MDTDLHQIIRSSQTlsddHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLA-RTT 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 255958318 181 GRTW----TLCGTPEYLAPEIILS-KGYNKAVDWWALGVLIYEMAAGYPPF 226
Cdd:cd07858  159 SEKGdfmtEYVVTRWYRAPELLLNcSEYTTAIDVWSVGCIFAELLGRKPLF 209
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
28-262 1.21e-13

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: 70.83  E-value: 1.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  28 LEDFERKKTLGTGSFGRVMlvkhKATEQYYAMKILDKQKVVKLKQIEHTLNEKR---ILQAVEFPFLVRL------EYSF 98
Cdd:cd07876   20 LKRYQQLKPIGSGAQGIVC----AAFDTVLGINVAVKKLSRPFQNQTHAKRAYRelvLLKCVNHKNIISLlnvftpQKSL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  99 KDNSNLYMVMEYvpggeMFSHLRRIGRFSEPHAR--FYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFA 176
Cdd:cd07876   96 EEFQDVYLVMEL-----MDANLCQVIHMELDHERmsYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLA 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 177 kRVKGRTWTLCG---TPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDL 253
Cdd:cd07876  171 -RTACTNFMMTPyvvTRYYRAPEVILGMGYKENVDIWSVGCIMGELVKGSVIFQGTDHIDQWNKVIEQLGTPSAEFMNRL 249

                 ....*....
gi 255958318 254 KDLLRNLLQ 262
Cdd:cd07876  250 QPTVRNYVE 258
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
37-226 1.40e-13

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: 69.85  E-value: 1.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKildkqKVvklkQIEH-TLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGGE 115
Cdd:cd13991   14 IGRGSFGEVHRMEDKQTGFQCAVK-----KV----RLEVfRAEELMACAGLTSPRVVPLYGAVREGPWVNIFMDLKEGGS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 116 MFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQG-YIQVTDFGFAKRVKGRTWTLC------- 187
Cdd:cd13991   85 LGQLIKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGsDAFLCDFGHAECLDPDGLGKSlftgdyi 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 255958318 188 -GTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPF 226
Cdd:cd13991  165 pGTETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGCHPW 204
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
135-222 1.51e-13

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


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 69.44  E-value: 1.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 135 AAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTWTLCGTPEYLAPEiILSKGYNKAVDWWALGV 214
Cdd:cd13975  108 ALDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGFCKPEAMMSGSIVGTPIHMAPE-LFSGKYDNSVDVYAFGI 186

                 ....*...
gi 255958318 215 LIYEMAAG 222
Cdd:cd13975  187 LFWYLCAG 194
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
28-262 1.59e-13

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


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 70.50  E-value: 1.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  28 LEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDK--------QKVVKLKQIEHTLNEKRILQAVEfpfLVRLEYSFK 99
Cdd:cd07874   16 LKRYQNLKPIGSGAQGIVCAAYDAVLDRNVAIKKLSRpfqnqthaKRAYRELVLMKCVNHKNIISLLN---VFTPQKSLE 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 100 DNSNLYMVMEYvpggeMFSHLRRIGRFSEPHAR--FYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAk 177
Cdd:cd07874   93 EFQDVYLVMEL-----MDANLCQVIQMELDHERmsYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLA- 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 178 RVKGRTWTLCG---TPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLK 254
Cdd:cd07874  167 RTAGTSFMMTPyvvTRYYRAPEVILGMGYKENVDIWSVGCIMGEMVRHKILFPGRDYIDQWNKVIEQLGTPCPEFMKKLQ 246

                 ....*...
gi 255958318 255 DLLRNLLQ 262
Cdd:cd07874  247 PTVRNYVE 254
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
38-285 1.61e-13

Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK8, CDC2L6, and similar proteins. CDK8 functions as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II-dependent transcription. CDC2L6 also associates with Mediator in complexes lacking CDK8. In VP16-dependent transcriptional activation, CDK8 and CDC2L6 exerts opposing effects by positive and negative regulation, respectively, in similar conditions. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 70.01  E-value: 1.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  38 GTGSFGRVmlvkHKATeqyyaMKILDKQKVVKLKQIE-----------HTLNEKRILQAVEFPFLVRLEYSFKDNSN--L 104
Cdd:cd07842    9 GRGTYGRV----YKAK-----RKNGKDGKEYAIKKFKgdkeqytgisqSACREIALLRELKHENVVSLVEVFLEHADksV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 105 YMVMEYVPG--GEMFSHLRRIGRFSEPHARFYAA--QIVLTFEYLHSLDLIYRDLKPENLLI----DHQGYIQVTDFGFA 176
Cdd:cd07842   80 YLLFDYAEHdlWQIIKFHRQAKRVSIPPSMVKSLlwQILNGIHYLHSNWVLHRDLKPANILVmgegPERGVVKIGDLGLA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 177 KRVKGRTWTLCG------TPEYLAPEIIL-SKGYNKAVDWWALGVLIYEMAAGYPPFFADQ-------PIQI--YEKIVS 240
Cdd:cd07842  160 RLFNAPLKPLADldpvvvTIWYRAPELLLgARHYTKAIDIWAIGCIFAELLTLEPIFKGREakikksnPFQRdqLERIFE 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 241 ----------------------GKVRFPSHF---------------SSDLKDLLRNLLQVDLTKRFgnlknGVSDIKTHK 283
Cdd:cd07842  240 vlgtptekdwpdikkmpeydtlKSDTKASTYpnsllakwmhkhkkpDSQGFDLLRKLLEYDPTKRI-----TAEEALEHP 314

                 ..
gi 255958318 284 WF 285
Cdd:cd07842  315 YF 316
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
35-268 1.74e-13

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: 69.99  E-value: 1.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVmlVKHKATE-------QYYAMKILDKQKvvKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMV 107
Cdd:cd05045    6 KTLGEGEFGKV--VKATAFRlkgragyTTVAVKMLKENA--SSSELRDLLSEFNLLKQVNHPHVIKLYGACSQDGPLLLI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 108 MEYVPGGEMFSHLR---RIG-------------RFSEPHARFYAAQIVLTF--------EYLHSLDLIYRDLKPENLLID 163
Cdd:cd05045   82 VEYAKYGSLRSFLResrKVGpsylgsdgnrnssYLDNPDERALTMGDLISFawqisrgmQYLAEMKLVHRDLAARNVLVA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 164 HQGYIQVTDFG----------FAKRVKGRTwtlcgTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAA-GYPPFFADQPI 232
Cdd:cd05045  162 EGRKMKISDFGlsrdvyeedsYVKRSKGRI-----PVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIAPE 236
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 255958318 233 QIYEKIVSG-KVRFPSHFSSDLKDLLRNLLQVDLTKR 268
Cdd:cd05045  237 RLFNLLKTGyRMERPENCSEEMYNLMLTCWKQEPDKR 273
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
33-274 1.77e-13

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: 69.62  E-value: 1.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  33 RKKTLGTGSFGRV---MLVKHKATEQYYAMKILDKQKVVKLKQieHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVME 109
Cdd:cd05063    9 KQKVIGAGEFGEVfrgILKMPGRKEVAVAIKTLKPGYTEKQRQ--DFLSEASIMGQFSHHNIIRLEGVVTKFKPAMIITE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 110 YVPGGEMFSHLR-RIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKG---RTWT 185
Cdd:cd05063   87 YMENGALDKYLRdHDGEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSRVLEDdpeGTYT 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 186 LCGTP---EYLAPEIILSKGYNKAVDWWALGVLIYE-MAAGYPPFFaDQPIQIYEKIVSGKVRFPSHFS--SDLKDLLRN 259
Cdd:cd05063  167 TSGGKipiRWTAPEAIAYRKFTSASDVWSFGIVMWEvMSFGERPYW-DMSNHEVMKAINDGFRLPAPMDcpSAVYQLMLQ 245
                        250
                 ....*....|....*..
gi 255958318 260 LLQVDLTKR--FGNLKN 274
Cdd:cd05063  246 CWQQDRARRprFVDIVN 262
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
35-268 1.97e-13

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: 69.58  E-value: 1.97e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVM---LVKHKATEQYYAMKILdKQKVVKLKQIEHTLNEKRILQAVEFPFLVRL-----EYSFKDNSNLYM 106
Cdd:cd14204   13 KVLGEGEFGSVMegeLQQPDGTNHKVAVKTM-KLDNFSQREIEEFLSEAACMKDFNHPNVIRLlgvclEVGSQRIPKPMV 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 107 VMEYVPGGEMFSHLRRIGRFSEPhaRFYAAQIVLTF--------EYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKR 178
Cdd:cd14204   92 ILPFMKYGDLHSFLLRSRLGSGP--QHVPLQTLLKFmidialgmEYLSSRNFLHRDLAARNCMLRDDMTVCVADFGLSKK 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 179 VKG----RTWTLCGTP-EYLAPEIILSKGYNKAVDWWALGVLIYEMAA-GYPPFFADQPIQIYEKIVSG-KVRFPSHFSS 251
Cdd:cd14204  170 IYSgdyyRQGRIAKMPvKWIAVESLADRVYTVKSDVWAFGVTMWEIATrGMTPYPGVQNHEIYDYLLHGhRLKQPEDCLD 249
                        250
                 ....*....|....*..
gi 255958318 252 DLKDLLRNLLQVDLTKR 268
Cdd:cd14204  250 ELYDIMYSCWRSDPTDR 266
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
30-268 2.34e-13

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


Pssm-ID: 270953 [Multi-domain]  Cd Length: 275  Bit Score: 69.35  E-value: 2.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  30 DFERKKTLGTGSFGRVMLVKHKATEQYYAMKildKQKvvklKQIEHTLNEKRILQAV-------EFPFLVRLEYSFKDNS 102
Cdd:cd14051    1 EFHEVEKIGSGEFGSVYKCINRLDGCVYAIK---KSK----KPVAGSVDEQNALNEVyahavlgKHPHVVRYYSAWAEDD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 103 NLYMVMEYVPGGEMF----SHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVT------- 171
Cdd:cd14051   74 HMIIQNEYCNGGSLAdaisENEKAGERFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIFISRTPNPVSSeeeeedf 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 172 -----------------DFGFAKRVKGRTwTLCGTPEYLAPEiILSKGYN---KAvDWWALGVLIYEMAAGYP-PFFADQ 230
Cdd:cd14051  154 egeednpesnevtykigDLGHVTSISNPQ-VEEGDCRFLANE-ILQENYShlpKA-DIFALALTVYEAAGGGPlPKNGDE 230
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 255958318 231 piqiYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKR 268
Cdd:cd14051  231 ----WHEIRQGNLPPLPQCSPEFNELLRSMIHPDPEKR 264
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
35-248 2.52e-13

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: 69.03  E-value: 2.52e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKA-----TEQYYAMKILDKQKVvklkqiEHTLNEKR----ILQAVEFPFLVRLEYSFKDNSNLY 105
Cdd:cd05046   11 TTLGRGEFGEVFLAKAKGieeegGETLVLVKALQKTKD------ENLQSEFRreldMFRKLSHKNVVRLLGLCREAEPHY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 106 MVMEYVPGGEMFSHLR---------RIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFA 176
Cdd:cd05046   85 MILEYTDLGDLKQFLRatkskdeklKPPPLSTKQKVALCTQIALGMDHLSNARFVHRDLAARNCLVSSQREVKVSLLSLS 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 177 KRVKGR-------TWTlcgtP-EYLAPEIILSKGYNKAVDWWALGVLIYEM-AAGYPPFFADQPIQIYEKIVSGKVRFPS 247
Cdd:cd05046  165 KDVYNSeyyklrnALI----PlRWLAPEAVQEDDFSTKSDVWSFGVLMWEVfTQGELPFYGLSDEEVLNRLQAGKLELPV 240

                 .
gi 255958318 248 H 248
Cdd:cd05046  241 P 241
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
87-268 2.57e-13

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


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 68.84  E-value: 2.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  87 EFPFLVRLEYSFKDNSNLYMVME--------YVPGGEMFSHLRRIGRfsEPHARFYaaQIVLTFEYLHSLDLIYRDLKPE 158
Cdd:cd13982   53 EHPNVIRYFCTEKDRQFLYIALElcaaslqdLVESPRESKLFLRPGL--EPVRLLR--QIASGLAHLHSLNIVHRDLKPQ 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 159 NLLID-----HQGYIQVTDFGFAKRVK------GRTWTLCGTPEYLAPEIILS---KGYNKAVDWWALGVLI-YEMAAGY 223
Cdd:cd13982  129 NILIStpnahGNVRAMISDFGLCKKLDvgrssfSRRSGVAGTSGWIAPEMLSGstkRRQTRAVDIFSLGCVFyYVLSGGS 208
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 255958318 224 PPFfaDQPIQIYEKIVSGKVRFPS-----HFSSDLKDLLRNLLQVDLTKR 268
Cdd:cd13982  209 HPF--GDKLEREANILKGKYSLDKllslgEHGPEAQDLIERMIDFDPEKR 256
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
30-226 2.64e-13

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: 69.67  E-value: 2.64e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  30 DFERKKTLGTGSFGRVmlvkhkateqYYAMKILDKQKV---VKLKQI---------EHTLNEKRILQAVEFPFLVRLeYS 97
Cdd:cd05108    8 EFKKIKVLGSGAFGTV----------YKGLWIPEGEKVkipVAIKELreatspkanKEILDEAYVMASVDNPHVCRL-LG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  98 FKDNSNLYMVMEYVPGGEMFSHLRR-IGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFA 176
Cdd:cd05108   77 ICLTSTVQLITQLMPFGCLLDYVREhKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLA 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 255958318 177 KRVKG--RTWTLCG--TP-EYLAPEIILSKGYNKAVDWWALGVLIYE-MAAGYPPF 226
Cdd:cd05108  157 KLLGAeeKEYHAEGgkVPiKWMALESILHRIYTHQSDVWSYGVTVWElMTFGSKPY 212
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
18-219 3.75e-13

Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristylation sites (Srm) and Breast tumor kinase (Brk); PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Srm and Brk (also called protein tyrosine kinase 6) are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Brk has been found to be overexpressed in a majority of breast tumors. Src kinases in general contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr; they are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Srm and Brk however, lack the N-terminal myristylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. The Srm/Brk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133248 [Multi-domain]  Cd Length: 261  Bit Score: 68.23  E-value: 3.75e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  18 WENPPpsnaglEDFERKKTLGTGSFGRVMLVKHKATEQYyAMKILDKQKVVKLKQIEhtlNEKRILQAVEFPFLVRLEYS 97
Cdd:cd05148    1 WERPR------EEFTLERKLGSGYFGEVWEGLWKNRVRV-AIKILKSDDLLKQQDFQ---KEVQALKRLRHKHLISLFAV 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  98 FKDNSNLYMVMEYVPGGEMFSHLRRI-GR-FSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGF 175
Cdd:cd05148   71 CSVGEPVYIITELMEKGSLLAFLRSPeGQvLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGL 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 255958318 176 AKRVKGRTWTLCGTP---EYLAPEIILSKGYNKAVDWWALGVLIYEM 219
Cdd:cd05148  151 ARLIKEDVYLSSDKKipyKWTAPEAASHGTFSTKSDVWSFGILLYEM 197
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
31-235 4.37e-13

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK5 is unusual in that it is regulated by non-cyclin proteins, p35 and p39. It is highly expressed in the nervous system and is critical in normal neural development and function. It plays a role in neuronal migration and differentiation, and is also important in synaptic plasticity and learning. CDK5 also participates in protecting against cell death and promoting angiogenesis. Impaired CDK5 activity is implicated in Alzheimer's disease, amyotrophic lateral sclerosis, Parkinson's disease, Huntington's disease and acute neuronal injury. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 68.61  E-value: 4.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMK---ILDKQKVVKlkqiEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMV 107
Cdd:cd07839    2 YEKLEKIGEGTYGTVFKAKNRETHEIVALKrvrLDDDDEGVP----SSALREICLLKELKHKNIVRLYDVLHSDKKLTLV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 108 MEYVPGG--EMFSHLRriGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKR----VKg 181
Cdd:cd07839   78 FEYCDQDlkKYFDSCN--GDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARAfgipVR- 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255958318 182 rtwtlCGTPE-----YLAPEIIL-SKGYNKAVDWWALGVLIYEMAAGYPPFF-----ADQPIQIY 235
Cdd:cd07839  155 -----CYSAEvvtlwYRPPDVLFgAKLYSTSIDMWSAGCIFAELANAGRPLFpgndvDDQLKRIF 214
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
31-219 5.20e-13

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: 68.42  E-value: 5.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKA----TEQYYAMKILDKQKvvKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDN--SNL 104
Cdd:cd05079    6 LKRIRDLGEGHFGKVELCRYDPegdnTGEQVAVKSLKPES--GGNHIADLKKEIEILRNLYHENIVKYKGICTEDggNGI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 105 YMVMEYVPGGEMFSHL-RRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRT 183
Cdd:cd05079   84 KLIMEFLPSGSLKEYLpRNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDK 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 255958318 184 --WTL---CGTPEY-LAPEIILSKGYNKAVDWWALGVLIYEM 219
Cdd:cd05079  164 eyYTVkddLDSPVFwYAPECLIQSKFYIASDVWSFGVTLYEL 205
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
29-280 5.41e-13

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: 68.22  E-value: 5.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVmlvkHKATeqyYAMKILDKQKV-VKLKQIEHT-------LNEKRILQAVEFPFLVRLEYSFKD 100
Cdd:cd05056    6 EDITLGRCIGEGQFGDV----YQGV---YMSPENEKIAVaVKTCKNCTSpsvrekfLQEAYIMRQFDHPHIVKLIGVITE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 101 NSnLYMVMEYVPGGEMFSHLRRiGRFSEPHARF--YAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKR 178
Cdd:cd05056   79 NP-VWIVMELAPLGELRSYLQV-NKYSLDLASLilYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLSRY 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 179 VKGRTW---TLCGTP-EYLAPEIILSKGYNKAVDWWALGVLIYE-MAAGYPPFFADQPIQIYEKIVSG-KVRFPSHFSSD 252
Cdd:cd05056  157 MEDESYykaSKGKLPiKWMAPESINFRRFTSASDVWMFGVCMWEiLMLGVKPFQGVKNNDVIGRIENGeRLPMPPNCPPT 236
                        250       260       270
                 ....*....|....*....|....*....|
gi 255958318 253 LKDLLRNLLQVDLTKR--FGNLKNGVSDIK 280
Cdd:cd05056  237 LYSLMTKCWAYDPSKRprFTELKAQLSDIL 266
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
31-226 7.05e-13

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK1 plays a role in neuronal differentiation. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK1/4 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: 271115 [Multi-domain]  Cd Length: 330  Bit Score: 68.34  E-value: 7.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVM-LVKHKATEQYYAMKILD------KQKVVKLKQIEH--TLNEKRILQAVEFpflvrLEYsFKDN 101
Cdd:cd14213   14 YEIVDTLGEGAFGKVVeCIDHKMGGMHVAVKIVKnvdryrEAARSEIQVLEHlnTTDPNSTFRCVQM-----LEW-FDHH 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 102 SNLYMVMEYVpGGEMFSHLRRIG--RFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGY------------ 167
Cdd:cd14213   88 GHVCIVFELL-GLSTYDFIKENSflPFPIDHIRNMAYQICKSVNFLHHNKLTHTDLKPENILFVQSDYvvkynpkmkrde 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255958318 168 -------IQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPF 226
Cdd:cd14213  167 rtlknpdIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVF 232
PTZ00284 PTZ00284
protein kinase; Provisional
37-222 8.14e-13

protein kinase; Provisional


Pssm-ID: 140307 [Multi-domain]  Cd Length: 467  Bit Score: 68.84  E-value: 8.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKIL-DKQKVVKLKQIEHTLNEKRILQAVE--FPFLVRLEYSFKDNSNLYMVM-EYVP 112
Cdd:PTZ00284 137 LGEGTFGKVVEAWDRKRKEYCAVKIVrNVPKYTRDAKIEIQFMEKVRQADPAdrFPLMKIQRYFQNETGHMCIVMpKYGP 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 113 GgeMFSHLRRIGRFSEPHArfyaAQIVL----TFEYLHS-LDLIYRDLKPENLLIDHQGY----------------IQVT 171
Cdd:PTZ00284 217 C--LLDWIMKHGPFSHRHL----AQIIFqtgvALDYFHTeLHLMHTDLKPENILMETSDTvvdpvtnralppdpcrVRIC 290
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 255958318 172 DFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAG 222
Cdd:PTZ00284 291 DLGGCCDERHSRTAIVSTRHYRSPEVVLGLGWMYSTDMWSMGCIIYELYTG 341
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
31-219 8.51e-13

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: 67.62  E-value: 8.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHK----ATEQYYAMKILDKQKVVKLKqiEHTLNEKRILQAVEFPFLVRLEYSFKDNSN--L 104
Cdd:cd05080    6 LKKIRDLGEGHFGKVSLYCYDptndGTGEMVAVKALKADCGPQHR--SGWKQEIDILKTLYHENIVKYKGCCSEQGGksL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 105 YMVMEYVPGGEMFSHLRRiGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKG--- 181
Cdd:cd05080   84 QLIMEYVPLGSLRDYLPK-HSIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAKAVPEghe 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 255958318 182 --RTWTLCGTPEY-LAPEIILSKGYNKAVDWWALGVLIYEM 219
Cdd:cd05080  163 yyRVREDGDSPVFwYAPECLKEYKFYYASDVWSFGVTLYEL 203
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
37-174 9.92e-13

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: 64.39  E-value: 9.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHtlnEKRILQAVEFPFL--VRLEYSFKDNSNLYMVMEYVPGG 114
Cdd:cd13968    1 MGEGASAKVFWAEGECTTIGVAVKIGDDVNNEEGEDLES---EMDILRRLKGLELniPKVLVTEDVDGPNILLMELVKGG 77
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 115 EMFSHLRrIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFG 174
Cdd:cd13968   78 TLIAYTQ-EEELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
37-226 1.05e-12

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: 67.28  E-value: 1.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVM--LVKHKATEQYYAMKILDKQ--KVVKlkqiEHTLNEKRILQAVEFPFLVRLeYSFKDNSNLYMVMEYVP 112
Cdd:cd05115   12 LGSGNFGCVKkgVYKMRKKQIDVAIKVLKQGneKAVR----DEMMREAQIMHQLDNPYIVRM-IGVCEAEALMLVMEMAS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 113 GGEMFSHLR-RIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRV-------KGRT- 183
Cdd:cd05115   87 GGPLNKFLSgKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFGLSKALgaddsyyKARSa 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 255958318 184 --WTLcgtpEYLAPEIILSKGYNKAVDWWALGVLIYE-MAAGYPPF 226
Cdd:cd05115  167 gkWPL----KWYAPECINFRKFSSRSDVWSYGVTMWEaFSYGQKPY 208
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
30-246 1.13e-12

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


Pssm-ID: 270684 [Multi-domain]  Cd Length: 279  Bit Score: 67.36  E-value: 1.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  30 DFERKKTLGTGSFGRVM----LVKHKATEQYYAMKILDKQKVVKLKQieHTLNEKRILQAVEFPFLVRLeYSFKDNSNLY 105
Cdd:cd05109    8 ELKKVKVLGSGAFGTVYkgiwIPDGENVKIPVAIKVLRENTSPKANK--EILDEAYVMAGVGSPYVCRL-LGICLTSTVQ 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 106 MVMEYVPGGEMFSHLRR-IGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAK--RVKGR 182
Cdd:cd05109   85 LVTQLMPYGCLLDYVREnKDRIGSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPNHVKITDFGLARllDIDET 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255958318 183 TWTLCG--TP-EYLAPEIILSKGYNKAVDWWALGVLIYE-MAAGYPPFFADQPIQIYEKIVSGKvRFP 246
Cdd:cd05109  165 EYHADGgkVPiKWMALESILHRRFTHQSDVWSYGVTVWElMTFGAKPYDGIPAREIPDLLEKGE-RLP 231
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
37-241 1.19e-12

Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of RIP4, ankyrin (ANK) repeat and kinase domain containing 1 (ANKK1), and similar proteins, all of which harbor C-terminal ANK repeats. RIP4, also called Protein Kinase C-associated kinase (PKK), regulates keratinocyte differentiation and cutaneous inflammation. It activates NF-kappaB and is important in the survival of diffuse large B-cell lymphoma cells. The ANKK1 protein, also called PKK2, has not been studied extensively. The ANKK1 gene, located less than 10kb downstream of the D2 dopamine receptor (DRD2) locus, is altered in the Taq1 A1 polymorphism, which is related to a reduced DRD2 binding affinity and consequently, to mental disorders. The RIP4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 67.13  E-value: 1.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMK-----ILDKQKVVKLkqiehtLNEKRILQAVEFPFLVRLEYSFKDNSNLymVMEYV 111
Cdd:cd14025    4 VGSGGFGQVYKVRHKHWKTWLAIKcppslHVDDSERMEL------LEEAKKMEMAKFRHILPVYGICSEPVGL--VMEYM 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 112 PGGEMFSHLRrigrfSEP---HARFYAA-QIVLTFEYLHSLD--LIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTW- 184
Cdd:cd14025   76 ETGSLEKLLA-----SEPlpwELRFRIIhETAVGMNFLHCMKppLLHLDLKPANILLDAHYHVKISDFGLAKWNGLSHSh 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255958318 185 -----TLCGTPEYLAPEIIL--SKGYNKAVDWWALGVLIYEMAAGYPPFFADQPI-QIYEKIVSG 241
Cdd:cd14025  151 dlsrdGLRGTIAYLPPERFKekNRCPDTKHDVYSFAIVIWGILTQKKPFAGENNIlHIMVKVVKG 215
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
35-268 2.01e-12

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: 66.09  E-value: 2.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYyAMKILDKQKVVKlkqiEHTLNEKRILQAVEFPFLVRLeYSFKDNSNLYMVMEYVPGG 114
Cdd:cd14203    1 VKLGQGCFGEVWMGTWNGTTKV-AIKTLKPGTMSP----EAFLEEAQIMKKLRHDKLVQL-YAVVSEEPIYIVTEFMSKG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 115 EMFSHLRR-IGRFSE-PHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTWTLCGTPEY 192
Cdd:cd14203   75 SLLDFLKDgEGKYLKlPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTARQGAKF 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 193 ----LAPEIILSKGYNKAVDWWALGVLIYEMAA-GYPPFFADQPIQIYEKIVSG-KVRFPSHFSSDLKDLLRNLLQVDLT 266
Cdd:cd14203  155 pikwTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMNNREVLEQVERGyRMPCPPGCPESLHELMCQCWRKDPE 234

                 ..
gi 255958318 267 KR 268
Cdd:cd14203  235 ER 236
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
17-272 2.48e-12

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR1 (or Flt1) binds VEGFA, VEGFB, and placenta growth factor (PLGF). It regulates monocyte and macrophage migration, vascular permeability, haematopoiesis, and the recruitment of haematopietic progenitor cells from the bone marrow. VEGFR1 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 66.95  E-value: 2.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  17 KWEnpppsnAGLEDFERKKTLGTGSFGRVML-----VKHKATEQYYAMKILD--------KQKVVKLK---QIEHTLNEK 80
Cdd:cd14207    1 KWE------FARERLKLGKSLGRGAFGKVVQasafgIKKSPTCRVVAVKMLKegataseyKALMTELKiliHIGHHLNVV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  81 RILQAVEF---PFLVRLEYS--------FKDNSNLYMV--------------------------MEYVPGGEMFSH---- 119
Cdd:cd14207   75 NLLGACTKsggPLMVIVEYCkygnlsnyLKSKRDFFVTnkdtslqeelikekkeaeptggkkkrLESVTSSESFASsgfq 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 120 ----LRRIGRFSEPHARFY------------AAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRV-KGR 182
Cdd:cd14207  155 edksLSDVEEEEEDSGDFYkrpltmedlisySFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLARDIyKNP 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 183 TWTLCGTP----EYLAPEIILSKGYNKAVDWWALGVLIYEM----AAGYPPFFADQpiQIYEKIVSG-KVRFPSHFSSDL 253
Cdd:cd14207  235 DYVRKGDArlplKWMAPESIFDKIYSTKSDVWSYGVLLWEIfslgASPYPGVQIDE--DFCSKLKEGiRMRAPEFATSEI 312
                        330       340
                 ....*....|....*....|....*...
gi 255958318 254 KDLLRNLLQVD---------LTKRFGNL 272
Cdd:cd14207  313 YQIMLDCWQGDpnerprfseLVERLGDL 340
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
37-226 2.80e-12

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: 66.73  E-value: 2.80e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKildkqkvvKLKQI-EHTLNEKRILQAVEFPFLVR-----------LEYSFKDNSNL 104
Cdd:cd07859    8 IGKGSYGVVCSAIDTHTGEKVAIK--------KINDVfEHVSDATRILREIKLLRLLRhpdiveikhimLPPSRREFKDI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 105 YMVMEYvpggeMFSHLRRIGR----FSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVK 180
Cdd:cd07859   80 YVVFEL-----MESDLHQVIKanddLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGLARVAF 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 255958318 181 GRT-----WT-LCGTPEYLAPEI---ILSKgYNKAVDWWALGVLIYEMAAGYPPF 226
Cdd:cd07859  155 NDTptaifWTdYVATRWYRAPELcgsFFSK-YTPAIDIWSIGCIFAEVLTGKPLF 208
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
32-223 3.57e-12

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


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 66.06  E-value: 3.57e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  32 ERKktLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKlkqiEHTLNEKRILQAV-----EFPF---LVRLEYSFKDNSN 103
Cdd:cd14136   15 VRK--LGWGHFSTVWLCWDLQNKRFVALKVVKSAQHYT----EAALDEIKLLKCVreadpKDPGrehVVQLLDDFKHTGP 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 104 ----LYMVMEYvpggeMFSHLRRIGRFSEPHA------RFYAAQIVLTFEYLHS-LDLIYRDLKPENLLIDHQGyIQV-- 170
Cdd:cd14136   89 ngthVCMVFEV-----LGPNLLKLIKRYNYRGiplplvKKIARQVLQGLDYLHTkCGIIHTDIKPENVLLCISK-IEVki 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 255958318 171 TDFGFAkrvkgrTWTL------CGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGY 223
Cdd:cd14136  163 ADLGNA------CWTDkhftedIQTRQYRSPEVILGAGYGTPADIWSTACMAFELATGD 215
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
17-268 4.31e-12

Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The FGFR subfamily consists of FGFR1, FGFR2, FGFR3, FGFR4, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, and to heparin/heparan sulfate (HS) results in the formation of a ternary complex, which leads to receptor dimerization and activation, and intracellular signaling. There are at least 23 FGFs and four types of FGFRs. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. FGF/FGFR signaling is important in the regulation of embryonic development, homeostasis, and regenerative processes. Depending on the cell type and stage, FGFR signaling produces diverse cellular responses including proliferation, growth arrest, differentiation, and apoptosis. Aberrant signaling leads to many human diseases such as skeletal, olfactory, and metabolic disorders, as well as cancer. The FGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 65.90  E-value: 4.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  17 KWENPppsnagLEDFERKKTLGTGSFGRVMLVKHKATEqyyamKILDKQKVVKLKQIEHTLNEKRILQAV---------- 86
Cdd:cd05053    6 EWELP------RDRLTLGKPLGEGAFGQVVKAEAVGLD-----NKPNEVVTVAVKMLKDDATEKDLSDLVsememmkmig 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  87 EFPFLVRLEYSFKDNSNLYMVMEYVPGGEMFSHLRR----------------IGRFSEPHARFYAAQIVLTFEYLHSLDL 150
Cdd:cd05053   75 KHKNIINLLGACTQDGPLYVVVEYASKGNLREFLRArrppgeeaspddprvpEEQLTQKDLVSFAYQVARGMEYLASKKC 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 151 IYRDLKPENLLIDHQGYIQVTDFGFA----------KRVKGRtwtlcgTP-EYLAPEIILSKGYNKAVDWWALGVLIYE- 218
Cdd:cd05053  155 IHRDLAARNVLVTEDNVMKIADFGLArdihhidyyrKTTNGR------LPvKWMAPEALFDRVYTHQSDVWSFGVLLWEi 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 255958318 219 MAAGYPPFFADQPIQIYEKIVSG-KVRFPSHFSSDLKDLLRNLLQVDLTKR 268
Cdd:cd05053  229 FTLGGSPYPGIPVEELFKLLKEGhRMEKPQNCTQELYMLMRDCWHEVPSQR 279
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
34-243 4.93e-12

Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Trk subfamily consists of TrkA, TrkB, TrkC, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, the nerve growth factor (NGF) family of neutrotrophins, leads to Trk receptor oligomerization and activation of the catalytic domain. Trk receptors are mainly expressed in the peripheral and central nervous systems. They play important roles in cell fate determination, neuronal survival and differentiation, as well as in the regulation of synaptic plasticity. Altered expression of Trk receptors is associated with many human diseases. The Trk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 65.56  E-value: 4.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  34 KKTLGTGSFGRVMLVKHKATEQ-----YYAMKILDKQKVVKLKQIEHtlNEKRILQAVEFPFLVRLEYSFKDNSNLYMVM 108
Cdd:cd05049   10 KRELGEGAFGKVFLGECYNLEPeqdkmLVAVKTLKDASSPDARKDFE--REAELLTNLQHENIVKFYGVCTEGDPLLMVF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 109 EYVPGGEMFSHLRRIGrfsePHARFY------------------AAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQV 170
Cdd:cd05049   88 EYMEHGDLNKFLRSHG----PDAAFLasedsapgeltlsqllhiAVQIASGMVYLASQHFVHRDLATRNCLVGTNLVVKI 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 171 TDFGFAK--------RVKGRTWtlcgTP-EYLAPEIILSKGYNKAVDWWALGVLIYEM-AAGYPPFFADQPIQIYEKIVS 240
Cdd:cd05049  164 GDFGMSRdiystdyyRVGGHTM----LPiRWMPPESILYRKFTTESDVWSFGVVLWEIfTYGKQPWFQLSNTEVIECITQ 239

                 ...
gi 255958318 241 GKV 243
Cdd:cd05049  240 GRL 242
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
29-241 5.02e-12

Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Itk, also known as Tsk or Emt, is a member of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Itk contains the Tec homology (TH) domain containing one proline-rich region and a zinc-binding region. Itk is expressed in T-cells and mast cells, and is important in their development and differentiation. Of the three Tec kinases expressed in T-cells, Itk plays the predominant role in T-cell receptor (TCR) signaling. It is activated by phosphorylation upon TCR crosslinking and is involved in the pathway resulting in phospholipase C-gamma1 activation and actin polymerization. It also plays a role in the downstream signaling of the T-cell costimulatory receptor CD28, the T-cell surface receptor CD2, and the chemokine receptor CXCR4. In addition, Itk is crucial for the development of T-helper(Th)2 effector responses. The Itk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133243 [Multi-domain]  Cd Length: 256  Bit Score: 64.97  E-value: 5.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLvkhkateQYYamkiLDKQKVVkLKQI-------EHTLNEKRILQAVEFPFLVRLEYSFKDN 101
Cdd:cd05112    4 SELTFVQEIGSGQFGLVHL-------GYW----LNKDKVA-IKTIregamseEDFIEEAEVMMKLSHPKLVQLYGVCLEQ 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 102 SNLYMVMEYVPGGEMFSHLR-RIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVK 180
Cdd:cd05112   72 APICLVFEFMEHGCLSDYLRtQRGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMTRFVL 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255958318 181 GRTWTLC-GTP---EYLAPEIILSKGYNKAVDWWALGVLIYEM-AAGYPPFFADQPIQIYEKIVSG 241
Cdd:cd05112  152 DDQYTSStGTKfpvKWSSPEVFSFSRYSSKSDVWSFGVLMWEVfSEGKIPYENRSNSEVVEDINAG 217
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
18-268 5.12e-12

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: 65.48  E-value: 5.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  18 WENPPpsnaglEDFERKKTLGTGSFGRVMLVKHKATEQYyAMKILDKQKVVKlkqiEHTLNEKRILQAVEFPFLVRLeYS 97
Cdd:cd05071    4 WEIPR------ESLRLEVKLGQGCFGEVWMGTWNGTTRV-AIKTLKPGTMSP----EAFLQEAQVMKKLRHEKLVQL-YA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  98 FKDNSNLYMVMEYVPGGEMFSHLRriGRFSE----PHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDF 173
Cdd:cd05071   72 VVSEEPIYIVTEYMSKGSLLDFLK--GEMGKylrlPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADF 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 174 GFAKRVKGRTWTLCGTPEY----LAPEIILSKGYNKAVDWWALGVLIYEMAA-GYPPFFADQPIQIYEKIVSG-KVRFPS 247
Cdd:cd05071  150 GLARLIEDNEYTARQGAKFpikwTAPEAALYGRFTIKSDVWSFGILLTELTTkGRVPYPGMVNREVLDQVERGyRMPCPP 229
                        250       260
                 ....*....|....*....|.
gi 255958318 248 HFSSDLKDLLRNLLQVDLTKR 268
Cdd:cd05071  230 ECPESLHDLMCQCWRKEPEER 250
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
37-238 5.56e-12

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: 65.78  E-value: 5.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVM--LVKHKATEQYYAMKI--LDKQKVVKLKQIEHTLNEKRILQaveFPFLVRLEYSFKDNSNLYMVMEYVP 112
Cdd:cd08216    6 IGKCFKGGGVvhLAKHKPTNTLVAVKKinLESDSKEDLKFLQQEILTSRQLQ---HPNILPYVTSFVVDNDLYVVTPLMA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 113 GGEMFSHLRRigRFSEPHARFYAAQI----VLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFA-------KRVKg 181
Cdd:cd08216   83 YGSCRDLLKT--HFPEGLPELAIAFIlrdvLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGLRYAysmvkhgKRQR- 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255958318 182 rtwTLCGTPEY-------LAPEII---LSkGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIY-EKI 238
Cdd:cd08216  160 ---VVHDFPKSseknlpwLSPEVLqqnLL-GYNEKSDIYSVGITACELANGVVPFSDMPATQMLlEKV 223
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
17-268 5.70e-12

Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The PDGFR subfamily consists of PDGFR alpha, PDGFR beta, KIT, CSF-1R, the mammalian FLT3, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. PDGFR kinase domains are autoinhibited by their juxtamembrane regions containing tyr residues. The binding to their ligands leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR subfamily receptors are important in the development of a variety of cells. PDGFRs are expressed in a many cells including fibroblasts, neurons, endometrial cells, mammary epithelial cells, and vascular smooth muscle cells. PDGFR signaling is critical in normal embryonic development, angiogenesis, and wound healing. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. Mammalian FLT3 plays an important role in the survival, proliferation, and differentiation of stem cells. The PDGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 65.58  E-value: 5.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  17 KWENPPpsnaglEDFERKKTLGTGSFGRVM------LVKHKATEQyYAMKILdkQKVVKLKQIEHTLNEKRILQAV-EFP 89
Cdd:cd05055   29 KWEFPR------NNLSFGKTLGAGAFGKVVeataygLSKSDAVMK-VAVKML--KPTAHSSEREALMSELKIMSHLgNHE 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  90 FLVRLEYSFKDNSNLYMVMEYVPGGEMFSHLRRIgrfSEPHARF-----YAAQIVLTFEYLHSLDLIYRDLKPENLLIDH 164
Cdd:cd05055  100 NIVNLLGACTIGGPILVITEYCCYGDLLNFLRRK---RESFLTLedllsFSYQVAKGMAFLASKNCIHRDLAARNVLLTH 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 165 QGYIQVTDFGFAKR--------VKGRTWtlcgTP-EYLAPEIILSKGYNKAVDWWALGVLIYEM----AAGYPPFFADQp 231
Cdd:cd05055  177 GKIVKICDFGLARDimndsnyvVKGNAR----LPvKWMAPESIFNCVYTFESDVWSYGILLWEIfslgSNPYPGMPVDS- 251
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 255958318 232 iQIYEKIVSG-KVRFPSHFSSDLKDLLRNLLQVDLTKR 268
Cdd:cd05055  252 -KFYKLIKEGyRMAQPEHAPAEIYDIMKTCWDADPLKR 288
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
35-259 5.96e-12

Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily contains c-ros, Sevenless, and similar proteins. The proto-oncogene c-ros encodes an orphan receptor PTK (RTK) with an unknown ligand. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. C-ros is expressed in embryonic cells of the kidney, intestine and lung, but disappears soon after birth. It persists only in the adult epididymis. Male mice bearing inactive mutations of c-ros lack the initial segment of the epididymis and are infertile. The Drosophila protein, Sevenless, is required for the specification of the R7 photoreceptor cell during eye development. The c-ros subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 65.13  E-value: 5.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVM------LVKHKATEQYYAMKILDKQKVVKLKqiEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVM 108
Cdd:cd05044    1 KFLGSGAFGEVFegtakdILGDGSGETKVAVKTLRKGATDQEK--AEFLKEAHLMSNFKHPNILKLLGVCLDNDPQYIIL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 109 EYVPGGEMFSHLRRigrfSEPhARFYAAQIVLT------------FEYLHSLDLIYRDLKPENLLIDHQGY----IQVTD 172
Cdd:cd05044   79 ELMEGGDLLSYLRA----ARP-TAFTPPLLTLKdllsicvdvakgCVYLEDMHFVHRDLAARNCLVSSKDYrervVKIGD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 173 FGFAK--------RVKGR-----TWtlcgtpeyLAPEIILSKGYNKAVDWWALGVLIYE-MAAGYPPFFADQPIQIYEKI 238
Cdd:cd05044  154 FGLARdiykndyyRKEGEgllpvRW--------MAPESLVDGVFTTQSDVWAFGVLMWEiLTLGQQPYPARNNLEVLHFV 225
                        250       260
                 ....*....|....*....|..
gi 255958318 239 VS-GKVRFPSHFSSDLKDLLRN 259
Cdd:cd05044  226 RAgGRLDQPDNCPDDLYELMLR 247
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
30-268 7.43e-12

Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1a, Xenopus laevis Wee1b (XeWee1b) and similar vertebrate proteins. Members of this subfamily show a wide expression pattern. XeWee1b functions after the first zygotic cell divisions. It is expressed in all tissues and is also present after the gastrulation stage of embryos. 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 Wee1a 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: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 65.04  E-value: 7.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  30 DFERKKTLGTGSFGRVMLVKHKATEQYYAMKildKQKvvklKQIEHTLNEKRILQAV-------EFPFLVRLEYSFKDNS 102
Cdd:cd14138    6 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIK---RSK----KPLAGSVDEQNALREVyahavlgQHSHVVRYYSAWAEDD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 103 NLYMVMEYVPGGEMFSHL----RRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGY----------- 167
Cdd:cd14138   79 HMLIQNEYCNGGSLADAIsenyRIMSYFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFISRTSIpnaaseegded 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 168 --------IQVTDFGFAKRVKGRTwTLCGTPEYLAPEiILSKGYN--KAVDWWALGVLIYEMAAGYP-PFFADQpiqiYE 236
Cdd:cd14138  159 ewasnkviFKIGDLGHVTRVSSPQ-VEEGDSRFLANE-VLQENYThlPKADIFALALTVVCAAGAEPlPTNGDQ----WH 232
                        250       260       270
                 ....*....|....*....|....*....|...
gi 255958318 237 KIVSGKV-RFPSHFSSDLKDLLRNLLQVDLTKR 268
Cdd:cd14138  233 EIRQGKLpRIPQVLSQEFLDLLKVMIHPDPERR 265
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
37-221 7.96e-12

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: 64.42  E-value: 7.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKI--LDKQKVvklkqieHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGG 114
Cdd:cd14155    1 IGSGFFSEVYKVRHRTSGQVMALKMntLSSNRA-------NMLREVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 115 EMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLI--DHQGYIQVT-DFGFAKRV-----KGRTWTL 186
Cdd:cd14155   74 NLEQLLDSNEPLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIkrDENGYTAVVgDFGLAEKIpdysdGKEKLAV 153
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 255958318 187 CGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAA 221
Cdd:cd14155  154 VGSPYWMAPEVLRGEPYNEKADVFSYGIILCEIIA 188
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
31-279 8.43e-12

Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyro3 (or Sky) is predominantly expressed in the central nervous system and the brain, and functions as a neurotrophic factor. It is also expressed in osteoclasts and has a role in bone resorption. Tyro3 is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Tyro3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 64.94  E-value: 8.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRV---MLVKHKATEQYYAMKILdKQKVVKLKQIEHTLNEKRILQAVEFPFL-----VRLEYSFKDNS 102
Cdd:cd05074   11 FTLGRMLGKGEFGSVreaQLKSEDGSFQKVAVKML-KADIFSSSDIEEFLREAACMKEFDHPNVikligVSLRSRAKGRL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 103 NLYMV-MEYVPGGEMFSHL--RRIGR--FSEPHARF--YAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGF 175
Cdd:cd05074   90 PIPMViLPFMKHGDLHTFLlmSRIGEepFTLPLQTLvrFMIDIASGMEYLSSKNFIHRDLAARNCMLNENMTVCVADFGL 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 176 AKRVKGRTWTLCGTP-----EYLAPEIILSKGYNKAVDWWALGVLIYE-MAAGYPPFFADQPIQIYEKIVSG-KVRFPSH 248
Cdd:cd05074  170 SKKIYSGDYYRQGCAsklpvKWLALESLADNVYTTHSDVWAFGVTMWEiMTRGQTPYAGVENSEIYNYLIKGnRLKQPPD 249
                        250       260       270
                 ....*....|....*....|....*....|...
gi 255958318 249 FSSDLKDLLRNLLQVDLTKR--FGNLKNGVSDI 279
Cdd:cd05074  250 CLEDVYELMCQCWSPEPKCRpsFQHLRDQLELI 282
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
36-222 9.76e-12

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


Pssm-ID: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 64.94  E-value: 9.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  36 TLGTGSFGRVMLVKHKATE-QYYAMKILDKQKVVK---LKQIE--HTLNE------KRILqavefpflvRLEYSFKDNSN 103
Cdd:cd14135    7 YLGKGVFSNVVRARDLARGnQEVAIKIIRNNELMHkagLKELEilKKLNDadpddkKHCI---------RLLRHFEHKNH 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 104 LYMVMEYvpggeMFSHLRRI----GR---FSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQ-GYIQVTDFGF 175
Cdd:cd14135   78 LCLVFES-----LSMNLREVlkkyGKnvgLNIKAVRSYAQQLFLALKHLKKCNILHADIKPDNILVNEKkNTLKLCDFGS 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 255958318 176 AKRVKGRTWTlcgtpEYL------APEIILSKGYNKAVDWWALGVLIYEMAAG 222
Cdd:cd14135  153 ASDIGENEIT-----PYLvsrfyrAPEIILGLPYDYPIDMWSVGCTLYELYTG 200
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
35-226 1.33e-11

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: 63.93  E-value: 1.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATeqyYAMKILDKQKVVKlKQIEHTLNEKRILQAVE-FPFLVRLEYSFKdnSNLYMVMEYVPG 113
Cdd:cd14151   14 QRIGSGSFGTVYKGKWHGD---VAVKMLNVTAPTP-QQLQAFKNEVGVLRKTRhVNILLFMGYSTK--PQLAIVTQWCEG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 114 GEMFSHLRRI-GRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKrVKGRtWT------- 185
Cdd:cd14151   88 SSLYHHLHIIeTKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAT-VKSR-WSgshqfeq 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 255958318 186 LCGTPEYLAPEIIL---SKGYNKAVDWWALGVLIYEMAAGYPPF 226
Cdd:cd14151  166 LSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPY 209
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
28-226 1.43e-11

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 1; 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. Mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A was previously called minibrain kinase homolog (MNBH) or dual-specificity YAK1-related kinase. It phosphorylates various substrates and is involved in many cellular events. It phosphorylates and inhibits the transcription factors, nuclear factor of activated T cells (NFAT) and forkhead in rhabdomyosarcoma (FKHR). It regulates neuronal differentiation by targetting CREB (cAMP response element-binding protein). It also targets many endocytic proteins including dynamin and amphiphysin and may play a role in the endocytic pathway. The gene encoding DYRK1A is located in the DSCR (Down syndrome critical region) of human chromosome 21 and DYRK1A has been implicated in the pathogenesis of DS. DYRK1B, also called minibrain-related kinase (MIRK), is highly expressed in muscle and 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. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 64.65  E-value: 1.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  28 LEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILdKQKVVKLKQIEHtlnEKRILQAVEFP------FLVRLEYSFKDN 101
Cdd:cd14226   12 MDRYEIDSLIGKGSFGQVVKAYDHVEQEWVAIKII-KNKKAFLNQAQI---EVRLLELMNKHdtenkyYIVRLKRHFMFR 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 102 SNLYMVMEyvpggeMFSH----LRRIGRF---SEPHARFYAAQIVLTFEYLHS--LDLIYRDLKPENLLIDH--QGYIQV 170
Cdd:cd14226   88 NHLCLVFE------LLSYnlydLLRNTNFrgvSLNLTRKFAQQLCTALLFLSTpeLSIIHCDLKPENILLCNpkRSAIKI 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 255958318 171 TDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPF 226
Cdd:cd14226  162 IDFGSSCQLGQRIYQYIQSRFYRSPEVLLGLPYDLAIDMWSLGCILVEMHTGEPLF 217
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
17-219 1.59e-11

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: 63.75  E-value: 1.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  17 KWENPPpsnaglEDFERKKTLGTGSFGRVMLVKHKATEQYyAMKILDKQKVvklkQIEHTLNEKRILQAVEFPFLVRLeY 96
Cdd:cd05067    1 EWEVPR------ETLKLVERLGAGQFGEVWMGYYNGHTKV-AIKSLKQGSM----SPDAFLAEANLMKQLQHQRLVRL-Y 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  97 SFKDNSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARF--YAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFG 174
Cdd:cd05067   69 AVVTQEPIYIITEYMENGSLVDFLKTPSGIKLTINKLldMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFG 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 255958318 175 FAKRVKGRTWTL---CGTP-EYLAPEIILSKGYNKAVDWWALGVLIYEM 219
Cdd:cd05067  149 LARLIEDNEYTAregAKFPiKWTAPEAINYGTFTIKSDVWSFGILLTEI 197
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
28-226 1.71e-11

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: 63.68  E-value: 1.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  28 LEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHtLNEKRILQAVEFPFLVRLEYSFKDNSN--LY 105
Cdd:cd14049    5 LNEFEEIARLGKGGYGKVYKVRNKLDGQYYAIKKILIKKVTKRDCMKV-LREVKVLAGLQHPNIVGYHTAWMEHVQlmLY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 106 MVMEYVPGG--EMFSHLRRIGRFSEPHARFYA-----------AQIVLTFEYLHSLDLIYRDLKPENLLI---DHQgyIQ 169
Cdd:cd14049   84 IQMQLCELSlwDWIVERNKRPCEEEFKSAPYTpvdvdvttkilQQLLEGVTYIHSMGIVHRDLKPRNIFLhgsDIH--VR 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255958318 170 VTDFGFAKR---VKGRTWTLC------------GTPEYLAPEIILSKGYNKAVDWWALGVLIYEMaagYPPF 226
Cdd:cd14049  162 IGDFGLACPdilQDGNDSTTMsrlnglthtsgvGTCLYAAPEQLEGSHYDFKSDMYSIGVILLEL---FQPF 230
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
137-268 1.84e-11

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


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 63.88  E-value: 1.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 137 QIVLTFEYLH-SLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRT---WTLCG-----------TPEYLAPEIILSK 201
Cdd:cd14011  122 QISEALSFLHnDVKLVHGNICPESVVINSNGEWKLAGFDFCISSEQATdqfPYFREydpnlpplaqpNLNYLAPEYILSK 201
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255958318 202 GYNKAVDWWALGVLIYEM-AAGYPPFFADQPIQIYEKIVSgKVRFPSHFS-----SDLKDLLRNLLQVDLTKR 268
Cdd:cd14011  202 TCDPASDMFSLGVLIYAIyNKGKPLFDCVNNLLSYKKNSN-QLRQLSLSLlekvpEELRDHVKTLLNVTPEVR 273
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
110-241 3.71e-11

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK1 is one of two vertebrate LRRKs which show complementary expression in the brain. It can form heterodimers with LRRK2, and may influence the age of onset of LRRK2-associated Parkinson's disease. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 62.67  E-value: 3.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 110 YVPGGEMFSHlrRIgrfsepharfyAAQIVLTFEYLHSLDLIYRDLKPENLLI---DHQGYIQV--TDFGFAKR-VKGRT 183
Cdd:cd14067  108 FMPLGHMLTF--KI-----------AYQIAAGLAYLHKKNIIFCDLKSDNILVwslDVQEHINIklSDYGISRQsFHEGA 174
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 255958318 184 WTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSG 241
Cdd:cd14067  175 LGVEGTPGYQAPEIRPRIVYDEKVDMFSYGMVLYELLSGQRPSLGHHQLQIAKKLSKG 232
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
34-235 3.80e-11

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR1 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR1 results in a slow but sustained receptor activation. DDR1 binds to all collagens tested to date (types I-IV). It is widely expressed in many tissues. It is abundant in the brain and is also found in keratinocytes, colonic mucosa epithelium, lung epithelium, thyroid follicles, and the islets of Langerhans. During embryonic development, it is found in the developing neuroectoderm. DDR1 is a key regulator of cell morphogenesis, differentiation and proliferation. It is important in the development of the mammary gland, the vasculator and the kidney. DDR1 is also found in human leukocytes, where it facilitates cell adhesion, migration, maturation, and cytokine production. The DDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133227 [Multi-domain]  Cd Length: 304  Bit Score: 63.03  E-value: 3.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  34 KKTLGTGSFGRVMLVK----------------HKATEQYYAMKIL--DKQKVVKlkqiEHTLNEKRILQAVEFPFLVRLE 95
Cdd:cd05096   10 KEKLGEGQFGEVHLCEvvnpqdlptlqfpfnvRKGRPLLVAVKILrpDANKNAR----NDFLKEVKILSRLKDPNIIRLL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  96 YSFKDNSNLYMVMEYVPGGEMFSHL--RRIGRFSEPHARFY-----------------AAQIVLTFEYLHSLDLIYRDLK 156
Cdd:cd05096   86 GVCVDEDPLCMITEYMENGDLNQFLssHHLDDKEENGNDAVppahclpaisyssllhvALQIASGMKYLSSLNFVHRDLA 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 157 PENLLIDHQGYIQVTDFGFAK--------RVKGRTWtlcgTP-EYLAPEIILSKGYNKAVDWWALGVLIYEMA------- 220
Cdd:cd05096  166 TRNCLVGENLTIKIADFGMSRnlyagdyyRIQGRAV----LPiRWMAWECILMGKFTTASDVWAFGVTLWEILmlckeqp 241
                        250       260
                 ....*....|....*....|....*..
gi 255958318 221 ------------AGypPFFADQPIQIY 235
Cdd:cd05096  242 ygeltdeqvienAG--EFFRDQGRQVY 266
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
35-219 4.04e-11

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. There are many splice variants of FGFR2 which show differential expression and binding to FGF ligands. Disruption of either FGFR2 or FGFR2b is lethal in mice, due to defects in the placenta or severe impairment of tissue development including lung, limb, and thyroid, respectively. Disruption of FGFR2c in mice results in defective bone and skull development. Genetic alterations of FGFR2 are associated with many human skeletal disorders including Apert syndrome, Crouzon syndrome, Jackson-Weiss syndrome, and Pfeiffer syndrome. FGFR2 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 63.11  E-value: 4.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLV------KHKATEQY-YAMKILDKQKVVKlkQIEHTLNEKRILQAV-EFPFLVRLEYSFKDNSNLYM 106
Cdd:cd05101   30 KPLGEGCFGQVVMAeavgidKDKPKEAVtVAVKMLKDDATEK--DLSDLVSEMEMMKMIgKHKNIINLLGACTQDGPLYV 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 107 VMEYVPGGEMFSHLRR-----------IGRFSEPHARFY-----AAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQV 170
Cdd:cd05101  108 IVEYASKGNLREYLRArrppgmeysydINRVPEEQMTFKdlvscTYQLARGMEYLASQKCIHRDLAARNVLVTENNVMKI 187
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 255958318 171 TDFGFAKRVKGRTWTLCGTP-----EYLAPEIILSKGYNKAVDWWALGVLIYEM 219
Cdd:cd05101  188 ADFGLARDINNIDYYKKTTNgrlpvKWMAPEALFDRVYTHQSDVWSFGVLMWEI 241
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
17-219 4.67e-11

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: 62.42  E-value: 4.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  17 KWENPPPSnagledFERKKTLGTGSFGRVML-VKHKATEqyYAMKILDKQKVvklkQIEHTLNEKRILQAVEFPFLVRLE 95
Cdd:cd05068    2 QWEIDRKS------LKLLRKLGSGQFGEVWEgLWNNTTP--VAVKTLKPGTM----DPEDFLREAQIMKKLRHPKLIQLY 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  96 YSFKDNSNLYMVMEYVPGGEMFSHLRRIGR-FSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFG 174
Cdd:cd05068   70 AVCTLEEPIYIITELMKHGSLLEYLQGKGRsLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVGENNICKVADFG 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 255958318 175 FAKRVKGRT-------------WTlcgtpeylAPEIILSKGYNKAVDWWALGVLIYEM 219
Cdd:cd05068  150 LARVIKVEDeyearegakfpikWT--------APEAANYNRFSIKSDVWSFGILLTEI 199
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
31-179 4.71e-11

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


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 62.28  E-value: 4.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  31 FERKKTLGTGSFGRVMLVKHKATEQYYAMKI--LDKQKVVkLKQIEHTLneKRILQAvefPFLVRLEYSFKDNSNLYMVM 108
Cdd:cd14017    2 WKVVKKIGGGGFGEIYKVRDVVDGEEVAMKVesKSQPKQV-LKMEVAVL--KKLQGK---PHFCRLIGCGRTERYNYIVM 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 109 EYVpgGEMFSHLRRI---GRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLI------DHQGYIqvTDFGFAKRV 179
Cdd:cd14017   76 TLL--GPNLAELRRSqprGKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAIgrgpsdERTVYI--LDFGLARQY 151
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
34-226 5.63e-11

Catalytic domain of the Dual-specificity protein kinase, YAK1; 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 proteins with similarity to Saccharomyces cerevisiae YAK1 (or Yak1p), a dual-specificity kinase that autophosphorylates at tyrosine residues and phosphorylates substrates on S/T residues. YAK1 phosphorylates and activates the transcription factors Hsf1 and Msn2, which play important roles in cellular homeostasis during stress conditions including heat shock, oxidative stress, and nutrient deficiency. It also phosphorylates the protein POP2, a component of a complex that regulates transcription, under glucose-deprived conditions. It functions as a part of a glucose-sensing system that is involved in controlling growth in yeast. The YAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 62.65  E-value: 5.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  34 KKTLGTGSFGRVMLVKHKATEQYYAMKILdKQKVVKLKQ------IEHTLNEKRILQAVEFpfLVRLEYSFKDNSNLYMV 107
Cdd:cd14212    4 LDLLGQGTFGQVVKCQDLKTNKLVAVKVL-KNKPAYFRQamleiaILTLLNTKYDPEDKHH--IVRLLDHFMHHGHLCIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 108 ME------YvpggEMFSHLRRIGrFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQ--GYIQVTDFGFAKRV 179
Cdd:cd14212   81 FEllgvnlY----ELLKQNQFRG-LSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVNLdsPEIKLIDFGSACFE 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 255958318 180 KGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPF 226
Cdd:cd14212  156 NYTLYTYIQSRFYRSPEVLLGLPYSTAIDMWSLGCIAAELFLGLPLF 202
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
134-257 5.71e-11

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR alpha is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR alpha forms homodimers or heterodimers with PDGFR beta, depending on the nature of the PDGF ligand. PDGF-AA, PDGF-AB, and PDGF-CC induce PDGFR alpha homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR alpha signaling is important in the formation of lung alveoli, intestinal villi, mesenchymal dermis, and hair follicles, as well as in the development of oligodendrocytes, retinal astrocytes, neural crest cells, and testicular cells. Aberrant PDGFR alpha expression is associated with some human cancers. Mutations in PDGFR alpha have been found within a subset of gastrointestinal stromal tumors (GISTs). An active fusion protein FIP1L1-PDGFR alpha, derived from interstitial deletion, is associated with idiopathic hypereosinophilic syndrome and chronic eosinophilic leukemia. The PDGFR alpha subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173653 [Multi-domain]  Cd Length: 400  Bit Score: 63.12  E-value: 5.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 134 YAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRV--------KGRTWTlcgTPEYLAPEIILSKGYNK 205
Cdd:cd05105  242 FTYQVARGMEFLASKNCVHRDLAARNVLLAQGKIVKICDFGLARDImhdsnyvsKGSTFL---PVKWMAPESIFDNLYTT 318
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 255958318 206 AVDWWALGVLIYEM----AAGYPPFFADQpiQIYEKIVSG-KVRFPSHFSSDLKDLL 257
Cdd:cd05105  319 LSDVWSYGILLWEIfslgGTPYPGMIVDS--TFYNKIKSGyRMAKPDHATQEVYDIM 373
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
30-243 5.82e-11

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkC is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkC to its ligand, neurotrophin 3 (NT3), results in receptor oligomerization and activation of the catalytic domain. TrkC is broadly expressed in the nervous system and in some non-neural tissues including the developing heart. NT3/TrkC signaling plays an important role in the innervation of the cardiac conducting system and the development of smooth muscle cells. Mice deficient with NT3 and TrkC have multiple heart defects. NT3/TrkC signaling is also critical for the development and maintenance of enteric neurons that are important for the control of gut peristalsis. The TrkC subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 62.34  E-value: 5.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  30 DFERKKTLGTGSFGRVMLVK-----HKATEQYYAMKILDKQKVVKLKQIEHtlnEKRILQAVEFPFLVRLEYSFKDNSNL 104
Cdd:cd05094    6 DIVLKRELGEGAFGKVFLAEcynlsPTKDKMLVAVKTLKDPTLAARKDFQR---EAELLTNLQHDHIVKFYGVCGDGDPL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 105 YMVMEYVPGGEMFSHLR----------------RIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYI 168
Cdd:cd05094   83 IMVFEYMKHGDLNKFLRahgpdamilvdgqprqAKGELGLSQMLHIATQIASGMVYLASQHFVHRDLATRNCLVGANLLV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 169 QVTDFGFAKRVKGRTWTLCGTP-----EYLAPEIILSKGYNKAVDWWALGVLIYEM-AAGYPPFFADQPIQIYEKIVSGK 242
Cdd:cd05094  163 KIGDFGMSRDVYSTDYYRVGGHtmlpiRWMPPESIMYRKFTTESDVWSFGVILWEIfTYGKQPWFQLSNTEVIECITQGR 242

                 .
gi 255958318 243 V 243
Cdd:cd05094  243 V 243
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
35-219 6.16e-11

Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, and Yes. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, and Lyn show a limited expression pattern. The Src-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270630 [Multi-domain]  Cd Length: 248  Bit Score: 61.91  E-value: 6.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRV-MLVKHKATEqyYAMKILdKQKVVKLkqiEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPG 113
Cdd:cd05034    1 KKLGAGQFGEVwMGVWNGTTK--VAVKTL-KPGTMSP---EAFLQEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTELMSK 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 114 GEMFSHLR--RIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRT-------- 183
Cdd:cd05034   75 GSLLDYLRtgEGRALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNVCKVADFGLARLIEDDEytaregak 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 255958318 184 ----WTlcgtpeylAPEIILSKGYNKAVDWWALGVLIYEM 219
Cdd:cd05034  155 fpikWT--------APEAALYGRFTIKSDVWSFGILLYEI 186
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
18-226 6.48e-11

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: 61.97  E-value: 6.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  18 WENPPPSnagledFERKKTLGTGSFGRV-MLVKHKATEqyYAMKILDKQKVvklkQIEHTLNEKRILQAVEFPFLVRLeY 96
Cdd:cd05073    6 WEIPRES------LKLEKKLGAGQFGEVwMATYNKHTK--VAVKTMKPGSM----SVEAFLAEANVMKTLQHDKLVKL-H 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  97 SFKDNSNLYMVMEYVPGGEMFSHLR--RIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFG 174
Cdd:cd05073   73 AVVTKEPIYIITEFMAKGSLLDFLKsdEGSKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFG 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 255958318 175 FAKRVKGRTWTL---CGTP-EYLAPEIILSKGYNKAVDWWALGVLIYEMAA-GYPPF 226
Cdd:cd05073  153 LARVIEDNEYTAregAKFPiKWTAPEAINFGSFTIKSDVWSFGILLMEIVTyGRIPY 209
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
35-230 6.56e-11

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 62.94  E-value: 6.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVML-VKHKATEQyyamkildKQKVVKLKQIEHTL-NEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEyVP 112
Cdd:PHA03207  98 SSLTPGSEGEVFVcTKHGDEQR--------KKVIVKAVTGGKTPgREIDILKTISHRAIINLIHAYRWKSTVCMVMP-KY 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 113 GGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTWT-----LC 187
Cdd:PHA03207 169 KCDLFTYVDRSGPLPLEQAITIQRRLLEALAYLHGRGIIHRDVKTENIFLDEPENAVLGDFGAACKLDAHPDTpqcygWS 248
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 255958318 188 GTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQ 230
Cdd:PHA03207 249 GTLETNSPELLALDPYCAKTDIWSAGLVLFEMSVKNVTLFGKQ 291
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
104-219 7.17e-11

Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDIK1L is also called STK35 or CLIK-1. It is predominantly a nuclear protein which is capable of autophosphorylation. Through its interaction with the PDZ-LIM protein CLP-36, it is localized to actin stress fibers. The PDIK1L subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 62.19  E-value: 7.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 104 LYMVMEYVPGGEMFSHL--RRigrfsePHARF---YAAQIVLTFEYLHSLDLIYRDLKPENLLIDH---QGYIQVTDFGF 175
Cdd:cd13977  110 LWFVMEFCDGGDMNEYLlsRR------PDRQTntsFMLQLSSALAFLHRNQIVHRDLKPDNILISHkrgEPILKVADFGL 183
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 255958318 176 AKRVKG--------------RTWTLCGTPEYLAPEiILSKGYNKAVDWWALGVLIYEM 219
Cdd:cd13977  184 SKVCSGsglnpeepanvnkhFLSSACGSDFYMAPE-VWEGHYTAKADIFALGIIIWAM 240
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
37-258 7.31e-11

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: 61.98  E-value: 7.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVM--LVKHKATEQYYAMKILdKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGG 114
Cdd:cd05047    3 IGEGNFGQVLkaRIKKDGLRMDAAIKRM-KEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPHG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 115 EMFSHLRRiGRFSEPHARF-----------------YAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFG--- 174
Cdd:cd05047   82 NLLDFLRK-SRVLETDPAFaianstastlssqqllhFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGlsr 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 175 ----FAKRVKGRTwtlcgTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAA-GYPPFFADQPIQIYEKIVSG-KVRFPSH 248
Cdd:cd05047  161 gqevYVKKTMGRL-----PVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQGyRLEKPLN 235
                        250
                 ....*....|
gi 255958318 249 FSSDLKDLLR 258
Cdd:cd05047  236 CDDEVYDLMR 245
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
30-234 7.36e-11

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


Pssm-ID: 173656 [Multi-domain]  Cd Length: 279  Bit Score: 61.90  E-value: 7.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  30 DFERKKTLGTGSFGRVmlvkHKA--TEQYYAMKILDKQKVVKLKQIEHTLNE----KRILQAVEFPFLVRLeYSFKDNSN 103
Cdd:cd05111    8 ELRKLKVLGSGVFGTV----HKGiwIPEGDSIKIPVAIKVIQDRSGRQSFQAvtdhMLAIGSLDHAYIVRL-LGICPGAS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 104 LYMVMEYVPGGEMFSHLR-RIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRV--- 179
Cdd:cd05111   83 LQLVTQLLPLGSLLDHVRqHRGSLGPQLLLNWCVQIAKGMYYLEEHRMVHRNLAARNVLLKSPSQVQVADFGVADLLypd 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 255958318 180 -KGRTWTLCGTP-EYLAPEIILSKGYNKAVDWWALGVLIYEMAA-GYPPFFADQPIQI 234
Cdd:cd05111  163 dKKYFYSEAKTPiKWMALESIHFGKYTHQSDVWSYGVTVWEMMTfGAEPYAGMRLAEV 220
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
34-243 9.07e-11

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkB is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkB to its ligands, brain-derived neurotrophic factor (BDNF) or neurotrophin 4 (NT4), results in receptor oligomerization and activation of the catalytic domain. TrkB is broadly expressed in the nervous system and in some non-neural tissues. It plays important roles in cell proliferation, differentiation, and survival. BDNF/Trk signaling plays a key role in regulating activity-dependent synaptic plasticity. TrkB also contributes to protection against gp120-induced neuronal cell death. TrkB overexpression is associated with poor prognosis in neuroblastoma (NB) and other human cancers. It acts as a suppressor of anoikis (detachment-induced apoptosis) and contributes to tumor metastasis. The TrkB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 61.59  E-value: 9.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  34 KKTLGTGSFGRVMLVK--HKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYV 111
Cdd:cd05093   10 KRELGEGAFGKVFLAEcyNLCPEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYM 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 112 PGGEMFSHLRRIG-------------RFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKR 178
Cdd:cd05093   90 KHGDLNKFLRAHGpdavlmaegnrpaELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRD 169
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255958318 179 VKGRTWTLCGTP-----EYLAPEIILSKGYNKAVDWWALGVLIYEM-AAGYPPFFADQPIQIYEKIVSGKV 243
Cdd:cd05093  170 VYSTDYYRVGGHtmlpiRWMPPESIMYRKFTTESDVWSLGVVLWEIfTYGKQPWYQLSNNEVIECITQGRV 240
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
34-227 9.47e-11

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: 61.42  E-value: 9.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  34 KKTLGTGSFGRVMLVKHKAT---EQYYAMKILdkQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEY 110
Cdd:cd05065    9 EEVIGAGEFGEVCRGRLKLPgkrEIFVAIKTL--KSGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTKSRPVMIITEF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 111 VPGGEMFSHLR-RIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGR----TWT 185
Cdd:cd05065   87 MENGALDSFLRqNDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRFLEDDtsdpTYT 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 255958318 186 LC---GTP-EYLAPEIILSKGYNKAVDWWALGVLIYE-MAAGYPPFF 227
Cdd:cd05065  167 SSlggKIPiRWTAPEAIAYRKFTSASDVWSYGIVMWEvMSYGERPYW 213
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
135-242 9.79e-11

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


Pssm-ID: 270639 [Multi-domain]  Cd Length: 279  Bit Score: 61.70  E-value: 9.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 135 AAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTWTLCGTPEY-----LAPEIILSKGYNKAVDW 209
Cdd:cd05043  122 ALQIACGMSYLHRRGVIHKDIAARNCVIDDELQVKITDNALSRDLFPMDYHCLGDNENrpikwMSLESLVNKEYSSASDV 201
                         90       100       110
                 ....*....|....*....|....*....|....
gi 255958318 210 WALGVLIYEMAA-GYPPFFADQPIQIYEKIVSGK 242
Cdd:cd05043  202 WSFGVLLWELMTlGQTPYVEIDPFEMAAYLKDGY 235
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
17-268 1.01e-10

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Unlike other FGFRs, there is only one splice form of FGFR4. It binds FGF1, FGF2, FGF6, FGF19, and FGF23. FGF19 is a selective ligand for FGFR4. Although disruption of FGFR4 in mice causes no obvious phenotype, in vivo inhibition of FGFR4 in cultured skeletal muscle cells resulted in an arrest of muscle progenitor differentiation. FGF6 and FGFR4 are uniquely expressed in myofibers and satellite cells. FGF6/FGFR4 signaling appears to play a key role in the regulation of muscle regeneration. A polymorphism in FGFR4 is found in head and neck squamous cell carcinoma. FGFR4 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 61.90  E-value: 1.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  17 KWENPPpsnaglEDFERKKTLGTGSFGRVM---------------------LVKHKATEQYYA--------MKILDKQK- 66
Cdd:cd05099    6 KWEFPR------DRLVLGKPLGEGCFGQVVraeaygidksrpdqtvtvavkMLKDNATDKDLAdlisemelMKLIGKHKn 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  67 VVKLKQIehtlnekrilQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGGEMFSHLRRI--GRFSEPHARFYAAQIVLTFEY 144
Cdd:cd05099   80 IINLLGV----------CTQEGPLYVIVEYAAKGNLREFLRARRPPGPDYTFDITKVpeEQLSFKDLVSCAYQVARGMEY 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 145 LHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRV----------KGRTwtlcgTPEYLAPEIILSKGYNKAVDWWALGV 214
Cdd:cd05099  150 LESRRCIHRDLAARNVLVTEDNVMKIADFGLARGVhdidyykktsNGRL-----PVKWMAPEALFDRVYTHQSDVWSFGI 224
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 215 LIYEM-AAGYPPFfadqPIQIYEKIVS-----GKVRFPSHFSSDLKDLLRNLLQVDLTKR 268
Cdd:cd05099  225 LMWEIfTLGGSPY----PGIPVEELFKllregHRMDKPSNCTHELYMLMRECWHAVPTQR 280
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
29-246 1.24e-10

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: 61.24  E-value: 1.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVMLVKHKATEQYyAMKILDKQKVVKlkqiEHTLNEKRILQAVEFPFLVRLeYSFKDNSNLYMVM 108
Cdd:cd05070    9 ESLQLIKRLGNGQFGEVWMGTWNGNTKV-AIKTLKPGTMSP----ESFLEEAQIMKKLKHDKLVQL-YAVVSEEPIYIVT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 109 EYVPGGEMFSHLRR-IGR-FSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTWTL 186
Cdd:cd05070   83 EYMSKGSLLDFLKDgEGRaLKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIEDNEYTA 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255958318 187 CGTPEY----LAPEIILSKGYNKAVDWWALGVLIYEMAA-GYPPFFADQPIQIYEKIVSGkVRFP 246
Cdd:cd05070  163 RQGAKFpikwTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMNNREVLEQVERG-YRMP 226
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
115-253 1.26e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 62.22  E-value: 1.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 115 EMFSHL-RRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGrTWT------LC 187
Cdd:PHA03211 245 DLYTYLgARLRPLGLAQVTAVARQLLSAIDYIHGEGIIHRDIKTENVLVNGPEDICLGDFGAACFARG-SWStpfhygIA 323
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255958318 188 GTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQ--------PIQIYEKIVSGKV---RFPSHFSSDL 253
Cdd:PHA03211 324 GTVDTNAPEVLAGDPYTPSVDIWSAGLVIFEAAVHTASLFSASrgderrpyDAQILRIIRQAQVhvdEFPQHAGSRL 400
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
133-268 1.27e-10

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


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 61.37  E-value: 1.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 133 FYaaQIVLTFEYLH--SLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVK---GRTW------------TLCGTPEYLAP 195
Cdd:cd14036  114 FY--QTCRAVQHMHkqSPPIIHRDLKIENLLIGNQGQIKLCDFGSATTEAhypDYSWsaqkrslvedeiTRNTTPMYRTP 191
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255958318 196 EII-LSKGY--NKAVDWWALGVLIYEMAAGYPPFFADQPIQiyekIVSGKVRFPSHFS--SDLKDLLRNLLQVDLTKR 268
Cdd:cd14036  192 EMIdLYSNYpiGEKQDIWALGCILYLLCFRKHPFEDGAKLR----IINAKYTIPPNDTqyTVFHDLIRSTLKVNPEER 265
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
35-233 1.73e-10

Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. InsR is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the insulin ligand to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR signaling plays an important role in many cellular processes including glucose homeostasis, glycogen synthesis, lipid and protein metabolism, ion and amino acid transport, cell cycle and proliferation, cell differentiation, gene transcription, and nitric oxide synthesis. Insulin resistance, caused by abnormalities in InsR signaling, has been described in diabetes, hypertension, cardiovascular disease, metabolic syndrome, heart failure, and female infertility. The InsR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133192 [Multi-domain]  Cd Length: 288  Bit Score: 60.75  E-value: 1.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVM------LVKHKAtEQYYAMKILDKQKVVKlKQIEHtLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVM 108
Cdd:cd05061   12 RELGQGSFGMVYegnardIIKGEA-ETRVAVKTVNESASLR-ERIEF-LNEASVMKGFTCHHVVRLLGVVSKGQPTLVVM 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 109 EYVPGGEMFSHLRRIGRFSE-------PHAR---FYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKR 178
Cdd:cd05061   89 ELMAHGDLKSYLRSLRPEAEnnpgrppPTLQemiQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVKIGDFGMTRD 168
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 179 VKGRTWTLCGTP-----EYLAPEIILSKGYNKAVDWWALGVLIYEMAAgyppfFADQPIQ 233
Cdd:cd05061  169 IYETDYYRKGGKgllpvRWMAPESLKDGVFTTSSDMWSFGVVLWEITS-----LAEQPYQ 223
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
34-227 1.86e-10

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


Pssm-ID: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 60.65  E-value: 1.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  34 KKTLGTGSFGRVMLVKHK---ATEQYYAMKILDKQKVVKlkQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEY 110
Cdd:cd05066    9 EKVIGAGEFGEVCSGRLKlpgKREIPVAIKTLKAGYTEK--QRRDFLSEASIMGQFDHPNIIHLEGVVTRSKPVMIVTEY 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 111 VPGGEMFSHLRR-IGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKG---RTWTL 186
Cdd:cd05066   87 MENGSLDAFLRKhDGQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDdpeAAYTT 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 255958318 187 CGTP---EYLAPEIILSKGYNKAVDWWALGVLIYE-MAAGYPPFF 227
Cdd:cd05066  167 RGGKipiRWTAPEAIAYRKFTSASDVWSYGIVMWEvMSYGERPYW 211
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
35-241 2.06e-10

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: 60.41  E-value: 2.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMlvKHKATEQYYAMKILDKQKVVKL---KQIEHTLNEKRILQAVEFPFLVRLEYSFKDNS------NLY 105
Cdd:cd05075    6 KTLGEGEFGSVM--EGQLNQDDSVLKVAVKTMKIAIctrSEMEDFLSEAVCMKEFDHPNVMRLIGVCLQNTesegypSPV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 106 MVMEYVPGGEMFSHL--RRIGrfSEPhaRFYAAQIVLTF--------EYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGF 175
Cdd:cd05075   84 VILPFMKHGDLHSFLlySRLG--DCP--VYLPTQMLVKFmtdiasgmEYLSSKNFIHRDLAARNCMLNENMNVCVADFGL 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255958318 176 AKRVKG----RTWTLCGTP-EYLAPEIILSKGYNKAVDWWALGVLIYEMAA-GYPPFFADQPIQIYEKIVSG 241
Cdd:cd05075  160 SKKIYNgdyyRQGRISKMPvKWIAIESLADRVYTTKSDVWSFGVTMWEIATrGQTPYPGVENSEIYDYLRQG 231
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
37-226 3.44e-10

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: 60.04  E-value: 3.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKQKvvklKQIEHTLNEKRILQAVE-FPFLVRLEYSFKDNsnLYMVMEYVPGGE 115
Cdd:cd14149   20 IGSGSFGTVYKGKWHGDVAVKILKVVDPTP----EQFQAFRNEVAVLRKTRhVNILLFMGYMTKDN--LAIVTQWCEGSS 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 116 MFSHLRRI-GRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKrVKGRtWT-------LC 187
Cdd:cd14149   94 LYKHLHVQeTKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAT-VKSR-WSgsqqveqPT 171
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 255958318 188 GTPEYLAPEIILSKGYNK---AVDWWALGVLIYEMAAGYPPF 226
Cdd:cd14149  172 GSILWMAPEVIRMQDNNPfsfQSDVYSYGIVLYELMTGELPY 213
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
35-268 3.53e-10

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: 59.86  E-value: 3.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVM---LVKHKATEQYYAMKILdKQKVVKLKQIEHTLNEKRILQAVEFPFLVRL-----EYSFKDNSNLYM 106
Cdd:cd05035    5 KILGEGEFGSVMeaqLKQDDGSQLKVAVKTM-KVDIHTYSEIEEFLSEAACMKDFDHPNVMRLigvcfTASDLNKPPSPM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 107 V-MEYVPGGEMFSHL--RRIGRFSE--PHARF--YAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRV 179
Cdd:cd05035   84 ViLPFMKHGDLHSYLlySRLGGLPEklPLQTLlkFMVDIAKGMEYLSNRNFIHRDLAARNCMLDENMTVCVADFGLSRKI 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 180 KG----RTWTLCGTP-EYLAPEIILSKGYNKAVDWWALGVLIYEMAA-GYPPFFADQPIQIYEKIVSG-KVRFPSHFSSD 252
Cdd:cd05035  164 YSgdyyRQGRISKMPvKWIALESLADNVYTSKSDVWSFGVTMWEIATrGQTPYPGVENHEIYDYLRNGnRLKQPEDCLDE 243
                        250
                 ....*....|....*.
gi 255958318 253 LKDLLRNLLQVDLTKR 268
Cdd:cd05035  244 VYFLMYFCWTVDPKDR 259
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
18-268 3.56e-10

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


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 60.09  E-value: 3.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  18 WENPPpsnaglEDFERKKTLGTGSFGRVMLVKHKATEQYyAMKILDKQKVVKlkqiEHTLNEKRILQAVEFPFLVRLeYS 97
Cdd:cd05069    7 WEIPR------ESLRLDVKLGQGCFGEVWMGTWNGTTKV-AIKTLKPGTMMP----EAFLQEAQIMKKLRHDKLVPL-YA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  98 FKDNSNLYMVMEYVPGGEMFSHLRR-IGRFSE-PHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGF 175
Cdd:cd05069   75 VVSEEPIYIVTEFMGKGSLLDFLKEgDGKYLKlPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 176 AKRVKGRTWTLCGTPEY----LAPEIILSKGYNKAVDWWALGVLIYEMAA-GYPPFFADQPIQIYEKIVSG-KVRFPSHF 249
Cdd:cd05069  155 ARLIEDNEYTARQGAKFpikwTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMVNREVLEQVERGyRMPCPQGC 234
                        250
                 ....*....|....*....
gi 255958318 250 SSDLKDLLRNLLQVDLTKR 268
Cdd:cd05069  235 PESLHELMKLCWKKDPDER 253
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
17-248 3.84e-10

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The VEGFR subfamily consists of VEGFR1 (Flt1), VEGFR2 (Flk1), VEGFR3 (Flt4), and similar proteins. VEGFR subfamily members are receptor PTKss (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. There are five VEGF ligands in mammals, which bind, in an overlapping pattern to the three VEGFRs, which can form homo or heterodimers. VEGFRs regulate the cardiovascular system. They are critical for vascular development during embryogenesis and blood vessel formation in adults. They induce cellular functions common to other growth factor receptors such as cell migration, survival, and proliferation. The VEGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 59.81  E-value: 3.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  17 KWENPPpsnaglEDFERKKTLGTGSFGRVML-----VKHKATEQYYAMKILD--------KQKVVKLK---QIEHTLNEK 80
Cdd:cd05054    1 KWEFPR------DRLKLGKPLGRGAFGKVIQasafgIDKSATCRTVAVKMLKegatasehKALMTELKiliHIGHHLNVV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  81 RILQAVEfpflvrleysfKDNSNLYMVMEYVPGGEMFSHLR--RIGRFSEPHARF------------------------Y 134
Cdd:cd05054   75 NLLGACT-----------KPGGPLMVIVEFCKFGNLSNYLRskREEFVPYRDKGArdveeeedddelykepltledlicY 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 135 AAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRV-KGRTWTLCGTP----EYLAPEIILSKGYNKAVDW 209
Cdd:cd05054  144 SFQVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIyKDPDYVRKGDArlplKWMAPESIFDKVYTTQSDV 223
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 255958318 210 WALGVLIYEM----AAGYPPFFADQpiQIYEKIVSG-KVRFPSH 248
Cdd:cd05054  224 WSFGVLLWEIfslgASPYPGVQMDE--EFCRRLKEGtRMRAPEY 265
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
37-241 4.15e-10

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP2, also called RICK or CARDIAK, harbors a C-terminal Caspase Activation and Recruitment domain (CARD) belonging to the Death domain (DD) superfamily. It functions as an effector kinase downstream of the pattern recognition receptors from the Nod-like (NLR) family, Nod1 and Nod2, which recognizes bacterial peptidoglycans released upon infection. RIP2 may also be involved in regulating wound healing and keratinocyte proliferation. RIP kinases serve as essential sensors of cellular stress. The RIP2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270928 [Multi-domain]  Cd Length: 284  Bit Score: 59.93  E-value: 4.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGGEM 116
Cdd:cd14026    5 LSRGAFGTVSRARHADWRVTVAIKCLKLDSPVGDSERNCLLKEAEILHKARFSYILPILGICNEPEFLGIVTEYMTNGSL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 117 FSHLRRIGRFSE---PHARFYAAQIVLTFEYLHSLD--LIYRDLKPENLLIDHQGYIQVTDFGFAK-RV----KGRTWT- 185
Cdd:cd14026   85 NELLHEKDIYPDvawPLRLRILYEIALGVNYLHNMSppLLHHDLKTQNILLDGEFHVKIADFGLSKwRQlsisQSRSSKs 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255958318 186 --LCGTPEYLAPEIILSKGYNKAV---DWWALGVLIYEMAAGYPPFF-ADQPIQIYEKIVSG 241
Cdd:cd14026  165 apEGGTIIYMPPEEYEPSQKRRASvkhDIYSYAIIMWEVLSRKIPFEeVTNPLQIMYSVSQG 226
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
22-226 4.23e-10

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: 59.69  E-value: 4.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  22 PPSNAGLEdferkKTLGTGSFGRV---MLVKHKATEQYYAMKIL-----DKQKVvklkqieHTLNEKRILQAVEFPFLVR 93
Cdd:cd05033    2 DASYVTIE-----KVIGGGEFGEVcsgSLKLPGKKEIDVAIKTLksgysDKQRL-------DFLTEASIMGQFDHPNVIR 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  94 LEYSFKDNSNLYMVMEYVPGGEMFSHLRrigrfsEPHARFYAAQIV-------LTFEYLHSLDLIYRDLKPENLLIDHQG 166
Cdd:cd05033   70 LEGVVTKSRPVMIVTEYMENGSLDKFLR------ENDGKFTVTQLVgmlrgiaSGMKYLSEMNYVHRDLAARNILVNSDL 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255958318 167 YIQVTDFGFAKRVKGR--TWTLCG--TP-EYLAPEIILSKGYNKAVDWWALGVLIYE-MAAGYPPF 226
Cdd:cd05033  144 VCKVSDFGLSRRLEDSeaTYTTKGgkIPiRWTAPEAIAYRKFTSASDVWSFGIVMWEvMSYGERPY 209
pknD PRK13184
serine/threonine-protein kinase PknD;
37-219 4.70e-10

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 60.94  E-value: 4.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQYYAMKIL--DKQKVVKLKQieHTLNEKRILQAVEFPFLVRLeYSFKDNSNL-YMVMEYVPG 113
Cdd:PRK13184  10 IGKGGMGEVYLAYDPVCSRRVALKKIreDLSENPLLKK--RFLREAKIAADLIHPGIVPV-YSICSDGDPvYYTMPYIEG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 114 GEMFSHLRRIGR---FSEPHAR----------FYaaQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVK 180
Cdd:PRK13184  87 YTLKSLLKSVWQkesLSKELAEktsvgaflsiFH--KICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGAAIFKK 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 181 GRTWTL---------------------CGTPEYLAPEIILSKGYNKAVDWWALGVLIYEM 219
Cdd:PRK13184 165 LEEEDLldidvdernicyssmtipgkiVGTPDYMAPERLLGVPASESTDIYALGVILYQM 224
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
35-315 4.82e-10

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: 60.03  E-value: 4.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQ-------YYAMKILDKQKVVKlkQIEHTLNEKRILQAV-EFPFLVRLEYSFKDNSNLYM 106
Cdd:cd05100   18 KPLGEGCFGQVVMAEAIGIDKdkpnkpvTVAVKMLKDDATDK--DLSDLVSEMEMMKMIgKHKNIINLLGACTQDGPLYV 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 107 VMEYVPGGEMFSHLRR-----------IGRFSEPHARFY-----AAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQV 170
Cdd:cd05100   96 LVEYASKGNLREYLRArrppgmdysfdTCKLPEEQLTFKdlvscAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKI 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 171 TDFGFAKRVKGRTWTLCGTP-----EYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRF 245
Cdd:cd05100  176 ADFGLARDVHNIDYYKKTTNgrlpvKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGHRM 255
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255958318 246 --PSHFSSDLKDLLRNLLQVDLTKRfGNLKNGVSDIKTHKWFATTD-----WIAIYQRKVEAPFIPKFRGSGDTSNF 315
Cdd:cd05100  256 dkPANCTHELYMIMRECWHAVPSQR-PTFKQLVEDLDRVLTVTSTDeyldlSVPFEQYSPGCPDSPSSCSSGDDSVF 331
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
35-220 5.32e-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: 59.59  E-value: 5.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKatEQYYAMKI---LDKQKVVKLKQIEHT--LNEKRILQavefpFLVRLEYSFKDNSNLYMVME 109
Cdd:cd14056    1 KTIGKGRYGEVWLGKYR--GEKVAVKIfssRDEDSWFRETEIYQTvmLRHENILG-----FIAADIKSTGSWTQLWLITE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 110 YVPGGEMFSHLRRiGRFSEPHARFYAAQIVLTFEYLHS--------LDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKG 181
Cdd:cd14056   74 YHEHGSLYDYLQR-NTLDTEEALRLAYSAASGLAHLHTeivgtqgkPAIAHRDLKSKNILVKRDGTCCIADLGLAVRYDS 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 255958318 182 RTWTL-------CGTPEYLAPEiILSKGYN-------KAVDWWALGVLIYEMA 220
Cdd:cd14056  153 DTNTIdippnprVGTKRYMAPE-VLDDSINpksfesfKMADIYSFGLVLWEIA 204
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
35-259 5.49e-10

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: 59.64  E-value: 5.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  35 KTLGTGSFGRVMLVKHKATEQYYAMKIldKQKVVKL-------KQIEHTLNEKRILQAV-EFPFLVRLEYSFKDNSNLYM 106
Cdd:cd05098   19 KPLGEGCFGQVVLAEAIGLDKDKPNRV--TKVAVKMlksdateKDLSDLISEMEMMKMIgKHKNIINLLGACTQDGPLYV 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 107 VMEYVPGGemfsHLRRIGRFSEPHARFY--------------------AAQIVLTFEYLHSLDLIYRDLKPENLLIDHQG 166
Cdd:cd05098   97 IVEYASKG----NLREYLQARRPPGMEYcynpshnpeeqlsskdlvscAYQVARGMEYLASKKCIHRDLAARNVLVTEDN 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 167 YIQVTDFGFAKRVKGRTWTLCGTP-----EYLAPEIILSKGYNKAVDWWALGVLIYEM--AAGYPpfFADQPIQIYEKIV 239
Cdd:cd05098  173 VMKIADFGLARDIHHIDYYKKTTNgrlpvKWMAPEALFDRIYTHQSDVWSFGVLLWEIftLGGSP--YPGVPVEELFKLL 250
                        250       260
                 ....*....|....*....|..
gi 255958318 240 SGKVRF--PSHFSSDLKDLLRN 259
Cdd:cd05098  251 KEGHRMdkPSNCTNELYMMMRD 272
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
74-219 5.50e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 60.48  E-value: 5.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  74 EHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGGEMFSHLRRIGRfsepharfyaaQIVLTFEYLHSLDLIYR 153
Cdd:PHA03210 223 ENILKIEEILRSEANTYMITQKYDFDLYSFMYDEAFDWKDRPLLKQTRAIMK-----------QLLCAVEYIHDKKLIHR 291
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 154 DLKPENLLIDHQGYIQVTDFG----FAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEM 219
Cdd:PHA03210 292 DIKLENIFLNCDGKIVLGDFGtampFEKEREAFDYGWVGTVATNSPEILAGDGYCEITDIWSCGLILLDM 361
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
29-258 5.51e-10

Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; Tie1; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie1 is a receptor tyr kinase (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. No specific ligand has been identified for Tie1, although the angiopoietin, Ang-1, binds to Tie1 through integrins at high concentrations. In vivo studies of Tie1 show that it is critical in vascular development.


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 59.63  E-value: 5.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  29 EDFERKKTLGTGSFGRVM--LVKHKATEQYYAMKILdKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYM 106
Cdd:cd05089    2 EDIKFEDVIGEGNFGQVIkaMIKKDGLKMNAAIKML-KEFASENDHRDFAGELEVLCKLGHHPNIINLLGACENRGYLYI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 107 VMEYVPGGEMFSHLRRiGRFSEPHARF-----------------YAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQ 169
Cdd:cd05089   81 AIEYAPYGNLLDFLRK-SRVLETDPAFakehgtastltsqqllqFASDVAKGMQYLSEKQFIHRDLAARNVLVGENLVSK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 170 VTDFG-------FAKRVKGRTwtlcgTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAA-GYPPFFADQPIQIYEKIVSG 241
Cdd:cd05089  160 IADFGlsrgeevYVKKTMGRL-----PVRWMAIESLNYSVYTTKSDVWSFGVLLWEIVSlGGTPYCGMTCAELYEKLPQG 234
                        250
                 ....*....|....*...
gi 255958318 242 -KVRFPSHFSSDLKDLLR 258
Cdd:cd05089  235 yRMEKPRNCDDEVYELMR 252
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
37-229 6.65e-10

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: 59.07  E-value: 6.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEqyYAMKILDKQKVVKLKQIEHT-LNEKRILQAVEFPFLVRLE-YSFkDNSNLYMVMEYVPGG 114
Cdd:cd14159    1 IGEGGFGCVYQAVMRNTE--YAVKRLKEDSELDWSVVKNSfLTEVEKLSRFRHPNIVDLAgYSA-QQGNYCLIYVYLPNG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 115 EMFSHLRRIGRF---SEPHARFYAAQIVLTFEYLHSLD--LIYRDLKPENLLIDHQGYIQVTDFGFAK-----------R 178
Cdd:cd14159   78 SLEDRLHCQVSCpclSWSQRLHVLLGTARAIQYLHSDSpsLIHGDVKSSNILLDAALNPKLGDFGLARfsrrpkqpgmsS 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 255958318 179 VKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFAD 229
Cdd:cd14159  158 TLARTQTVRGTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELLTGRRAMEVD 208
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
135-226 7.12e-10

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: 58.56  E-value: 7.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 135 AAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKrVKGRtWTLCGTPE-------YLAPEIILSKG---YN 204
Cdd:cd14062   95 ARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLAT-VKTR-WSGSQQFEqptgsilWMAPEVIRMQDenpYS 172
                         90       100
                 ....*....|....*....|..
gi 255958318 205 KAVDWWALGVLIYEMAAGYPPF 226
Cdd:cd14062  173 FQSDVYAFGIVLYELLTGQLPY 194
S_TK_X smart00133
Extension to Ser/Thr-type protein kinases;
288-326 9.64e-10

Extension to Ser/Thr-type protein kinases;


Pssm-ID: 214529  Cd Length: 64  Bit Score: 53.90  E-value: 9.64e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 255958318   288 TDWIAIYQRKVEAPFIPKFRGSGDTSNFD-DYEEEEIRVS 326
Cdd:smart00133   3 IDWDKLENKEIEPPFVPKIKSPTDTSNFDpEFTEETPVLT 42
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
37-226 1.20e-09

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


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 58.28  E-value: 1.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVML----VKHKATEQYYAMKILDKQKVVKlkQIEHTLNekrILQAVEFPFLVRLEYSFKDNSNLYMVMEYVP 112
Cdd:cd14158   23 LGEGGFGVVFKgyinDKNVAVKKLAAMVDISTEDLTK--QFEQEIQ---VMAKCQHENLVELLGYSCDGPQLCLVYTYMP 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 113 GGemfSHLRRIGRFSEPHARFYAAQIVLT------FEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTWTL 186
Cdd:cd14158   98 NG---SLLDRLACLNDTPPLSWHMRCKIAqgtangINYLHENNHIHRDIKSANILLDETFVPKISDFGLARASEKFSQTI 174
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 255958318 187 -----CGTPEYLAPEIILSKGYNKAvDWWALGVLIYEMAAGYPPF 226
Cdd:cd14158  175 mteriVGTTAYMAPEALRGEITPKS-DIFSFGVVLLEIITGLPPV 218
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
30-226 1.21e-09

Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER4 (ErbB4) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands that bind HER4 fall into two groups, the neuregulins (or heregulins) and some EGFR (HER1) ligands including betacellulin, HBEGF, and epiregulin. All four neuregulins (NRG1-4) interact with HER4. Upon ligand binding, HER4 forms homo- or heterodimers with other HER proteins. HER4 is essential in embryonic development. It is implicated in mammary gland, cardiac, and neural development. As a postsynaptic receptor of NRG1, HER4 plays an important role in synaptic plasticity and maturation. The impairment of NRG1/HER4 signaling may contribute to schizophrenia. The HER4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173655 [Multi-domain]  Cd Length: 303  Bit Score: 58.54  E-value: 1.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  30 DFERKKTLGTGSFGRVM----LVKHKATEQYYAMKILDKQKVVKlKQIEHtLNEKRILQAVEFPFLVRLeYSFKDNSNLY 105
Cdd:cd05110    8 ELKRVKVLGSGAFGTVYkgiwVPEGETVKIPVAIKILNETTGPK-ANVEF-MDEALIMASMDHPHLVRL-LGVCLSPTIQ 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 106 MVMEYVPGGEMFSHLRRigrfsepHARFYAAQIVLTF--------EYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAK 177
Cdd:cd05110   85 LVTQLMPHGCLLDYVHE-------HKDNIGSQLLLNWcvqiakgmMYLEERRLVHRDLAARNVLVKSPNHVKITDFGLAR 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 255958318 178 RVKG--RTWTLCGTP---EYLAPEIILSKGYNKAVDWWALGVLIYE-MAAGYPPF 226
Cdd:cd05110  158 LLEGdeKEYNADGGKmpiKWMALECIHYRKFTHQSDVWSYGVTIWElMTFGGKPY 212
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
134-268 1.26e-09

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR beta is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR beta forms homodimers or heterodimers with PDGFR alpha, depending on the nature of the PDGF ligand. PDGF-BB and PDGF-DD induce PDGFR beta homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR beta signaling leads to a variety of cellular effects including the stimulation of cell growth and chemotaxis, as well as the inhibition of apoptosis and GAP junctional communication. It is critical in normal angiogenesis as it is involved in the recruitment of pericytes and smooth muscle cells essential for vessel stability. Aberrant PDGFR beta expression is associated with some human cancers. The continuously-active fusion proteins of PDGFR beta with COL1A1 and TEL are associated with dermatofibrosarcoma protuberans (DFSP) and a subset of chronic myelomonocytic leukemia (CMML), respectively. The PDGFR beta subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133238 [Multi-domain]  Cd Length: 401  Bit Score: 58.87  E-value: 1.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 134 YAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRV--------KGRTWtlcgTP-EYLAPEIILSKGYN 204
Cdd:cd05107  244 FSYQVANGMEFLASKNCVHRDLAARNVLICEGKLVKICDFGLARDImrdsnyisKGSTF----LPlKWMAPESIFNNLYT 319
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255958318 205 KAVDWWALGVLIYEM--AAGYPpfFADQPI--QIYEKIVSG-KVRFPSHFSSDLKDLLRNLLQVDLTKR 268
Cdd:cd05107  320 TLSDVWSFGILLWEIftLGGTP--YPELPMneQFYNAIKRGyRMAKPAHASDEIYEIMQKCWEEKFEIR 386
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
27-219 1.43e-09

Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The DDR subfamily consists of homologs of mammalian DDR1, DDR2, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270644 [Multi-domain]  Cd Length: 297  Bit Score: 58.12  E-value: 1.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  27 GLEDFERKKTLGTGSFGRVMLVkhkateqyyAMKILDKQKVVKLKqiEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYM 106
Cdd:cd05051   28 GLSDLTSDDFIGNDNKDEPVLV---------AVKMLRPDASKNAR--EDFLKEVKIMSQLKDPNIVRLLGVCTRDEPLCM 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 107 VMEYVPGGEMFSHLR-RIGRFSEPHAR-----------FYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFG 174
Cdd:cd05051   97 IVEYMENGDLNQFLQkHEAETQGASATnsktlsygtllYMATQIASGMKYLESLNFVHRDLATRNCLVGPNYTIKIADFG 176
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 255958318 175 FAK--------RVKGRT-----WtlcgtpeyLAPEIILSKGYNKAVDWWALGVLIYEM 219
Cdd:cd05051  177 MSRnlysgdyyRIEGRAvlpirW--------MAWESILLGKFTTKSDVWAFGVTLWEI 226
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
38-253 1.53e-09

Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. There are two types of TGFbeta receptors included in this subfamily, I and II, that play different roles in signaling. For signaling to occur, the ligand first binds to the high-affinity type II receptor, which is followed by the recruitment of the low-affinity type I receptor to the complex and its activation through trans-phosphorylation by the type II receptor. The active type I receptor kinase starts intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. Different ligands interact with various combinations of types I and II receptors to elicit a specific signaling pathway. Activins primarily signal through combinations of ACVR1b/ALK7 and ACVR2a/b; myostatin and GDF11 through TGFbR1/ALK4 and ACVR2a/b; BMPs through ACVR1/ALK1 and BMPR2; and TGFbeta through TGFbR1 and TGFbR2. The TGFbR-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270900 [Multi-domain]  Cd Length: 289  Bit Score: 58.22  E-value: 1.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  38 GTGSFGRVMlvKHKATEQYYAMKIL---DKQKVVKLKQIEHTLNEKR--ILQavefpFLVRLEYSFKDNSNLYMVMEYVP 112
Cdd:cd13998    4 GKGRFGEVW--KASLKNEPVAVKIFssrDKQSWFREKEIYRTPMLKHenILQ-----FIAADERDTALRTELWLVTAFHP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 113 GGEMFSHLRR-------IGRFSEPHARFYAaqivltfeYLHS---------LDLIYRDLKPENLLIDHQGYIQVTDFGFA 176
Cdd:cd13998   77 NGSL*DYLSLhtidwvsLCRLALSVARGLA--------HLHSeipgctqgkPAIAHRDLKSKNILVKNDGTCCIADFGLA 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 177 KRVKGRTWTL-------CGTPEYLAPEiILSKGYN-------KAVDWWALGVLIYEMAA----------GY-PPFFADQP 231
Cdd:cd13998  149 VRLSPSTGEEdnanngqVGTKRYMAPE-VLEGAINlrdfesfKRVDIYAMGLVLWEMASrctdlfgiveEYkPPFYSEVP 227
                        250       260
                 ....*....|....*....|....*....
gi 255958318 232 I-----QIYEKIVSGKVR--FPSHFSSDL 253
Cdd:cd13998  228 NhpsfeDMQEVVVRDKQRpnIPNRWLSHP 256
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
134-230 1.78e-09

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR2 (or Flk1) binds the ligands VEGFA, VEGFC, VEGFD and VEGFE. VEGFR2 signaling is implicated in all aspects of normal and pathological vascular endothelial cell biology. It induces a variety of cellular effects including migration, survival, and proliferation. It is critical in regulating embryonic vascular development and angiogenesis. VEGFR2 is the major signal transducer in pathological angiogenesis including cancer and diabetic retinopathy, and is a target for inhibition in cancer therapy. The carboxyl terminus of VEGFR2 plays an important role in its autophosphorylation and activation. VEGFR2 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 58.45  E-value: 1.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 134 YAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRV-KGRTWTLCGTP----EYLAPEIILSKGYNKAVD 208
Cdd:cd05103  184 YSFQVAKGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIyKDPDYVRKGDArlplKWMAPETIFDRVYTIQSD 263
                         90       100
                 ....*....|....*....|....*.
gi 255958318 209 WWALGVLIYEM----AAGYPPFFADQ 230
Cdd:cd05103  264 VWSFGVLLWEIfslgASPYPGVKIDE 289
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
37-230 1.83e-09

Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L6 is also called CDK8-like and was previously referred to as CDK11. However, this is a confusing nomenclature as CDC2L6 is distinct from CDC2L1, which is represented by the two protein products from its gene, called CDK11(p110) and CDK11(p58), as well as the caspase-processed CDK11(p46). CDK11(p110), CDK11(p58), and CDK11(p46)do not belong to this subfamily. CDC2L6 is an associated protein of Mediator, a multiprotein complex that provides a platform to connect transcriptional and chromatin regulators and cofactors, in order to activate and mediate RNA polymerase II transcription. CDC2L6 is localized mainly in the nucleus amd exerts an opposing effect to CDK8 in VP16-dependent transcriptional activation by being a negative regulator. 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 CDC2L6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270850 [Multi-domain]  Cd Length: 318  Bit Score: 58.16  E-value: 1.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQyyamkildkQKVVKLKQIEHT------LNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEY 110
Cdd:cd07867   10 VGRGTYGHVYKAKRKDGKD---------EKEYALKQIEGTgismsaCREIALLRELKHPNVIALQKVFLSHSDRKVWLLF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 111 VPGGEMFSHLRRIGRFSEPH----------ARFYAAQIVLTFEYLHSLDLIYRDLKPENLLI----DHQGYIQVTDFGFA 176
Cdd:cd07867   81 DYAEHDLWHIIKFHRASKANkkpmqlprsmVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFA 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255958318 177 KRVKGRTWTLCG------TPEYLAPEIIL-SKGYNKAVDWWALGVLIYEMAAGYPPFFADQ 230
Cdd:cd07867  161 RLFNSPLKPLADldpvvvTFWYRAPELLLgARHYTKAIDIWAIGCIFAELLTSEPIFHCRQ 221
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
134-268 1.98e-09

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR3 (or Flt4) preferentially binds the ligands VEGFC and VEGFD. VEGFR3 is essential for lymphatic endothelial cell (EC) development and function. It has been shown to regulate adaptive immunity during corneal transplantation. VEGFR3 is upregulated on blood vascular ECs in pathological conditions such as vascular tumors and the periphery of solid tumors. It plays a role in cancer progression and lymph node metastasis. Missense mutations in the VEGFR3 gene are associated with primary human lymphedema. VEGFR3 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 58.07  E-value: 1.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 134 YAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRV-KGRTWTLCGTP----EYLAPEIILSKGYNKAVD 208
Cdd:cd05102  177 YSFQVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIyKDPDYVRKGSArlplKWMAPESIFDKVYTTQSD 256
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255958318 209 WWALGVLIYEM----AAGYPpffadqPIQIYEKIVS-----GKVRFPSHFSSDLKDLLRNLLQVDLTKR 268
Cdd:cd05102  257 VWSFGVLLWEIfslgASPYP------GVQINEEFCQrlkdgTRMRAPEYATPEIYRIMLSCWHGDPKER 319
STKc_CK1_gamma cd14126
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1 gamma; STKs catalyze ...
30-270 5.87e-09

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1 gamma; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. CK1gamma proteins are unique within the CK1 subfamily in that they are palmitoylated at the C-termini and are anchored to the plasma membrane. CK1gamma is involved in transducing the signaling of LDL-receptor-related protein 6 (LRP6) through direct phosphorylation following Wnt stimulation, resulting in the recruitment of the scaffold protein Axin. In Xenopus embryos, CK1gamma is required during anterio-posterior patterning. In higher vertebrates, three CK1gamma (gamma1-3) isoforms exist. In mammalian cells, CK1gamma2 has been implicated in regulating the synthesis of sphingomyelin, a phospholipid that is found in the outer leaflet of the plasma membrane, by hyperphosphorylating and inactivating the ceramide transfer protein CERT. CK1gamma2 also phosphorylates the transcription factor Smad-3 resulting in its ubiquitination and degradation. It inhibits Smad-3 mediated responses of Transforming Growth Factor-beta (TGF-beta) including cell growth arrest. The CK1 gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271028 [Multi-domain]  Cd Length: 288  Bit Score: 56.28  E-value: 5.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  30 DFERKKTLGTGSFGRVMLVKHKATEQYYAMKILD-KQKVVKLkQIEHTLnEKRILQAVEFPFLVRLEYSFKDNSnlyMVM 108
Cdd:cd14126    1 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPmKSRAPQL-HLEYRF-YKLLGQAEGLPQVYYFGPCGKYNA---MVL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 109 EYV-PGGE-MFSHLRRigRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGY-----IQVTDFGFAKR-VK 180
Cdd:cd14126   76 ELLgPSLEdLFDLCDR--TFSLKTVLMIAIQLISRIEYVHSKHLIYRDVKPENFLIGRQSTkkqhvIHIIDFGLAKEyID 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 181 GRT---------WTLCGTPEYLAPEIILSKGYNKAVDWWALG-VLIYEMAAGYP--PFFADQPIQIYEKIVSGKVR---- 244
Cdd:cd14126  154 PETnkhipyrehKSLTGTARYMSINTHLGKEQSRRDDLEALGhMFMYFLRGSLPwqGLKADTLKERYQKIGDTKRAtpie 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 255958318 245 -----FPSHFSSDLK-------------DLLRNLLQvDLTKRFG 270
Cdd:cd14126  234 vlcenFPEEMATYLRyvrrldffetpdyDYLRKLFT-DLFDRKG 276
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
37-230 5.95e-09

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK8 can act as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II (RNAP II)-dependent transcription. CDK8 phosphorylates cyclin H, a subunit of the general transcription factor TFIIH, which results in the inhibition of TFIIH-dependent phosphorylation of the C-terminal domain of RNAP II, facilitating the inhibition of transcription. It has also been shown to promote transcription by a mechanism that is likely to involve RNAP II phosphorylation. CDK8 also functions as a stimulus-specific positive coregulator of p53 transcriptional responses. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270851 [Multi-domain]  Cd Length: 333  Bit Score: 56.60  E-value: 5.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRVMLVKHKATEQyyamkildkQKVVKLKQIEHT------LNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEY 110
Cdd:cd07868   25 VGRGTYGHVYKAKRKDGKD---------DKDYALKQIEGTgismsaCREIALLRELKHPNVISLQKVFLSHADRKVWLLF 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 111 VPGGEMFSHLRRIGRFSEPH----------ARFYAAQIVLTFEYLHSLDLIYRDLKPENLLI----DHQGYIQVTDFGFA 176
Cdd:cd07868   96 DYAEHDLWHIIKFHRASKANkkpvqlprgmVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFA 175
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255958318 177 KRVKGRTWTLCG------TPEYLAPEIIL-SKGYNKAVDWWALGVLIYEMAAGYPPFFADQ 230
Cdd:cd07868  176 RLFNSPLKPLADldpvvvTFWYRAPELLLgARHYTKAIDIWAIGCIFAELLTSEPIFHCRQ 236
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
37-232 1.02e-08

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror kinases are expressed in many tissues during development. Avian Ror1 was found to be involved in late limb development. Studies in mice reveal that Ror1 is important in the regulation of neurite growth in central neurons, as well as in respiratory development. Loss of Ror1 also enhances the heart and skeletal abnormalities found in Ror2-deficient mice. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 55.40  E-value: 1.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318  37 LGTGSFGRV----MLVKHKATEQYYAMKILdkQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVP 112
Cdd:cd05090   13 LGECAFGKIykghLYLPGMDHAQLVAIKTL--KDYNNPQQWNEFQQEASLMTELHHPNIVCLLGVVTQEQPVCMLFEFMN 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958318 113 GGEMFSHL------RRIGRFSEP---------HARFY--AAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGF 175
Cdd:cd05090   91 QGDLHEFLimrsphSDVGCSSDEdgtvkssldHGDFLhiAIQIAAGMEYLSSHFFVHKDLAARNILVGEQLHVKISDLGL 170
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255958318 176 AKRVKGRTWtLCGTPE------YLAPEIILSKGYNKAVDWWALGVLIYEM-AAGYPPF--FADQPI 232
Cdd:cd05090  171 SREIYSSDY-YRVQNKsllpirWMPPEAIMYGKFSSDSDIWSFGVVLWEIfSFGLQPYygFSNQEV 235
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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