NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2056392213|ref|NP_001382220|]
View 

death-associated protein kinase 2 isoform 14 [Homo sapiens]

Protein Classification

death-associated protein kinase 2( domain architecture ID 10197723)

death-associated protein kinase 2 (DAPK2) 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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
17-285 0e+00

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: 569.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  17 QKVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVSREEIEREVSILRQVLHHNVITLHDVYENR 96
Cdd:cd14196     1 QKVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVSREEIEREVSILRQVLHPNIITLHDVYENR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  97 TDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLAH 176
Cdd:cd14196    81 TDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLAH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 177 EIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSE 256
Cdd:cd14196   161 EIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSHTSE 240
                         250       260
                  ....*....|....*....|....*....
gi 2056392213 257 LAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14196   241 LAKDFIRKLLVKETRKRLTIQEALRHPWI 269
 
Name Accession Description Interval E-value
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
17-285 0e+00

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: 569.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  17 QKVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVSREEIEREVSILRQVLHHNVITLHDVYENR 96
Cdd:cd14196     1 QKVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVSREEIEREVSILRQVLHPNIITLHDVYENR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  97 TDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLAH 176
Cdd:cd14196    81 TDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLAH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 177 EIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSE 256
Cdd:cd14196   161 EIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSHTSE 240
                         250       260
                  ....*....|....*....|....*....
gi 2056392213 257 LAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14196   241 LAKDFIRKLLVKETRKRLTIQEALRHPWI 269
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
23-285 6.65e-101

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 300.99  E-value: 6.65e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213   23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRasrrgVSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIK-----KDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  103 LELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAHEIEDGV 182
Cdd:smart00220  76 MEYCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENI-LLDED---GHVKLADFGLARQLDPGE 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  183 EFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSELAKDFI 262
Cdd:smart00220 152 KLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDLI 231
                          250       260
                   ....*....|....*....|...
gi 2056392213  263 RKLLVKETRKRLTIQEALRHPWI 285
Cdd:smart00220 232 RKLLVKDPEKRLTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
23-285 1.11e-63

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 204.40  E-value: 1.11e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRqsraSRRGVSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKE----KIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQKESLSEEEATSFIKQILDGVnylhtkkiahfdlkpenimlldknipiphiklidfglaheiEDGV 182
Cdd:pfam00069  77 LEYVEGGSLFDLLSEKGAFSEREAKFIMKQILEGL-----------------------------------------ESGS 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 183 EFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSElAKDFI 262
Cdd:pfam00069 116 SLTTFVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELPSNLSEE-AKDLL 194
                         250       260
                  ....*....|....*....|...
gi 2056392213 263 RKLLVKETRKRLTIQEALRHPWI 285
Cdd:pfam00069 195 KKLLKKDPSKRLTATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
23-282 7.79e-48

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 170.58  E-value: 7.79e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRrgvSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:COG0515     9 YRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPE---ARERFRREARALARLNHPNIVRVYDVGEEDGRPYLV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIEDGV 182
Cdd:COG0515    86 MEYVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDG----RVKLIDFGIARALGGAT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 183 --EFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSELAKD 260
Cdd:COG0515   162 ltQTGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRPDLPPALDA 241
                         250       260
                  ....*....|....*....|..
gi 2056392213 261 FIRKLLVKETRKRLTIQEALRH 282
Cdd:COG0515   242 IVLRALAKDPEERYQSAAELAA 263
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
18-289 1.44e-39

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 144.58  E-value: 1.44e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  18 KVEDFyDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRgvsREEIEREVSILRQVLHHNVITLHDVYENRT 97
Cdd:PTZ00263   16 KLSDF-EMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQ---VQHVAQEKSILMELSHPFIVNMMCSFQDEN 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  98 DVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAHE 177
Cdd:PTZ00263   92 RVYFLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENL-LLDNK---GHVKVTDFGFAKK 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 178 IEDgvEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQtsel 257
Cdd:PTZ00263  168 VPD--RTFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWFDGR---- 241
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2056392213 258 AKDFIRKLLVKETRKRL-----TIQEALRHPWITPVD 289
Cdd:PTZ00263  242 ARDLVKGLLQTDHTKRLgtlkgGVADVKNHPYFHGAN 278
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
45-236 2.72e-19

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 90.67  E-value: 2.72e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213   45 TGLEYAAKFIKKRQSRASRRgvsREEIEREVSILRQVLHHNVITLHDVYENRTDVVL-ILELVSGGELFDFLAQKESLSE 123
Cdd:TIGR03903    2 TGHEVAIKLLRTDAPEEEHQ---RARFRRETALCARLYHPNIVALLDSGEAPPGLLFaVFEYVPGRTLREVLAADGALPA 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  124 EEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPiPHIKLIDFG---LAHEIEDGVEFK-----NIFGTPEFVA 195
Cdd:TIGR03903   79 GETGRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVR-PHAKVLDFGigtLLPGVRDADVATltrttEVLGTPTYCA 157
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2056392213  196 PEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETL 236
Cdd:TIGR03903  158 PEQLRGEPVTPNSDLYAWGLIFLECLTGQRVVQGASVAEIL 198
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
83-231 1.67e-13

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 72.14  E-value: 1.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  83 HHNVITLHDVYENRTDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNI 162
Cdd:NF033483   66 HPNIVSVYDVGEDGGIPYIVMEYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGR 145
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2056392213 163 piphIKLIDFGLAHEI-EDGVEFKN-IFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDT 231
Cdd:NF033483  146 ----VKVTDFGIARALsSTTMTQTNsVLGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPFDGDS 212
 
Name Accession Description Interval E-value
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
17-285 0e+00

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: 569.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  17 QKVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVSREEIEREVSILRQVLHHNVITLHDVYENR 96
Cdd:cd14196     1 QKVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVSREEIEREVSILRQVLHPNIITLHDVYENR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  97 TDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLAH 176
Cdd:cd14196    81 TDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLAH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 177 EIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSE 256
Cdd:cd14196   161 EIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSHTSE 240
                         250       260
                  ....*....|....*....|....*....
gi 2056392213 257 LAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14196   241 LAKDFIRKLLVKETRKRLTIQEALRHPWI 269
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
17-285 0e+00

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: 549.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  17 QKVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVSREEIEREVSILRQVLHHNVITLHDVYENR 96
Cdd:cd14105     1 ENVEDFYDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSKASRRGVSREDIEREVSILRQVLHPNIITLHDVFENK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  97 TDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLAH 176
Cdd:cd14105    81 TDVVLILELVAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNVPIPRIKLIDFGLAH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 177 EIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSE 256
Cdd:cd14105   161 KIEDGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVNYDFDDEYFSNTSE 240
                         250       260
                  ....*....|....*....|....*....
gi 2056392213 257 LAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14105   241 LAKDFIRQLLVKDPRKRMTIQESLRHPWI 269
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
17-285 0e+00

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: 514.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  17 QKVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVSREEIEREVSILRQVLHHNVITLHDVYENR 96
Cdd:cd14194     1 ENVDDYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSRRGVSREDIEREVSILKEIQHPNVITLHEVYENK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  97 TDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLAH 176
Cdd:cd14194    81 TDVILILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVPKPRIKIIDFGLAH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 177 EIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSE 256
Cdd:cd14194   161 KIDFGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDEYFSNTSA 240
                         250       260
                  ....*....|....*....|....*....
gi 2056392213 257 LAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14194   241 LAKDFIRRLLVKDPKKRMTIQDSLQHPWI 269
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
17-285 1.82e-171

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: 481.04  E-value: 1.82e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  17 QKVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVSREEIEREVSILRQVLHHNVITLHDVYENR 96
Cdd:cd14195     1 SMVEDHYEMGEELGSGQFAIVRKCREKGTGKEYAAKFIKKRRLSSSRRGVSREEIEREVNILREIQHPNIITLHDIFENK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  97 TDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLAH 176
Cdd:cd14195    81 TDVVLILELVSGGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNVPNPRIKLIDFGIAH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 177 EIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSE 256
Cdd:cd14195   161 KIEAGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDEEYFSNTSE 240
                         250       260
                  ....*....|....*....|....*....
gi 2056392213 257 LAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14195   241 LAKDFIRRLLVKDPKKRMTIAQSLEHSWI 269
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
29-284 4.43e-143

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: 408.19  E-value: 4.43e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRasrrgvsREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSG 108
Cdd:cd14006     1 LGRGRFGVVKRCIEKATGREFAAKFIPKRDKK-------KEAVLREISILNQLQHPRIIQLHEAYESPTELVLILELCSG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 109 GELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKniPIPHIKLIDFGLAHEIEDGVEFKNIF 188
Cdd:cd14006    74 GELLDRLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADR--PSPQIKIIDFGLARKLNPGEELKEIF 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 189 GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSELAKDFIRKLLVK 268
Cdd:cd14006   152 GTPEFVAPEIVNGEPVSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISACRVDFSEEYFSSVSQEAKDFIRKLLVK 231
                         250
                  ....*....|....*.
gi 2056392213 269 ETRKRLTIQEALRHPW 284
Cdd:cd14006   232 EPRKRPTAQEALQHPW 247
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
29-285 1.11e-121

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: 353.84  E-value: 1.11e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRasrrgvSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSG 108
Cdd:cd14103     1 LGRGKFGTVYRCVEKATGKELAAKFIKCRKAK------DREDVRNEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 109 GELFD-FLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPipHIKLIDFGLAHEIEDGVEFKNI 187
Cdd:cd14103    75 GELFErVVDDDFELTERDCILFMRQICEGVQYMHKQGILHLDLKPENILCVSRTGN--QIKIIDFGLARKYDPDKKLKVL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 188 FGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSELAKDFIRKLLV 267
Cdd:cd14103   153 FGTPEFVAPEVVNYEPISYATDMWSVGVICYVLLSGLSPFMGDNDAETLANVTRAKWDFDDEAFDDISDEAKDFISKLLV 232
                         250
                  ....*....|....*...
gi 2056392213 268 KETRKRLTIQEALRHPWI 285
Cdd:cd14103   233 KDPRKRMSAAQCLQHPWL 250
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
22-284 2.01e-118

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: 346.00  E-value: 2.01e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  22 FYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRgvsrEEIEREVSILRQVLHHNVITLHDVYENRTDVVL 101
Cdd:cd05117     1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSEDE----EMLRREIEILKRLDHPNIVKLYEVFEDDKNLYL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 102 ILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNiPIPHIKLIDFGLAHEIEDG 181
Cdd:cd05117    77 VMELCTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKD-PDSPIKIIDFGLAKIFEEG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 182 VEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSELAKDF 261
Cdd:cd05117   156 EKLKTVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFDSPEWKNVSEEAKDL 235
                         250       260
                  ....*....|....*....|...
gi 2056392213 262 IRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd05117   236 IKRLLVVDPKKRLTAAEALNHPW 258
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
19-285 3.02e-116

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: 340.87  E-value: 3.02e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  19 VEDFYDI-GEELGSGQFAIVKKCREKSTGLEYAAKFIKKRqsrasRRGVS-REEIEREVSILRQVLHHN-VITLHDVYEN 95
Cdd:cd14106     5 INEVYTVeSTPLGRGKFAVVRKCIHKETGKEYAAKFLRKR-----RRGQDcRNEILHEIAVLELCKDCPrVVNLHEVYET 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  96 RTDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNIPIPHIKLIDFGLA 175
Cdd:cd14106    80 RSELILILELAAGGELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNI-LLTSEFPLGDIKLCDFGIS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 176 HEIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTS 255
Cdd:cd14106   159 RVIGEGEEIREILGTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNISQCNLDFPEELFKDVS 238
                         250       260       270
                  ....*....|....*....|....*....|
gi 2056392213 256 ELAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14106   239 PLAIDFIKRLLVKDPEKRLTAKECLEHPWL 268
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
23-285 6.65e-101

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 300.99  E-value: 6.65e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213   23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRasrrgVSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIK-----KDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  103 LELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAHEIEDGV 182
Cdd:smart00220  76 MEYCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENI-LLDED---GHVKLADFGLARQLDPGE 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  183 EFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSELAKDFI 262
Cdd:smart00220 152 KLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDLI 231
                          250       260
                   ....*....|....*....|...
gi 2056392213  263 RKLLVKETRKRLTIQEALRHPWI 285
Cdd:smart00220 232 RKLLVKDPEKRLTAEEALQHPFF 254
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
11-285 3.38e-99

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: 297.22  E-value: 3.38e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  11 MEPFkqqkvEDFYDIG-EELGSGQFAIVKKCREKSTGLEYAAKFIKKRqsrasRRGVS-REEIEREVSILRQVLHH-NVI 87
Cdd:cd14198     2 MDNF-----NNFYILTsKELGRGKFAVVRQCISKSTGQEYAAKFLKKR-----RRGQDcRAEILHEIAVLELAKSNpRVV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  88 TLHDVYENRTDVVLILELVSGGELFDFLAQKES--LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNiPIP 165
Cdd:cd14198    72 NLHEVYETTSEIILILEYAAGGEIFNLCVPDLAemVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIY-PLG 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 166 HIKLIDFGLAHEIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYD 245
Cdd:cd14198   151 DIKIVDFGMSRKIGHACELREIMGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFVGEDNQETFLNISQVNVD 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2056392213 246 FDEEFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14198   231 YSEETFSSVSQLATDFIQKLLVKNPEKRPTAEICLSHSWL 270
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
20-285 6.77e-95

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: 286.13  E-value: 6.77e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  20 EDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRasrrgvSREEIEREVSILRQVLHHNVITLHDVYENRTDV 99
Cdd:cd14191     1 SDFYDIEERLGSGKFGQVFRLVEKKTKKVWAGKFFKAYSAK------EKENIRQEISIMNCLHHPKLVQCVDAFEEKANI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 100 VLILELVSGGELFDFLAQKE-SLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPipHIKLIDFGLAHEI 178
Cdd:cd14191    75 VMVLEMVSGGELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGT--KIKLIDFGLARRL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 179 EDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSELA 258
Cdd:cd14191   153 ENAGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDA 232
                         250       260
                  ....*....|....*....|....*..
gi 2056392213 259 KDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14191   233 KDFISNLLKKDMKARLTCTQCLQHPWL 259
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
21-285 1.20e-91

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: 277.54  E-value: 1.20e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  21 DFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSrasrrgVSREEIEREVSILRQVLHHNVITLHDVYENRTDVV 100
Cdd:cd14114     2 DHYDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPHE------SDKETVRKEIQIMNQLHHPKLINLHDAFEDDNEMV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 101 LILELVSGGELFDFLAQKE-SLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPipHIKLIDFGLAHEIE 179
Cdd:cd14114    76 LILEFLSGGELFERIAAEHyKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTKRSN--EVKLIDFGLATHLD 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 180 DGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSELAK 259
Cdd:cd14114   154 PKESVKVTTGTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVKSCDWNFDDSAFSGISEEAK 233
                         250       260
                  ....*....|....*....|....*.
gi 2056392213 260 DFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14114   234 DFIRKLLLADPNKRMTIHQALEHPWL 259
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
21-285 2.47e-90

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: 274.48  E-value: 2.47e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  21 DFYDIGEE--LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRasrrgvSREEIEREVSILRQVLHHNVITLHDVYENRTD 98
Cdd:cd14193     2 SYYNVNKEeiLGGGRFGQVHKCEEKSSGLKLAAKIIKARSQK------EKEEVKNEIEVMNQLNHANLIQLYDAFESRND 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  99 VVLILELVSGGELFD-FLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPipHIKLIDFGLAHE 177
Cdd:cd14193    76 IVLVMEYVDGGELFDrIIDENYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCVSREAN--QVKIIDFGLARR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 178 IEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSEL 257
Cdd:cd14193   154 YKPREKLRVNFGTPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILACQWDFEDEEFADISEE 233
                         250       260
                  ....*....|....*....|....*...
gi 2056392213 258 AKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14193   234 AKDFISKLLIKEKSWRMSASEALKHPWL 261
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
23-284 4.20e-89

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: 270.93  E-value: 4.20e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASrrgvSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd14003     2 YELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEE----IEEKIKREIEIMKLLNHPNIIKLYEVIETENKIYLV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAHEIEDGV 182
Cdd:cd14003    78 MEYASGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENI-LLDKN---GNLKIIDFGLSNEFRGGS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 183 EFKNIFGTPEFVAPEIVNYEP-LGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYdfdeEFFSQTSELAKDF 261
Cdd:cd14003   154 LLKTFCGTPAYAAPEVLLGRKyDGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKY----PIPSHLSPDARDL 229
                         250       260
                  ....*....|....*....|...
gi 2056392213 262 IRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd14003   230 IRRMLVVDPSKRITIEEILNHPW 252
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
12-285 7.41e-89

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: 271.04  E-value: 7.41e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  12 EPFKQQkvedfYDI--GEELGSGQFAIVKKCREKSTGLEYAAKFIKKRqsrasRRGVS-REEIEREVSILrQVLHHN--V 86
Cdd:cd14197     3 EPFQER-----YSLspGRELGRGKFAVVRKCVEKDSGKEFAAKFMRKR-----RKGQDcRMEIIHEIAVL-ELAQANpwV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  87 ITLHDVYENRTDVVLILELVSGGELFD--FLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNiPI 164
Cdd:cd14197    72 INLHEVYETASEMILVLEYAAGGEIFNqcVADREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSES-PL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 165 PHIKLIDFGLAHEIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSY 244
Cdd:cd14197   151 GDIKIVDFGLSRILKNSEELREIMGTPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQMNV 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2056392213 245 DFDEEFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14197   231 SYSEEEFEHLSESAIDFIKTLLIKKPENRATAEDCLKHPWL 271
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
27-285 2.05e-87

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: 266.83  E-value: 2.05e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRasrrgvSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELV 106
Cdd:cd14192    10 EVLGGGRFGQVHKCTELSTGLTLAAKIIKVKGAK------EREEVKNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 107 SGGELFDFLA-QKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLdkNIPIPHIKLIDFGLAHEIEDGVEFK 185
Cdd:cd14192    84 DGGELFDRITdESYQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILCV--NSTGNQIKIIDFGLARRYKPREKLK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 186 NIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSELAKDFIRKL 265
Cdd:cd14192   162 VNFGTPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNNIVNCKWDFDAEAFENLSEEAKDFISRL 241
                         250       260
                  ....*....|....*....|
gi 2056392213 266 LVKETRKRLTIQEALRHPWI 285
Cdd:cd14192   242 LVKEKSCRMSATQCLKHEWL 261
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
19-284 2.89e-83

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: 256.14  E-value: 2.89e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  19 VEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRAsrrgvsREE-IEREVSILRQVLHHNVITLHDVYENRT 97
Cdd:cd14083     1 IRDKYEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKALKG------KEDsLENEIAVLRKIKHPNIVQLLDIYESKS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  98 DVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLL----DKNIPIPhikliDFG 173
Cdd:cd14083    75 HLYLVMELVTGGELFDRIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYYspdeDSKIMIS-----DFG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 174 LAHeIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQ 253
Cdd:cd14083   150 LSK-MEDSGVMSTACGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILKAEYEFDSPYWDD 228
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2056392213 254 TSELAKDFIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd14083   229 ISDSAKDFIRHLMEKDPNKRYTCEQALEHPW 259
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
27-285 3.53e-81

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: 250.99  E-value: 3.53e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRasrrgvSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELV 106
Cdd:cd14190    10 EVLGGGKFGKVHTCTEKRTGLKLAAKVINKQNSK------DKEMVLLEIQVMNQLNHRNLIQLYEAIETPNEIVLFMEYV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 107 SGGELFDFLAQKES-LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLdkNIPIPHIKLIDFGLAHEIEDGVEFK 185
Cdd:cd14190    84 EGGELFERIVDEDYhLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCV--NRTGHQVKIIDFGLARRYNPREKLK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 186 NIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSELAKDFIRKL 265
Cdd:cd14190   162 VNFGTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETLNNVLMGNWYFDEETFEHVSDEAKDFVSNL 241
                         250       260
                  ....*....|....*....|
gi 2056392213 266 LVKETRKRLTIQEALRHPWI 285
Cdd:cd14190   242 IIKERSARMSATQCLKHPWL 261
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
29-284 3.84e-79

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: 245.26  E-value: 3.84e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRasrrgvsREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSG 108
Cdd:cd14115     1 IGRGRFSIVKKCLHKATRKDVAVKFVSKKMKK-------KEQAAHEAALLQHLQHPQYITLHDTYESPTSYILVLELMDD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 109 GELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENiMLLDKNIPIPHIKLIDFGLAHEIEDGVEFKNIF 188
Cdd:cd14115    74 GRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPEN-LLIDLRIPVPRVKLIDLEDAVQISGHRHVHHLL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 189 GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSELAKDFIRKLLVK 268
Cdd:cd14115   153 GNPEFAAPEVIQGTPVSLATDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPDEYFGDVSQAARDFINVILQE 232
                         250
                  ....*....|....*.
gi 2056392213 269 ETRKRLTIQEALRHPW 284
Cdd:cd14115   233 DPRRRPTAATCLQHPW 248
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
23-284 1.02e-77

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: 241.85  E-value: 1.02e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRAsrrgvsREE-IEREVSILRQVLHHNVITLHDVYENRTDVVL 101
Cdd:cd14095     2 YDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKCKG------KEHmIENEVAILRRVKHPNIVQLIEEYDTDTELYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 102 ILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLAHEIEDG 181
Cdd:cd14095    76 VMELVKGGDLFDAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHEDGSKSLKLADFGLATEVKEP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 182 VefKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLG-DTKQETLAN-ITAVSYDFDEEFFSQTSELAK 259
Cdd:cd14095   156 L--FTVCGTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFRSpDRDQEELFDlILAGEFEFLSPYWDNISDSAK 233
                         250       260
                  ....*....|....*....|....*
gi 2056392213 260 DFIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd14095   234 DLISRMLVVDPEKRYSAGQVLDHPW 258
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
23-284 1.19e-77

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: 242.26  E-value: 1.19e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVS--REEIEREVSILRQVLHH-NVITLHDVYENRTDV 99
Cdd:cd14093     5 YEPKEILGRGVSSTVRRCIEKETGQEFAVKIIDITGEKSSENEAEelREATRREIEILRQVSGHpNIIELHDVFESPTFI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 100 VLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNIpipHIKLIDFGLAHEIE 179
Cdd:cd14093    85 FLVFELCRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENI-LLDDNL---NVKISDFGFATRLD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 180 DGVEFKNIFGTPEFVAPEIV------NYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQ 253
Cdd:cd14093   161 EGEKLRELCGTPGYLAPEVLkcsmydNAPGYGKEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNIMEGKYEFGSPEWDD 240
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2056392213 254 TSELAKDFIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd14093   241 ISDTAKDLISKLLVVDPKKRLTAEEALEHPF 271
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
21-286 1.56e-77

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: 241.22  E-value: 1.56e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  21 DFyDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRasRRGVSrEEIEREVSILRQVLHHNVITLHDVYENRTDVV 100
Cdd:cd14007     1 DF-EIGKPLGKGKFGNVYLAREKKSGFIVALKVISKSQLQ--KSGLE-HQLRREIEIQSHLRHPNILRLYGYFEDKKRIY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 101 LILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIED 180
Cdd:cd14007    77 LILEYAPNGELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNG----ELKLADFGWSVHAPS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 181 GVEfKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDeeffSQTSELAKD 260
Cdd:cd14007   153 NRR-KTFCGTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNVDIKFP----SSVSPEAKD 227
                         250       260
                  ....*....|....*....|....*.
gi 2056392213 261 FIRKLLVKETRKRLTIQEALRHPWIT 286
Cdd:cd14007   228 LISKLLQKDPSKRLSLEQVLNHPWIK 253
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
21-316 6.26e-77

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: 241.17  E-value: 6.26e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  21 DFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASrrgvSREEIEREVSILRQVLHHNVITLHDVYENRTDVV 100
Cdd:cd14086     1 DEYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSAR----DHQKLEREARICRLLKHPNIVRLHDSISEEGFHY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 101 LILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPhIKLIDFGLAHEIED 180
Cdd:cd14086    77 LVFDLVTGGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSKGAA-VKLADFGLAIEVQG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 181 GVEFKNIF-GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDF-DEEFFSQTSElA 258
Cdd:cd14086   156 DQQAWFGFaGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYpSPEWDTVTPE-A 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2056392213 259 KDFIRKLLVKETRKRLTIQEALRHPWITPVDNQQAMV-RRESVVNLENFRkqyVRRRWK 316
Cdd:cd14086   235 KDLINQMLTVNPAKRITAAEALKHPWICQRDRVASMVhRQETVDCLKKFN---ARRKLK 290
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
19-286 3.81e-76

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: 239.34  E-value: 3.81e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  19 VEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRqsrasrrgVSREEIEREVSILRQVLHHNVITLHDVYENRTD 98
Cdd:cd14085     1 LEDFFEIESELGRGATSVVYRCRQKGTQKPYAVKKLKKT--------VDKKIVRTEIGVLLRLSHPNIIKLKEIFETPTE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  99 VVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPhIKLIDFGLAHEI 178
Cdd:cd14085    73 ISLVLELVTGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPDAP-LKIADFGLSKIV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 179 EDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGD-TKQETLANITAVSYDFDEEFFSQTSEL 257
Cdd:cd14085   152 DQQVTMKTVCGTPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEPFYDErGDQYMFKRILNCDYDFVSPWWDDVSLN 231
                         250       260
                  ....*....|....*....|....*....
gi 2056392213 258 AKDFIRKLLVKETRKRLTIQEALRHPWIT 286
Cdd:cd14085   232 AKDLVKKLIVLDPKKRLTTQQALQHPWVT 260
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
19-285 4.12e-75

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: 236.43  E-value: 4.12e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  19 VEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSrasrrgVSREEIEREVSILRQVLHHNVITLHDVYENRTD 98
Cdd:cd14166     1 IRETFIFMEVLGSGAFSEVYLVKQRSTGKLYALKCIKKSPL------SRDSSLENEIAVLKRIKHENIVTLEDIYESTTH 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  99 VVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLL--DKNipiPHIKLIDFGLAH 176
Cdd:cd14166    75 YYLVMQLVSGGELFDRILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYLtpDEN---SKIMITDFGLSK 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 177 EIEDGVeFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSE 256
Cdd:cd14166   152 MEQNGI-MSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEETESRLFEKIKEGYYEFESPFWDDISE 230
                         250       260
                  ....*....|....*....|....*....
gi 2056392213 257 LAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14166   231 SAKDFIRHLLEKNPSKRYTCEKALSHPWI 259
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
23-286 3.83e-74

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: 233.60  E-value: 3.83e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRasrrgvsREEIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd14104     2 YMIAEELGRGQFGIVHRCVETSSKKTYMAKFVKVKGAD-------QVLVKKEISILNIARHRNILRLHESFESHEELVMI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQKE-SLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPipHIKLIDFGLAHEIEDG 181
Cdd:cd14104    75 FEFISGVDIFERITTARfELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTRRGS--YIKIIEFGQSRQLKPG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 182 VEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSELAKDF 261
Cdd:cd14104   153 DKFRLQYTSAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNAEYAFDDEAFKNISIEALDF 232
                         250       260
                  ....*....|....*....|....*
gi 2056392213 262 IRKLLVKETRKRLTIQEALRHPWIT 286
Cdd:cd14104   233 VDRLLVKERKSRMTAQEALNHPWLK 257
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
19-285 1.27e-73

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: 231.25  E-value: 1.27e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  19 VEDFYDIGEE-LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRAsrrgvsreeieREVSILRQVLHHNVITLHDVYE-NR 96
Cdd:cd14109     1 VRELYEIGEEdEKRAAQGAPFHVTERSTGRNFLAQLRYGDPFLM-----------REVDIHNSLDHPNIVQMHDAYDdEK 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  97 TDVVLILELVSGGELF--DFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKnipipHIKLIDFGL 174
Cdd:cd14109    70 LAVTVIDNLASTIELVrdNLLPGKDYYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQDD-----KLKLADFGQ 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 175 AHEIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQT 254
Cdd:cd14109   145 SRRLLRGKLTTLIYGSPEFVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISPFLGDNDRETLTNVRSGKWSFDSSPLGNI 224
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2056392213 255 SELAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14109   225 SDDARDFIKKLLVYIPESRLTVDEALNHPWF 255
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
20-285 2.03e-71

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: 226.01  E-value: 2.03e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  20 EDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRasrrgvsREEIEREVSILRQVLHHNVITLHDVYENRTDV 99
Cdd:cd14113     6 DSFYSEVAELGRGRFSVVKKCDQRGTKRAVATKFVNKKLMK-------RDQVTHELGVLQSLQHPQLVGLLDTFETPTSY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 100 VLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNIPIPHIKLIDFGLAHEIE 179
Cdd:cd14113    79 ILVLEMADQGRLLDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENI-LVDQSLSKPTIKLADFGDAVQLN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 180 DGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSELAK 259
Cdd:cd14113   158 TTYYIHQLLGSPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFLDESVEETCLNICRLDFSFPDDYFKGVSQKAK 237
                         250       260
                  ....*....|....*....|....*.
gi 2056392213 260 DFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14113   238 DFVCFLLQMDPAKRPSAALCLQEQWL 263
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
23-286 2.78e-69

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: 220.92  E-value: 2.78e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVsreeiEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd14169     5 YELKEKLGEGAFSEVVLAQERGSQRLVALKCIPKKALRGKEAMV-----ENEIAVLRRINHENIVSLEDIYESPTHLYLA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENiMLLDKNIPIPHIKLIDFGLAhEIEDGV 182
Cdd:cd14169    80 MELVTGGELFDRIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPEN-LLYATPFEDSKIMISDFGLS-KIEAQG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 183 EFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSELAKDFI 262
Cdd:cd14169   158 MLSTACGTPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDENDSELFNQILKAEYEFDSPYWDDISESAKDFI 237
                         250       260
                  ....*....|....*....|....
gi 2056392213 263 RKLLVKETRKRLTIQEALRHPWIT 286
Cdd:cd14169   238 RHLLERDPEKRFTCEQALQHPWIS 261
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
23-285 4.24e-69

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: 219.71  E-value: 4.24e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSrasrrgvSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd14087     3 YDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIETKCR-------GREVCESELNVLRRVRHTNIIQLIEVFETKERVYMV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDkniPIPHIKLI--DFGLAHEIED 180
Cdd:cd14087    76 MELATGGELFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYH---PGPDSKIMitDFGLASTRKK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 181 GVE--FKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSELA 258
Cdd:cd14087   153 GPNclMKTTCGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRAKYSYSGEPWPSVSNLA 232
                         250       260
                  ....*....|....*....|....*..
gi 2056392213 259 KDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14087   233 KDFIDRLLTVNPGERLSATQALKHPWI 259
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
19-285 4.36e-69

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: 219.90  E-value: 4.36e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  19 VEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRrgvsrEEIEREVSILRQVLHHNVITLHDVYENRTD 98
Cdd:cd14167     1 IRDIYDFREVLGTGAFSEVVLAEEKRTQKLVAIKCIAKKALEGKE-----TSIENEIAVLHKIKHPNIVALDDIYESGGH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  99 VVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIML--LDKNipiPHIKLIDFGLAH 176
Cdd:cd14167    76 LYLIMQLVSGGELFDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLYysLDED---SKIMISDFGLSK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 177 EIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSE 256
Cdd:cd14167   153 IEGSGSVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAEYEFDSPYWDDISD 232
                         250       260
                  ....*....|....*....|....*....
gi 2056392213 257 LAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14167   233 SAKDFIQHLMEKDPEKRFTCEQALQHPWI 261
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
23-285 1.27e-68

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: 218.28  E-value: 1.27e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQsrASRRGVSREeIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd14081     3 YRLGKTLGKGQTGLVKLAKHCVTGQKVAIKIVNKEK--LSKESVLMK-VEREIAIMKLIEHPNVLKLYDVYENKKYLYLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIEDGV 182
Cdd:cd14081    80 LEYVSGGELFDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKN----NIKIADFGMASLQPEGS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 183 EFKNIFGTPEFVAPEIVNYEPL-GLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFfsqtSELAKDF 261
Cdd:cd14081   156 LLETSCGSPHYACPEVIKGEKYdGRKADIWSCGVILYALLVGALPFDDDNLRQLLEKVKRGVFHIPHFI----SPDAQDL 231
                         250       260
                  ....*....|....*....|....
gi 2056392213 262 IRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14081   232 LRRMLEVNPEKRITIEEIKKHPWF 255
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
21-284 1.75e-67

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: 215.54  E-value: 1.75e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  21 DFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKkrqSRASRRGVSReeieREVSILRQVLHHNVITLHDVYENRTDVV 100
Cdd:cd14108     2 DYYDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIP---VRAKKKTSAR----RELALLAELDHKSIVRFHDAFEKRRVVI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 101 LILELVSGGELFDfLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPipHIKLIDFGLAHEIED 180
Cdd:cd14108    75 IVTELCHEELLER-ITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKTD--QVRICDFGNAQELTP 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 181 GVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSELAKD 260
Cdd:cd14108   152 NEPQYCKYGTPEFVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPFVGENDRTTLMNIRNYNVAFEESMFKDLCREAKG 231
                         250       260
                  ....*....|....*....|....
gi 2056392213 261 FIRKLLVKEtRKRLTIQEALRHPW 284
Cdd:cd14108   232 FIIKVLVSD-RLRPDAEETLEHPW 254
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
23-285 3.66e-66

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: 212.03  E-value: 3.66e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKrqSRASRRGvSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd14099     3 YRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVPK--SSLTKPK-QREKLKSEIKIHRSLKHPNIVKFHDCFEDEENVYIL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMlLDKNIpipHIKLIDFGLAHEIE-DG 181
Cdd:cd14099    80 LELCSNGSLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLF-LDENM---NVKIGDFGLAARLEyDG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 182 VEFKNIFGTPEFVAPEIVN-YEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEffSQTSELAKD 260
Cdd:cd14099   156 ERKKTLCGTPNYIAPEVLEkKKGHSFEVDIWSLGVILYTLLVGKPPFETSDVKETYKRIKKNEYSFPSH--LSISDEAKD 233
                         250       260
                  ....*....|....*....|....*
gi 2056392213 261 FIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14099   234 LIRSMLQPDPTKRPSLDEILSHPFF 258
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
17-320 3.98e-66

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: 213.76  E-value: 3.98e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  17 QKVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRrgvsrEEIEREVSILRQVLHHNVITLHDVYENR 96
Cdd:cd14168     6 EDIKKIFEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKALKGKE-----SSIENEIAVLRKIKHENIVALEDIYESP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  97 TDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPiPHIKLIDFGLAH 176
Cdd:cd14168    81 NHLYLVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYFSQDEE-SKIMISDFGLSK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 177 EIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSE 256
Cdd:cd14168   160 MEGKGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKADYEFDSPYWDDISD 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2056392213 257 LAKDFIRKLLVKETRKRLTIQEALRHPWITPvDNQQAMVRRESVVnlENFRKQYVRRRWKLSFS 320
Cdd:cd14168   240 SAKDFIRNLMEKDPNKRYTCEQALRHPWIAG-DTALCKNIHESVS--AQIRKNFAKSKWRQAFN 300
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
23-284 6.01e-66

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: 211.95  E-value: 6.01e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVsrEEIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd14098     2 YQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKRKVAGNDKNL--QLFQREINILKSLEHPGIVRLIDWYEDDQHIYLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNIPIpHIKLIDFGLAHEIEDGV 182
Cdd:cd14098    80 MEYVEGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENI-LITQDDPV-IVKISDFGLAKVIHTGT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 183 EFKNIFGTPEFVAPEIV----NYEPLGLE--ADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSE 256
Cdd:cd14098   158 FLVTFCGTMAYLAPEILmskeQNLQGGYSnlVDMWSVGCLVYVMLTGALPFDGSSQLPVEKRIRKGRYTQPPLVDFNISE 237
                         250       260
                  ....*....|....*....|....*...
gi 2056392213 257 LAKDFIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd14098   238 EAIDFILRLLDVDPEKRMTAAQALDHPW 265
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
23-284 8.25e-66

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: 210.97  E-value: 8.25e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRrgvSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd14079     4 YILGKTLGVGSFGKVKLAEHELTGHKVAVKILNRQKIKSLD---MEEKIRREIQILKLFRHPHIIRLYEVIETPTDIFMV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNIpipHIKLIDFGLAHEIEDGV 182
Cdd:cd14079    81 MEYVSGGELFDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENL-LLDSNM---NVKIADFGLSNIMRDGE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 183 EFKNIFGTPEFVAPEIVN---YepLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFfsqtSELAK 259
Cdd:cd14079   157 FLKTSCGSPNYAAPEVISgklY--AGPEVDVWSCGVILYALLCGSLPFDDEHIPNLFKKIKSGIYTIPSHL----SPGAR 230
                         250       260
                  ....*....|....*....|....*
gi 2056392213 260 DFIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd14079   231 DLIKRMLVVDPLKRITIPEIRQHPW 255
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
23-285 6.28e-65

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: 209.56  E-value: 6.28e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQ-SRASRRGVSR-EEIEREVSILRQVLHHNVITLHDVYENRTDVV 100
Cdd:cd14084     8 YIMSRTLGSGACGEVKLAYDKSTCKKVAIKIINKRKfTIGSRREINKpRNIETEIEILKKLSHPCIIKIEDFFDAEDDYY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 101 LILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNiPIPHIKLIDFGLAHEIED 180
Cdd:cd14084    88 IVLELMEGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQE-EECLIKITDFGLSKILGE 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 181 GVEFKNIFGTPEFVAPEIVNY---EPLGLEADMWSIGVITYILLSGASPFLGDTKQETLAN-ITAVSYDFDEEFFSQTSE 256
Cdd:cd14084   167 TSLMKTLCGTPTYLAPEVLRSfgtEGYTRAVDCWSLGVILFICLSGYPPFSEEYTQMSLKEqILSGKYTFIPKAWKNVSE 246
                         250       260
                  ....*....|....*....|....*....
gi 2056392213 257 LAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14084   247 EAKDLVKKMLVVDPSRRPSIEEALEHPWL 275
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
23-286 9.26e-65

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: 209.80  E-value: 9.26e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKrqsraSRRGVSrEEIErevsILRQVLHH-NVITLHDVYENRTDVVL 101
Cdd:cd14091     2 YEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIDK-----SKRDPS-EEIE----ILLRYGQHpNIITLRDVYDDGNSVYL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 102 ILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLAHEI--E 179
Cdd:cd14091    72 VTELLRGGELLDRILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGDPESLRICDFGFAKQLraE 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 180 DGvefknIFGTP----EFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFL---GDTKQETLANITAVSYDFDEEFFS 252
Cdd:cd14091   152 NG-----LLMTPcytaNFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPFAsgpNDTPEVILARIGSGKIDLSGGNWD 226
                         250       260       270
                  ....*....|....*....|....*....|....
gi 2056392213 253 QTSELAKDFIRKLLVKETRKRLTIQEALRHPWIT 286
Cdd:cd14091   227 HVSDSAKDLVRKMLHVDPSQRPTAAQVLQHPWIR 260
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
21-285 3.40e-64

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: 208.04  E-value: 3.40e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  21 DFYDI-GEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQsrasrrGVSREEIEREVSILRQVL-HHNVITLHDVYENRTD 98
Cdd:cd14090     1 DLYKLtGELLGEGAYASVQTCINLYTGKEYAVKIIEKHP------GHSRSRVFREVETLHQCQgHPNILQLIEYFEDDER 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  99 VVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNIPIPHIKLIDFGLAHEI 178
Cdd:cd14090    75 FYLVFEKMRGGPLLSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENI-LCESMDKVSPVKICDFDLGSGI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 179 EDGV---------EFKNIFGTPEFVAPEIVN---YEPLGLE--ADMWSIGVITYILLSGASPFLGD-------------- 230
Cdd:cd14090   154 KLSStsmtpvttpELLTPVGSAEYMAPEVVDafvGEALSYDkrCDLWSLGVILYIMLCGYPPFYGRcgedcgwdrgeacq 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2056392213 231 TKQETL-ANITAVSYDFDEEFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14090   234 DCQELLfHSIQEGEYEFPEKEWSHISAEAKDLISHLLVRDASQRYTAEQVLQHPWV 289
Pkinase pfam00069
Protein kinase domain;
23-285 1.11e-63

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 204.40  E-value: 1.11e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRqsraSRRGVSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKE----KIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQKESLSEEEATSFIKQILDGVnylhtkkiahfdlkpenimlldknipiphiklidfglaheiEDGV 182
Cdd:pfam00069  77 LEYVEGGSLFDLLSEKGAFSEREAKFIMKQILEGL-----------------------------------------ESGS 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 183 EFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSElAKDFI 262
Cdd:pfam00069 116 SLTTFVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELPSNLSEE-AKDLL 194
                         250       260
                  ....*....|....*....|...
gi 2056392213 263 RKLLVKETRKRLTIQEALRHPWI 285
Cdd:pfam00069 195 KKLLKKDPSKRLTATQALQHPWF 217
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
22-284 1.11e-63

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: 205.95  E-value: 1.11e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  22 FYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRrgvsrEEIEREVSILRQVLHHNVITLHDVYENRTDVVL 101
Cdd:cd14185     1 HYEIGRTIGDGNFAVVKECRHWNENQEYAMKIIDKSKLKGKE-----DMIESEILIIKSLSHPNIVKLFEVYETEKEIYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 102 ILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLAHEIEdg 181
Cdd:cd14185    76 ILEYVRGGDLFDAIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQHNPDKSTTLKLADFGLAKYVT-- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 182 vefKNIF---GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLG-DTKQETLANITAVS-YDFDEEFFSQTSE 256
Cdd:cd14185   154 ---GPIFtvcGTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFRSpERDQEELFQIIQLGhYEFLPPYWDNISE 230
                         250       260
                  ....*....|....*....|....*...
gi 2056392213 257 LAKDFIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd14185   231 AAKDLISRLLVVDPEKRYTAKQVLQHPW 258
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
23-287 1.84e-63

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: 206.77  E-value: 1.84e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIG---EELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRAsrrgvsreeieREVSILRQVLHH-NVITLHDVYENRTD 98
Cdd:cd14092     5 YELDlreEALGDGSFSVCRKCVHKKTGQEFAVKIVSRRLDTS-----------REVQLLRLCQGHpNIVKLHEVFQDELH 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  99 VVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPhIKLIDFGLAhEI 178
Cdd:cd14092    74 TYLVMELLRGGELLERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDEDDDAE-IKIVDFGFA-RL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 179 EDGVEFKNifgTPEFV----APEIVN---YEPLGLEA-DMWSIGVITYILLSGASPFLGDTKQETLAN----ITAVSYDF 246
Cdd:cd14092   152 KPENQPLK---TPCFTlpyaAPEVLKqalSTQGYDEScDLWSLGVILYTMLSGQVPFQSPSRNESAAEimkrIKSGDFSF 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2056392213 247 DEEFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWITP 287
Cdd:cd14092   229 DGEEWKNVSSEAKSLIQGLLTVDPSKRLTMSELRNHPWLQG 269
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
23-284 2.72e-63

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: 205.53  E-value: 2.72e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQsrasrrgVSREE------IEREVsiLRQVLHHNVITLHDVYENR 96
Cdd:cd05581     3 FKFGKPLGEGSYSTVVLAKEKETGKEYAIKVLDKRH-------IIKEKkvkyvtIEKEV--LSRLAHPGIVKLYYTFQDE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  97 TDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNIpipHIKLIDFGLA- 175
Cdd:cd05581    74 SKLYFVLEYAPNGDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENI-LLDEDM---HIKITDFGTAk 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 176 -------HEIEDGVEFKNIF----------GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLAN 238
Cdd:cd05581   150 vlgpdssPESTKGDADSQIAynqaraasfvGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQK 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2056392213 239 ITAVSYDFDEEFFsqtsELAKDFIRKLLVKETRKRLTIQEA------LRHPW 284
Cdd:cd05581   230 IVKLEYEFPENFP----PDAKDLIQKLLVLDPSKRLGVNENggydelKAHPF 277
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
29-285 2.75e-63

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: 205.09  E-value: 2.75e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVSR--------EEIEREVSILRQVLHHNVITLHDV--YENRTD 98
Cdd:cd14008     1 LGRGSFGKVKLALDTETGQLYAIKIFNKSRLRKRREGKNDrgkiknalDDVRREIAIMKKLDHPNIVRLYEVidDPESDK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  99 VVLILELVSGGELFDFLAQKES--LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAH 176
Cdd:cd14008    81 LYLVLEYCEGGPVMELDSGDRVppLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADG----TVKISDFGVSE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 177 EIEDG-VEFKNIFGTPEFVAPEI--VNYEPL-GLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDeeFFS 252
Cdd:cd14008   157 MFEDGnDTLQKTAGTPAFLAPELcdGDSKTYsGKAADIWALGVTLYCLVFGRLPFNGDNILELYEAIQNQNDEFP--IPP 234
                         250       260       270
                  ....*....|....*....|....*....|...
gi 2056392213 253 QTSELAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14008   235 ELSPELKDLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
29-284 2.62e-62

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: 201.98  E-value: 2.62e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRAsRRGVSREEIERevSILRQVLHHNVITLHDVYENRTDVVLILELVSG 108
Cdd:cd05123     1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIIK-RKEVEHTLNER--NILERVNHPFIVKLHYAFQTEEKLYLVLDYVPG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 109 GELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAHEIEDGVEFKNIF 188
Cdd:cd05123    78 GELFSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENI-LLDSD---GHIKLTDFGLAKELSSDGDRTYTF 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 189 -GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFfsqtSELAKDFIRKLLV 267
Cdd:cd05123   154 cGTPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKSPLKFPEYV----SPEAKSLISGLLQ 229
                         250       260
                  ....*....|....*....|
gi 2056392213 268 KETRKRLT---IQEALRHPW 284
Cdd:cd05123   230 KDPTKRLGsggAEEIKAHPF 249
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
22-284 3.24e-62

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: 202.04  E-value: 3.24e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  22 FYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSrasrrgvSREEIEREVSILRQVLHHNVITLHDVYENRTDVVL 101
Cdd:cd14107     3 VYEVKEEIGRGTFGFVKRVTHKGNGECCAAKFIPLRSS-------TRARAFQERDILARLSHRRLTCLLDQFETRKTLIL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 102 ILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPipHIKLIDFGLAHEIEDG 181
Cdd:cd14107    76 ILELCSSEELLDRLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVSPTRE--DIKICDFGFAQEITPS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 182 VEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSELAKDF 261
Cdd:cd14107   154 EHQFSKYGSPEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEGVVSWDTPEITHLSEDAKDF 233
                         250       260
                  ....*....|....*....|...
gi 2056392213 262 IRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd14107   234 IKRVLQPDPEKRPSASECLSHEW 256
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
19-285 7.31e-62

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: 201.07  E-value: 7.31e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  19 VEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQsrasrRGVSREEIEREVSILRQVLHHNVITLHDVYENRTD 98
Cdd:cd14078     1 LLKYYELHETIGSGGFAKVKLATHILTGEKVAIKIMDKKA-----LGDDLPRVKTEIEALKNLSHQHICRLYHVIETDNK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  99 VVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAHEI 178
Cdd:cd14078    76 IFMVLEYCPGGELFDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENL-LLDED---QNLKLIDFGLCAKP 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 179 EDGVEF--KNIFGTPEFVAPEIVNYEP-LGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDfDEEFFSQTS 255
Cdd:cd14078   152 KGGMDHhlETCCGSPAYAAPELIQGKPyIGSEADVWSMGVLLYALLCGFLPFDDDNVMALYRKIQSGKYE-EPEWLSPSS 230
                         250       260       270
                  ....*....|....*....|....*....|
gi 2056392213 256 elaKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14078   231 ---KLLLDQMLQVDPKKRITVKELLNHPWV 257
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
23-285 6.77e-61

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: 198.38  E-value: 6.77e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRrgvSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd14073     3 YELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKIEDEQ---DMVRIRREIEIMSSLNHPHIIRIYEVFENKDKIVIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNIpipHIKLIDFGLAHEIEDGV 182
Cdd:cd14073    80 MEYASGGELYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENI-LLDQNG---NAKIADFGLSNLYSKDK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 183 EFKNIFGTPEFVAPEIVNYEPL-GLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYdFDEEFFSQTSELakdf 261
Cdd:cd14073   156 LLQTFCGSPLYASPEIVNGTPYqGPEVDCWSLGVLLYTLVYGTMPFDGSDFKRLVKQISSGDY-REPTQPSDASGL---- 230
                         250       260
                  ....*....|....*....|....
gi 2056392213 262 IRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14073   231 IRWMLTVNPKRRATIEDIANHWWV 254
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
23-284 3.16e-60

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: 197.50  E-value: 3.16e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVS--REEIEREVSILRQVLHH-NVITLHDVYENRTDV 99
Cdd:cd14181    12 YDPKEVIGRGVSSVVRRCVHRHTGQEFAVKIIEVTAERLSPEQLEevRSSTLKEIHILRQVSGHpSIITLIDSYESSTFI 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 100 VLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNIpipHIKLIDFGLAHEIE 179
Cdd:cd14181    92 FLVFDLMRRGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENI-LLDDQL---HIKLSDFGFSCHLE 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 180 DGVEFKNIFGTPEFVAPEIV------NYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQ 253
Cdd:cd14181   168 PGEKLRELCGTPGYLAPEILkcsmdeTHPGYGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMIMEGRYQFSSPEWDD 247
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2056392213 254 TSELAKDFIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd14181   248 RSSTVKDLISRLLVVDPEIRLTAEQALQHPF 278
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
29-283 4.08e-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: 194.80  E-value: 4.08e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRrgvsrEEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSG 108
Cdd:cd00180     1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKKLL-----EELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 109 GELFDFLAQKE-SLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIEDGVEFKNI 187
Cdd:cd00180    76 GSLKDLLKENKgPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDG----TVKLADFGLAKDLDSDDSLLKT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 188 FGTPEFV---APEIVNYEPLGLEADMWSIGVITYILlsgaspflgdtkqetlanitavsydfdeeffsqtsELAKDFIRK 264
Cdd:cd00180   152 TGGTTPPyyaPPELLGGRYYGPKVDIWSLGVILYEL-----------------------------------EELKDLIRR 196
                         250
                  ....*....|....*....
gi 2056392213 265 LLVKETRKRLTIQEALRHP 283
Cdd:cd00180   197 MLQYDPKKRPSAKELLEHL 215
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
21-285 5.60e-60

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: 196.40  E-value: 5.60e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  21 DFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVsreeiEREVSILRQVLHHNVITLHDVYENRTDVV 100
Cdd:cd14088     1 DRYDLGQVIKTEEFCEIFRAKDKTTGKLYTCKKFLKRDGRKVRKAA-----KNEINILKMVKHPNILQLVDVFETRKEYF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 101 LILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKnipIPHIKLI--DFGLAhEI 178
Cdd:cd14088    76 IFLELATGREVFDWILDQGYYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYYNR---LKNSKIVisDFHLA-KL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 179 EDGVeFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLAN--------ITAVSYDFDEEF 250
Cdd:cd14088   152 ENGL-IKEPCGTPEYLAPEVVGRQRYGRPVDCWAIGVIMYILLSGNPPFYDEAEEDDYENhdknlfrkILAGDYEFDSPY 230
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2056392213 251 FSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14088   231 WDDISQAAKDLVTRLMEVEQDQRITAEEAISHEWI 265
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
23-284 1.07e-59

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: 195.32  E-value: 1.07e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKrqSRASRRGVSrEEIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd14663     2 YELGRTLGEGTFAKVKFARNTKTGESVAIKIIDK--EQVAREGMV-EQIKREIAIMKLLRHPNIVELHEVMATKTKIFFV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAH---EIE 179
Cdd:cd14663    79 MELVTGGELFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENL-LLDED---GNLKISDFGLSAlseQFR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 180 DGVEFKNIFGTPEFVAPEIV---NYEplGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFfsqtSE 256
Cdd:cd14663   155 QDGLLHTTCGTPNYVAPEVLarrGYD--GAKADIWSCGVILFVLLAGYLPFDDENLMALYRKIMKGEFEYPRWF----SP 228
                         250       260
                  ....*....|....*....|....*...
gi 2056392213 257 LAKDFIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd14663   229 GAKSLIKRILDPNPSTRITVEQIMASPW 256
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
21-284 1.33e-59

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: 195.25  E-value: 1.33e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  21 DFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRrgvsrEEIEREVSILRQVLHHNVITLHDVYENRTDVV 100
Cdd:cd14184     1 EKYKIGKVIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGKE-----HLIENEVSILRRVKHPNIIMLIEEMDTPAELY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 101 LILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLAHEIED 180
Cdd:cd14184    76 LVMELVKGGDLFDAITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVCEYPDGTKSLKLGDFGLATVVEG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 181 gvEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTK-QETLAN-ITAVSYDFDEEFFSQTSELA 258
Cdd:cd14184   156 --PLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSENNlQEDLFDqILLGKLEFPSPYWDNITDSA 233
                         250       260
                  ....*....|....*....|....*.
gi 2056392213 259 KDFIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd14184   234 KELISHMLQVNVEARYTAEQILSHPW 259
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
23-284 3.94e-59

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: 194.75  E-value: 3.94e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRAsrrgVSREEIE-------REVSILRQVL-HHNVITLHDVYE 94
Cdd:cd14182     5 YEPKEILGRGVSSVVRRCIHKPTRQEYAVKIIDITGGGS----FSPEEVQelreatlKEIDILRKVSgHPNIIQLKDTYE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  95 NRTDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNIpipHIKLIDFGL 174
Cdd:cd14182    81 TNTFFFLVFDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENI-LLDDDM---NIKLTDFGF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 175 AHEIEDGVEFKNIFGTPEFVAPEIV------NYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDE 248
Cdd:cd14182   157 SCQLDPGEKLREVCGTPGYLAPEIIecsmddNHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMSGNYQFGS 236
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2056392213 249 EFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd14182   237 PEWDDRSDTVKDLISRFLVVQPQKRYTAEEALAHPF 272
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
21-289 5.26e-59

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: 196.39  E-value: 5.26e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  21 DFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKrqsraSRRGVSrEEIErevSILRQVLHHNVITLHDVYENRTDVV 100
Cdd:cd14176    19 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDK-----SKRDPT-EEIE---ILLRYGQHPNIITLKDVYDDGKYVY 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 101 LILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLAHEI-- 178
Cdd:cd14176    90 VVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPESIRICDFGFAKQLra 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 179 EDGVEFKNIFgTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLG---DTKQETLANITAVSYDFDEEFFSQTS 255
Cdd:cd14176   170 ENGLLMTPCY-TANFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPFANgpdDTPEEILARIGSGKFSLSGGYWNSVS 248
                         250       260       270
                  ....*....|....*....|....*....|....
gi 2056392213 256 ELAKDFIRKLLVKETRKRLTIQEALRHPWITPVD 289
Cdd:cd14176   249 DTAKDLVSKMLHVDPHQRLTAALVLRHPWIVHWD 282
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
21-289 3.88e-58

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: 192.55  E-value: 3.88e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  21 DFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASrrgvsrEEIErevSILRQVLHHNVITLHDVYENRTDVV 100
Cdd:cd14175     1 DGYVVKETIGVGSYSVCKRCVHKATNMEYAVKVIDKSKRDPS------EEIE---ILLRYGQHPNIITLKDVYDDGKHVY 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 101 LILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLAHEI-- 178
Cdd:cd14175    72 LVTELMRGGELLDKILRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYVDESGNPESLRICDFGFAKQLra 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 179 EDGVEFKNIFgTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPF---LGDTKQETLANITAVSYDFDEEFFSQTS 255
Cdd:cd14175   152 ENGLLMTPCY-TANFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFangPSDTPEEILTRIGSGKFTLSGGNWNTVS 230
                         250       260       270
                  ....*....|....*....|....*....|....
gi 2056392213 256 ELAKDFIRKLLVKETRKRLTIQEALRHPWITPVD 289
Cdd:cd14175   231 DAAKDLVSKMLHVDPHQRLTAKQVLQHPWITQKD 264
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
19-286 8.37e-58

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: 190.98  E-value: 8.37e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  19 VEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRrgvsrEEIEREVSILRQVLHHNVITLHDVYENRTD 98
Cdd:cd14183     4 ISERYKVGRTIGDGNFAVVKECVERSTGREYALKIINKSKCRGKE-----HMIQNEVSILRRVKHPNIVLLIEEMDMPTE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  99 VVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLAhEI 178
Cdd:cd14183    79 LYLVMELVKGGDLFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEHQDGSKSLKLGDFGLA-TV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 179 EDGVEFkNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTK-QETLAN-ITAVSYDFDEEFFSQTSE 256
Cdd:cd14183   158 VDGPLY-TVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGSGDdQEVLFDqILMGQVDFPSPYWDNVSD 236
                         250       260       270
                  ....*....|....*....|....*....|
gi 2056392213 257 LAKDFIRKLLVKETRKRLTIQEALRHPWIT 286
Cdd:cd14183   237 SAKELITMMLQVDVDQRYSALQVLEHPWVN 266
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
21-298 1.49e-57

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: 191.00  E-value: 1.49e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  21 DFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKrqsraSRRGVSrEEIErevSILRQVLHHNVITLHDVYENRTDVV 100
Cdd:cd14178     3 DGYEIKEDIGIGSYSVCKRCVHKATSTEYAVKIIDK-----SKRDPS-EEIE---ILLRYGQHPNIITLKDVYDDGKFVY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 101 LILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLAHEI-- 178
Cdd:cd14178    74 LVMELMRGGELLDRILRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYMDESGNPESIRICDFGFAKQLra 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 179 EDGVEFKNIFgTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLG---DTKQETLANITAVSYDFDEEFFSQTS 255
Cdd:cd14178   154 ENGLLMTPCY-TANFVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPFANgpdDTPEEILARIGSGKYALSGGNWDSIS 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2056392213 256 ELAKDFIRKLLVKETRKRLTIQEALRHPWITPVD--NQQAMVRRE 298
Cdd:cd14178   233 DAAKDIVSKMLHVDPHQRLTAPQVLRHPWIVNREylSQNQLSRQD 277
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
29-284 6.39e-57

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: 187.81  E-value: 6.39e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRqsRASRRgvSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSG 108
Cdd:cd14009     1 IGRGSFATVWKGRHKQTGEVVAIKEISRK--KLNKK--LQENLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 109 GELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNIPIPHIKLIDFGLAHEIEDGVEFKNIF 188
Cdd:cd14009    77 GDLSQYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNL-LLSTSGDDPVLKIADFGFARSLQPASMAETLC 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 189 GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSELAKDFIRKLLVK 268
Cdd:cd14009   156 GSPLYMAPEILQFQKYDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIERSDAVIPFPIAAQLSPDCKDLLRRLLRR 235
                         250
                  ....*....|....*.
gi 2056392213 269 ETRKRLTIQEALRHPW 284
Cdd:cd14009   236 DPAERISFEEFFAHPF 251
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
23-281 1.33e-56

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: 187.41  E-value: 1.33e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIkkrQSRASRRGVSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd14014     2 YRLVRLLGRGGMGEVYRARDTLLGRPVAIKVL---RPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIEDGV 182
Cdd:cd14014    79 MEYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDG----RVKLTDFGIARALGDSG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 183 E--FKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSELAKD 260
Cdd:cd14014   155 LtqTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPALDA 234
                         250       260
                  ....*....|....*....|.
gi 2056392213 261 FIRKLLVKETRKRLTIQEALR 281
Cdd:cd14014   235 IILRALAKDPEERPQSAAELL 255
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
22-285 2.38e-55

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: 184.13  E-value: 2.38e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  22 FYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASrrgvSREEIEREVSILRQVLHHNVITLHDVYENRTDVVL 101
Cdd:cd14071     1 FYDIERTIGKGNFAVVKLARHRITKTEVAIKIIDKSQLDEE----NLKKIYREVQIMKMLNHPHIIKLYQVMETKDMLYL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 102 ILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENiMLLDKNIpipHIKLIDFGLAHEIEDG 181
Cdd:cd14071    77 VTEYASNGEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAEN-LLLDANM---NIKIADFGFSNFFKPG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 182 VEFKNIFGTPEFVAPEIVN-YEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANItaVSYDFDEEFFsqTSELAKD 260
Cdd:cd14071   153 ELLKTWCGSPPYAAPEVFEgKEYEGPQLDIWSLGVVLYVLVCGALPFDGSTLQTLRDRV--LSGRFRIPFF--MSTDCEH 228
                         250       260
                  ....*....|....*....|....*
gi 2056392213 261 FIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14071   229 LIRRMLVLDPSKRLTIEQIKKHKWM 253
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
23-285 3.48e-54

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: 180.86  E-value: 3.48e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRasrrgvSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd05122     2 FEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESKE------KKESILNEIAILKKCKHPNIVKYYGSYLKKDELWIV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQK-ESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIEDG 181
Cdd:cd05122    76 MEFCSGGSLKDLLKNTnKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDG----EVKLIDFGLSAQLSDG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 182 VEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANI-TAVSYDFDEEffSQTSELAKD 260
Cdd:cd05122   152 KTRNTFVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSELPPMKALFLIaTNGPPGLRNP--KKWSKEFKD 229
                         250       260
                  ....*....|....*....|....*
gi 2056392213 261 FIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd05122   230 FLKKCLQKDPEKRPTAEQLLKHPFI 254
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
23-284 3.49e-54

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: 181.33  E-value: 3.49e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDI-GEELGSGQFAIVKKCREKSTGLEYAAKFIkkRQSRASRRgvsreeierEVSI-LRQVLHHNVITLHDVYENRTD-- 98
Cdd:cd14089     2 YTIsKQVLGLGINGKVLECFHKKTGEKFALKVL--RDNPKARR---------EVELhWRASGCPHIVRIIDVYENTYQgr 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  99 --VVLILELVSGGELFDFLAQK--ESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNiPIPHIKLIDFGL 174
Cdd:cd14089    71 kcLLVVMECMEGGELFSRIQERadSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKG-PNAILKLTDFGF 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 175 AHEIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQE----TLANITAVSYDFDEEF 250
Cdd:cd14089   150 AKETTTKKSLQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAispgMKKRIRNGQYEFPNPE 229
                         250       260       270
                  ....*....|....*....|....*....|....
gi 2056392213 251 FSQTSELAKDFIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd14089   230 WSNVSEEAKDLIRGLLKTDPSERLTIEEVMNHPW 263
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
23-285 9.69e-54

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: 180.05  E-value: 9.69e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVsreeIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd14097     3 YTFGRKLGQGSFGVVIEATHKETQTKWAIKKINREKAGSSAVKL----LEREVDILKHVNHAHIIHLEEVFETPKRMYLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIM----LLDKNIPIpHIKLIDFGLAHEI 178
Cdd:cd14097    79 MELCEDGELKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILvkssIIDNNDKL-NIKVTDFGLSVQK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 179 EDGVE--FKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSE 256
Cdd:cd14097   158 YGLGEdmLQETCGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRKGDLTFTQSVWQSVSD 237
                         250       260
                  ....*....|....*....|....*....
gi 2056392213 257 LAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14097   238 AAKNVLQQLLKVDPAHRMTASELLDNPWI 266
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
20-316 1.55e-53

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: 180.82  E-value: 1.55e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  20 EDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRrGVSREEIEREVSILRQVLHHNVITLHDVYENRTDV 99
Cdd:cd14094     2 EDVYELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVAKFTSSP-GLSTEDLKREASICHMLKHPHIVELLETYSSDGML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 100 VLILELVSGGELFDFLAQKES----LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPhIKLIDFGLA 175
Cdd:cd14094    81 YMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAP-VKLGGFGVA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 176 HEI-EDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGdTKQETLANITAVSYDFDEEFFSQT 254
Cdd:cd14094   160 IQLgESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQWSHI 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2056392213 255 SELAKDFIRKLLVKETRKRLTIQEALRHPWITPVDNQQAMVRRESVVnlENFRKQYVRRRWK 316
Cdd:cd14094   239 SESAKDLVRRMLMLDPAERITVYEALNHPWIKERDRYAYRIHLPETV--EQLRKFNARRKLK 298
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
23-285 1.14e-52

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: 177.22  E-value: 1.14e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQsrasRRGVSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd14074     5 YDLEETLGRGHFAVVKLARHVFTGEKVAVKVIDKTK----LDDVSKAHLFQEVRCMKLVQHPNVVRLYEVIDTQTKLYLI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQKES-LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipiPHIKLIDFGLAHEIEDG 181
Cdd:cd14074    81 LELGDGGDMYDYIMKHENgLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFFEKQ---GLVKLTDFGFSNKFQPG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 182 VEFKNIFGTPEFVAPEIVnyepLGLE-----ADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDeeffSQTSE 256
Cdd:cd14074   158 EKLETSCGSLAYSAPEIL----LGDEydapaVDIWSLGVILYMLVCGQPPFQEANDSETLTMIMDCKYTVP----AHVSP 229
                         250       260
                  ....*....|....*....|....*....
gi 2056392213 257 LAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14074   230 ECKDLIRRMLIRDPKKRASLEEIENHPWL 258
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
21-285 1.79e-52

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: 177.65  E-value: 1.79e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  21 DFYDI--GEELGSGQFAIVKKCREKSTGLEYAAKFIkkrqsrasrrgVSREEIEREVSILRQVL-HHNVITLHDVYEN-- 95
Cdd:cd14171     4 EEYEVnwTQKLGTGISGPVRVCVKKSTGERFALKIL-----------LDRPKARTEVRLHMMCSgHPNIVQIYDVYANsv 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  96 --------RTDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPhI 167
Cdd:cd14171    73 qfpgesspRARLLIVMELMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNSEDAP-I 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 168 KLIDFGLAhEIEDGVEFKNIFgTPEFVAPEIvnyeplgLEA------------------------DMWSIGVITYILLSG 223
Cdd:cd14171   152 KLCDFGFA-KVDQGDLMTPQF-TPYYVAPQV-------LEAqrrhrkersgiptsptpytydkscDMWSLGVIIYIMLCG 222
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2056392213 224 ASPFLGDTKQETLAN-----ITAVSYDFDEEFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14171   223 YPPFYSEHPSRTITKdmkrkIMTGSYEFPEEEWSQISEMAKDIVRKLLCVDPEERMTIEEVLHHPWL 289
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
23-285 3.14e-52

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: 175.78  E-value: 3.14e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRrgvsreeIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd14111     5 YTFLDEKARGRFGVIRRCRENATGKNFPAKIVPYQAEEKQG-------VLQEYEILKSLHHERIMALHEAYITPRYLVLI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIEDGV 182
Cdd:cd14111    78 AEFCSGKELLHSLIDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNA----IKIVDFGSAQSFNPLS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 183 --EFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDfDEEFFSQTSELAKD 260
Cdd:cd14111   154 lrQLGRRTGTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFEDQDPQETEAKILVAKFD-AFKLYPNVSQSASL 232
                         250       260
                  ....*....|....*....|....*
gi 2056392213 261 FIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14111   233 FLKKVLSSYPWSRPTTKDCFAHAWL 257
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
23-285 8.32e-52

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: 174.76  E-value: 8.32e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKStGLEYAAKFIKKRQSRASRRGVsreEIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd14161     5 YEFLETLGKGTYGRVKKARDSS-GRLVAIKSIRKDRIKDEQDLL---HIRREIEIMSSLNHPHIISVYEVFENSSKIVIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAHEIEDGV 182
Cdd:cd14161    81 MEYASRGDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENI-LLDAN---GNIKIADFGLSNLYNQDK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 183 EFKNIFGTPEFVAPEIVNYEP-LGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDeeffSQTSElAKDF 261
Cdd:cd14161   157 FLQTYCGSPLYASPEIVNGRPyIGPEVDSWSLGVLLYILVHGTMPFDGHDYKILVKQISSGAYREP----TKPSD-ACGL 231
                         250       260
                  ....*....|....*....|....
gi 2056392213 262 IRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14161   232 IRWLLMVNPERRATLEDVASHWWV 255
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
23-285 8.99e-52

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: 174.75  E-value: 8.99e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRqsrasrrGVSREEIE---REVSILRQVLHHNVITLHDVYENRTDV 99
Cdd:cd14002     3 YHVLELIGEGSFGKVYKGRRKYTGQVVALKFIPKR-------GKSEKELRnlrQEIEILRKLNHPNIIEMLDSFETKKEF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 100 VLILELVSGgELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAHEI- 178
Cdd:cd14002    76 VVVTEYAQG-ELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNI-LIGKG---GVVKLCDFGFARAMs 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 179 EDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITavsYDfDEEFFSQTSELA 258
Cdd:cd14002   151 CNTLVLTSIKGTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYTNSIYQLVQMIV---KD-PVKWPSNMSPEF 226
                         250       260
                  ....*....|....*....|....*..
gi 2056392213 259 KDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14002   227 KSFLQGLLNKDPSKRLSWPDLLEHPFV 253
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
31-289 1.66e-51

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: 174.33  E-value: 1.66e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  31 SGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRgVSREEIEREvsILRQVLHHNVITLHDVYENRTDVVLILELVSGGE 110
Cdd:cd05579     3 RGAYGRVYLAKKKSTGDLYAIKVIKKRDMIRKNQ-VDSVLAERN--ILSQAQNPFVVKLYYSFQGKKNLYLVMEYLPGGD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 111 LFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGL--------------AH 176
Cdd:cd05579    80 LYSLLENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNI-LIDAN---GHLKLTDFGLskvglvrrqiklsiQK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 177 EIEDGVEFKN--IFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFfsQT 254
Cdd:cd05579   156 KSNGAPEKEDrrIVGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNILNGKIEWPEDP--EV 233
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2056392213 255 SELAKDFIRKLLVKETRKRL---TIQEALRHPWITPVD 289
Cdd:cd05579   234 SDEAKDLISKLLTPDPEKRLgakGIEEIKNHPFFKGID 271
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
26-285 2.32e-51

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: 173.48  E-value: 2.32e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  26 GEELGSGQFAIVKKCREKSTGLEYAAKfikkrQSRASRRGVSR-EEIEREVSILRQVLHHNVITLHDVYENRTDVVLILE 104
Cdd:cd06606     5 GELLGKGSFGSVYLALNLDTGELMAVK-----EVELSGDSEEElEALEREIRILSSLKHPNIVRYLGTERTENTLNIFLE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 105 LVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLA---HEIEDG 181
Cdd:cd06606    80 YVPGGSLASLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGV----VKLADFGCAkrlAEIATG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 182 VEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFlgDTKQETLANITAVSYDFDE-EFFSQTSELAKD 260
Cdd:cd06606   156 EGTKSLRGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPW--SELGNPVAALFKIGSSGEPpPIPEHLSEEAKD 233
                         250       260
                  ....*....|....*....|....*
gi 2056392213 261 FIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd06606   234 FLRKCLQRDPKKRPTADELLQHPFL 258
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
21-289 5.16e-51

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: 174.05  E-value: 5.16e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  21 DFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKrqsraSRRGVSrEEIErevSILRQVLHHNVITLHDVYENRTDVV 100
Cdd:cd14177     4 DVYELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDK-----SKRDPS-EEIE---ILMRYGQHPNIITLKDVYDDGRYVY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 101 LILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLAHEI-- 178
Cdd:cd14177    75 LVTELMKGGELLDRILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDDSANADSIRICDFGFAKQLrg 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 179 EDGVEFKNIFgTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFL---GDTKQETLANITAVSYDFDEEFFSQTS 255
Cdd:cd14177   155 ENGLLLTPCY-TANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPFAngpNDTPEEILLRIGSGKFSLSGGNWDTVS 233
                         250       260       270
                  ....*....|....*....|....*....|....
gi 2056392213 256 ELAKDFIRKLLVKETRKRLTIQEALRHPWITPVD 289
Cdd:cd14177   234 DAAKDLLSHMLHVDPHQRYTAEQVLKHSWIACRD 267
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
23-285 1.38e-50

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: 171.55  E-value: 1.38e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASrrgvSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd14072     2 YRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQLNPS----SLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENiMLLDKNIpipHIKLIDFGLAHEIEDGV 182
Cdd:cd14072    78 MEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAEN-LLLDADM---NIKIADFGFSNEFTPGN 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 183 EFKNIFGTPEFVAPEIVN---YEplGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFdeEFFSQTSelAK 259
Cdd:cd14072   154 KLDTFCGSPPYAAPELFQgkkYD--GPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRI--PFYMSTD--CE 227
                         250       260
                  ....*....|....*....|....*.
gi 2056392213 260 DFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14072   228 NLLKKFLVLNPSKRGTLEQIMKDRWM 253
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
27-284 1.51e-50

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: 171.83  E-value: 1.51e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFAIVKKCREKSTGLEYAAKFIKKrqSRASRRGVSReeIEREVSILRQVLHHNVITLHDVYENRTDVVLILELV 106
Cdd:cd14082     9 EVLGSGQFGIVYGGKHRKTGRDVAIKVIDK--LRFPTKQESQ--LRNEVAILQQLSHPGVVNLECMFETPERVFVVMEKL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 107 SGGELFDFLAQKESLSEEEATSF-IKQILDGVNYLHTKKIAHFDLKPENImLLDKNIPIPHIKLIDFGLAHEIEDGVEFK 185
Cdd:cd14082    85 HGDMLEMILSSEKGRLPERITKFlVTQILVALRYLHSKNIVHCDLKPENV-LLASAEPFPQVKLCDFGFARIIGEKSFRR 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 186 NIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDtkQETLANITAVSYDFDEEFFSQTSELAKDFIRKL 265
Cdd:cd14082   164 SVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNED--EDINDQIQNAAFMYPPNPWKEISPDAIDLINNL 241
                         250
                  ....*....|....*....
gi 2056392213 266 LVKETRKRLTIQEALRHPW 284
Cdd:cd14082   242 LQVKMRKRYSVDKSLSHPW 260
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
23-285 3.13e-50

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: 171.85  E-value: 3.13e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCR-EKSTGLEYAAKFIKKRQ-SRASRRGVSREEIEREVSILRQVLHHNVITLHDVYENRTDVV 100
Cdd:cd14096     3 YRLINKIGEGAFSNVYKAVpLRNTGKPVAIKVVRKADlSSDNLKGSSRANILKEVQIMKRLSHPNIVKLLDFQESDEYYY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 101 LILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIML---------------------LD 159
Cdd:cd14096    83 IVLELADGGEIFHQIVRLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFepipfipsivklrkadddetkVD 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 160 KNIPIP--------HIKLIDFGLAHEIEDGvEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDT 231
Cdd:cd14096   163 EGEFIPgvggggigIVKLADFGLSKQVWDS-NTKTPCGTVGYTAPEVVKDERYSKKVDMWALGCVLYTLLCGFPPFYDES 241
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2056392213 232 KQETLANITAVSYDFDEEFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14096   242 IETLTEKISRGDYTFLSPWWDEISKSAKDLISHLLTVDPAKRYDIDEFLAHPWI 295
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
23-285 7.76e-50

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: 169.67  E-value: 7.76e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKC--REKSTGLEYAAKFIKKRQSrasrrgvSREEIE----REVSILRQVLHHNVITLHDVYENR 96
Cdd:cd14080     2 YRLGKTIGEGSYSKVKLAeyTKSGLKEKVACKIIDKKKA-------PKDFLEkflpRELEILRKLRHPNIIQVYSIFERG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  97 TDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNIpipHIKLIDFGLAH 176
Cdd:cd14080    75 SKVFIFMEYAEHGDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENI-LLDSNN---NVKLSDFGFAR 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 177 EIED--GVEFKNIF-GTPEFVAPEIVN---YEPLGleADMWSIGVITYILLSGASPFlGDTkqetlaNITAVSYDFDEE- 249
Cdd:cd14080   151 LCPDddGDVLSKTFcGSAAYAAPEILQgipYDPKK--YDIWSLGVILYIMLCGSMPF-DDS------NIKKMLKDQQNRk 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2056392213 250 -FFSQT----SELAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14080   222 vRFPSSvkklSPECKDLIDQLLEPDPTKRATIEEILNHPWL 262
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
23-285 1.77e-49

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: 168.80  E-value: 1.77e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIkkRQSRASRRgvSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd08215     2 YEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEI--DLSNMSEK--EREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFL----AQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEI 178
Cdd:cd08215    78 MEYADGGDLAQKIkkqkKKGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGV----VKLGDFGISKVL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 179 EDGVEFKNIF-GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQtsEL 257
Cdd:cd08215   154 ESTTDLAKTVvGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQYPPIPSQYSS--EL 231
                         250       260
                  ....*....|....*....|....*...
gi 2056392213 258 aKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd08215   232 -RDLVNSMLQKDPEKRPSANEILSSPFI 258
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
13-285 2.44e-49

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: 170.22  E-value: 2.44e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  13 PFKQQKVEDFYDigEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQsrasrrgvsREEIEREVSILRQVLHH-NVITLHD 91
Cdd:cd14179     1 PFYQHYELDLKD--KPLGEGSFSICRKCLHKKTNQEYAVKIVSKRM---------EANTQREIAALKLCEGHpNIVKLHE 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  92 VYENRTDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNiPIPHIKLID 171
Cdd:cd14179    70 VYHDQLHTFLVMELLKGGELLERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDES-DNSEIKIID 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 172 FGLAH-EIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTK-------QETLANITAVS 243
Cdd:cd14179   149 FGFARlKPPDNQPLKTPCFTLHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFQCHDKsltctsaEEIMKKIKQGD 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2056392213 244 YDFDEEFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14179   229 FSFEGEAWKNVSQEAKDLIQGLLTVDPNKRIKMSGLRYNEWL 270
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
21-285 2.25e-48

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: 166.74  E-value: 2.25e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  21 DFYDIGEE-LGSGQFAIVKKCREKSTGLEYAAKFIKKRQsrasrrGVSREEIEREVSILRQVL-HHNVITLHDVYENRTD 98
Cdd:cd14173     1 DVYQLQEEvLGEGAYARVQTCINLITNKEYAVKIIEKRP------GHSRSRVFREVEMLYQCQgHRNVLELIEFFEEEDK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  99 VVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPhIKLIDFGLAHEI 178
Cdd:cd14173    75 FYLVFEKMRGGSILSHIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQVSP-VKICDFDLGSGI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 179 E--------DGVEFKNIFGTPEFVAPEIVnyEPLGLEA-------DMWSIGVITYILLSGASPFLGDTKQET-------- 235
Cdd:cd14173   154 KlnsdcspiSTPELLTPCGSAEYMAPEVV--EAFNEEAsiydkrcDLWSLGVILYIMLSGYPPFVGRCGSDCgwdrgeac 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2056392213 236 -------LANITAVSYDFDEEFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14173   232 pacqnmlFESIQEGKYEFPEKDWAHISCAAKDLISKLLVRDAKQRLSAAQVLQHPWV 288
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
21-285 7.35e-48

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: 165.59  E-value: 7.35e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  21 DFYDIGEEL-GSGQFAIVKKCREKSTGLEYAAKFIKKRQsrasrrGVSREEIEREVSILRQVL-HHNVITLHDVYENRTD 98
Cdd:cd14174     1 DLYRLTDELlGEGAYAKVQGCVSLQNGKEYAVKIIEKNA------GHSRSRVFREVETLYQCQgNKNILELIEFFEDDTR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  99 VVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPhIKLIDFGLAHEI 178
Cdd:cd14174    75 FYLVFEKLRGGSILAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESPDKVSP-VKICDFDLGSGV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 179 E--------DGVEFKNIFGTPEFVAPEIVnyEPLGLEA-------DMWSIGVITYILLSGASPFLGD------------- 230
Cdd:cd14174   154 KlnsactpiTTPELTTPCGSAEYMAPEVV--EVFTDEAtfydkrcDLWSLGVILYIMLSGYPPFVGHcgtdcgwdrgevc 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2056392213 231 --TKQETLANITAVSYDFDEEFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14174   232 rvCQNKLFESIQEGKYEFPDKDWSHISSEAKDLISKLLVRDAKERLSAAQVLQHPWV 288
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
23-282 7.79e-48

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 170.58  E-value: 7.79e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRrgvSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:COG0515     9 YRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPE---ARERFRREARALARLNHPNIVRVYDVGEEDGRPYLV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIEDGV 182
Cdd:COG0515    86 MEYVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDG----RVKLIDFGIARALGGAT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 183 --EFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSELAKD 260
Cdd:COG0515   162 ltQTGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRPDLPPALDA 241
                         250       260
                  ....*....|....*....|..
gi 2056392213 261 FIRKLLVKETRKRLTIQEALRH 282
Cdd:COG0515   242 IVLRALAKDPEERYQSAAELAA 263
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
20-289 2.84e-47

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: 163.90  E-value: 2.84e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  20 EDFyDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRgvsREEIEREVSILRQVLHHNVITLHDVYENRTDV 99
Cdd:cd05580     1 DDF-EFLKTLGTGSFGRVRLVKHKDSGKYYALKILKKAKIIKLKQ---VEHVLNEKRILSEVRHPFIVNLLGSFQDDRNL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 100 VLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAHEIE 179
Cdd:cd05580    77 YMVMEYVPGGELFSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENL-LLDSD---GHIKITDFGFAKRVK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 180 DgvEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFfsqtSELAK 259
Cdd:cd05580   153 D--RTYTLCGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKILEGKIRFPSFF----DPDAK 226
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2056392213 260 DFIRKLLVKETRKRL-----TIQEALRHPWITPVD 289
Cdd:cd05580   227 DLIKRLLVVDLTKRLgnlknGVEDIKNHPWFAGID 261
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
23-285 4.63e-47

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: 162.65  E-value: 4.63e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVK-----KCREKSTGLEYAAKFIKK----RQSRASRrgvsreeIEREVSILRQVLHHNVITLHDVY 93
Cdd:cd14076     3 YILGRTLGEGEFGKVKlgwplPKANHRSGVQVAIKLIRRdtqqENCQTSK-------IMREINILKGLTHPNIVRLLDVL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  94 ENRTDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFG 173
Cdd:cd14076    76 KTKKYIGIVLEFVSGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENL-LLDKN---RNLVITDFG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 174 LAHEIE--DGVEFKNIFGTPEFVAPEIVNYEPL--GLEADMWSIGVITYILLSGASPFLGDTKQETLAN-------ITAV 242
Cdd:cd14076   152 FANTFDhfNGDLMSTSCGSPCYAAPELVVSDSMyaGRKADIWSCGVILYAMLAGYLPFDDDPHNPNGDNvprlyryICNT 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 2056392213 243 SYDFDEEFfsqtSELAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14076   232 PLIFPEYV----TPKARDLLRRILVPNPRKRIRLSAIMRHAWL 270
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
29-285 4.86e-47

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: 163.89  E-value: 4.86e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQsrasrrgvsREEIEREVSILRQVLHH-NVITLHDVYENRTDVVLILELVS 107
Cdd:cd14180    14 LGEGSFSVCRKCRHRQSGQEYAVKIISRRM---------EANTQREVAALRLCQSHpNIVALHEVLHDQYHTYLVMELLR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 108 GGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPhIKLIDFGLAHEIEDGVE-FKN 186
Cdd:cd14180    85 GGELLDRIKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDGAV-LKVIDFGFARLRPQGSRpLQT 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 187 IFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQ-------ETLANITAVSYDFDEEFFSQTSELAK 259
Cdd:cd14180   164 PCFTLQYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFQSKRGKmfhnhaaDIMHKIKEGDFSLEGEAWKGVSEEAK 243
                         250       260
                  ....*....|....*....|....*.
gi 2056392213 260 DFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14180   244 DLVRGLLTVDPAKRLKLSELRESDWL 269
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
23-284 5.08e-46

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: 159.80  E-value: 5.08e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKrqsrASRRGVSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd14069     3 WDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDM----KRAPGDCPENIKKEVCIQKMLSHKNVVRFYGHRREGEFQYLF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAHE-IEDG 181
Cdd:cd14069    79 LEYASGGELFDKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENL-LLDEN---DNLKISDFGLATVfRYKG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 182 VE--FKNIFGTPEFVAPEIVNYEPL-GLEADMWSIGVITYILLSGASPFlgdtKQETLANITAVSYDFDEEF----FSQT 254
Cdd:cd14069   155 KErlLNKMCGTLPYVAPELLAKKKYrAEPVDVWSCGIVLFAMLAGELPW----DQPSDSCQEYSDWKENKKTyltpWKKI 230
                         250       260       270
                  ....*....|....*....|....*....|
gi 2056392213 255 SELAKDFIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd14069   231 DTAALSLLRKILTENPNKRITIEDIKKHPW 260
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
29-283 1.31e-45

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: 158.69  E-value: 1.31e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREK-STGLEYAAKFI-KKRQSRasrrgvSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELV 106
Cdd:cd14120     1 IGHGAFAVVFKGRHRkKPDLPVAIKCItKKNLSK------SQNLLGKEIKILKELSHENVVALLDCQETSSSVYLVMEYC 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 107 SGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPH-----IKLIDFGLAHEIEDG 181
Cdd:cd14120    75 NGGDLADYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSGRKPSpndirLKIADFGFARFLQDG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 182 VEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQEtLANITAVSYDFDEEFFSQTSELAKDF 261
Cdd:cd14120   155 MMAATLCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFQAQTPQE-LKAFYEKNANLRPNIPSGTSPALKDL 233
                         250       260
                  ....*....|....*....|..
gi 2056392213 262 IRKLLVKETRKRLTIQEALRHP 283
Cdd:cd14120   234 LLGLLKRNPKDRIDFEDFFSHP 255
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
23-285 1.60e-45

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: 158.32  E-value: 1.60e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVSRE--EIEREVSILRQV---LHHNVITLHDVYENRT 97
Cdd:cd14004     2 YTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFKERILVDTWVRDRKlgTVPLEIHILDTLnkrSHPNIVKLLDFFEDDE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  98 DVVLILELV-SGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNIpipHIKLIDFGLAH 176
Cdd:cd14004    82 FYYLVMEKHgSGMDLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENV-ILDGNG---TIKLIDFGSAA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 177 EIEDGvEFKNIFGTPEFVAPEIVNYEP-LGLEADMWSIGVITYILLSGASPFLgdTKQETLanitavsyDFDEEFFSQTS 255
Cdd:cd14004   158 YIKSG-PFDTFVGTIDYAAPEVLRGNPyGGKEQDIWALGVLLYTLVFKENPFY--NIEEIL--------EADLRIPYAVS 226
                         250       260       270
                  ....*....|....*....|....*....|
gi 2056392213 256 ELAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14004   227 EDLIDLISRMLNRDVGDRPTIEELLTDPWL 256
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
20-285 1.86e-45

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: 158.10  E-value: 1.86e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  20 EDFyDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRqsrASRRGVSREEIEREVSILRQVLHHNVITLHDVYENRTDV 99
Cdd:cd14186     1 EDF-KVLNLLGKGSFACVYRARSLHTGLEVAIKMIDKK---AMQKAGMVQRVRNEVEIHCQLKHPSILELYNYFEDSNYV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 100 VLILELVSGGELFDFLAQ-KESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNIpipHIKLIDFGLAHEI 178
Cdd:cd14186    77 YLVLEMCHNGEMSRYLKNrKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNL-LLTRNM---NIKIADFGLATQL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 179 EDGVE-FKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYdfdeEFFSQTSEL 257
Cdd:cd14186   153 KMPHEkHFTMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVLADY----EMPAFLSRE 228
                         250       260
                  ....*....|....*....|....*...
gi 2056392213 258 AKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14186   229 AQDLIHQLLRKNPADRLSLSSVLDHPFM 256
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
29-285 2.17e-45

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: 158.24  E-value: 2.17e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKC--REKSTGLEYAAKFIKKRqSRASRRGVSREEIEREVSILRQVLHHNVITLHDVYENRTD-VVLILEL 105
Cdd:cd13994     1 IGKGATSVVRIVtkKNPRSGVLYAVKEYRRR-DDESKRKDYVKRLTSEYIISSKLHHPNIVKVLDLCQDLHGkWCLVMEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 106 VSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIEDGVE-- 183
Cdd:cd13994    80 CPGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDG----VLKLTDFGTAEVFGMPAEke 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 184 ---FKNIFGTPEFVAPEIVN---YEPLGleADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSEL 257
Cdd:cd13994   156 spmSAGLCGSEPYMAPEVFTsgsYDGRA--VDVWSCGIVLFALFTGRFPWRSAKKSDSAYKAYEKSGDFTNGPYEPIENL 233
                         250       260       270
                  ....*....|....*....|....*....|..
gi 2056392213 258 ----AKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd13994   234 lpseCRRLIYRMLHPDPEKRITIDEALNDPWV 265
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
29-284 3.22e-45

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: 157.77  E-value: 3.22e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRgvsREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSG 108
Cdd:cd05572     1 LGVGGFGRVELVQLKSKGRTFALKCVKKRHIVQTRQ---QEHIFSEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 109 GELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAHEIEDGVEFKNIF 188
Cdd:cd05572    78 GELWTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENL-LLDSN---GYVKLVDFGFAKKLGSGRKTWTFC 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 189 GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQ--ETLANITAVSYDFdeEFFSQTSELAKDFIRKLL 266
Cdd:cd05572   154 GTPEYVAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFGGDDEDpmKIYNIILKGIDKI--EFPKYIDKNAKNLIKQLL 231
                         250       260
                  ....*....|....*....|...
gi 2056392213 267 VKETRKRLTIQ----EALR-HPW 284
Cdd:cd05572   232 RRNPEERLGYLkggiRDIKkHKW 254
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
20-290 5.19e-45

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: 157.37  E-value: 5.19e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  20 EDFyDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKkrqsrASRRGVSREEIEREVSILRQVLHHNVITLHDVYENRTDV 99
Cdd:cd06623     1 SDL-ERVKVLGQGSSGVVYKVRHKPTGKIYALKKIH-----VDGDEEFRKQLLRELKTLRSCESPYVVKCYGAFYKEGEI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 100 VLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTK-KIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEI 178
Cdd:cd06623    75 SIVLEYMDGGSLADLLKKVGKIPEPVLAYIARQILKGLDYLHTKrHIIHRDIKPSNLLINSKG----EVKIADFGISKVL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 179 EDGVEFKNIF-GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLgDTKQETLANITAV-----SYDFDEEFFS 252
Cdd:cd06623   151 ENTLDQCNTFvGTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFL-PPGQPSFFELMQAicdgpPPSLPAEEFS 229
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2056392213 253 QtsELaKDFIRKLLVKETRKRLTIQEALRHPWITPVDN 290
Cdd:cd06623   230 P--EF-RDFISACLQKDPKKRPSAAELLQHPFIKKADN 264
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
29-284 6.76e-45

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: 156.65  E-value: 6.76e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGvsREEIEREVSILRQVLHHNVITLHDVY--ENRTDVVLILELV 106
Cdd:cd14119     1 LGEGSYGKVKEVLDTETLCRRAVKILKKRKLRRIPNG--EANVKREIQILRRLNHRNVIKLVDVLynEEKQKLYMVMEYC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 107 SGG--ELFDFLAQKEsLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIE---DG 181
Cdd:cd14119    79 VGGlqEMLDSAPDKR-LPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGT----LKISDFGVAEALDlfaED 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 182 VEFKNIFGTPEFVAPEIVNYEP--LGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEffsqTSELAK 259
Cdd:cd14119   154 DTCTTSQGSPAFQPPEIANGQDsfSGFKVDIWSAGVTLYNMTTGKYPFEGDNIYKLFENIGKGEYTIPDD----VDPDLQ 229
                         250       260
                  ....*....|....*....|....*
gi 2056392213 260 DFIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd14119   230 DLLRGMLEKDPEKRFTIEQIRQHPW 254
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
23-284 1.91e-44

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: 155.70  E-value: 1.91e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKkrqsrasrRGVSREE-IEREVSILRQVLHHNVITLHDVYENRTDVVL 101
Cdd:cd14662     2 YELVKDIGSGNFGVARLMRNKETKELVAVKYIE--------RGLKIDEnVQREIINHRSLRHPNIIRFKEVVLTPTHLAI 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 102 ILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNiPIPHIKLIDFGLAHEIEDG 181
Cdd:cd14662    74 VMEYAAGGELFERICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENT-LLDGS-PAPRLKICDFGYSKSSVLH 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 182 VEFKNIFGTPEFVAPEIVNY-EPLGLEADMWSIGVITYILLSGASPF--LGDTK--QETLANITAVSYDFDEefFSQTSE 256
Cdd:cd14662   152 SQPKSTVGTPAYIAPEVLSRkEYDGKVADVWSCGVTLYVMLVGAYPFedPDDPKnfRKTIQRIMSVQYKIPD--YVRVSQ 229
                         250       260
                  ....*....|....*....|....*...
gi 2056392213 257 LAKDFIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd14662   230 DCRHLLSRIFVANPAKRITIPEIKNHPW 257
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
23-284 2.67e-44

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: 155.15  E-value: 2.67e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSrasrrgvSREEIE----REVSILRQVLHHNVITLHDVYENRTD 98
Cdd:cd14162     2 YIVGKTLGHGSYAVVKKAYSTKHKCKVAIKIVSKKKA-------PEDYLQkflpREIEVIKGLKHPNLICFYEAIETTSR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  99 VVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENiMLLDKNIpipHIKLIDFGLA--- 175
Cdd:cd14162    75 VYIIMELAENGDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCEN-LLLDKNN---NLKITDFGFArgv 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 176 HEIEDG--VEFKNIFGTPEFVAPEI---VNYEPlgLEADMWSIGVITYILLSGASPFlGDTKQETLANITAVSYDFDEEf 250
Cdd:cd14162   151 MKTKDGkpKLSETYCGSYAYASPEIlrgIPYDP--FLSDIWSMGVVLYTMVYGRLPF-DDSNLKVLLKQVQRRVVFPKN- 226
                         250       260       270
                  ....*....|....*....|....*....|....
gi 2056392213 251 fSQTSELAKDFIRKLLVKETrKRLTIQEALRHPW 284
Cdd:cd14162   227 -PTVSEECKDLILRMLSPVK-KRITIEEIKRDPW 258
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
16-286 3.30e-44

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: 155.12  E-value: 3.30e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  16 QQKVEDFyDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQsrASRRGVsREEIEREVSILRQVLHHNVITLHDVYEN 95
Cdd:cd14116     1 QWALEDF-EIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQ--LEKAGV-EHQLRREVEIQSHLRHPNILRLYGYFHD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  96 RTDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLA 175
Cdd:cd14116    77 ATRVYLILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAG----ELKIADFGWS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 176 HEIEDGVEfKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDeeffSQTS 255
Cdd:cd14116   153 VHAPSSRR-TTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFP----DFVT 227
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2056392213 256 ELAKDFIRKLLVKETRKRLTIQEALRHPWIT 286
Cdd:cd14116   228 EGARDLISRLLKHNPSQRPMLREVLEHPWIT 258
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
23-285 7.80e-44

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: 153.92  E-value: 7.80e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSrasrrgvSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd14110     5 YAFQTEINRGRFSVVRQCEEKRSGQMLAAKIIPYKPE-------DKQLVLREYQVLRRLSHPRIAQLHSAYLSPRHLVLI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIEDGV 182
Cdd:cd14110    78 EELCSGPELLYNLAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNL----LKIVDLGNAQPFNQGK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 183 -----EFKNIFgtpEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFdEEFFSQTSEL 257
Cdd:cd14110   154 vlmtdKKGDYV---ETMAPELLEGQGAGPQTDIWAIGVTAFIMLSADYPVSSDLNWERDRNIRKGKVQL-SRCYAGLSGG 229
                         250       260
                  ....*....|....*....|....*...
gi 2056392213 258 AKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14110   230 AVNFLKSTLCAKPWGRPTASECLQNPWL 257
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
23-284 3.94e-43

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: 152.06  E-value: 3.94e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSrasrrgvSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd14665     2 YELVKDIGSGNFGVARLMRDKQTKELVAVKYIERGEK-------IDENVQREIINHRSLRHPNIVRFKEVILTPTHLAIV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENiMLLDKNiPIPHIKLIDFGLAHEIEDGV 182
Cdd:cd14665    75 MEYAAGGELFERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLEN-TLLDGS-PAPRLKICDFGYSKSSVLHS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 183 EFKNIFGTPEFVAPEIV-NYEPLGLEADMWSIGVITYILLSGASPFLGDTK----QETLANITAVSYDFDEefFSQTSEL 257
Cdd:cd14665   153 QPKSTVGTPAYIAPEVLlKKEYDGKIADVWSCGVTLYVMLVGAYPFEDPEEprnfRKTIQRILSVQYSIPD--YVHISPE 230
                         250       260
                  ....*....|....*....|....*..
gi 2056392213 258 AKDFIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd14665   231 CRHLISRIFVADPATRITIPEIRNHEW 257
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
27-284 6.72e-43

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: 151.29  E-value: 6.72e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFAIVKKCREKSTGLEYAA-KFI-KKRQSRASRrgvsrEEIEREVSILRQVLHHNVITLHDVYENRTDVVLILE 104
Cdd:cd14121     1 EKLGSGTYATVYKAYRKSGAREVVAvKCVsKSSLNKAST-----ENLLTEIELLKKLKHPHIVELKDFQWDEEHIYLIME 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 105 LVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLldKNIPIPHIKLIDFGLAHEIEDGVEF 184
Cdd:cd14121    76 YCSGGDLSRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLL--SSRYNPVLKLADFGFAQHLKPNDEA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 185 KNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAvsydfDEEF----FSQTSELAKD 260
Cdd:cd14121   154 HSLRGSPLYMAPEMILKKKYDARVDLWSVGVILYECLFGRAPFASRSFEELEEKIRS-----SKPIeiptRPELSADCRD 228
                         250       260
                  ....*....|....*....|....
gi 2056392213 261 FIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd14121   229 LLLRLLQRDPDRRISFEEFFAHPF 252
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
23-285 1.26e-42

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: 151.06  E-value: 1.26e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFI--------KKRQSRASRRGVSREE-IEREVSILRQVLHHNVITLHDVY 93
Cdd:cd14077     3 WEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIprasnaglKKEREKRLEKEISRDIrTIREAALSSLLNHPHICRLRDFL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  94 ENRTDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMlLDKNipiPHIKLIDFG 173
Cdd:cd14077    83 RTPNHYYMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENIL-ISKS---GNIKIIDFG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 174 LAHEIEDGVEFKNIFGTPEFVAPEIVNYEP-LGLEADMWSIGVITYILLSGASPFLGDTKQETLANITavsyDFDEEFFS 252
Cdd:cd14077   159 LSNLYDPRRLLRTFCGSLYFAAPELLQAQPyTGPEVDVWSFGVVLYVLVCGKVPFDDENMPALHAKIK----KGKVEYPS 234
                         250       260       270
                  ....*....|....*....|....*....|...
gi 2056392213 253 QTSELAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14077   235 YLSSECKSLISRMLVVDPKKRATLEQVLNHPWM 267
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
23-285 5.78e-42

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: 149.55  E-value: 5.78e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRasrRGVSREEIeREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd07829     1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKIRLDNEE---EGIPSTAL-REISLLKELKHPNIVKLLDVIHTENKLYLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGgELFDFLAQKES-LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIedG 181
Cdd:cd07829    77 FEYCDQ-DLKKYLDKRPGpLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGV----LKLADFGLARAF--G 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 182 VEFKNIfgTPEFV-----APEIV----NYeplGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAV---------- 242
Cdd:cd07829   150 IPLRTY--THEVVtlwyrAPEILlgskHY---STAVDIWSVGCIFAELITGKPLFPGDSEIDQLFKIFQIlgtpteeswp 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2056392213 243 --------SYDFD-------EEFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd07829   225 gvtklpdyKPTFPkwpkndlEKVLPRLDPEGIDLLSKMLQYNPAKRISAKEALKHPYF 282
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
23-285 1.82e-41

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: 147.37  E-value: 1.82e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIkkrqSRASRRGVSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd06627     2 YQLGDLIGRGAFGSVYKGLNLNTGEFVAIKQI----SLEKIPKSDLKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYII 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAHEI-EDG 181
Cdd:cd06627    78 LEYVENGSLASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANI-LTTKD---GLVKLADFGVATKLnEVE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 182 VEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANItaVSydfDEE--FFSQTSELAK 259
Cdd:cd06627   154 KDENSVVGTPYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPYYDLQPMAALFRI--VQ---DDHppLPENISPELR 228
                         250       260
                  ....*....|....*....|....*.
gi 2056392213 260 DFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd06627   229 DFLLQCFQKDPTLRPSAKELLKHPWL 254
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
27-289 2.05e-41

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: 149.31  E-value: 2.05e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFAIVKKCREKSTGLEYAAKFIKKrQSRASRRGVSREEIEREvsILRQVLHHNVITLHDVYENRTDVVLILELV 106
Cdd:cd05574     7 KLLGKGDVGRVYLVRLKGTGKLFAMKVLDK-EEMIKRNKVKRVLTERE--ILATLDHPFLPTLYASFQTSTHLCFVMDYC 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 107 SGGELFDFLaQKES---LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLA-------- 175
Cdd:cd05574    84 PGGELFRLL-QKQPgkrLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESG----HIMLTDFDLSkqssvtpp 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 176 ---------------HEIED------GVEFKNIF-GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQ 233
Cdd:cd05574   159 pvrkslrkgsrrssvKSIEKetfvaePSARSNSFvGTEEYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGTTPFKGSNRD 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 234 ETLANITAVSYDFDEEffSQTSELAKDFIRKLLVKETRKRL----TIQEALRHPWITPVD 289
Cdd:cd05574   239 ETFSNILKKELTFPES--PPVSSEAKDLIRKLLVKDPSKRLgskrGASEIKRHPFFRGVN 296
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
23-289 2.62e-41

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: 148.35  E-value: 2.62e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRgvsREEIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd05612     3 FERIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPEVIRLKQ---EQHVHNEKRVLKEVSHPFIIRLFWTEHDQRFLYML 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMlLDKNipiPHIKLIDFGLAHEIEDgv 182
Cdd:cd05612    80 MEYVPGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENIL-LDKE---GHIKLTDFGFAKKLRD-- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 183 EFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFfsqtSELAKDFI 262
Cdd:cd05612   154 RTWTLCGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKILAGKLEFPRHL----DLYAKDLI 229
                         250       260       270
                  ....*....|....*....|....*....|..
gi 2056392213 263 RKLLVKETRKRL-----TIQEALRHPWITPVD 289
Cdd:cd05612   230 KKLLVVDRTRRLgnmknGADDVKNHRWFKSVD 261
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
23-284 3.97e-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: 147.05  E-value: 3.97e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQsrasrrgvsREEIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd14010     2 YVLYDEIGRGKHSVVYKGRRKGTIEFVAIKCVDKSK---------RPEVLNEVRLTHELKHPNVLKFYEWYETSNHLWLV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAHEIED-- 180
Cdd:cd14010    73 VEYCTGGDLETLLRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNI-LLDGN---GTLKLSDFGLARREGEil 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 181 --------------GVEFKNIF-GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANItaVSYD 245
Cdd:cd14010   149 kelfgqfsdegnvnKVSKKQAKrGTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGKPPFVAESFTELVEKI--LNED 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 2056392213 246 FDE---EFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHP-W 284
Cdd:cd14010   227 PPPpppKVSSKPSPDFKSLLKGLLEKDPAKRLSWDELVKHPfW 269
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
29-284 4.68e-41

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: 146.77  E-value: 4.68e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFA---IVKKCREKSTGLEYAAKFIKKrqSRASRRGVSREEIEREvsilRQVLHH-----NVITLHDVYENRTDVV 100
Cdd:cd05583     2 LGTGAYGkvfLVRKVGGHDAGKLYAMKVLKK--ATIVQKAKTAEHTMTE----RQVLEAvrqspFLVTLHYAFQTDAKLH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 101 LILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAHEIED 180
Cdd:cd05583    76 LILDYVNGGELFTHLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENI-LLDSE---GHVVLTDFGLSKEFLP 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 181 GVEFK-NIF-GTPEFVAPEIVNYEPLG--LEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSE 256
Cdd:cd05583   152 GENDRaYSFcGTIEYMAPEVVRGGSDGhdKAVDWWSLGVLTYELLTGASPFTVDGERNSQSEISKRILKSHPPIPKTFSA 231
                         250       260       270
                  ....*....|....*....|....*....|...
gi 2056392213 257 LAKDFIRKLLVKETRKRL-----TIQEALRHPW 284
Cdd:cd05583   232 EAKDFILKLLEKDPKKRLgagprGAHEIKEHPF 264
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
28-286 5.63e-41

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: 146.74  E-value: 5.63e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  28 ELGSGQFAIVKKCREKSTGLEYAAKFIKK----RQSRASRRGVSR-------------EEIEREVSILRQVLHHNVITLH 90
Cdd:cd14118     1 EIGKGSYGIVKLAYNEEDNTLYAMKILSKkkllKQAGFFRRPPPRrkpgalgkpldplDRVYREIAILKKLDHPNVVKLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  91 DVYE--NRTDVVLILELVSGGELFDFLAQKeSLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIK 168
Cdd:cd14118    81 EVLDdpNEDNLYMVFELVDKGAVMEVPTDN-PLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDG----HVK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 169 LIDFGLAHEIE-DGVEFKNIFGTPEFVAPEIVNYEPL---GLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSY 244
Cdd:cd14118   156 IADFGVSNEFEgDDALLSSTAGTPAFMAPEALSESRKkfsGKALDIWAMGVTLYCFVFGRCPFEDDHILGLHEKIKTDPV 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2056392213 245 DFDEEFfsQTSELAKDFIRKLLVKETRKRLTIQEALRHPWIT 286
Cdd:cd14118   236 VFPDDP--VVSEQLKDLILRMLDKNPSERITLPEIKEHPWVT 275
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
27-289 6.94e-41

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: 146.47  E-value: 6.94e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFAIVKKCREKSTGLEYAAKFIKKrQSRASRRGVSREEIEREVsILRQVLHHNVITLHDVYENRTDVVLILELV 106
Cdd:cd05611     2 KPISKGAFGSVYLAKKRSTGDYFAIKVLKK-SDMIAKNQVTNVKAERAI-MMIQGESPYVAKLYYSFQSKDYLYLVMEYL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 107 SGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENiMLLDKNipiPHIKLIDFGLAHEIEDGVEFKN 186
Cdd:cd05611    80 NGGDCASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPEN-LLIDQT---GHLKLTDFGLSRNGLEKRHNKK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 187 IFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSELAKDFIRKLL 266
Cdd:cd05611   156 FVGTPDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNILSRRINWPEEVKEFCSPEAVDLINRLL 235
                         250       260
                  ....*....|....*....|....*.
gi 2056392213 267 VKETRKRL---TIQEALRHPWITPVD 289
Cdd:cd05611   236 CMDPAKRLganGYQEIKSHPFFKSIN 261
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
23-285 7.51e-41

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: 145.84  E-value: 7.51e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRrgvsreeIEREVSILRQV----LHHNVITLHDVYENR-- 96
Cdd:cd05118     1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKIKNDFRHPKA-------ALREIKLLKHLndveGHPNIVKLLDVFEHRgg 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  97 TDVVLILELVsGGELFDFLA-QKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLldkNIPIPHIKLIDFGLA 175
Cdd:cd05118    74 NHLCLVFELM-GMNLYELIKdYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILI---NLELGQLKLADFGLA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 176 HEIEDGVEFKNIfGTPEFVAPE-IVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVsydfdeeffsQT 254
Cdd:cd05118   150 RSFTSPPYTPYV-ATRWYRAPEvLLGAKPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIVRL----------LG 218
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2056392213 255 SELAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd05118   219 TPEALDLLSKMLKYDPAKRITASQALAHPYF 249
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
29-274 1.33e-40

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: 146.30  E-value: 1.33e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFA---IVKKCREKSTGLEYAAKFIKKrqSRASRRGVSREEIEREvsilRQVLHH-----NVITLHDVYENRTDVV 100
Cdd:cd05613     8 LGTGAYGkvfLVRKVSGHDAGKLYAMKVLKK--ATIVQKAKTAEHTRTE----RQVLEHirqspFLVTLHYAFQTDTKLH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 101 LILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAHE-IE 179
Cdd:cd05613    82 LILDYINGGELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENI-LLDSS---GHVVLTDFGLSKEfLL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 180 DGVEFKNIF-GTPEFVAPEIVNYEPLGLE--ADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSE 256
Cdd:cd05613   158 DENERAYSFcGTIEYMAPEIVRGGDSGHDkaVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSA 237
                         250
                  ....*....|....*...
gi 2056392213 257 LAKDFIRKLLVKETRKRL 274
Cdd:cd05613   238 LAKDIIQRLLMKDPKKRL 255
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
22-286 1.33e-40

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: 145.05  E-value: 1.33e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  22 FYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRasrrgvsREEIEREVSILRQVLHHNVITLHDVYENRTDVVL 101
Cdd:cd06614     1 LYKNLEKIGEGASGEVYKATDRATGKEVAIKKMRLRKQN-------KELIINEILIMKECKHPNIVDYYDSYLVGDELWV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 102 ILELVSGGELFDFLAQKE-SLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAHEIED 180
Cdd:cd06614    74 VMEYMDGGSLTDIITQNPvRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNI-LLSKD---GSVKLADFGFAAQLTK 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 181 GVEFKN-IFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSY-DFDEEFFSqtSELA 258
Cdd:cd06614   150 EKSKRNsVVGTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPYLEEPPLRALFLITTKGIpPLKNPEKW--SPEF 227
                         250       260
                  ....*....|....*....|....*...
gi 2056392213 259 KDFIRKLLVKETRKRLTIQEALRHPWIT 286
Cdd:cd06614   228 KDFLNKCLVKDPEKRPSAEELLQHPFLK 255
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
29-298 2.07e-40

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: 146.73  E-value: 2.07e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSrasrrgVSREEIER---EVSILRQVLHHNVITLHDVYENRTDVVLILEL 105
Cdd:cd05571     3 LGKGTFGKVILCREKATGELYAIKILKKEVI------IAKDEVAHtltENRVLQNTRHPFLTSLKYSFQTNDRLCFVMEY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 106 VSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENiMLLDKNipiPHIKLIDFGLAHE-IEDGVEF 184
Cdd:cd05571    77 VNGGELFFHLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLEN-LLLDKD---GHIKITDFGLCKEeISYGATT 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 185 KNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLgDTKQETLANITAVSydfDEEFFSQTSELAKDFIRK 264
Cdd:cd05571   153 KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFY-NRDHEVLFELILME---EVRFPSTLSPEAKSLLAG 228
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2056392213 265 LLVKETRKRL-----TIQEALRHPWITPVdNQQAMVRRE 298
Cdd:cd05571   229 LLKKDPKKRLgggprDAKEIMEHPFFASI-NWDDLYQKK 266
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
29-285 4.05e-40

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: 144.38  E-value: 4.05e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKST-GLEYAAKFIKKRQsrasrRGVSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVS 107
Cdd:cd14202    10 IGHGAFAVVFKGRHKEKhDLEVAVKCINKKN-----LAKSQTLLGKEIKILKELKHENIVALYDFQEIANSVYLVMEYCN 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 108 GGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIML-----LDKNIPIPHIKLIDFGLAHEIEDGV 182
Cdd:cd14202    85 GGDLADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLsysggRKSNPNNIRIKIADFGFARYLQNNM 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 183 EFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQEtLANITAVSYDFDEEFFSQTSELAKDFI 262
Cdd:cd14202   165 MAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQD-LRLFYEKNKSLSPNIPRETSSHLRQLL 243
                         250       260
                  ....*....|....*....|...
gi 2056392213 263 RKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14202   244 LGLLQRNQKDRMDFDEFFHHPFL 266
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
22-285 4.05e-40

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: 144.02  E-value: 4.05e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  22 FYDIGEELGSGQFAIVKKCREKSTGLEYAAKFI-KKRQSRASRRGVSREeiereVSILRQVLHHNVITLHDVYENRTDVV 100
Cdd:cd14075     3 FYRIRGELGSGNFSQVKLGIHQLTKEKVAIKILdKTKLDQKTQRLLSRE-----ISSMEKLHHPNIIRLYEVVETLSKLH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 101 LILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLA-HEIE 179
Cdd:cd14075    78 LVMEYASGGELYTKISTEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNN----CVKVGDFGFStHAKR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 180 DgvEFKNIF-GTPEFVAPEIV---NYepLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDeeffSQTS 255
Cdd:cd14075   154 G--ETLNTFcGSPPYAAPELFkdeHY--IGIYVDIWALGVLLYFMVTGVMPFRAETVAKLKKCILEGTYTIP----SYVS 225
                         250       260       270
                  ....*....|....*....|....*....|
gi 2056392213 256 ELAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14075   226 EPCQELIRGILQPVPSDRYSIDEIKNSEWL 255
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
19-285 4.46e-40

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: 144.36  E-value: 4.46e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  19 VEDFYDIGEE-LGSGQFAIVKKCREKSTGLEYAAKFIkkRQSRASRRGVsreEIEREVSILRQVLHhnvitLHDVYEN-- 95
Cdd:cd14172     1 VTDDYKLSKQvLGLGVNGKVLECFHRRTGQKCALKLL--YDSPKARREV---EHHWRASGGPHIVH-----ILDVYENmh 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  96 --RTDVVLILELVSGGELFDFLAQK--ESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNiPIPHIKLID 171
Cdd:cd14172    71 hgKRCLLIIMECMEGGELFSRIQERgdQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSKE-KDAVLKLTD 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 172 FGLAHEIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLAN----ITAVSYDFD 247
Cdd:cd14172   150 FGFAKETTVQNALQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYSNTGQAISPGmkrrIRMGQYGFP 229
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2056392213 248 EEFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14172   230 NPEWAEVSEEAKQLIRHLLKTDPTERMTITQFMNHPWI 267
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
29-318 5.39e-40

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: 145.44  E-value: 5.39e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRqsrasrRGVSREEIE---REVSILRQVLHHNVIT-LHDVYENRTDVVLILE 104
Cdd:cd05570     3 LGKGSFGKVMLAERKKTDELYAIKVLKKE------VIIEDDDVEctmTEKRVLALANRHPFLTgLHACFQTEDRLYFVME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 105 LVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLlDKNipiPHIKLIDFGLAHE-IEDGVE 183
Cdd:cd05570    77 YVNGGDLMFHIQRARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLL-DAE---GHIKIADFGMCKEgIWGGNT 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 184 FKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITavsydFDE-EFFSQTSELAKDFI 262
Cdd:cd05570   153 TSTFCGTPDYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAIL-----NDEvLYPRWLSREAVSIL 227
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 263 RKLLVKETRKRL----TIQEALR-HPWITPVDNQQAMVRR---------ESVVNLENFRKQYVRRRWKLS 318
Cdd:cd05570   228 KGLLTKDPARRLgcgpKGEADIKaHPFFRNIDWDKLEKKEveppfkpkvKSPRDTSNFDPEFTSESPRLT 297
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
18-289 1.44e-39

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 144.58  E-value: 1.44e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  18 KVEDFyDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRgvsREEIEREVSILRQVLHHNVITLHDVYENRT 97
Cdd:PTZ00263   16 KLSDF-EMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQ---VQHVAQEKSILMELSHPFIVNMMCSFQDEN 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  98 DVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAHE 177
Cdd:PTZ00263   92 RVYFLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENL-LLDNK---GHVKVTDFGFAKK 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 178 IEDgvEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQtsel 257
Cdd:PTZ00263  168 VPD--RTFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWFDGR---- 241
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2056392213 258 AKDFIRKLLVKETRKRL-----TIQEALRHPWITPVD 289
Cdd:PTZ00263  242 ARDLVKGLLQTDHTKRLgtlkgGVADVKNHPYFHGAN 278
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
30-289 2.36e-39

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: 144.08  E-value: 2.36e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  30 GSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVSREEIERevSILRQVLHHNVITLHDVYENRTDVVLILELVSGG 109
Cdd:cd05584     8 GYGKVFQVRKTTGSDKGKIFAMKVLKKASIVRNQKDTAHTKAER--NILEAVKHPFIVDLHYAFQTGGKLYLILEYLSGG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 110 ELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMlLDKNipiPHIKLIDFGLAHE-IEDGVEFKNIF 188
Cdd:cd05584    86 ELFMHLEREGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENIL-LDAQ---GHVKLTDFGLCKEsIHDGTVTHTFC 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 189 GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETL-----ANITAVSYdfdeeffsQTSElAKDFIR 263
Cdd:cd05584   162 GTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIdkilkGKLNLPPY--------LTNE-ARDLLK 232
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2056392213 264 KLLVKETRKRL--TIQEAL---RHPWITPVD 289
Cdd:cd05584   233 KLLKRNVSSRLgsGPGDAEeikAHPFFRHIN 263
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
17-285 3.38e-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: 142.07  E-value: 3.38e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  17 QKVEDF-YDIGEELGSGQFAIVKKCR-EKSTGLEYAAKFIKKRQsrasrrgVSREEI--EREVSILRQVLHHNVITLHDV 92
Cdd:cd14201     1 EVVGDFeYSRKDLVGHGAFAVVFKGRhRKKTDWEVAIKSINKKN-------LSKSQIllGKEIKILKELQHENIVALYDV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  93 YENRTDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIML-----LDKNIPIPHI 167
Cdd:cd14201    74 QEMPNSVFLVMEYCNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLsyasrKKSSVSGIRI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 168 KLIDFGLAHEIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQEtLANITAVSYDFD 247
Cdd:cd14201   154 KIADFGFARYLQSNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQD-LRMFYEKNKNLQ 232
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2056392213 248 EEFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14201   233 PSIPRETSPYLADLLLGLLQRNQKDRMDFEAFFSHPFL 270
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
19-285 4.99e-39

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


Pssm-ID: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 141.13  E-value: 4.99e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  19 VEDFYDIGEELGSGQFAIVKKCREKS--TGLEYAAKFIKKrqsrasrrGVSREEIEREVSILRQVLHHNVITLHDVYENR 96
Cdd:cd14112     1 PTGRFSFGSEIFRGRFSVIVKAVDSTteTDAHCAVKIFEV--------SDEASEAVREFESLRTLQHENVQRLIAAFKPS 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  97 TDVVLILELVSGgELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipIPHIKLIDFGLAH 176
Cdd:cd14112    73 NFAYLVMEKLQE-DVFTRFSSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSVR--SWQVKLVDFGRAQ 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 177 EIEDGVEFKNIFGTpEFVAPEIVNYE-PLGLEADMWSIGVITYILLSGASPFLG--DTKQETLANITAVSYDFdEEFFSQ 253
Cdd:cd14112   150 KVSKLGKVPVDGDT-DWASPEFHNPEtPITVQSDIWGLGVLTFCLLSGFHPFTSeyDDEEETKENVIFVKCRP-NLIFVE 227
                         250       260       270
                  ....*....|....*....|....*....|..
gi 2056392213 254 TSELAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14112   228 ATQEALRFATWALKKSPTRRMRTDEALEHRWL 259
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
20-286 1.83e-38

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: 140.94  E-value: 1.83e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  20 EDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKkrQSRASRRGVsreEIEREVSilrQVLHhnVITLHDVYEN---- 95
Cdd:cd14170     1 DDYKVTSQVLGLGINGKVLQIFNKRTQEKFALKMLQ--DCPKARREV---ELHWRAS---QCPH--IVRIVDVYENlyag 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  96 RTDVVLILELVSGGELFDFLAQK--ESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNiPIPHIKLIDFG 173
Cdd:cd14170    71 RKCLLIVMECLDGGELFSRIQDRgdQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKR-PNAILKLTDFG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 174 LAHEIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGD----TKQETLANITAVSYDFDEE 249
Cdd:cd14170   150 FAKETTSHNSLTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNhglaISPGMKTRIRMGQYEFPNP 229
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2056392213 250 FFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWIT 286
Cdd:cd14170   230 EWSEVSEEVKMLIRNLLKTEPTQRMTITEFMNHPWIM 266
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
29-297 7.32e-38

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: 139.76  E-value: 7.32e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSrasrrgVSREEIEREVS---ILRQVLHHNVITLHDVYENRTDVVLILEL 105
Cdd:cd05595     3 LGKGTFGKVILVREKATGRYYAMKILRKEVI------IAKDEVAHTVTesrVLQNTRHPFLTALKYAFQTHDRLCFVMEY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 106 VSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMlLDKNipiPHIKLIDFGLAHE-IEDGVEF 184
Cdd:cd05595    77 ANGGELFFHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLM-LDKD---GHIKITDFGLCKEgITDGATM 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 185 KNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITavsydFDEEFFSQT-SELAKDFIR 263
Cdd:cd05595   153 KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELIL-----MEEIRFPRTlSPEAKSLLA 227
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2056392213 264 KLLVKETRKRL-----TIQEALRHPWITPVDNQQAMVRR 297
Cdd:cd05595   228 GLLKKDPKQRLgggpsDAKEVMEHRFFLSINWQDVVQKK 266
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
30-285 8.11e-38

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: 137.77  E-value: 8.11e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  30 GSGQFAIVKKCREKSTGLEYAAKFIKKRQSrasrrgVSREEIE---REVSILRQVLHHNVITLHDVYENRTDVVLILELV 106
Cdd:cd05578     9 GKGSFGKVCIVQKKDTKKMFAMKYMNKQKC------IEKDSVRnvlNELEILQELEHPFLVNLWYSFQDEEDMYMVVDLL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 107 SGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAHEIEDGVEFKN 186
Cdd:cd05578    83 LGGDLRYHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNI-LLDEQ---GHVHITDFNIATKLTDGTLATS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 187 IFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKqETLANITAVSYDFDEEFFSQTSELAKDFIRKLL 266
Cdd:cd05578   159 TSGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEIHSR-TSIEEIRAKFETASVLYPAGWSEEAIDLINKLL 237
                         250       260
                  ....*....|....*....|
gi 2056392213 267 VKETRKRL-TIQEALRHPWI 285
Cdd:cd05578   238 ERDPQKRLgDLSDLKNHPYF 257
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
23-282 9.36e-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: 137.75  E-value: 9.36e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKkrQSRASRRGvSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd14189     3 YCKGRLLGKGGFARCYEMTDLATNKTYAVKVIP--HSRVAKPH-QREKIVNEIELHRDLHHKHVVKFSHHFEDAENIYIF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENiMLLDKNIpipHIKLIDFGLAHEIEDGV 182
Cdd:cd14189    80 LELCSRKSLAHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGN-FFINENM---ELKVGDFGLAARLEPPE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 183 EF-KNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDeeffSQTSELAKDF 261
Cdd:cd14189   156 QRkKTICGTPNYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFETLDLKETYRCIKQVKYTLP----ASLSLPARHL 231
                         250       260
                  ....*....|....*....|.
gi 2056392213 262 IRKLLVKETRKRLTIQEALRH 282
Cdd:cd14189   232 LAGILKRNPGDRLTLDQILEH 252
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
20-289 2.64e-37

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: 138.96  E-value: 2.64e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  20 EDFyDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSrasrrgVSREEI-----EREVsilrQVLHHN--VITLHDV 92
Cdd:cd05573     1 DDF-EVIKVIGRGAFGEVWLVRDKDTGQVYAMKILRKSDM------LKREQIahvraERDI----LADADSpwIVRLHYA 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  93 YENRTDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENiMLLDKNipiPHIKLIDF 172
Cdd:cd05573    70 FQDEDHLYLVMEYMPGGDLMNLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDN-ILLDAD---GHIKLADF 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 173 GLAHEIEDG------------------------------VEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLS 222
Cdd:cd05573   146 GLCTKMNKSgdresylndsvntlfqdnvlarrrphkqrrVRAYSAVGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLY 225
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2056392213 223 GASPFLGDTKQETLANITavsyDFDEEF-FSQT---SELAKDFIRKLLvKETRKRLT-IQEALRHPWITPVD 289
Cdd:cd05573   226 GFPPFYSDSLVETYSKIM----NWKESLvFPDDpdvSPEAIDLIRRLL-CDPEDRLGsAEEIKAHPFFKGID 292
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
20-285 2.73e-37

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: 136.63  E-value: 2.73e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  20 EDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIkkrqsrasRRGVSREEIEREVSILRQVLHHNVITLHDVYENRTDV 99
Cdd:cd06612     2 EEVFDILEKLGEGSYGSVYKAIHKETGQVVAIKVV--------PVEEDLQEIIKEISILKQCDSPYIVKYYGSYFKNTDL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 100 VLILELVSGGELFDFL-AQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKnipIPHIKLIDFGLAHEI 178
Cdd:cd06612    74 WIVMEYCGAGSVSDIMkITNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNI-LLNE---EGQAKLADFGVSGQL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 179 EDGVEFKN-IFGTPEFVAPEIVNYEPLGLEADMWSIGvITYILLSGASPFLGD-----------TKQ-ETLANITAVSYD 245
Cdd:cd06612   150 TDTMAKRNtVIGTPFWMAPEVIQEIGYNNKADIWSLG-ITAIEMAEGKPPYSDihpmraifmipNKPpPTLSDPEKWSPE 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2056392213 246 FdeeffsqtselaKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd06612   229 F------------NDFVKKCLVKDPEERPSAIQLLQHPFI 256
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
19-285 3.34e-37

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: 136.53  E-value: 3.34e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  19 VEDFyDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKrqSRASRRGVsREEIEREVSILRQVLHHNVITLHDVYENRTD 98
Cdd:cd14117     5 IDDF-DIGRPLGKGKFGNVYLAREKQSKFIVALKVLFK--SQIEKEGV-EHQLRREIEIQSHLRHPNILRLYNYFHDRKR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  99 VVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEI 178
Cdd:cd14117    81 IYLILEYAPRGELYKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKG----ELKIADFGWSVHA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 179 EDgVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVsydfDEEFFSQTSELA 258
Cdd:cd14117   157 PS-LRRRTMCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKV----DLKFPPFLSDGS 231
                         250       260
                  ....*....|....*....|....*..
gi 2056392213 259 KDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14117   232 RDLISKLLRYHPSERLPLKGVMEHPWV 258
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
23-285 4.03e-37

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: 136.24  E-value: 4.03e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRAsrrgvsREEIErEVSILR------QVLHHNVITLHDVYENR 96
Cdd:cd14133     1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKIIKNNKDYL------DQSLD-EIRLLEllnkkdKADKYHIVRLKDVFYFK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  97 TDVVLILELVsGGELFDFLAQ--KESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLldKNIPIPHIKLIDFGL 174
Cdd:cd14133    74 NHLCIVFELL-SQNLYEFLKQnkFQYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILL--ASYSRCQIKIIDFGS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 175 AHEIEDGVEF--KNIFgtpeFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFS 252
Cdd:cd14133   151 SCFLTQRLYSyiQSRY----YRAPEVILGLPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIIGTIGIPPAHMLD 226
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2056392213 253 Q---TSELAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14133   227 QgkaDDELFVDFLKKLLEIDPKERPTASQALSHPWL 262
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
23-285 4.50e-37

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: 136.13  E-value: 4.50e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIkkRQSRASRRgvSREEIEREVSILRQVLHHNVITLHDVYENR--TDVV 100
Cdd:cd08217     2 YEVLETIGKGSFGTVRKVRRKSDGKILVWKEI--DYGKMSEK--EKQQLVSEVNILRELKHPNIVRYYDRIVDRanTTLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 101 LILELVSGGELFDFL----AQKESLSEEEATSFIKQILDGVNYLHT-----KKIAHFDLKPENIMLLDKNipipHIKLID 171
Cdd:cd08217    78 IVMEYCEGGDLAQLIkkckKENQYIPEEFIWKIFTQLLLALYECHNrsvggGKILHRDLKPANIFLDSDN----NVKLGD 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 172 FGLAHEIEDGVEFKNIF-GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEF 250
Cdd:cd08217   154 FGLARVLSHDSSFAKTYvGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPPFQAANQLELAKKIKEGKFPRIPSR 233
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2056392213 251 FSqtSELaKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd08217   234 YS--SEL-NEVIKSMLNVDPDKRPSVEELLQLPLI 265
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
26-285 4.67e-37

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: 135.95  E-value: 4.67e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  26 GEELGSGQFAIVKKCREKSTGLEYAAKFIK-KRQSRASRRGVsrEEIEREVSILRQVLHHNVITLHDVYENRTDVVLILE 104
Cdd:cd06625     5 GKLLGQGAFGQVYLCYDADTGRELAVKQVEiDPINTEASKEV--KALECEIQLLKNLQHERIVQYYGCLQDEKSLSIFME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 105 LVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAHEIE---DG 181
Cdd:cd06625    83 YMPGGSVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANI-LRDSN---GNVKLGDFGASKRLQticSS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 182 VEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFlgdTKQETLANI-TAVSYDFDEEFFSQTSELAKD 260
Cdd:cd06625   159 TGMKSVTGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPW---AEFEPMAAIfKIATQPTNPQLPPHVSEDARD 235
                         250       260
                  ....*....|....*....|....*
gi 2056392213 261 FIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd06625   236 FLSLIFVRNKKQRPSAEELLSHSFV 260
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
29-312 8.20e-37

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: 137.36  E-value: 8.20e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFA---IVKKCREKSTGLEYAAKFIKKRQSrasrrgVSREEIEREVSILRQVLHHN-----VITLHDVYENRTDVV 100
Cdd:cd05614     8 LGTGAYGkvfLVRKVSGHDANKLYAMKVLRKAAL------VQKAKTVEHTRTERNVLEHVrqspfLVTLHYAFQTDAKLH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 101 LILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAHEI-- 178
Cdd:cd05614    82 LILDYVSGGELFTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENI-LLDSE---GHVVLTDFGLSKEFlt 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 179 EDGVEFKNIFGTPEFVAPEIVNYEP-LGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSEL 257
Cdd:cd05614   158 EEKERTYSFCGTIEYMAPEIIRGKSgHGKAVDWWSLGILMFELLTGASPFTLEGEKNTQSEVSRRILKCDPPFPSFIGPV 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2056392213 258 AKDFIRKLLVKETRKRL-----TIQEALRHPWITPVDNQQAMVRR---------ESVVNLENFRKQYVR 312
Cdd:cd05614   238 ARDLLQKLLCKDPKKRLgagpqGAQEIKEHPFFKGLDWEALALRKvnppfrpsiRSELDVGNFAEEFTN 306
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
23-285 2.17e-36

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: 134.17  E-value: 2.17e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRqsRASRRGVSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd14070     4 YLIGRKLGEGSFAKVREGLHAVTGEKVAIKVIDKK--KAKKDSYVTKNLRREGRIQQMIRHPNITQLLDILETENSYYLV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENiMLLDKNIpipHIKLIDFGLAH--EIED 180
Cdd:cd14070    82 MELCPGGNLMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIEN-LLLDEND---NIKLIDFGLSNcaGILG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 181 GVE-FKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTkqetlANITAVSYDF-DEEFF---SQTS 255
Cdd:cd14070   158 YSDpFSTQCGSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPFTVEP-----FSLRALHQKMvDKEMNplpTDLS 232
                         250       260       270
                  ....*....|....*....|....*....|
gi 2056392213 256 ELAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14070   233 PGAISFLRSLLEPDPLKRPNIKQALANRWL 262
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
20-294 2.37e-36

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: 134.77  E-value: 2.37e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  20 EDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRqsrasrrgvSREEIER---EVSILRQVLHHNVITLHDVYENR 96
Cdd:cd06643     4 EDFWEIVGELGDGAFGKVYKAQNKETGILAAAKVIDTK---------SEEELEDymvEIDILASCDHPNIVKLLDAFYYE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  97 TDVVLILELVSGGELFDFLAQKE-SLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIML-LDKNipiphIKLIDFGL 174
Cdd:cd06643    75 NNLWILIEFCAGGAVDAVMLELErPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFtLDGD-----IKLADFGV 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 175 AHEIEDGVEFKNIF-GTPEFVAPEIVNYE-----PLGLEADMWSIGViTYILLSGASP----------FLGDTKQE--TL 236
Cdd:cd06643   150 SAKNTRTLQRRDSFiGTPYWMAPEVVMCEtskdrPYDYKADVWSLGV-TLIEMAQIEPphhelnpmrvLLKIAKSEppTL 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2056392213 237 ANITAVSYDFdeeffsqtselaKDFIRKLLVKETRKRLTIQEALRHPWITPVDNQQAM 294
Cdd:cd06643   229 AQPSRWSPEF------------KDFLRKCLEKNVDARWTTSQLLQHPFVSVLVSNKPL 274
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
23-286 2.63e-36

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: 134.29  E-value: 2.63e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRgvsREEIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd14187     9 YVRGRFLGKGGFAKCYEITDADTKEVFAGKIVPKSLLLKPHQ---KEKMSMEIAIHRSLAHQHVVGFHGFFEDNDFVYVV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIE-DG 181
Cdd:cd14187    86 LELCRRRSLLELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDM----EVKIGDFGLATKVEyDG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 182 VEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEeffsQTSELAKDF 261
Cdd:cd14187   162 ERKKTLCGTPNYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPK----HINPVAASL 237
                         250       260
                  ....*....|....*....|....*
gi 2056392213 262 IRKLLVKETRKRLTIQEALRHPWIT 286
Cdd:cd14187   238 IQKMLQTDPTARPTINELLNDEFFT 262
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
21-289 3.05e-36

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: 134.45  E-value: 3.05e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  21 DFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSrasrrgVSREEIER---EVSILRQVLHHNVITLHDVYENRT 97
Cdd:cd14209     1 DDFDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKV------VKLKQVEHtlnEKRILQAINFPFLVKLEYSFKDNS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  98 DVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAHE 177
Cdd:cd14209    75 NLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENL-LIDQQ---GYIKVTDFGFAKR 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 178 IEDgvEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFfsqTSEL 257
Cdd:cd14209   151 VKG--RTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHF---SSDL 225
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2056392213 258 aKDFIRKLLVKETRKRL-----TIQEALRHPWITPVD 289
Cdd:cd14209   226 -KDLLRNLLQVDLTKRFgnlknGVNDIKNHKWFATTD 261
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
23-284 3.12e-36

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: 133.52  E-value: 3.12e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQ--SRASRRGVSReeIEREVSILRQV--LHH-NVITLHDVYENRT 97
Cdd:cd14005     2 YEVGDLLGKGGFGTVYSGVRIRDGLPVAVKFVPKSRvtEWAMINGPVP--VPLEIALLLKAskPGVpGVIRLLDWYERPD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  98 DVVLILELVSGGE-LFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLldkNIPIPHIKLIDFGLAH 176
Cdd:cd14005    80 GFLLIMERPEPCQdLFDFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLI---NLRTGEVKLIDFGCGA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 177 EIEDGVeFKNIFGTPEFVAPE-IVNYEPLGLEADMWSIGVITYILLSGASPFLGDtKQETLANItavsydfdeeFFSQT- 254
Cdd:cd14005   157 LLKDSV-YTDFDGTRVYSPPEwIRHGRYHGRPATVWSLGILLYDMLCGDIPFEND-EQILRGNV----------LFRPRl 224
                         250       260       270
                  ....*....|....*....|....*....|
gi 2056392213 255 SELAKDFIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd14005   225 SKECCDLISRCLQFDPSKRPSLEQILSHPW 254
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
20-294 3.17e-36

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: 134.49  E-value: 3.17e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  20 EDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRqsrasrrgvSREEIER---EVSILRQVLHHNVITLHDVYENR 96
Cdd:cd06611     4 NDIWEIIGELGDGAFGKVYKAQHKETGLFAAAKIIQIE---------SEEELEDfmvEIDILSECKHPNIVGLYEAYFYE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  97 TDVVLILELVSGGELFDFLAQKES-LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIML-LDKNipiphIKLIDFGL 174
Cdd:cd06611    75 NKLWILIEFCDGGALDSIMLELERgLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLtLDGD-----VKLADFGV 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 175 AHEIEDGVEFKNIF-GTPEFVAPEIVNYE-----PLGLEADMWSIGvITYILLSGASPFLGDT----------KQE--TL 236
Cdd:cd06611   150 SAKNKSTLQKRDTFiGTPYWMAPEVVACEtfkdnPYDYKADIWSLG-ITLIELAQMEPPHHELnpmrvllkilKSEppTL 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2056392213 237 ANITAVSYDFdeeffsqtselaKDFIRKLLVKETRKRLTIQEALRHPWITPVDNQQAM 294
Cdd:cd06611   229 DQPSKWSSSF------------NDFLKSCLVKDPDDRPTAAELLKHPFVSDQSDNKAI 274
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
2-309 3.33e-36

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: 134.73  E-value: 3.33e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213   2 FQASMRSPNMEPFKQQKVEDFYDIGEelgsGQFAIVKKCREKSTGLEYAAKFIKKRQSRasrrgvSREEIEREVSILRQV 81
Cdd:cd06659     6 FKAALRMVVDQGDPRQLLENYVKIGE----GSTGVVCIAREKHSGRQVAVKMMDLRKQQ------RRELLFNEVVIMRDY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  82 LHHNVITLHDVYENRTDVVLILELVSGGELFDFLAQKEsLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIML-LDK 160
Cdd:cd06659    76 QHPNVVEMYKSYLVGEELWVLMEYLQGGALTDIVSQTR-LNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLtLDG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 161 nipipHIKLIDFGLAHEIEDGV-EFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKqetlanI 239
Cdd:cd06659   155 -----RVKLSDFGFCAQISKDVpKRKSLVGTPYWMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSP------V 223
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2056392213 240 TAVSYDFDE-----EFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWITpvdnqQAMVRRESVVNLENFRKQ 309
Cdd:cd06659   224 QAMKRLRDSpppklKNSHKASPVLRDFLERMLVRDPQERATAQELLDHPFLL-----QTGLPECLVPLIQQYRKR 293
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
29-289 3.46e-36

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: 135.22  E-value: 3.46e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFA---IVKKCREKSTGLEYAAKFIKKRQSRASRRgvSREEIEREvsILRQVLHHNVITLHDVYENRTDVVLILEL 105
Cdd:cd05582     3 LGQGSFGkvfLVRKITGPDAGTLYAMKVLKKATLKVRDR--VRTKMERD--ILADVNHPFIVKLHYAFQTEGKLYLILDF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 106 VSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAHE-IEDGVEF 184
Cdd:cd05582    79 LRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENI-LLDED---GHIKLTDFGLSKEsIDHEKKA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 185 KNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFdEEFFSQTselAKDFIRK 264
Cdd:cd05582   155 YSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAKLGM-PQFLSPE---AQSLLRA 230
                         250       260       270
                  ....*....|....*....|....*....|
gi 2056392213 265 LLVKETRKRL-----TIQEALRHPWITPVD 289
Cdd:cd05582   231 LFKRNPANRLgagpdGVEEIKRHPFFATID 260
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
15-291 4.21e-36

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: 135.98  E-value: 4.21e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  15 KQQKVEDFyDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSrasrrgVSREEIER---EVSILRQVLHHNVITLHD 91
Cdd:cd05593    10 KRKTMNDF-DYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVI------IAKDEVAHtltESRVLKNTRHPFLTSLKY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  92 VYENRTDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMlLDKNipiPHIKLID 171
Cdd:cd05593    83 SFQTKDRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLM-LDKD---GHIKITD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 172 FGLAHE-IEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLgDTKQETLANITAVSydfDEEF 250
Cdd:cd05593   159 FGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFY-NQDHEKLFELILME---DIKF 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2056392213 251 FSQTSELAKDFIRKLLVKETRKRL-----TIQEALRHPWITPVDNQ 291
Cdd:cd05593   235 PRTLSADAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFFTGVNWQ 280
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
20-289 4.83e-36

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: 135.13  E-value: 4.83e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  20 EDFyDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVSREEiEREvsILRQVLHHNVITLHDVYENRTDV 99
Cdd:cd05601     1 KDF-EVKNVIGRGHFGEVQVVKEKATGDIYAMKVLKKSETLAQEEVSFFEE-ERD--IMAKANSPWITKLQYAFQDSENL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 100 VLILELVSGGELFDFLAQKES-LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAHEI 178
Cdd:cd05601    77 YLVMEYHPGGDLLSLLSRYDDiFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENI-LIDRT---GHIKLADFGSAAKL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 179 EDG--VEFKNIFGTPEFVAPEI---VNYEP---LGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAV--SYDFDE 248
Cdd:cd05601   153 SSDktVTSKMPVGTPDYIAPEVltsMNGGSkgtYGVECDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNIMNFkkFLKFPE 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2056392213 249 EFfsQTSELAKDFIRKLLVkETRKRLTIQEALRHPWITPVD 289
Cdd:cd05601   233 DP--KVSESAVDLIKGLLT-DAKERLGYEGLCCHPFFSGID 270
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
23-282 6.89e-36

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: 132.83  E-value: 6.89e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKkrQSRASRRGvSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd14188     3 YCRGKVLGKGGFAKCYEMTDLTTNKVYAAKIIP--HSRVSKPH-QREKIDKEIELHRILHHKHVVQFYHYFEDKENIYIL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENiMLLDKNIpipHIKLIDFGLAHEIED-G 181
Cdd:cd14188    80 LEYCSRRSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGN-FFINENM---ELKVGDFGLAARLEPlE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 182 VEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQtselAKDF 261
Cdd:cd14188   156 HRRRTICGTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYSLPSSLLAP----AKHL 231
                         250       260
                  ....*....|....*....|.
gi 2056392213 262 IRKLLVKETRKRLTIQEALRH 282
Cdd:cd14188   232 IASMLSKNPEDRPSLDEIIRH 252
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
29-227 9.06e-36

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: 131.89  E-value: 9.06e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTglEYAAKFIKKRQSRASRRgvsrEEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSG 108
Cdd:cd13999     1 IGSGSFGEVYKGKWRGT--DVAIKKLKVEDDNDELL----KEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 109 GELFDFL-AQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAHEIEDGVEFKNI 187
Cdd:cd13999    75 GSLYDLLhKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNI-LLDEN---FTVKIADFGLSRIKNSTTEKMTG 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2056392213 188 F-GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPF 227
Cdd:cd13999   151 VvGTPRWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPF 191
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
18-285 9.91e-36

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: 132.57  E-value: 9.91e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  18 KVEDFYDIGEelgsGQFAIVKKCREKSTGLEYAakfIKKRQSRASRRgvsREEIEREVSILRQVLHHNVITLHDVYENRT 97
Cdd:cd06648     8 DLDNFVKIGE----GSTGIVCIATDKSTGRQVA---VKKMDLRKQQR---RELLFNEVVIMRDYQHPNIVEMYSSYLVGD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  98 DVVLILELVSGGELFDFLAQKEsLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHE 177
Cdd:cd06648    78 ELWVVMEFLEGGALTDIVTHTR-MNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDG----RVKLSDFGFCAQ 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 178 IEDGV-EFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSE 256
Cdd:cd06648   153 VSKEVpRRKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIRDNEPPKLKNLHKVSPR 232
                         250       260
                  ....*....|....*....|....*....
gi 2056392213 257 LaKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd06648   233 L-RSFLDRMLVRDPAQRATAAELLNHPFL 260
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
23-285 1.29e-35

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: 132.21  E-value: 1.29e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRqsRASRRGVSREeIEREVSILRQVLHHNVITLHDVYENRTD-VVL 101
Cdd:cd14165     3 YILGINLGEGSYAKVKSAYSERLKCNVAIKIIDKK--KAPDDFVEKF-LPRELEILARLNHKSIIKTYEIFETSDGkVYI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 102 ILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNIpipHIKLIDFGLAHEIE-D 180
Cdd:cd14165    80 VMELGVQGDLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENL-LLDKDF---NIKLTDFGFSKRCLrD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 181 G----VEFKNIFGTPEFVAPEIVN---YEPlgLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEfFSQ 253
Cdd:cd14165   156 EngriVLSKTFCGSAAYAAPEVLQgipYDP--RIYDIWSLGVILYIMVCGSMPYDDSNVKKMLKIQKEHRVRFPRS-KNL 232
                         250       260       270
                  ....*....|....*....|....*....|..
gi 2056392213 254 TSELaKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14165   233 TSEC-KDLIYRLLQPDVSQRLCIDEVLSHPWL 263
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
14-283 1.42e-35

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: 132.84  E-value: 1.42e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  14 FKQQKVedfydigeeLGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRaSRRGVSREEIEREvsILRQVLHHNVITLHDVY 93
Cdd:cd05630     2 FRQYRV---------LGKGGFGEVCACQVRATGKMYACKKLEKKRIK-KRKGEAMALNEKQ--ILEKVNSRFVVSLAYAY 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  94 ENRTDVVLILELVSGGEL-FDFLAQKES-LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLID 171
Cdd:cd05630    70 ETKDALCLVLTLMNGGDLkFHIYHMGQAgFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHG----HIRISD 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 172 FGLAHEIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFF 251
Cdd:cd05630   146 LGLAVHVPEGQTIKGRVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKREEVERLVKEVPEEYS 225
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2056392213 252 SQTSELAKDFIRKLLVKETRKRLTIQ-----EALRHP 283
Cdd:cd05630   226 EKFSPQARSLCSMLLCKDPAERLGCRgggarEVKEHP 262
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
23-286 1.55e-35

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: 132.78  E-value: 1.55e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKK----RQSRASRRGVSR----------------EEIEREVSILRQVL 82
Cdd:cd14199     4 YKLKDEIGKGSYGVVKLAYNEDDNTYYAMKVLSKkklmRQAGFPRRPPPRgaraapegctqprgpiERVYQEIAILKKLD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  83 HHNVITLHDVYENRTD--VVLILELVSGGELFDFLAQKeSLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDK 160
Cdd:cd14199    84 HPNVVKLVEVLDDPSEdhLYMVFELVKQGPVMEVPTLK-PLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLVGED 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 161 NipipHIKLIDFGLAHEIEDGVEF-KNIFGTPEFVAPEIVN--YEPLGLEA-DMWSIGVITYILLSGASPFLGDTKQETL 236
Cdd:cd14199   163 G----HIKIADFGVSNEFEGSDALlTNTVGTPAFMAPETLSetRKIFSGKAlDVWAMGVTLYCFVFGQCPFMDERILSLH 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2056392213 237 ANITAVSYDFDEEffSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWIT 286
Cdd:cd14199   239 SKIKTQPLEFPDQ--PDISDDLKDLLFRMLDKNPESRISVPEIKLHPWVT 286
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
23-286 2.83e-35

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: 132.31  E-value: 2.83e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVSREEIeREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd07841     2 YEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLGERKEAKDGINFTAL-REIKLLQELKHPNIIGLLDVFGHKSNINLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGgELFDFLAQKE-SLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAheiedg 181
Cdd:cd07841    81 FEFMET-DLEKVIKDKSiVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGV----LKLADFGLA------ 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 182 vefkNIFGTP-EFVAPEIVN--YEPL---------GLEADMWSIGVITYILLSGAsPFL-GDTKQETLANITAV------ 242
Cdd:cd07841   150 ----RSFGSPnRKMTHQVVTrwYRAPellfgarhyGVGVDMWSVGCIFAELLLRV-PFLpGDSDIDQLGKIFEAlgtpte 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2056392213 243 ----------SY-DFDE-------EFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWIT 286
Cdd:cd07841   225 enwpgvtslpDYvEFKPfpptplkQIFPAASDDALDLLQRLLTLNPNKRITARQALEHPYFS 286
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
23-280 5.63e-35

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: 130.55  E-value: 5.63e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKR--QSRASRRGVSREEIeREVSILRQVLHH-NVITLHDVYENRTDV 99
Cdd:cd13993     2 YQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLYKSgpNSKDGNDFQKLPQL-REIDLHRRVSRHpNIITLHDVFETEVAI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 100 VLILELVSGGELFDFLAQKES--LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpipHIKLIDFGLAHE 177
Cdd:cd13993    81 YIVLEYCPNGDLFEAITENRIyvGKTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDEG---TVKLCDFGLATT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 178 IEDGVEFKniFGTPEFVAPE-IVNYEPLG-----LEADMWSIGVITYILLSGASPFLGDTKQEtlaNITAVSYDFDEEFF 251
Cdd:cd13993   158 EKISMDFG--VGSEFYMAPEcFDEVGRSLkgypcAAGDIWSLGIILLNLTFGRNPWKIASESD---PIFYDYYLNSPNLF 232
                         250       260       270
                  ....*....|....*....|....*....|..
gi 2056392213 252 SQTSELAKDF---IRKLLVKETRKRLTIQEAL 280
Cdd:cd13993   233 DVILPMSDDFynlLRQIFTVNPNNRILLPELQ 264
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
23-286 5.68e-35

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: 131.22  E-value: 5.68e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKK---------------RQSRASRRGVSR-----EEIEREVSILRQVL 82
Cdd:cd14200     2 YKLQSEIGKGSYGVVKLAYNESDDKYYAMKVLSKkkllkqygfprrpppRGSKAAQGEQAKplaplERVYQEIAILKKLD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  83 HHNVITLHDVYEN--RTDVVLILELVSGGELFDFLAQKeSLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDK 160
Cdd:cd14200    82 HVNIVKLIEVLDDpaEDNLYMVFDLLRKGPVMEVPSDK-PFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGDD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 161 NipipHIKLIDFGLAHEIE-DGVEFKNIFGTPEFVAPEIVNYEPLGLEA---DMWSIGVITYILLSGASPFLGDTKQETL 236
Cdd:cd14200   161 G----HVKIADFGVSNQFEgNDALLSSTAGTPAFMAPETLSDSGQSFSGkalDVWAMGVTLYCFVYGKCPFIDEFILALH 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2056392213 237 ANITAVSYDFDEEffSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWIT 286
Cdd:cd14200   237 NKIKNKPVEFPEE--PEISEELKDLILKMLDKNPETRITVPEIKVHPWVT 284
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
14-285 6.52e-35

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: 131.63  E-value: 6.52e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  14 FKQQKVedfydigeeLGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRaSRRGVSREEIEREvsILRQVLHHNVITLHDVY 93
Cdd:cd05632     4 FRQYRV---------LGKGGFGEVCACQVRATGKMYACKRLEKKRIK-KRKGESMALNEKQ--ILEKVNSQFVVNLAYAY 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  94 ENRTDVVLILELVSGGEL--FDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLID 171
Cdd:cd05632    72 ETKDALCLVLTIMNGGDLkfHIYNMGNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYG----HIRISD 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 172 FGLAHEIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFF 251
Cdd:cd05632   148 LGLAVKIPEGESIRGRVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEKVKREEVDRRVLETEEVYS 227
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2056392213 252 SQTSELAKDFIRKLLVKETRKRLTIQ-----EALRHPWI 285
Cdd:cd05632   228 AKFSEEAKSICKMLLTKDPKQRLGCQeegagEVKRHPFF 266
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
29-284 8.70e-35

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: 130.55  E-value: 8.70e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFI-KKRQSRasRRGVSREEIEREvsILRQVLHHNVITLHDVYENRTDVVLILELVS 107
Cdd:cd05605     8 LGKGGFGEVCACQVRATGKMYACKKLeKKRIKK--RKGEAMALNEKQ--ILEKVNSRFVVSLAYAYETKDALCLVLTIMN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 108 GGEL-FDFLAQKES-LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIEDGVEFK 185
Cdd:cd05605    84 GGDLkFHIYNMGNPgFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHG----HVRISDLGLAVEIPEGETIR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 186 NIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSELAKDFIRKL 265
Cdd:cd05605   160 GRVGTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFRARKEKVKREEVDRRVKEDQEEYSEKFSEEAKSICSQL 239
                         250       260
                  ....*....|....*....|....
gi 2056392213 266 LVKETRKRLTIQEA-----LRHPW 284
Cdd:cd05605   240 LQKDPKTRLGCRGEgaedvKSHPF 263
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
26-285 8.72e-35

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: 130.12  E-value: 8.72e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  26 GEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASrrgvSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILEL 105
Cdd:cd06626     5 GNKIGEGTFGKVYTAVNLDTGELMAMKEIRFQDNDPK----TIKEIADEMKVLEGLDHPNLVRYYGVEVHREEVYIFMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 106 VSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIEDGV--- 182
Cdd:cd06626    81 CQEGTLEELLRHGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGL----IKLGDFGSAVKLKNNTttm 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 183 ---EFKNIFGTPEFVAPEIVNYEPL---GLEADMWSIGVITYILLSGASPFlgdtkqetlanitavsYDFDEEF---F-- 251
Cdd:cd06626   157 apgEVNSLVGTPAYMAPEVITGNKGeghGRAADIWSLGCVVLEMATGKRPW----------------SELDNEWaimYhv 220
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2056392213 252 -----------SQTSELAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd06626   221 gmghkppipdsLQLSPEGKDFLSRCLESDPKKRPTASELLDHPFI 265
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
26-285 8.75e-35

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: 129.86  E-value: 8.75e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  26 GEELGSGQFAIVKkCREKSTGLEYAAKFIKKRQSRASRRGVSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILEL 105
Cdd:cd06631     6 GNVLGKGAYGTVY-CGLTSTGQLIAVKQVELDTSDKEKAEKEYEKLQEEVDLLKTLKHVNIVGYLGTCLEDNVVSIFMEF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 106 VSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEI------- 178
Cdd:cd06631    85 VPGGSIASILARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGV----IKLIDFGCAKRLcinlssg 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 179 EDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFlgdTKQETLANITAVSYDFDE-----EFFSQ 253
Cdd:cd06631   161 SQSQLLKSMRGTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGKPPW---ADMNPMAAIFAIGSGRKPvprlpDKFSP 237
                         250       260       270
                  ....*....|....*....|....*....|..
gi 2056392213 254 TselAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd06631   238 E---ARDFVHACLTRDQDERPSAEQLLKHPFI 266
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
29-308 1.38e-34

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: 130.11  E-value: 1.38e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRaSRRGVSREEIEREvsILRQVLHHNVITLHDVYENRTDVVLILELVSG 108
Cdd:cd05631     8 LGKGGFGEVCACQVRATGKMYACKKLEKKRIK-KRKGEAMALNEKR--ILEKVNSRFVVSLAYAYETKDALCLVLTIMNG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 109 GEL-FDFLAQKES-LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIEDGVEFKN 186
Cdd:cd05631    85 GDLkFHIYNMGNPgFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRG----HIRISDLGLAVQIPEGETVRG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 187 IFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSELAKDFIRKLL 266
Cdd:cd05631   161 RVGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRKERVKREEVDRRVKEDQEEYSEKFSEDAKSICRMLL 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2056392213 267 VKETRKRLTIQEalrhpwitpvdNQQAMVRRESVVNLENFRK 308
Cdd:cd05631   241 TKNPKERLGCRG-----------NGAAGVKQHPIFKNINFKR 271
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
20-281 1.39e-34

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: 129.72  E-value: 1.39e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  20 EDFYDIgEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRasrrgVSREEIEREVSILRQVLHHNVITLHDVYENRTDV 99
Cdd:cd13996     6 NDFEEI-ELLGSGGFGSVYKVRNKVDGVTYAIKKIRLTEKS-----SASEKVLREVKALAKLNHPNIVRYYTAWVEEPPL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 100 VLILELVSGGELFDFLAQ---KESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLldkNIPIPHIKLIDFGLAH 176
Cdd:cd13996    80 YIQMELCEGGTLRDWIDRrnsSSKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFL---DNDDLQVKIGDFGLAT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 177 EIEDGVEFKNIF---------------GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLsgaSPFlgDTKQETLANITA 241
Cdd:cd13996   157 SIGNQKRELNNLnnnnngntsnnsvgiGTPLYASPEQLDGENYNEKADIYSLGIILFEML---HPF--KTAMERSTILTD 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2056392213 242 V-SYDFDEEFFSQTSELAkDFIRKLLVKETRKRLTIQEALR 281
Cdd:cd13996   232 LrNGILPESFKAKHPKEA-DLIQSLLSKNPEERPSAEQLLR 271
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
23-283 4.44e-34

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: 127.91  E-value: 4.44e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKkrQSRASRRgvSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd08529     2 FEILNKLGKGSFGVVYKVVRKVDGRVYALKQID--ISRMSRK--MREEAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLA--QKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAHEIED 180
Cdd:cd08529    78 MEYAENGDLHSLIKsqRGRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNI-FLDKG---DNVKIGDLGVAKILSD 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 181 GVEF-KNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYdfdEEFFSQTSELAK 259
Cdd:cd08529   154 TTNFaQTIVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIVRGKY---PPISASYSQDLS 230
                         250       260
                  ....*....|....*....|....
gi 2056392213 260 DFIRKLLVKETRKRLTIQEALRHP 283
Cdd:cd08529   231 QLIDSCLTKDYRQRPDTTELLRNP 254
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
23-286 1.72e-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: 127.06  E-value: 1.72e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAakfIKKRQSRASRRGVSREEIeREVSILRQV-LHHNVITLHDVYENRTDVVL 101
Cdd:cd07832     2 YKILGRIGEGAHGIVFKAKDRETGETVA---LKKVALRKLEGGIPNQAL-REIKALQACqGHPYVVKLRDVFPHGTGFVL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 102 ILELVsGGELFDFLAQKE-SLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEI-- 178
Cdd:cd07832    78 VFEYM-LSSLSEVLRDEErPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTG----VLKIADFGLARLFse 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 179 EDGVEFKNIFGTPEFVAPEIV----NYEPLgleADMWSIGVITYILLSGASPFLGDTKQETLANITAV--SYDFD----- 247
Cdd:cd07832   153 EDPRLYSHQVATRWYRAPELLygsrKYDEG---VDLWAVGCIFAELLNGSPLFPGENDIEQLAIVLRTlgTPNEKtwpel 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2056392213 248 -------------------EEFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWIT 286
Cdd:cd07832   230 tslpdynkitfpeskgirlEEIFPDCSPEAIDLLKGLLVYNPKKRLSAEEALRHPYFF 287
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
29-297 2.57e-33

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: 127.43  E-value: 2.57e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRaSRRGVSREEIEREVsILRQVLHHNVITLHDVYENRTDVVLILELVSG 108
Cdd:cd05575     3 IGKGSFGKVLLARHKAEGKLYAVKVLQKKAIL-KRNEVKHIMAERNV-LLKNVKHPFLVGLHYSFQTKDKLYFVLDYVNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 109 GELFdFLAQKE-SLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAHEIEDGVEFKNI 187
Cdd:cd05575    81 GELF-FHLQRErHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENI-LLDSQ---GHVVLTDFGLCKEGIEPSDTTST 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 188 F-GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEeffsQTSELAKDFIRKLL 266
Cdd:cd05575   156 FcGTPEYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRDTAEMYDNILHKPLRLRT----NVSPSARDLLEGLL 231
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2056392213 267 VKETRKRL----TIQEALRHPWITPVDNQQAMVRR 297
Cdd:cd05575   232 QKDRTKRLgsgnDFLEIKNHSFFRPINWDDLEAKK 266
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
29-274 3.01e-33

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: 126.53  E-value: 3.01e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRaSRRGVSREEIEREvsILRQVLHHNVITLHDVYENRTDVVLILELVSG 108
Cdd:cd05608     9 LGKGGFGEVSACQMRATGKLYACKKLNKKRLK-KRKGYEGAMVEKR--ILAKVHSRFIVSLAYAFQTKTDLCLVMTIMNG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 109 GEL----FDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIEDGVE- 183
Cdd:cd05608    86 GDLryhiYNVDEENPGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDG----NVRISDLGLAVELKDGQTk 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 184 FKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLG--------DTKQETLANitAVSYdfDEEFfsqtS 255
Cdd:cd05608   162 TKGYAGTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFRArgekvenkELKQRILND--SVTY--SEKF----S 233
                         250
                  ....*....|....*....
gi 2056392213 256 ELAKDFIRKLLVKETRKRL 274
Cdd:cd05608   234 PASKSICEALLAKDPEKRL 252
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
32-289 5.09e-33

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: 125.60  E-value: 5.09e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  32 GQFAIVKKCREKSTGLEYAAKFIKKrQSRASRRGVSREEIEREvsILRQVLHHNVITLHDVYENRTDVVLILELVSGGEL 111
Cdd:cd05609    11 GAYGAVYLVRHRETRQRFAMKKINK-QNLILRNQIQQVFVERD--ILTFAENPFVVSMYCSFETKRHLCMVMEYVEGGDC 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 112 FDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLldknIPIPHIKLIDFGLA--------------HE 177
Cdd:cd05609    88 ATLLKNIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLI----TSMGHIKLTDFGLSkiglmslttnlyegHI 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 178 IEDGVEF--KNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTS 255
Cdd:cd05609   164 EKDTREFldKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEIEWPEGDDALPD 243
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2056392213 256 ElAKDFIRKLLVKETRKRL---TIQEALRHPWITPVD 289
Cdd:cd05609   244 D-AQDLITRLLQQNPLERLgtgGAEEVKQHPFFQDLD 279
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
29-292 6.08e-33

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: 125.33  E-value: 6.08e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRaSRRGVSREEIEREvsILRQVLHHNVITLHDVYENRTDVVLILELVSG 108
Cdd:cd05577     1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIK-KKKGETMALNEKI--ILEKVSSPFIVSLAYAFETKDKLCLVLTLMNG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 109 GELFDFLAQ--KESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIEDGVEFKN 186
Cdd:cd05577    78 GDLKYHIYNvgTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHG----HVRISDLGLAVEFKGGKKIKG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 187 IFGTPEFVAPEIV-NYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSELAKDFIRKL 265
Cdd:cd05577   154 RVGTHGYMAPEVLqKEVAYDFSVDWFALGCMLYEMIAGRSPFRQRKEKVDKEELKRRTLEMAVEYPDSFSPEARSLCEGL 233
                         250       260       270
                  ....*....|....*....|....*....|..
gi 2056392213 266 LVKETRKRL-----TIQEALRHPWITPVDNQQ 292
Cdd:cd05577   234 LQKDPERRLgcrggSADEVKEHPFFRSLNWQR 265
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
26-285 6.45e-33

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: 124.82  E-value: 6.45e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  26 GEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVSrEEIEREVSILRQVLHHNVITLHDVYENRTDVVLILEL 105
Cdd:cd06632     5 GQLLGSGSFGSVYEGFNGDTGDFFAVKEVSLVDDDKKSRESV-KQLEQEIALLSKLRHPNIVQYYGTEREEDNLYIFLEY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 106 VSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAHEIEDGVEFK 185
Cdd:cd06632    84 VPGGSIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANI-LVDTN---GVVKLADFGMAKHVEAFSFAK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 186 NIFGTPEFVAPEIVN--YEPLGLEADMWSIGVITYILLSGASPFlgdTKQETLANITAVSYDFDEEFFSQT-SELAKDFI 262
Cdd:cd06632   160 SFKGSPYWMAPEVIMqkNSGYGLAVDIWSLGCTVLEMATGKPPW---SQYEGVAAIFKIGNSGELPPIPDHlSPDAKDFI 236
                         250       260
                  ....*....|....*....|...
gi 2056392213 263 RKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd06632   237 RLCLQRDPEDRPTASQLLEHPFV 259
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
23-285 2.00e-32

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: 123.56  E-value: 2.00e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRqsrasrrGVSREEIE----REVSILRQVLHHNVITLHDVYENrTD 98
Cdd:cd14163     2 YQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIIDKS-------GGPEEFIQrflpRELQIVERLDHKNIIHVYEMLES-AD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  99 --VVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipiphIKLIDFGLAH 176
Cdd:cd14163    74 gkIYLVMELAEDGDVFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQGFT-----LKLTDFGFAK 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 177 EI-EDGVEFKNIF-GTPEFVAPEIVNYEPL-GLEADMWSIGVITYILLSGASPFlGDTKQETLANITAVSYDFDEEFfsQ 253
Cdd:cd14163   149 QLpKGGRELSQTFcGSTAYAAPEVLQGVPHdSRKGDIWSMGVVLYVMLCAQLPF-DDTDIPKMLCQQQKGVSLPGHL--G 225
                         250       260       270
                  ....*....|....*....|....*....|..
gi 2056392213 254 TSELAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14163   226 VSRTCQDLLKRLLEPDMVLRPSIEEVSWHPWL 257
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
23-284 2.08e-32

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: 124.35  E-value: 2.08e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRAsrrgVSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd07833     3 YEVLGVVGEGAYGVVLKCRNKATGEIVAIKKFKESEDDE----DVKKTALREVKVLRQLRHENIVNLKEAFRRKGRLYLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNIPiphIKLIDFGLAHEIEDG- 181
Cdd:cd07833    79 FEYVERTLLELLEASPGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENI-LVSESGV---LKLCDFGFARALTARp 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 182 -VEFKNIFGTPEFVAPEI-VNYEPLGLEADMWSIGVITYILLSGASPFLGDTK-------QETLANIT-AVSYDFD---- 247
Cdd:cd07833   155 aSPLTDYVATRWYRAPELlVGDTNYGKPVDVWAIGCIMAELLDGEPLFPGDSDidqlyliQKCLGPLPpSHQELFSsnpr 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2056392213 248 ---EEFFSQ-------------TSELAKDFIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd07833   235 fagVAFPEPsqpeslerrypgkVSSPALDFLKACLRMDPKERLTCDELLQHPY 287
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
29-284 2.19e-32

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: 123.97  E-value: 2.19e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIK-KRQSRASRRGVSREEIEREVSILRQVLHHNVITLHDVYENRTD-VVLILELV 106
Cdd:cd13990     8 LGKGGFSEVYKAFDLVEQRYVACKIHQlNKDWSEEKKQNYIKHALREYEIHKSLDHPRIVKLYDVFEIDTDsFCTVLEYC 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 107 SGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKK--IAHFDLKPENImLLDKNIPIPHIKLIDFGLAHEIED---- 180
Cdd:cd13990    88 DGNDLDFYLKQHKSIPEREARSIIMQVVSALKYLNEIKppIIHYDLKPGNI-LLHSGNVSGEIKITDFGLSKIMDDesyn 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 181 --GVEFKNIF-GTPEFVAPEI--VNYEP--LGLEADMWSIGVITYILLSGASPFLGDTKQETLAN----ITAVSYDFDEE 249
Cdd:cd13990   167 sdGMELTSQGaGTYWYLPPECfvVGKTPpkISSKVDVWSVGVIFYQMLYGRKPFGHNQSQEAILEentiLKATEVEFPSK 246
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2056392213 250 ffSQTSELAKDFIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd13990   247 --PVVSSEAKDFIRRCLTYRKEDRPDVLQLANDPY 279
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
21-285 2.40e-32

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: 123.57  E-value: 2.40e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  21 DFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRasrrgvsREEIEREVSILRQVLHH-NVITLHDVYENRTDV 99
Cdd:cd06608     6 GIFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMDIIEDE-------EEEIKLEINILRKFSNHpNIATFYGAFIKKDPP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 100 V------LILELVSGGELFD----FLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKL 169
Cdd:cd06608    79 GgddqlwLVMEYCGGGSVTDlvkgLRKKGKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEA----EVKL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 170 IDFGLAHEIEDGVEFKNIF-GTPEFVAPEIV----NYEP-LGLEADMWSIGvITYILLSGASPFLGD------------T 231
Cdd:cd06608   155 VDFGVSAQLDSTLGRRNTFiGTPYWMAPEVIacdqQPDAsYDARCDVWSLG-ITAIELADGKPPLCDmhpmralfkiprN 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2056392213 232 KQETLANITAVSYDFDeeffsqtselakDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd06608   234 PPPTLKSPEKWSKEFN------------DFISECLIKNYEQRPFTEELLEHPFI 275
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
20-308 3.42e-32

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: 124.65  E-value: 3.42e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  20 EDFYDIgEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSrasrrgVSREEIER---EVSILRQVLHHNVITLHDVYENR 96
Cdd:cd05599     1 EDFEPL-KVIGRGAFGEVRLVRKKDTGHVYAMKKLRKSEM------LEKEQVAHvraERDILAEADNPWVVKLYYSFQDE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  97 TDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAH 176
Cdd:cd05599    74 ENLYLIMEFLPGGDMMTLLMKKDTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNL-LLDAR---GHIKLSDFGLCT 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 177 EIE-DGVEFKNIfGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANItaVSYDFDEEFFSQT- 254
Cdd:cd05599   150 GLKkSHLAYSTV-GTPDYIAPEVFLQKGYGKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKI--MNWRETLVFPPEVp 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2056392213 255 -SELAKDFIRKLLVkETRKRL---TIQEALRHPWITPVD-----NQQA--MVRRESVVNLENFRK 308
Cdd:cd05599   227 iSPEAKDLIERLLC-DAEHRLganGVEEIKSHPFFKGVDwdhirERPApiLPEVKSILDTSNFDE 290
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
21-286 3.67e-32

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: 123.12  E-value: 3.67e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  21 DFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRrgvsrEEIEREVSILRQVLHHNVITLHDVYENRTDVV 100
Cdd:cd06609     1 ELFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDLEEAEDEI-----EDIQQEIQFLSQCDSPYITKYYGSFLKGSKLW 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 101 LILELVSGGELFDFLaqKESLSEEEATSFI-KQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAHEIE 179
Cdd:cd06609    76 IIMEYCGGGSVLDLL--KPGPLDETYIAFIlREVLLGLEYLHSEGKIHRDIKAANI-LLSEE---GDVKLADFGVSGQLT 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 180 DGVEFKNIF-GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEffSQTSELA 258
Cdd:cd06609   150 STMSKRNTFvGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPLSDLHPMRVLFLIPKNNPPSLEG--NKFSKPF 227
                         250       260
                  ....*....|....*....|....*...
gi 2056392213 259 KDFIRKLLVKETRKRLTIQEALRHPWIT 286
Cdd:cd06609   228 KDFVELCLNKDPKERPSAKELLKHKFIK 255
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
29-320 4.16e-32

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: 124.03  E-value: 4.16e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKrqsrasrrGVSREEIEREVS-ILRQVL----HHNVIT-LHDVYENRTDVVLI 102
Cdd:cd05592     3 LGKGSFGKVMLAELKGTNQYFAIKALKK--------DVVLEDDDVECTmIERRVLalasQHPFLThLFCTFQTESHLFFV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLlDKNipiPHIKLIDFGLAHE-IEDG 181
Cdd:cd05592    75 MEYLNGGDLMFHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLL-DRE---GHIKIADFGMCKEnIYGE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 182 VEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAvsydfDEEFFSQT-SELAKD 260
Cdd:cd05592   151 NKASTFCGTPDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSICN-----DTPHYPRWlTKEAAS 225
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2056392213 261 FIRKLLVKETRKRLTIQEALR-----HPWITPVDNQQaMVRRE----------SVVNLENFRKQYVRRRWKLSFS 320
Cdd:cd05592   226 CLSLLLERNPEKRLGVPECPAgdirdHPFFKTIDWDK-LERREidppfkpkvkSANDVSNFDPDFTMEKPVLTPV 299
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
29-228 4.75e-32

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: 123.33  E-value: 4.75e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGlEYAAkfIKKRQSRASRRGVSREEIEREVSILRQVLHHNVITLHDVYE-----NRTDV-VLI 102
Cdd:cd13989     1 LGSGGFGYVTLWKHQDTG-EYVA--IKKCRQELSPSDKNRERWCLEVQIMKKLNHPNVVSARDVPPeleklSPNDLpLLA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQKES---LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHiKLIDFGLAHEIE 179
Cdd:cd13989    78 MEYCSGGDLRKVLNQPENccgLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGGRVIY-KLIDLGYAKELD 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2056392213 180 DGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFL 228
Cdd:cd13989   157 QGSLCTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPFL 205
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
23-284 4.92e-32

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: 123.15  E-value: 4.92e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAakfIKKRQSRASRRGVSREEIeREVSILRQVL---HHNVITLHDV-----YE 94
Cdd:cd07838     1 YEEVAEIGEGAYGTVYKARDLQDGRFVA---LKKVRVPLSEEGIPLSTI-REIALLKQLEsfeHPNVVRLLDVchgprTD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  95 NRTDVVLILELVSGgELFDFL--AQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDF 172
Cdd:cd07838    77 RELKLTLVFEHVDQ-DLATYLdkCPKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDG----QVKLADF 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 173 GLAHEIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANI------------- 239
Cdd:cd07838   152 GLARIYSFEMALTSVVVTLWYRAPEVLLQSSYATPVDMWSVGCIFAELFNRRPLFRGSSEADQLGKIfdviglpseeewp 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2056392213 240 --TAVSYD-FD-------EEFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd07838   232 rnSALPRSsFPsytprpfKSFVPEIDEEGLDLLKKMLTFNPHKRISAFEALQHPY 286
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
23-285 5.23e-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: 122.41  E-value: 5.23e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQsrasrrGVSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd06613     2 YELIQRIGSGTYGDVYKARNIATGELAAVKVIKLEP------GDDFEIIQQEISMLKECRHPNIVAYFGSYLRRDKLWIV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIEDGV 182
Cdd:cd06613    76 MEYCGGGSLQDIYQVTGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDG----DVKLADFGVSAQLTATI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 183 EFKNIF-GTPEFVAPEIVNYEPLG---LEADMWSIGvITYILLSGASPFLGDTK-QETLANITAVSYD----FDEEFFSQ 253
Cdd:cd06613   152 AKRKSFiGTPYWMAPEVAAVERKGgydGKCDIWALG-ITAIELAELQPPMFDLHpMRALFLIPKSNFDppklKDKEKWSP 230
                         250       260       270
                  ....*....|....*....|....*....|..
gi 2056392213 254 TselAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd06613   231 D---FHDFIKKCLTKNPKKRPTATKLLQHPFV 259
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
29-283 6.50e-32

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: 122.11  E-value: 6.50e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKR-QSRASRrgvsrEEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVS 107
Cdd:cd08530     8 LGKGSYGSVYKVKRLSDNQVYALKEVNLGsLSQKER-----EDSVNEIRLLASVNHPNIIRYKEAFLDGNRLCIVMEYAP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 108 GGELFDFL----AQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIEDGVE 183
Cdd:cd08530    83 FGDLSKLIskrkKKRRLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDL----VKIGDLGISKVLKKNLA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 184 FKNIfGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQtsELAKdFIR 263
Cdd:cd08530   159 KTQI-GTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFEARTMQELRYKVCRGKFPPIPPVYSQ--DLQQ-IIR 234
                         250       260
                  ....*....|....*....|
gi 2056392213 264 KLLVKETRKRLTIQEALRHP 283
Cdd:cd08530   235 SLLQVNPKKRPSCDKLLQSP 254
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
23-284 8.29e-32

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: 122.67  E-value: 8.29e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRasrRGVSREEIeREVSILRQVLHHNVITLHDVY------ENR 96
Cdd:cd07840     1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIRMENEK---EGFPITAI-REIKLLQKLDHPNVVRLKEIVtskgsaKYK 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  97 TDVVLILELVSggelFDF---LAQKES-LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDF 172
Cdd:cd07840    77 GSIYMVFEYMD----HDLtglLDNPEVkFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDG----VLKLADF 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 173 GLAHEIEDgvEFKNIFgTPEFV-----APEIV----NYEPlglEADMWSIGVITYILLSGASPFLGDTKQETLANITAV- 242
Cdd:cd07840   149 GLARPYTK--ENNADY-TNRVItlwyrPPELLlgatRYGP---EVDMWSVGCILAELFTGKPIFQGKTELEQLEKIFELc 222
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2056392213 243 ------------------------SYD--FDEEFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd07840   223 gspteenwpgvsdlpwfenlkpkkPYKrrLREVFKNVIDPSALDLLDKLLTLDPKKRISADQALQHEY 290
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
23-288 2.74e-31

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: 122.25  E-value: 2.74e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAakfIKKRQsRASRRGVSREEIEREVSILRQVLHHNVITLHDV-----YENRT 97
Cdd:cd07834     2 YELLKPIGSGAYGVVCSAYDKRTGRKVA---IKKIS-NVFDDLIDAKRILREIKILRHLKHENIIGLLDIlrppsPEEFN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  98 DVVLILELVsGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNIpipHIKLIDFGLAHE 177
Cdd:cd07834    78 DVYIVTELM-ETDLHKVIKSPQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNI-LVNSNC---DLKICDFGLARG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 178 IEDgvEFKNIFGTpEFV------APEIV----NYeplGLEADMWSIGVI------TYILLSGASP---------FLGDTK 232
Cdd:cd07834   153 VDP--DEDKGFLT-EYVvtrwyrAPELLlsskKY---TKAIDIWSVGCIfaelltRKPLFPGRDYidqlnliveVLGTPS 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2056392213 233 QETLANIT---AVSY----------DFdEEFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWITPV 288
Cdd:cd07834   227 EEDLKFISsekARNYlkslpkkpkkPL-SEVFPGASPEAIDLLEKMLVFNPKKRITADEALAHPYLAQL 294
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
18-334 4.50e-31

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: 121.57  E-value: 4.50e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  18 KVEDFYdIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRrGVSREEIEREVsiLRQVLHHNVIT-LHDVYENR 96
Cdd:cd05619     3 TIEDFV-LHKMLGKGSFGKVFLAELKGTNQFFAIKALKKDVVLMDD-DVECTMVEKRV--LSLAWEHPFLThLFCTFQTK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  97 TDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAH 176
Cdd:cd05619    79 ENLFFVMEYLNGGDLMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNI-LLDKD---GHIKIADFGMCK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 177 EIEDGVEFKNIF-GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITavsydFDEEFFSQ-T 254
Cdd:cd05619   155 ENMLGDAKTSTFcGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSIR-----MDNPFYPRwL 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 255 SELAKDFIRKLLVKETRKRLTIQEALR-HPWITPVDnQQAMVRRE----------SVVNLENFRKQYVRRRWKLSFSIVS 323
Cdd:cd05619   230 EKEAKDILVKLFVREPERRLGVRGDIRqHPFFREIN-WEALEEREieppfkpkvkSPFDCSNFDKEFLNEKPRLSFADRA 308
                         330
                  ....*....|.
gi 2056392213 324 LCNHLTRSLMK 334
Cdd:cd05619   309 LINSMDQNMFR 319
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
29-289 4.95e-31

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: 121.23  E-value: 4.95e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRqSRASRRGVSREEIEREVsILRQVLHHNVITLHDVYENRTDVVLILELVSG 108
Cdd:cd05603     3 IGKGSFGKVLLAKRKCDGKFYAVKVLQKK-TILKKKEQNHIMAERNV-LLKNLKHPFLVGLHYSFQTSEKLYFVLDYVNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 109 GELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAHEIEDGVEFKNIF 188
Cdd:cd05603    81 GELFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENI-LLDCQ---GHVVLTDFGLCKEGMEPEETTSTF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 189 -GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDeeffSQTSELAKDFIRKLLV 267
Cdd:cd05603   157 cGTPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFYSRDVSQMYDNILHKPLHLP----GGKTVAACDLLQGLLH 232
                         250       260
                  ....*....|....*....|....*.
gi 2056392213 268 KETRKRL----TIQEALRHPWITPVD 289
Cdd:cd05603   233 KDQRRRLgakaDFLEIKNHVFFSPIN 258
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
23-284 5.05e-31

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: 120.33  E-value: 5.05e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSrasrrgvSREEI--EREVSILRQVLHH-NVITLHDVYENRTDV 99
Cdd:cd07830     1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKMKKKFY-------SWEECmnLREVKSLRKLNEHpNIVKLKEVFRENDEL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 100 VLILELVSGgELFDFLAQKES--LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHE 177
Cdd:cd07830    74 YFVFEYMEG-NLYQLMKDRKGkpFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEV----VKIADFGLARE 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 178 IEDGVEFKNIFGTPEFVAPEIV----NYE-PLgleaDMWSIGVITYILLS------GASPF---------LGDTKQET-- 235
Cdd:cd07830   149 IRSRPPYTDYVSTRWYRAPEILlrstSYSsPV----DIWALGCIMAELYTlrplfpGSSEIdqlykicsvLGTPTKQDwp 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 236 ----LANitAVSYDFDE-------EFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd07830   225 egykLAS--KLGFRFPQfaptslhQLIPNASPEAIDLIKDMLRWDPKKRPTASQALQHPY 282
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
23-285 1.25e-30

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: 118.61  E-value: 1.25e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAakfIKKRQSRASRRGVSRE--EIEREVSILRQVLHHNVITLHDVYENRTDVV 100
Cdd:cd06652     4 WRLGKLLGQGAFGRVYLCYDADTGRELA---VKQVQFDPESPETSKEvnALECEIQLLKNLLHERIVQYYGCLRDPQERT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 101 L--ILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKnipIPHIKLIDFGLAHEI 178
Cdd:cd06652    81 LsiFMEYMPGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANI-LRDS---VGNVKLGDFGASKRL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 179 E----DGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFlgdTKQETLANITAVSYD-FDEEFFSQ 253
Cdd:cd06652   157 QticlSGTGMKSVTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPW---AEFEAMAAIFKIATQpTNPQLPAH 233
                         250       260       270
                  ....*....|....*....|....*....|..
gi 2056392213 254 TSELAKDFIRKLLVkETRKRLTIQEALRHPWI 285
Cdd:cd06652   234 VSDHCRDFLKRIFV-EAKLRPSADELLRHTFV 264
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
29-312 1.37e-30

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: 120.10  E-value: 1.37e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKrqsrasrrGVSREEIEREVSIL-RQVLHHN-----VITLHDVYENRTDVVLI 102
Cdd:cd05616     8 LGKGSFGKVMLAERKGTDELYAVKILKK--------DVVIQDDDVECTMVeKRVLALSgkppfLTQLHSCFQTMDRLYFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHE-IEDG 181
Cdd:cd05616    80 MEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEG----HIKIADFGMCKEnIWDG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 182 VEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITA--VSYDfdeeffSQTSELAK 259
Cdd:cd05616   156 VTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEhnVAYP------KSMSKEAV 229
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2056392213 260 DFIRKLLVKETRKRLTIQ------------------EALRHPWITPVDNQQAMVRresvvNLENFRKQYVR 312
Cdd:cd05616   230 AICKGLMTKHPGKRLGCGpegerdikehaffryidwEKLERKEIQPPYKPKACGR-----NAENFDRFFTR 295
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
29-239 3.79e-30

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: 118.91  E-value: 3.79e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSrASRRGVSREEIEREVsILRQVLHHNVITLHDVYENRTDVVLILELVSG 108
Cdd:cd05604     4 IGKGSFGKVLLAKRKRDGKYYAVKVLQKKVI-LNRKEQKHIMAERNV-LLKNVKHPFLVGLHYSFQTTDKLYFVLDFVNG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 109 GELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHE-IEDGVEFKNI 187
Cdd:cd05604    82 GELFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQG----HIVLTDFGLCKEgISNSDTTTTF 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2056392213 188 FGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANI 239
Cdd:cd05604   158 CGTPEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENI 209
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
26-284 3.92e-30

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: 117.49  E-value: 3.92e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  26 GEELGSGQFAIVKKCREKSTGLEYAAKFIK-KRQSRASRRGVSreEIEREVSILRQVLHHNVITLHDVYENRTD--VVLI 102
Cdd:cd06651    12 GKLLGQGAFGRVYLCYDVDTGRELAAKQVQfDPESPETSKEVS--ALECEIQLLKNLQHERIVQYYGCLRDRAEktLTIF 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIE--- 179
Cdd:cd06651    90 MEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAG----NVKLGDFGASKRLQtic 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 180 -DGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFlgdTKQETLANITAVSYD-FDEEFFSQTSEL 257
Cdd:cd06651   166 mSGTGIRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW---AEYEAMAAIFKIATQpTNPQLPSHISEH 242
                         250       260
                  ....*....|....*....|....*..
gi 2056392213 258 AKDFIRKLLVkETRKRLTIQEALRHPW 284
Cdd:cd06651   243 ARDFLGCIFV-EARHRPSAEELLRHPF 268
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
29-274 4.17e-30

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: 119.36  E-value: 4.17e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSrasrrgVSREEIER---EVSILRQVLHHNVITLHDVYENRTDVVLILEL 105
Cdd:cd05594    33 LGKGTFGKVILVKEKATGRYYAMKILKKEVI------VAKDEVAHtltENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 106 VSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKK-IAHFDLKPENIMLlDKNipiPHIKLIDFGLAHE-IEDGVE 183
Cdd:cd05594   107 ANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLML-DKD---GHIKITDFGLCKEgIKDGAT 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 184 FKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLgDTKQETLANITAVSydfDEEFFSQTSELAKDFIR 263
Cdd:cd05594   183 MKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFY-NQDHEKLFELILME---EIRFPRTLSPEAKSLLS 258
                         250
                  ....*....|.
gi 2056392213 264 KLLVKETRKRL 274
Cdd:cd05594   259 GLLKKDPKQRL 269
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
21-300 8.64e-30

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: 117.05  E-value: 8.64e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  21 DFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRqsrasrrgvSREEIER---EVSILRQVLHHNVITLHDVYENRT 97
Cdd:cd06644    12 EVWEIIGELGDGAFGKVYKAKNKETGALAAAKVIETK---------SEEELEDymvEIEILATCNHPYIVKLLGAFYWDG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  98 DVVLILELVSGGEL-FDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIML-LDKNipiphIKLIDFGLA 175
Cdd:cd06644    83 KLWIMIEFCPGGAVdAIMLELDRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLtLDGD-----IKLADFGVS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 176 HEIEDGVEFKNIF-GTPEFVAPEIVNYE-----PLGLEADMWSIGvITYILLSGASP----------FLGDTKQE--TLA 237
Cdd:cd06644   158 AKNVKTLQRRDSFiGTPYWMAPEVVMCEtmkdtPYDYKADIWSLG-ITLIEMAQIEPphhelnpmrvLLKIAKSEppTLS 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2056392213 238 NITAVSYDFdeeffsqtselaKDFIRKLLVKETRKRLTIQEALRHPWITPVDNQQAMvrRESV 300
Cdd:cd06644   237 QPSKWSMEF------------RDFLKTALDKHPETRPSAAQLLEHPFVSSVTSNRPL--RELV 285
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
27-285 8.79e-30

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: 116.17  E-value: 8.79e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFAIVKKCREKSTGLEYAAKFIKKRQsrasrrgVSREEIER---EVSILRQVLHHNVITLHDVYEN--RTDVVL 101
Cdd:cd13983     7 EVLGRGSFKTVYRAFDTEEGIEVAWNEIKLRK-------LPKAERQRfkqEIEILKSLKHPNIIKFYDSWESksKKEVIF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 102 ILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKK--IAHFDLKPENIMLldkNIPIPHIKLIDFGLAHEIE 179
Cdd:cd13983    80 ITELMTSGTLKQYLKRFKRLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFI---NGNTGEVKIGDLGLATLLR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 180 DGVEfKNIFGTPEFVAPEIV--NYEPLgleADMWSIGVITYILLSGASPFL-----GDTKQETLANITAVSYDfdeeffS 252
Cdd:cd13983   157 QSFA-KSVIGTPEFMAPEMYeeHYDEK---VDIYAFGMCLLEMATGEYPYSectnaAQIYKKVTSGIKPESLS------K 226
                         250       260       270
                  ....*....|....*....|....*....|...
gi 2056392213 253 QTSELAKDFIRKLLVKETRkRLTIQEALRHPWI 285
Cdd:cd13983   227 VKDPELKDFIEKCLKPPDE-RPSARELLEHPFF 258
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
23-285 8.95e-30

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: 116.28  E-value: 8.95e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIK-KRQSRASRRGVSreEIEREVSILRQVLHHNVITLHDVYENRTD--V 99
Cdd:cd06653     4 WRLGKLLGRGAFGEVYLCYDADTGRELAVKQVPfDPDSQETSKEVN--ALECEIQLLKNLRHDRIVQYYGCLRDPEEkkL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 100 VLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAHEIE 179
Cdd:cd06653    82 SIFVEYMPGGSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANI-LRDSA---GNVKLGDFGASKRIQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 180 ----DGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFlgdTKQETLANITAVSYDFDEEFFSQ-T 254
Cdd:cd06653   158 ticmSGTGIKSVTGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPW---AEYEAMAAIFKIATQPTKPQLPDgV 234
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2056392213 255 SELAKDFIRKLLVKETRkRLTIQEALRHPWI 285
Cdd:cd06653   235 SDACRDFLRQIFVEEKR-RPTAEFLLRHPFV 264
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
25-239 9.71e-30

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: 116.06  E-value: 9.71e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  25 IGEELGSGQFAIVKKCREKSTGLEYAAK-FIKKRQSRASRRgvSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLIL 103
Cdd:pfam07714   3 LGEKLGEGAFGEVYKGTLKGEGENTKIKvAVKTLKEGADEE--EREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 104 ELVSGGELFDFL-AQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAHEIEDGV 182
Cdd:pfam07714  81 EYMPGGDLLDFLrKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNC-LVSEN---LVVKISDFGLSRDIYDDD 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2056392213 183 EFKNIFGTPEFV---APEIVNYEPLGLEADMWSIGVITYILLS-GASPFLGDTKQETLANI 239
Cdd:pfam07714 157 YYRKRGGGKLPIkwmAPESLKDGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEEVLEFL 217
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
16-285 1.42e-29

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: 116.68  E-value: 1.42e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  16 QQKVEDFYDIGEelgsGQFAIVKKCREKSTGLEYAakfIKKRQSRASRRgvsREEIEREVSILRQVLHHNVITLHDVYEN 95
Cdd:cd06658    21 REYLDSFIKIGE----GSTGIVCIATEKHTGKQVA---VKKMDLRKQQR---RELLFNEVVIMRDYHHENVVDMYNSYLV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  96 RTDVVLILELVSGGELFDFLAQKEsLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLA 175
Cdd:cd06658    91 GDELWVVMEFLEGGALTDIVTHTR-MNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDG----RIKLSDFGFC 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 176 HEIEDGV-EFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAvSYDFDEEFFSQT 254
Cdd:cd06658   166 AQVSKEVpKRKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIRD-NLPPRVKDSHKV 244
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2056392213 255 SELAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd06658   245 SSVLRGFLDLMLVREPSQRATAQELLQHPFL 275
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
19-287 1.72e-29

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: 117.39  E-value: 1.72e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  19 VEDFYDIGEELGSGQFAIVKKCREKSTGLEYAakfIKKrQSRASRRGVSREEIEREVSILRQVLHHNVITLHDVY----- 93
Cdd:cd07851    13 VPDRYQNLSPVGSGAYGQVCSAFDTKTGRKVA---IKK-LSRPFQSAIHAKRTYRELRLLKHMKHENVIGLLDVFtpass 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  94 -ENRTDVVLILELVsGGELFDFLAQKEsLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMlLDKNIpipHIKLIDF 172
Cdd:cd07851    89 lEDFQDVYLVTHLM-GADLNNIVKCQK-LSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLA-VNEDC---ELKILDF 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 173 GLAHEIEDgvEFKNIFGTPEFVAPEIV----NYEPLgleADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDE 248
Cdd:cd07851   163 GLARHTDD--EMTGYVATRWYRAPEIMlnwmHYNQT---VDIWSVGCIMAELLTGKTLFPGSDHIDQLKRIMNLVGTPDE 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2056392213 249 EF---------------------------FSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWITP 287
Cdd:cd07851   238 ELlkkissesarnyiqslpqmpkkdfkevFSGANPLAIDLLEKMLVLDPDKRITAAEALAHPYLAE 303
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
29-331 1.82e-29

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: 116.97  E-value: 1.82e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRrGVSREEIEREVSIL---RQVLHHnvitLHDVYENRTDVVLILEL 105
Cdd:cd05620     3 LGKGSFGKVLLAELKGKGEYFAVKALKKDVVLIDD-DVECTMVEKRVLALaweNPFLTH----LYCTFQTKEHLFFVMEF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 106 VSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLlDKNipiPHIKLIDFGLAHEIEDGVEFK 185
Cdd:cd05620    78 LNGGDLMFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVML-DRD---GHIKIADFGMCKENVFGDNRA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 186 NIF-GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTselaKDFIRK 264
Cdd:cd05620   154 STFcGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTPHYPRWITKES----KDILEK 229
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2056392213 265 LLVKETRKRLTIQEALR-HPWITPVdNQQAMVRRE----------SVVNLENFRKQYVRRRWKLSFSIVSLCNHLTRS 331
Cdd:cd05620   230 LFERDPTRRLGVVGNIRgHPFFKTI-NWTALEKREldppfkpkvkSPSDYSNFDREFLSEKPRLSYSDKNLIDSMDQS 306
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
26-285 2.06e-29

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: 115.32  E-value: 2.06e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  26 GEELGSGQFAIVKKCREKSTGLEYAAKFIK---KRQSRASRRGVSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd06628     5 GALIGSGSFGSVYLGMNASSGELMAVKQVElpsVSAENKDRKKSMLDALQREIALLRELQHENIVQYLGSSSDANHLNIF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIE--- 179
Cdd:cd06628    85 LEYVPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKG----GIKISDFGISKKLEans 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 180 ----DGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFlgdTKQETLANITAVSYDFDEEFFSQTS 255
Cdd:cd06628   161 lstkNNGARPSLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPF---PDCTQMQAIFKIGENASPTIPSNIS 237
                         250       260       270
                  ....*....|....*....|....*....|
gi 2056392213 256 ELAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd06628   238 SEARDFLEKTFEIDHNKRPTADELLKHPFL 267
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
23-285 2.75e-29

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: 114.91  E-value: 2.75e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKkrQSRASRRgvSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd08218     2 YVRIKKIGEGSFGKALLVKSKEDGKQYVIKEIN--ISKMSPK--EREESRKEVAVLSKMKHPNIVQYQESFEENGNLYIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFL-AQKESL-SEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIED 180
Cdd:cd08218    78 MDYCDGGDLYKRInAQRGVLfPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGI----IKLGDFGIARVLNS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 181 GVEF-KNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSqtSELaK 259
Cdd:cd08218   154 TVELaRTCIGTPYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFEAGNMKNLVLKIIRGSYPPVPSRYS--YDL-R 230
                         250       260
                  ....*....|....*....|....*.
gi 2056392213 260 DFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd08218   231 SLVSQLFKRNPRDRPSINSILEKPFI 256
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
28-276 3.87e-29

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: 114.74  E-value: 3.87e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  28 ELGSGQFAIVKKCREKSTGLEYAAKfikkrqsRASRRGVSR-EEIEREVSILRQVLHH-NVITLHD--VY--ENRTDVVL 101
Cdd:cd13985     7 QLGEGGFSYVYLAHDVNTGRRYALK-------RMYFNDEEQlRVAIKEIEIMKRLCGHpNIVQYYDsaILssEGRKEVLL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 102 ILELVsGGELFDFLAQKES--LSEEEATSFIKQILDGVNYLHTKK--IAHFDLKPENIMLLDKNipipHIKLIDFGLA-- 175
Cdd:cd13985    80 LMEYC-PGSLVDILEKSPPspLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTG----RFKLCDFGSAtt 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 176 --------HEIEDGVEFKNIFGTPEFVAPEIVN---YEPLGLEADMWSIGVITYILLSGASPFLGDTKqetLAnITAVSY 244
Cdd:cd13985   155 ehypleraEEVNIIEEEIQKNTTPMYRAPEMIDlysKKPIGEKADIWALGCLLYKLCFFKLPFDESSK---LA-IVAGKY 230
                         250       260       270
                  ....*....|....*....|....*....|..
gi 2056392213 245 DFDEefFSQTSELAKDFIRKLLVKETRKRLTI 276
Cdd:cd13985   231 SIPE--QPRYSPELHDLIRHMLTPDPAERPDI 260
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
29-285 5.10e-29

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 116.46  E-value: 5.10e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRgvsreEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSG 108
Cdd:PLN00034   82 IGSGAGGTVYKVIHRPTGRLYALKVIYGNHEDTVRR-----QICREIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDG 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 109 GElfdfLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIEDGVEFKN-I 187
Cdd:PLN00034  157 GS----LEGTHIADEQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAK----NVKIADFGVSRILAQTMDPCNsS 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 188 FGTPEFVAPEIVN-------YEplGLEADMWSIGVITYILLSGASPFlGDTKQETLANIT-AVSYDFDEEFFSQTSELAK 259
Cdd:PLN00034  229 VGTIAYMSPERINtdlnhgaYD--GYAGDIWSLGVSILEFYLGRFPF-GVGRQGDWASLMcAICMSQPPEAPATASREFR 305
                         250       260
                  ....*....|....*....|....*.
gi 2056392213 260 DFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:PLN00034  306 HFISCCLQREPAKRWSAMQLLQHPFI 331
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
23-285 6.14e-29

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: 113.99  E-value: 6.14e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRrgvsrEEIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd06610     3 YELIEVIGSGATAVVYAAYCLPKKEKVAIKRIDLEKCQTSM-----DELRKEIQAMSQCNHPNVVSYYTSFVVGDELWLV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQKES---LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAHEIE 179
Cdd:cd06610    78 MPLLSGGSLLDIMKSSYPrggLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNI-LLGED---GSVKIADFGVSASLA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 180 DGVEF-----KNIFGTPEFVAPEIVN-YEPLGLEADMWSIGvITYI-LLSGASPFLGDTKQETLANI---TAVSYDFDEE 249
Cdd:cd06610   154 TGGDRtrkvrKTFVGTPCWMAPEVMEqVRGYDFKADIWSFG-ITAIeLATGAAPYSKYPPMKVLMLTlqnDPPSLETGAD 232
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2056392213 250 fFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd06610   233 -YKKYSKSFRKMISLCLQKDPSKRPTAEELLKHKFF 267
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
18-289 6.63e-29

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: 115.88  E-value: 6.63e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  18 KVEDFyDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKR---QSRASRRGVSreeiEREVsILRQVLHHNVITLHDVYE 94
Cdd:cd05602     5 KPSDF-HFLKVIGKGSFGKVLLARHKSDEKFYAVKVLQKKailKKKEEKHIMS----ERNV-LLKNVKHPFLVGLHFSFQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  95 NRTDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGL 174
Cdd:cd05602    79 TTDKLYFVLDYINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQG----HIVLTDFGL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 175 AHE-IEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDeeffSQ 253
Cdd:cd05602   155 CKEnIEPNGTTSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQLK----PN 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2056392213 254 TSELAKDFIRKLLVKETRKRLTIQ----EALRHPWITPVD 289
Cdd:cd05602   231 ITNSARHLLEGLLQKDRTKRLGAKddftEIKNHIFFSPIN 270
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
23-285 1.50e-28

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: 114.18  E-value: 1.50e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQsRASRRGVSreeierEVSILRQVLH------HNVITLHDVYENR 96
Cdd:cd14210    15 YEVLSVLGKGSFGQVVKCLDHKTGQLVAIKIIRNKK-RFHQQALV------EVKILKHLNDndpddkHNIVRYKDSFIFR 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  97 TDVVLILELVSGgELFDFLAQK--ESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDknipiPH---IKLID 171
Cdd:cd14210    88 GHLCIVFELLSI-NLYELLKSNnfQGLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQ-----PSkssIKVID 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 172 FG---LAHEIedgvefknIFgtpEFV------APEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAV 242
Cdd:cd14210   162 FGsscFEGEK--------VY---TYIqsrfyrAPEVILGLPYDTAIDMWSLGCILAELYTGYPLFPGENEEEQLACIMEV 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 243 ---------------SYDFDEEFF---------------SQTSELAK--------DFIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd14210   231 lgvppkslidkasrrKKFFDSNGKprpttnskgkkrrpgSKSLAQVLkcddpsflDFLKKCLRWDPSERMTPEEALQHPW 310

                  .
gi 2056392213 285 I 285
Cdd:cd14210   311 I 311
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
25-239 2.01e-28

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 112.62  E-value: 2.01e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213   25 IGEELGSGQFAIVKKCR----EKSTGLEYAAKFIKKRQSRASRrgvsrEEIEREVSILRQVLHHNVITLHDVYENRTDVV 100
Cdd:smart00219   3 LGKKLGEGAFGEVYKGKlkgkGGKKKVEVAVKTLKEDASEQQI-----EEFLREARIMRKLDHPNVVKLLGVCTEEEPLY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  101 LILELVSGGELFDFL-AQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAHEIE 179
Cdd:smart00219  78 IVMEYMEGGDLLSYLrKNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNC-LVGEN---LVVKISDFGLSRDLY 153
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2056392213  180 DGvEFKNIFGTPEFV---APEIVNYEPLGLEADMWSIGVITYILLS-GASPFLGDTKQETLANI 239
Cdd:smart00219 154 DD-DYYRKRGGKLPIrwmAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEEVLEYL 216
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
20-289 2.52e-28

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: 113.98  E-value: 2.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  20 EDFyDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKK-----RQSRASrrgvSREEierevsilRQVLHHN----VITLH 90
Cdd:cd05597     1 DDF-EILKVIGRGAFGEVAVVKLKSTEKVYAMKILNKwemlkRAETAC----FREE--------RDVLVNGdrrwITKLH 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  91 DVYENRTDVVLILELVSGGELFDFLAQKES-LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKL 169
Cdd:cd05597    68 YAFQDENYLYLVMDYYCGGDLLTLLSKFEDrLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNV-LLDRN---GHIRL 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 170 IDFGLAHEI-EDGVEFKNI-FGTPEFVAPEIV--------NYeplGLEADMWSIGVITYILLSGASPFLGDTKQETLANI 239
Cdd:cd05597   144 ADFGSCLKLrEDGTVQSSVaVGTPDYISPEILqamedgkgRY---GPECDWWSLGVCMYEMLYGETPFYAESLVETYGKI 220
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2056392213 240 ----TAVSYDFDEEffsQTSELAKDFIRKLL-VKETR-KRLTIQEALRHPWITPVD 289
Cdd:cd05597   221 mnhkEHFSFPDDED---DVSEEAKDLIRRLIcSRERRlGQNGIDDFKKHPFFEGID 273
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
23-284 2.56e-28

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: 112.75  E-value: 2.56e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSrasrrgvSREEIE--REVSILRQVLHH-NVITLHDV-YENRTD 98
Cdd:cd07831     1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIKCMKKHFK-------SLEQVNnlREIQALRRLSPHpNILRLIEVlFDRKTG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  99 -VVLILELVSGgELFDFL-AQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKnipipHIKLIDFGLAH 176
Cdd:cd07831    74 rLALVFELMDM-NLYELIkGRKRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDD-----ILKLADFGSCR 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 177 EIEDGVEFKNIFGTPEFVAPEIV----NYEPlglEADMWSIGVITYILLSGASPFLGDTKQETLANI------------- 239
Cdd:cd07831   148 GIYSKPPYTEYISTRWYRAPECLltdgYYGP---KMDIWAVGCVFFEILSLFPLFPGTNELDQIAKIhdvlgtpdaevlk 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 240 -----TAVSYDFDEEffsQTSELAK----------DFIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd07831   225 kfrksRHMNYNFPSK---KGTGLRKllpnasaeglDLLKKLLAYDPDERITAKQALRHPY 281
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
29-241 2.86e-28

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: 113.74  E-value: 2.86e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAakfIKKRQSRASRRGVsrEEIEREVSILRQVLHHNVITLHDVYENRT--DVVLILELV 106
Cdd:cd13988     1 LGQGATANVFRGRHKKTGDLYA---VKVFNNLSFMRPL--DVQMREFEVLKKLNHKNIVKLFAIEEELTtrHKVLVMELC 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 107 SGGELFDFLAQKES---LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLAHEIEDGVE 183
Cdd:cd13988    76 PCGSLYTVLEEPSNaygLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMRVIGEDGQSVYKLTDFGAARELEDDEQ 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2056392213 184 FKNIFGTPEFVAPEIvnYE----------PLGLEADMWSIGVITYILLSGASPF----LGDTKQETLANITA 241
Cdd:cd13988   156 FVSLYGTEEYLHPDM--YEravlrkdhqkKYGATVDLWSIGVTFYHAATGSLPFrpfeGPRRNKEVMYKIIT 225
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
29-318 3.30e-28

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: 113.64  E-value: 3.30e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKR---QSRasrrGVSREEIEREVSILRQVLHHnVITLHDVYENRTDVVLILEL 105
Cdd:cd05587     4 LGKGSFGKVMLAERKGTDELYAIKILKKDviiQDD----DVECTMVEKRVLALSGKPPF-LTQLHSCFQTMDRLYFVMEY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 106 VSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLlDKNipiPHIKLIDFGLAHE-IEDGVEF 184
Cdd:cd05587    79 VNGGDLMYHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVML-DAE---GHIKIADFGMCKEgIFGGKTT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 185 KNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANIT--AVSYDfdeeffSQTSELAKDFI 262
Cdd:cd05587   155 RTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMehNVSYP------KSLSKEAVSIC 228
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2056392213 263 RKLLVKETRKRL--------TIQEalrHPWITPVDNQQaMVRRE----------SVVNLENFRKQYVRRRWKLS 318
Cdd:cd05587   229 KGLLTKHPAKRLgcgptgerDIKE---HPFFRRIDWEK-LERREiqppfkpkikSPRDAENFDKEFTKEPPVLT 298
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
23-279 3.32e-28

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: 112.21  E-value: 3.32e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLE-YAAKFIKKRQSRASRRGVSRE----EIEREVSILRQVLHH-NVITLHDVYENR 96
Cdd:cd08528     2 YAVLELLGSGAFGCVYKVRKKSNGQTlLALKEINMTNPAFGRTEQERDksvgDIISEVNIIKEQLRHpNIVRYYKTFLEN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  97 TDVVLILELVSG---GELFDFLAQK-ESLSEEEATSFIKQILDGVNYLHT-KKIAHFDLKPENIMLLDKNipipHIKLID 171
Cdd:cd08528    82 DRLYIVMELIEGaplGEHFSSLKEKnEHFTEDRIWNIFVQMVLALRYLHKeKQIVHRDLKPNNIMLGEDD----KVTITD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 172 FGLAHE-IEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYD-FDEE 249
Cdd:cd08528   158 FGLAKQkGPESSKMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPFYSTNMLTLATKIVEAEYEpLPEG 237
                         250       260       270
                  ....*....|....*....|....*....|
gi 2056392213 250 FFSQTSElakDFIRKLLVKETRKRLTIQEA 279
Cdd:cd08528   238 MYSDDIT---FVIRSCLTPDPEARPDIVEV 264
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
12-304 3.41e-28

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: 115.11  E-value: 3.41e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  12 EPFKQ-----QKVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQS-RASRRGVSREEierevsilRQVLHHN 85
Cdd:cd05624    58 KPFTQlvkemQLHRDDFEIIKVIGRGAFGEVAVVKMKNTERIYAMKILNKWEMlKRAETACFREE--------RNVLVNG 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  86 ----VITLHDVYENRTDVVLILELVSGGELFDFLAQKES-LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDK 160
Cdd:cd05624   130 dcqwITTLHYAFQDENYLYLVMDYYVGGDLLTLLSKFEDkLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNV-LLDM 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 161 NipiPHIKLIDFGLAHEI-EDG-VEFKNIFGTPEFVAPEIVNYEPLGL-----EADMWSIGVITYILLSGASPFLGDTKQ 233
Cdd:cd05624   209 N---GHIRLADFGSCLKMnDDGtVQSSVAVGTPDYISPEILQAMEDGMgkygpECDWWSLGVCMYEMLYGETPFYAESLV 285
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2056392213 234 ETLANITavsyDFDEEF-----FSQTSELAKDFIRKLLVKETRK--RLTIQEALRHPWITPVDnqqamvrRESVVNLE 304
Cdd:cd05624   286 ETYGKIM----NHEERFqfpshVTDVSEEAKDLIQRLICSRERRlgQNGIEDFKKHAFFEGLN-------WENIRNLE 352
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
29-228 3.53e-28

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: 112.70  E-value: 3.53e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRrgvsrEEIEREVSILRQVLHHNVITLHDVYENRTDVV-----LIL 103
Cdd:cd14039     1 LGTGGFGNVCLYQNQETGEKIAIKSCRLELSVKNK-----DRWCHEIQIMKKLNHPNVVKACDVPEEMNFLVndvplLAM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 104 ELVSGGELFDFLAQKES---LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHiKLIDFGLAHEIED 180
Cdd:cd14039    76 EYCSGGDLRKLLNKPENccgLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEINGKIVH-KIIDLGYAKDLDQ 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2056392213 181 GVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFL 228
Cdd:cd14039   155 GSLCTSFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFRPFL 202
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
23-285 3.87e-28

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: 111.88  E-value: 3.87e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRqsRASRRGVSREeIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd14164     2 YTLGTTIGEGSFSKVKLATSQKYCCKVAIKIVDRR--RASPDFVQKF-LPRELSILRRVNHPNIVQMFECIEVANGRLYI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipiPHIKLIDFGLAHEIEDGV 182
Cdd:cd14164    79 VMEAAATDLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADD---RKIKIADFGFARFVEDYP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 183 EFKNIF-GTPEFVAPEIVN---YEPLGLeaDMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFfsqtSELA 258
Cdd:cd14164   156 ELSTTFcGSRAYTPPEVILgtpYDPKKY--DVWSLGVVLYVMVTGTMPFDETNVRRLRLQQRGVLYPSGVAL----EEPC 229
                         250       260
                  ....*....|....*....|....*..
gi 2056392213 259 KDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14164   230 RALIRTLLQFNPSTRPSIQQVAGNSWL 256
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
29-274 4.79e-28

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: 113.55  E-value: 4.79e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSrasrrgVSREEIE---REVSILRQVLHHNVIT-LHDVYENRTDVVLILE 104
Cdd:cd05615    18 LGKGSFGKVMLAERKGSDELYAIKILKKDVV------IQDDDVEctmVEKRVLALQDKPPFLTqLHSCFQTVDRLYFVME 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 105 LVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHE-IEDGVE 183
Cdd:cd05615    92 YVNGGDLMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEG----HIKIADFGMCKEhMVEGVT 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 184 FKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITA--VSYDfdeeffSQTSELAKDF 261
Cdd:cd05615   168 TRTFCGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEhnVSYP------KSLSKEAVSI 241
                         250
                  ....*....|...
gi 2056392213 262 IRKLLVKETRKRL 274
Cdd:cd05615   242 CKGLMTKHPAKRL 254
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
27-283 7.59e-28

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: 110.94  E-value: 7.59e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFAIVKKCREKSTGLEYAAKfikkrQSRASRRGVS-REEIEREVSILRQVLHH-NVITLHDVYENRTDVVLILE 104
Cdd:cd13997     6 EQIGSGSFSEVFKVRSKVDGCLYAVK-----KSKKPFRGPKeRARALREVEAHAALGQHpNIVRYYSSWEEGGHLYIQME 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 105 LVSGGELFDFLA---QKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIEDG 181
Cdd:cd13997    81 LCENGSLQDALEelsPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGT----CKIGDFGLATRLETS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 182 VEFKNifGTPEFVAPEIVN--YEPLGlEADMWSIGVITYILLSGAS-PFLGDTKQETLANITAvsydfDEEFFSQTSELa 258
Cdd:cd13997   157 GDVEE--GDSRYLAPELLNenYTHLP-KADIFSLGVTVYEAATGEPlPRNGQQWQQLRQGKLP-----LPPGLVLSQEL- 227
                         250       260
                  ....*....|....*....|....*
gi 2056392213 259 KDFIRKLLVKETRKRLTIQEALRHP 283
Cdd:cd13997   228 TRLLKVMLDPDPTRRPTADQLLAHD 252
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
19-287 8.37e-28

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: 112.65  E-value: 8.37e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  19 VEDFYDIGEELGSGQFAIVKKCREKSTGLEYAakfIKK------RQSRASRrgvsreeIEREVSILRQVLHH-NVITLHD 91
Cdd:cd07852     5 ILRRYEILKKLGKGAYGIVWKAIDKKTGEVVA---LKKifdafrNATDAQR-------TFREIMFLQELNDHpNIIKLLN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  92 VY--ENRTDVVLIlelvsggelFDFLaqkeslsEEEATSFIK--------------QILDGVNYLHTKKIAHFDLKPENI 155
Cdd:cd07852    75 VIraENDKDIYLV---------FEYM-------ETDLHAVIRaniledihkqyimyQLLKALKYLHSGGVIHRDLKPSNI 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 156 mLLDKNIpipHIKLIDFGLAHEIEDGVEFKNIFGTPEFVA------PEIVnyepLGLEA-----DMWSIGVITYILLSG- 223
Cdd:cd07852   139 -LLNSDC---RVKLADFGLARSLSQLEEDDENPVLTDYVAtrwyraPEIL----LGSTRytkgvDMWSVGCILGEMLLGk 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 224 ------------------------------ASPFlGDTKQETLANITAVSYDfdeEFFSQTSELAKDFIRKLLVKETRKR 273
Cdd:cd07852   211 plfpgtstlnqlekiievigrpsaediesiQSPF-AATMLESLPPSRPKSLD---ELFPKASPDALDLLKKLLVFNPNKR 286
                         330
                  ....*....|....
gi 2056392213 274 LTIQEALRHPWITP 287
Cdd:cd07852   287 LTAEEALRHPYVAQ 300
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
29-233 9.60e-28

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: 110.62  E-value: 9.60e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRgvsrEEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSG 108
Cdd:cd13978     1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNCIEER----KALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMEN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 109 GELfdflaqkESLSEEEATS--------FIKQILDGVNYLH--TKKIAHFDLKPENImLLDKNIpipHIKLIDFGLA--- 175
Cdd:cd13978    77 GSL-------KSLLEREIQDvpwslrfrIIHEIALGMNFLHnmDPPLLHHDLKPENI-LLDNHF---HVKISDFGLSklg 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2056392213 176 ---HEIEDGVEFKNIFGTPEFVAPEI---VNYEPlGLEADMWSIGVITYILLSGASPFLGDTKQ 233
Cdd:cd13978   146 mksISANRRRGTENLGGTPIYMAPEAfddFNKKP-TSKSDVYSFAIVIWAVLTRKEPFENAINP 208
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
18-289 1.04e-27

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: 113.20  E-value: 1.04e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  18 KVEDFyDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKR--QSRASRRGVSREEierevSILRQVLHHNVITLHDVYEN 95
Cdd:cd05600     9 KLSDF-QILTQVGQGGYGSVFLARKKDTGEICALKIMKKKvlFKLNEVNHVLTER-----DILTTTNSPWLVKLLYAFQD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  96 RTDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENiMLLDKNipiPHIKLIDFGLA 175
Cdd:cd05600    83 PENVYLAMEYVPGGDFRTLLNNSGILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPEN-FLIDSS---GHIKLTDFGLA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 176 HEI--------------------------------------EDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVIT 217
Cdd:cd05600   159 SGTlspkkiesmkirleevkntafleltakerrniyramrkEDQNYANSVVGSPDYMAPEVLRGEGYDLTVDYWSLGCIL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 218 YILLSGASPFLGDTKQETLANIT--------AVSYDFDEEFFsqTSELAKDFIRKLLVKETRKRLTIQEALRHPWITPVD 289
Cdd:cd05600   239 FECLVGFPPFSGSTPNETWANLYhwkktlqrPVYTDPDLEFN--LSDEAWDLITKLITDPQDRLQSPEQIKNHPFFKNID 316
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
29-312 1.33e-27

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: 111.92  E-value: 1.33e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSrasrrgVSREEIE---REVSILRQVLHHNVIT-LHDVYENRTDVVLILE 104
Cdd:cd05590     3 LGKGSFGKVMLARLKESGRLYAVKVLKKDVI------LQDDDVEctmTEKRILSLARNHPFLTqLYCCFQTPDRLFFVME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 105 LVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAHE-IEDGVE 183
Cdd:cd05590    77 FVNGGDLMFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNV-LLDHE---GHCKLADFGMCKEgIFNGKT 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 184 FKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAvsydfDEEFFSQ-TSELAKDFI 262
Cdd:cd05590   153 TSTFCGTPDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILN-----DEVVYPTwLSQDAVDIL 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2056392213 263 RKLLVKETRKRLTI-----QEA-LRHPWITPVD----NQQAMV-----RRESVVNLENFRKQYVR 312
Cdd:cd05590   228 KAFMTKNPTMRLGSltlggEEAiLRHPFFKELDweklNRRQIEppfrpRIKSREDVSNFDPDFIK 292
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
29-312 1.34e-27

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: 111.51  E-value: 1.34e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSrasrrgVSREEIER---EVSILRQVLHHNVITLHDVYENRTDVVLILEL 105
Cdd:cd05585     2 IGKGSFGKVMQVRKKDTSRIYALKTIRKAHI------VSRSEVTHtlaERTVLAQVDCPFIVPLKFSFQSPEKLYLVLAF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 106 VSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAHEIEDGVEFK 185
Cdd:cd05585    76 INGGELFHHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENI-LLDYT---GHIALCDFGLCKLNMKDDDKT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 186 NIF-GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQtselAKDFIRK 264
Cdd:cd05585   152 NTFcGTPEYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQEPLRFPDGFDRD----AKDLLIG 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 265 LLVKETRKRLTI---QEALRHPWITPVDNQQAMVRR---------ESVVNLENFRKQYVR 312
Cdd:cd05585   228 LLNRDPTKRLGYngaQEIKNHPFFDQIDWKRLLMKKiqppfkpavENAIDTSNFDEEFTR 287
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
29-284 2.40e-27

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: 109.72  E-value: 2.40e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQsrasrrgVSREEIEREVSILRQV-LHHNVITLHDVY-ENRTDVVLILELV 106
Cdd:cd13987     1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPS-------TKLKDFLREYNISLELsVHPHIIKTYDVAfETEDYYVFAQEYA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 107 SGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipIPHIKLIDFGLAHEIEDGVEFKN 186
Cdd:cd13987    74 PYGDLFSIIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKD--CRRVKLCDFGLTRRVGSTVKRVS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 187 ifGTPEFVAPE---IVNYEPLGLE--ADMWSIGVITYILLSGASPFlgdtkQEtlanitAVSYD-FDEEF---------- 250
Cdd:cd13987   152 --GTIPYTAPEvceAKKNEGFVVDpsIDVWAFGVLLFCCLTGNFPW-----EK------ADSDDqFYEEFvrwqkrknta 218
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2056392213 251 ----FSQTSELAKDFIRKLLVKETRKRLTIQEALR---HPW 284
Cdd:cd13987   219 vpsqWRRFTPKALRMFKKLLAPEPERRCSIKEVFKylgDRW 259
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
25-239 2.50e-27

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: 109.56  E-value: 2.50e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213   25 IGEELGSGQFAIVKKCR----EKSTGLEYAAKFIKKRQSRASRrgvsrEEIEREVSILRQVLHHNVITLHDVYENRTDVV 100
Cdd:smart00221   3 LGKKLGEGAFGEVYKGTlkgkGDGKEVEVAVKTLKEDASEQQI-----EEFLREARIMRKLDHPNIVKLLGVCTEEEPLM 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  101 LILELVSGGELFDFL--AQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEI 178
Cdd:smart00221  78 IVMEYMPGGDLLDYLrkNRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLV----VKISDFGLSRDL 153
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2056392213  179 EDGVEFKnIFGTPEFV---APEIVNYEPLGLEADMWSIGVITYILLS-GASPFLGDTKQETLANI 239
Cdd:smart00221 154 YDDDYYK-VKGGKLPIrwmAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEEPYPGMSNAEVLEYL 217
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
23-280 2.66e-27

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: 109.67  E-value: 2.66e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAakfIKKRQSRASRRGVSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd08224     2 YEIEKKIGKGQFSVVYRARCLLDGRLVA---LKKVQIFEMMDAKARQDCLKEIDLLQQLNHPNIIKYLASFIENNELNIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELF----DFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEI 178
Cdd:cd08224    79 LELADAGDLSrlikHFKKQKRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGV----VKLGDLGLGRFF 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 179 -EDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQ--ETLANITAVSYD-FDEEFFSQt 254
Cdd:cd08224   155 sSKTTAAHSLVGTPYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFYGEKMNlySLCKKIEKCEYPpLPADLYSQ- 233
                         250       260
                  ....*....|....*....|....*.
gi 2056392213 255 sELaKDFIRKLLVKETRKRLTIQEAL 280
Cdd:cd08224   234 -EL-RDLVAACIQPDPEKRPDISYVL 257
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
20-286 2.98e-27

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: 109.36  E-value: 2.98e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  20 EDFYDIGEeLGSGQFAIVKKCREKSTGLEYAAKFIkkrqsRASRRGVSREEIEREVSILRQVLHHNVITLHDVYENRTDV 99
Cdd:cd06605     1 DDLEYLGE-LGEGNGGVVSKVRHRPSGQIMAVKVI-----RLEIDEALQKQILRELDVLHKCNSPYIVGFYGAFYSEGDI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 100 VLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTK-KIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEI 178
Cdd:cd06605    75 SICMEYMDGGSLDKILKEVGRIPERILGKIAVAVVKGLIYLHEKhKIIHRDVKPSNILVNSRG----QVKLCDFGVSGQL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 179 EDGVEfKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEE--------F 250
Cdd:cd06605   151 VDSLA-KTFVGTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGRFPYPPPNAKPSMMIFELLSYIVDEPppllpsgkF 229
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2056392213 251 fsqtSELAKDFIRKLLVKETRKRLTIQEALRHPWIT 286
Cdd:cd06605   230 ----SPDFQDFVSQCLQKDPTERPSYKELMEHPFIK 261
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
10-285 3.16e-27

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 109.56  E-value: 3.16e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  10 NMEPFKQQKVEDfydigeelgsGQFAIVKKCREKSTGLEYAAKFIKKRQSRAsrrgvsreeIEREVSILRQVlHHNVITL 89
Cdd:PHA03390   15 NCEIVKKLKLID----------GKFGKVSVLKHKPTQKLFVQKIIKAKNFNA---------IEPMVHQLMKD-NPNFIKL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  90 HDVYENRTDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipiPHIKL 169
Cdd:PHA03390   75 YYSVTTLKGHVLIMDYIKDGDLFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDRAK---DRIYL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 170 IDFGLAHEI-----EDgvefknifGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSY 244
Cdd:PHA03390  152 CDYGLCKIIgtpscYD--------GTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFKEDEDEELDLESLLKRQ 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2056392213 245 DFDEEFFSQTSELAKDFIRKLLVKETRKRL-TIQEALRHPWI 285
Cdd:PHA03390  224 QKKLPFIKNVSKNANDFVQSMLKYNINYRLtNYNEIIKHPFL 265
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
18-284 3.23e-27

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: 111.28  E-value: 3.23e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  18 KVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKfikkRQSRASRRGVSREEIEREVSILRQVLHHNVITLHDVY---- 93
Cdd:cd07877    14 EVPERYQNLSPVGSGAYGSVCAAFDTKTGLRVAVK----KLSRPFQSIIHAKRTYRELRLLKHMKHENVIGLLDVFtpar 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  94 --ENRTDVVLILELVsGGELFDfLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLID 171
Cdd:cd07877    90 slEEFNDVYLVTHLM-GADLNN-IVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDC----ELKILD 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 172 FGLAHEIEDgvEFKNIFGTPEFVAPEI-VNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANI----------- 239
Cdd:cd07877   164 FGLARHTDD--EMTGYVATRWYRAPEImLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLIlrlvgtpgael 241
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2056392213 240 -------TAVSY----------DFdEEFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd07877   242 lkkisseSARNYiqsltqmpkmNF-ANVFIGANPLAVDLLEKMLVLDSDKRITAAQALAHAY 302
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
29-316 4.48e-27

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: 110.91  E-value: 4.48e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVkkCREKSTGLEyaAKFIKKRQSRASRRGVSREEIEREVSILRQVLHHNVITLHDVY------ENRTDVVLI 102
Cdd:cd07878    23 VGSGAYGSV--CSAYDTRLR--QKVAVKKLSRPFQSLIHARRTYRELRLLKHMKHENVIGLLDVFtpatsiENFNEVYLV 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVsGGELFDfLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIEDgv 182
Cdd:cd07878    99 TNLM-GADLNN-IVKCQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDC----ELRILDFGLARQADD-- 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 183 EFKNIFGTPEFVAPEI-VNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSE----- 256
Cdd:cd07878   171 EMTGYVATRWYRAPEImLNWMHYNQTVDIWSVGCIMAELLKGKALFPGNDYIDQLKRIMEVVGTPSPEVLKKISSehark 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 257 ----------------------LAKDFIRKLLVKETRKRLTIQEALRHPWIT----PVDNQQAMVRRESVVNlenfrKQY 310
Cdd:cd07878   251 yiqslphmpqqdlkkifrganpLAIDLLEKMLVLDSDKRISASEALAHPYFSqyhdPEDEPEAEPYDESPEN-----KER 325

                  ....*.
gi 2056392213 311 VRRRWK 316
Cdd:cd07878   326 TIEEWK 331
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
18-285 4.93e-27

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: 110.53  E-value: 4.93e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  18 KVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIkkrqSRASRRGVSREEIEREVSILRQVLHHNVITLHDV----- 92
Cdd:cd07855     2 DVGDRYEPIETIGSGAYGVVCSAIDTKSGQKVAIKKI----PNAFDVVTTAKRTLRELKILRHFKHDNIIAIRDIlrpkv 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  93 -YENRTDVVLILELVSGgELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENiMLLDKNIpipHIKLID 171
Cdd:cd07855    78 pYADFKDVYVVLDLMES-DLHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSN-LLVNENC---ELKIGD 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 172 FGLAHEIEDGVEFKNIFGTpEFV------APEIVNYEPLGLEA-DMWSIG------VITYILLSGASP---------FLG 229
Cdd:cd07855   153 FGMARGLCTSPEEHKYFMT-EYVatrwyrAPELMLSLPEYTQAiDMWSVGcifaemLGRRQLFPGKNYvhqlqliltVLG 231
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2056392213 230 DTKQ---------------ETLANITAVSYDfdeEFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd07855   232 TPSQavinaigadrvrryiQNLPNKQPVPWE---TLYPKADQQALDLLSQMLRFDPSERITVAEALQHPFL 299
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
29-228 1.16e-26

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: 108.51  E-value: 1.16e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKfiKKRQSRASRrgvSREEIEREVSILRQVLHHNVITLHDVYENRTDV------VLI 102
Cdd:cd14038     2 LGTGGFGNVLRWINQETGEQVAIK--QCRQELSPK---NRERWCLEIQIMKRLNHPNVVAARDVPEGLQKLapndlpLLA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQKES---LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHiKLIDFGLAHEIE 179
Cdd:cd14038    77 MEYCQGGDLRKYLNQFENccgLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQGEQRLIH-KIIDLGYAKELD 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2056392213 180 DGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFL 228
Cdd:cd14038   156 QGSLCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPFL 204
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
28-286 1.34e-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: 108.57  E-value: 1.34e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  28 ELGSGQFAIVKKCREKSTGLEYAakfIKKRQSRASRRgvsREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVS 107
Cdd:cd06657    27 KIGEGSTGIVCIATVKSSGKLVA---VKKMDLRKQQR---RELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLE 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 108 GGELFDFLAQKEsLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIEDGVEF-KN 186
Cdd:cd06657   101 GGALTDIVTHTR-MNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDG----RVKLSDFGFCAQVSKEVPRrKS 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 187 IFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAvSYDFDEEFFSQTSELAKDFIRKLL 266
Cdd:cd06657   176 LVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRD-NLPPKLKNLHKVSPSLKGFLDRLL 254
                         250       260
                  ....*....|....*....|
gi 2056392213 267 VKETRKRLTIQEALRHPWIT 286
Cdd:cd06657   255 VRDPAQRATAAELLKHPFLA 274
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
27-284 1.49e-26

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: 108.15  E-value: 1.49e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRasrRGVSREEIeREVSILRQVLHHNVITLHDVY--ENRtdvvliLE 104
Cdd:cd07835     5 EKIGEGTYGVVYKARDKLTGEIVALKKIRLETED---EGVPSTAI-REISLLKELNHPNIVRLLDVVhsENK------LY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 105 LVsggelFDFLAQ----------KESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGL 174
Cdd:cd07835    75 LV-----FEFLDLdlkkymdsspLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGA----LKLADFGL 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 175 AHeiedgvefknIFGTP------EFV-----APEIVnyepLGLE-----ADMWSIGVITYILLSGASPFLGDTKQETLAN 238
Cdd:cd07835   146 AR----------AFGVPvrtythEVVtlwyrAPEIL----LGSKhystpVDIWSVGCIFAEMVTRRPLFPGDSEIDQLFR 211
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2056392213 239 I------------TAVSY--DFDEEF-----------FSQTSELAKDFIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd07835   212 IfrtlgtpdedvwPGVTSlpDYKPTFpkwarqdlskvVPSLDEDGLDLLSQMLVYDPAKRISAKAALQHPY 282
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
12-289 1.58e-26

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: 110.49  E-value: 1.58e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  12 EPF----KQQKV--EDFyDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQS-RASRRGVSREEierevsilRQVLHH 84
Cdd:cd05623    58 KPFtskvKQMRLhkEDF-EILKVIGRGAFGEVAVVKLKNADKVFAMKILNKWEMlKRAETACFREE--------RDVLVN 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  85 N----VITLHDVYENRTDVVLILELVSGGELFDFLAQKES-LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLD 159
Cdd:cd05623   129 GdsqwITTLHYAFQDDNNLYLVMDYYVGGDLLTLLSKFEDrLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNI-LMD 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 160 KNipiPHIKLIDFGLAHEI-EDG-VEFKNIFGTPEFVAPEIVN--------YEPlglEADMWSIGVITYILLSGASPFLG 229
Cdd:cd05623   208 MN---GHIRLADFGSCLKLmEDGtVQSSVAVGTPDYISPEILQamedgkgkYGP---ECDWWSLGVCMYEMLYGETPFYA 281
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2056392213 230 DTKQETLANITAVSYDFdeEFFSQ---TSELAKDFIRKLLVKETRK--RLTIQEALRHPWITPVD 289
Cdd:cd05623   282 ESLVETYGKIMNHKERF--QFPTQvtdVSENAKDLIRRLICSREHRlgQNGIEDFKNHPFFVGID 344
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
29-289 1.69e-26

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: 108.81  E-value: 1.69e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSrasrrgVSREEIER---EVSILRQVLHHN---VITLHDVYENRTDVVLI 102
Cdd:cd05586     1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVI------VAKKEVAHtigERNILVRTALDEspfIVGLKFSFQTPTDLYLV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAHEIEDGV 182
Cdd:cd05586    75 TDYMSGGELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENI-LLDAN---GHIALCDFGLSKADLTDN 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 183 EFKNIF-GTPEFVAPEIVNYEP-LGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTselAKD 260
Cdd:cd05586   151 KTTNTFcGTTEYLAPEVLLDEKgYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIAFGKVRFPKDVLSDE---GRS 227
                         250       260       270
                  ....*....|....*....|....*....|...
gi 2056392213 261 FIRKLLVKETRKRL----TIQEALRHPWITPVD 289
Cdd:cd05586   228 FVKGLLNRNPKHRLgahdDAVELKEHPFFADID 260
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
27-309 2.01e-26

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: 107.89  E-value: 2.01e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFAIVKKCREKSTGLEYAAKFIkkrqSRASRRGVSREeIEREVSILRQVLHHNVITLHDVY--ENRTDVVLILE 104
Cdd:cd06621     7 SSLGEGAGGSVTKCRLRNTKTIFALKTI----TTDPNPDVQKQ-ILRELEINKSCASPYIVKYYGAFldEQDSSIGIAME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 105 LVSGGEL----FDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIED 180
Cdd:cd06621    82 YCEGGSLdsiyKKVKKKGGRIGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKG----QVKLCDFGVSGELVN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 181 GVEfKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQeTLANITAVSY----------DfDEEF 250
Cdd:cd06621   158 SLA-GTFTGTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPFPPEGEP-PLGPIELLSYivnmpnpelkD-EPEN 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2056392213 251 FSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWITPVDNQQamvrresvVNLENFRKQ 309
Cdd:cd06621   235 GIKWSESFKDFIEKCLEKDGTRRPGPWQMLAHPWIKAQEKKK--------VNMAKFVKQ 285
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
21-285 2.21e-26

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: 107.97  E-value: 2.21e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  21 DFYDIGEELGSGQFAIVKKCREKSTGLEYAakfIKKRQSRASRRGVSREEIeREVSILRQVLHHNVITLHDVYENRTDVV 100
Cdd:cd07864     7 DKFDIIGIIGEGTYGQVYKAKDKDTGELVA---LKKVRLDNEKEGFPITAI-REIKILRQLNHRSVVNLKEIVTDKQDAL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 101 ----------LILELVSggelFDFLAQKES----LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipH 166
Cdd:cd07864    83 dfkkdkgafyLVFEYMD----HDLMGLLESglvhFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKG----Q 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 167 IKLIDFGLA--HEIEDGVEFKNIFGTPEFVAPE-IVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANIT--- 240
Cdd:cd07864   155 IKLADFGLArlYNSEESRPYTNKVITLWYRPPElLLGEERYGPAIDVWSCGCILGELFTKKPIFQANQELAQLELISrlc 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2056392213 241 -----AVSYDFDE------------------EFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd07864   235 gspcpAVWPDVIKlpyfntmkpkkqyrrrlrEEFSFIPTPALDLLDHMLTLDPSKRCTAEQALNSPWL 302
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
23-285 2.23e-26

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: 106.98  E-value: 2.23e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKrqSRASRRG--VSREEIEREVSILRQVLH--HNVITLHDVYENRTD 98
Cdd:cd14100     2 YQVGPLLGSGGFGSVYSGIRVADGAPVAIKHVEK--DRVSEWGelPNGTRVPMEIVLLKKVGSgfRGVIRLLDWFERPDS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  99 VVLILELVSG-GELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLldkNIPIPHIKLIDFGLAHE 177
Cdd:cd14100    80 FVLVLERPEPvQDLFDFITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILI---DLNTGELKLIDFGSGAL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 178 IEDGVeFKNIFGTPEFVAPEIVNYEPL-GLEADMWSIGVITYILLSGASPFLGDtkQETLANitavsydfdEEFFSQ-TS 255
Cdd:cd14100   157 LKDTV-YTDFDGTRVYSPPEWIRFHRYhGRSAAVWSLGILLYDMVCGDIPFEHD--EEIIRG---------QVFFRQrVS 224
                         250       260       270
                  ....*....|....*....|....*....|
gi 2056392213 256 ELAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14100   225 SECQHLIKWCLALRPSDRPSFEDIQNHPWM 254
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
23-284 2.60e-26

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: 108.42  E-value: 2.60e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIK--KRQSRASRrgvsreeIEREVsiLRQVLH------HNVITLHDVYE 94
Cdd:cd14134    14 YKILRLLGEGTFGKVLECWDRKRKRYVAVKIIRnvEKYREAAK-------IEIDV--LETLAEkdpngkSHCVQLRDWFD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  95 NRTDVVLILELVsGGELFDFLAQK--ESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLD------------- 159
Cdd:cd14134    85 YRGHMCIVFELL-GPSLYDFLKKNnyGPFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLVDsdyvkvynpkkkr 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 160 -KNIPI-PHIKLIDFGLAheiedgvEFKN-----IFGTPEFVAPEIVnyepLGL----EADMWSIGVITYILLSGASPFl 228
Cdd:cd14134   164 qIRVPKsTDIKLIDFGSA-------TFDDeyhssIVSTRHYRAPEVI----LGLgwsyPCDVWSIGCILVELYTGELLF- 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 229 gDTKQ--ETLA-----------NITAVSYDFDEEFFSQTSELAK--------------------------------DFIR 263
Cdd:cd14134   232 -QTHDnlEHLAmmerilgplpkRMIRRAKKGAKYFYFYHGRLDWpegsssgrsikrvckplkrlmllvdpehrllfDLIR 310
                         330       340
                  ....*....|....*....|.
gi 2056392213 264 KLLVKETRKRLTIQEALRHPW 284
Cdd:cd14134   311 KMLEYDPSKRITAKEALKHPF 331
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
23-285 3.52e-26

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: 106.47  E-value: 3.52e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVSREEIEREVSILRQVL----HHNVITLHDVYENRTD 98
Cdd:cd14101     2 YTMGNLLGKGGFGTVYAGHRISDGLQVAIKQISRNRVQQWSKLPGVNPVPNEVALLQSVGggpgHRGVIRLLDWFEIPEG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  99 VVLILEL-VSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLldkNIPIPHIKLIDFGLAHE 177
Cdd:cd14101    82 FLLVLERpQHCQDLFDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILV---DLRTGDIKLIDFGSGAT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 178 IEDGVeFKNIFGTPEFVAPEIVNYEPL-GLEADMWSIGVITYILLSGASPFLGDTkqetlaNITAVSYdfdeEFFSQTSE 256
Cdd:cd14101   159 LKDSM-YTDFDGTRVYSPPEWILYHQYhALPATVWSLGILLYDMVCGDIPFERDT------DILKAKP----SFNKRVSN 227
                         250       260
                  ....*....|....*....|....*....
gi 2056392213 257 LAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14101   228 DCRSLIRSCLAYNPSDRPSLEQILLHPWM 256
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
27-284 3.92e-26

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: 107.40  E-value: 3.92e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFAIVKKCREKSTGLEYAAKFIKKRQsrasRRGVSREEIeREVSILRQVLHHNVITLHDVYENRTDVVLILELV 106
Cdd:cd07873     8 DKLGEGTYATVYKGRSKLTDNLVALKEIRLEH----EEGAPCTAI-REVSLLKDLKHANIVTLHDIIHTEKSLTLVFEYL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 107 SGgELFDFLAQ-KESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIEDGVE-F 184
Cdd:cd07873    83 DK-DLKQYLDDcGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERG----ELKLADFGLARAKSIPTKtY 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 185 KNIFGTPEFVAPEI-VNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETL-------------------ANITAVSY 244
Cdd:cd07873   158 SNEVVTLWYRPPDIlLGSTDYSTQIDMWGVGCIFYEMSTGRPLFPGSTVEEQLhfifrilgtpteetwpgilSNEEFKSY 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2056392213 245 DFD----EEFFSQTSELAKD---FIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd07873   238 NYPkyraDALHNHAPRLDSDgadLLSKLLQFEGRKRISAEEAMKHPY 284
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
22-274 4.96e-26

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: 106.53  E-value: 4.96e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  22 FYDIgEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRaSRRGVSREEIEREvsILRQVLHHNVITLHDVYENRTDVVL 101
Cdd:cd05607     4 FYEF-RVLGKGGFGEVCAVQVKNTGQMYACKKLDKKRLK-KKSGEKMALLEKE--ILEKVNSPFIVSLAYAFETKTHLCL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 102 ILELVSGGEL--FDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIE 179
Cdd:cd05607    80 VMSLMNGGDLkyHIYNVGERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNG----NCRLSDLGLAVEVK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 180 DGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLG--------DTKQETLANITAVSYD-FDEEf 250
Cdd:cd05607   156 EGKPITQRAGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFRDhkekvskeELKRRTLEDEVKFEHQnFTEE- 234
                         250       260
                  ....*....|....*....|....
gi 2056392213 251 fsqtselAKDFIRKLLVKETRKRL 274
Cdd:cd05607   235 -------AKDICRLFLAKKPENRL 251
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
29-285 5.80e-26

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: 105.59  E-value: 5.80e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRgvsrEEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSG 108
Cdd:cd08220     8 VGRGAYGTVYLCRRKDDNKLVIIKQIPVEQMTKEER----QAALNEVKVLSMLHHPNIIEYYESFLEDKALMIVMEYAPG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 109 GELFDFLAQK--ESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNIPIphIKLIDFGLAHEIEDGVEFKN 186
Cdd:cd08220    84 GTLFEYIQQRkgSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNI-LLNKKRTV--VKIGDFGISKILSSKSKAYT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 187 IFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQtsELaKDFIRKLL 266
Cdd:cd08220   161 VVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAFEAANLPALVLKIMRGTFAPISDRYSE--EL-RHLILSML 237
                         250
                  ....*....|....*....
gi 2056392213 267 VKETRKRLTIQEALRHPWI 285
Cdd:cd08220   238 HLDPNKRPTLSEIMAQPII 256
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
27-285 7.24e-26

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: 105.78  E-value: 7.24e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRasrrgvSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELV 106
Cdd:cd06647    13 EKIGQGASGTVYTAIDVATGQEVAIKQMNLQQQP------KKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 107 SGGELFDFLAQKeSLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIML-LDKNIpiphiKLIDFGLAHEIE-DGVEF 184
Cdd:cd06647    87 AGGSLTDVVTET-CMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLgMDGSV-----KLTDFGFCAQITpEQSKR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 185 KNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANI-TAVSYDFDEEffSQTSELAKDFIR 263
Cdd:cd06647   161 STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIaTNGTPELQNP--EKLSAIFRDFLN 238
                         250       260
                  ....*....|....*....|..
gi 2056392213 264 KLLVKETRKRLTIQEALRHPWI 285
Cdd:cd06647   239 RCLEMDVEKRGSAKELLQHPFL 260
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
27-284 9.40e-26

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: 105.64  E-value: 9.40e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFAIVKKCREKSTGLEYAAKFIKkrqsRASRRGVSREEIeREVSILRQVLHHNVITLHDVYENRTDVVLILELV 106
Cdd:cd07836     6 EKLGEGTYATVYKGRNRTTGEIVALKEIH----LDAEEGTPSTAI-REISLMKELKHENIVRLHDVIHTENKLMLVFEYM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 107 SGG--ELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIEDGVE- 183
Cdd:cd07836    81 DKDlkKYMDTHGVRGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRG----ELKLADFGLARAFGIPVNt 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 184 FKNIFGTPEFVAPEIVnyepLGLEA-----DMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSELA 258
Cdd:cd07836   157 FSNEVVTLWYRAPDVL----LGSRTystsiDIWSVGCIMAEMITGRPLFPGTNNEDQLLKIFRIMGTPTESTWPGISQLP 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2056392213 259 K-------------------------DFIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd07836   233 EykptfpryppqdlqqlfphadplgiDLLHRLLQLNPELRISAHDALQHPW 283
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
51-302 1.05e-25

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 108.95  E-value: 1.05e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  51 AKFIKKRQSRASRRGVSREEI---EREVSILRQVLH------HNVITLH-DVYENRTDVVLILELVSGGELFDFLAQ--K 118
Cdd:PTZ00267   82 AAFVATRGSDPKEKVVAKFVMlndERQAAYARSELHclaacdHFGIVKHfDDFKSDDKLLLIMEYGSGGDLNKQIKQrlK 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 119 ESL--SEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIEDGVEF---KNIFGTPEF 193
Cdd:PTZ00267  162 EHLpfQEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTGI----IKLGDFGFSKQYSDSVSLdvaSSFCGTPYY 237
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 194 VAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDfdeEFFSQTSELAKDFIRKLLVKETRKR 273
Cdd:PTZ00267  238 LAPELWERKRYSKKADMWSLGVILYELLTLHRPFKGPSQREIMQQVLYGKYD---PFPCPVSSGMKALLDPLLSKNPALR 314
                         250       260       270
                  ....*....|....*....|....*....|
gi 2056392213 274 LTIQEALRHPWITPVDNQ-QAMVRRESVVN 302
Cdd:PTZ00267  315 PTTQQLLHTEFLKYVANLfQDIVRHSETIS 344
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
23-287 1.61e-25

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: 106.23  E-value: 1.61e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIK--KRQSRASRrgvsreeIEREVSILRQVLHHNVITLHDV-----YEN 95
Cdd:cd07849     7 YQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKISpfEHQTYCLR-------TLREIKILLRFKHENIIGILDIqrpptFES 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  96 RTDVVLILELVSGgELFDFLAQkESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNIpipHIKLIDFGLA 175
Cdd:cd07849    80 FKDVYIVQELMET-DLYKLIKT-QHLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNL-LLNTNC---DLKICDFGLA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 176 hEIEDGVEFKNIFGTpEFVA------PEI-VNYEPLGLEADMWSIGVITYILLSGASPF---------------LGDTKQ 233
Cdd:cd07849   154 -RIADPEHDHTGFLT-EYVAtrwyraPEImLNSKGYTKAIDIWSVGCILAEMLSNRPLFpgkdylhqlnlilgiLGTPSQ 231
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2056392213 234 ETLANI---------------TAVSYDfdeEFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWITP 287
Cdd:cd07849   232 EDLNCIislkarnyikslpfkPKVPWN---KLFPNADPKALDLLDKMLTFNPHKRITVEEALAHPYLEQ 297
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
23-285 1.97e-25

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: 104.27  E-value: 1.97e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVSReeieREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd08225     2 YEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPVKEKEASK----KEVILLAKMKHPNIVTFFASFQENGRLFIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQKESL--SEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNIPIPhiKLIDFGLAHEIED 180
Cdd:cd08225    78 MEYCDGGDLMKRINRQRGVlfSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNI-FLSKNGMVA--KLGDFGIARQLND 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 181 GVEF-KNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANI-----TAVSYDFDEEFFSQT 254
Cdd:cd08225   155 SMELaYTCVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFEGNNLHQLVLKIcqgyfAPISPNFSRDLRSLI 234
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2056392213 255 SELAKdfirkllvKETRKRLTIQEALRHPWI 285
Cdd:cd08225   235 SQLFK--------VSPRDRPSITSILKRPFL 257
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
27-284 3.14e-25

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: 104.51  E-value: 3.14e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFAIVKKCREKSTGLEYAakfIKKRQSRASRRGVSREEIeREVSILRQVLHHNVITLHDVYENRTDVVLILELV 106
Cdd:cd07860     6 EKIGEGTYGVVYKARNKLTGEVVA---LKKIRLDTETEGVPSTAI-REISLLKELNHPNIVKLLDVIHTENKLYLVFEFL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 107 SGgELFDFL--AQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENiMLLDKNipiPHIKLIDFGLAHEIedGVEF 184
Cdd:cd07860    82 HQ-DLKKFMdaSALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQN-LLINTE---GAIKLADFGLARAF--GVPV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 185 KNIfgTPEFV-----APEIVnyepLGLE-----ADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQT 254
Cdd:cd07860   155 RTY--THEVVtlwyrAPEIL----LGCKyystaVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGV 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2056392213 255 SEL-------------------------AKDFIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd07860   229 TSMpdykpsfpkwarqdfskvvppldedGRDLLSQMLHYDPNKRISAKAALAHPF 283
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
18-284 3.19e-25

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: 104.32  E-value: 3.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  18 KVEDFYDIGEeLGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRasrrGVSREEIeREVSILRQVLHHNVITLHDVYENRT 97
Cdd:cd07871     3 KLETYVKLDK-LGEGTYATVFKGRSKLTENLVALKEIRLEHEE----GAPCTAI-REVSLLKNLKHANIVTLHDIIHTER 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  98 DVVLILELVSGgELFDFLAQKESL-SEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAH 176
Cdd:cd07871    77 CLTLVFEYLDS-DLKQYLDNCGNLmSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKG----ELKLADFGLAR 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 177 EIEDGVE-FKNIFGTPEFVAPEI-VNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETL------------------ 236
Cdd:cd07871   152 AKSVPTKtYSNEVVTLWYRPPDVlLGSTEYSTPIDMWGVGCILYEMATGRPMFPGSTVKEELhlifrllgtpteetwpgv 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2056392213 237 -ANITAVSYDFD----EEFFSQTSELAKD---FIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd07871   232 tSNEEFRSYLFPqyraQPLINHAPRLDTDgidLLSSLLLYETKSRISAEAALRHSY 287
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
20-286 3.58e-25

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: 103.98  E-value: 3.58e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  20 EDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRrgvsrEEIEREVSILRQVLHHNVITLHDVYENRTDV 99
Cdd:cd06642     3 EELFTKLERIGKGSFGEVYKGIDNRTKEVVAIKIIDLEEAEDEI-----EDIQQEITVLSQCDSPYITRYYGSYLKGTKL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 100 VLILELVSGGELFDFLaQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIE 179
Cdd:cd06642    78 WIIMEYLGGGSALDLL-KPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQG----DVKLADFGVAGQLT 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 180 DGVEFKNIF-GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFlgdTKQETLANITAVSYDFDEEFFSQTSELA 258
Cdd:cd06642   153 DTQIKRNTFvGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPN---SDLHPMRVLFLIPKNSPPTLEGQHSKPF 229
                         250       260
                  ....*....|....*....|....*...
gi 2056392213 259 KDFIRKLLVKETRKRLTIQEALRHPWIT 286
Cdd:cd06642   230 KEFVEACLNKDPRFRPTAKELLKHKFIT 257
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
27-241 3.62e-25

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: 103.77  E-value: 3.62e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFAIVKKCR---EKSTGLEYAAKFIKKRQSRASRrgvsrEEIEREVSILRQVLHHNVITLHDVYENRTDVVLIL 103
Cdd:cd00192     1 KKLGEGAFGEVYKGKlkgGDGKTVDVAVKTLKEDASESER-----KDFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 104 ELVSGGELFDFL---------AQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGL 174
Cdd:cd00192    76 EYMEGGDLLDFLrksrpvfpsPEPSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLV----VKISDFGL 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2056392213 175 AHEIEDGVEFKNIFGTPEFV---APEIVNYEPLGLEADMWSIGVITYILLS-GASPFLGDTKQETLANITA 241
Cdd:cd00192   152 SRDIYDDDYYRKKTGGKLPIrwmAPESLKDGIFTSKSDVWSFGVLLWEIFTlGATPYPGLSNEEVLEYLRK 222
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
23-283 7.07e-25

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: 103.35  E-value: 7.07e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAakfIKKrqsrasrrgV--SREEIEREVSILRQVLHHNVITLHDVY----ENR 96
Cdd:cd14137     6 YTIEKVIGSGSFGVVYQAKLLETGEVVA---IKK---------VlqDKRYKNRELQIMRRLKHPNIVKLKYFFyssgEKK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  97 TDVVLILELvsggE-----LFDFLAQKESLSEEEATSFIK----QILDGVNYLHTKKIAHFDLKPENIMLLDKNIpipHI 167
Cdd:cd14137    74 DEVYLNLVM----EympetLYRVIRHYSKNKQTIPIIYVKlysyQLFRGLAYLHSLGICHRDIKPQNLLVDPETG---VL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 168 KLIDFGLAHEIEDGVefKNIfgtPEFV-----APE-IVNYEPLGLEADMWSIG-VIT-----YILLSGASP--------- 226
Cdd:cd14137   147 KLCDFGSAKRLVPGE--PNV---SYICsryyrAPElIFGATDYTTAIDIWSAGcVLAelllgQPLFPGESSvdqlveiik 221
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2056392213 227 FLG-DTKQETLA-NITAVSYDFD-------EEFFSQ-TSELAKDFIRKLLVKETRKRLTIQEALRHP 283
Cdd:cd14137   222 VLGtPTREQIKAmNPNYTEFKFPqikphpwEKVFPKrTPPDAIDLLSKILVYNPSKRLTALEALAHP 288
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
21-285 7.71e-25

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: 103.17  E-value: 7.71e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  21 DFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSrasrrgvSREEIEREVSILRQVLHH-NVITLHDVYENRtDV 99
Cdd:cd06638    18 DTWEIIETIGKGTYGKVFKVLNKKNGSKAAVKILDPIHD-------IDEEIEAEYNILKALSDHpNVVKFYGMYYKK-DV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 100 V------LILELVSGGELFD----FLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKL 169
Cdd:cd06638    90 KngdqlwLVLELCNGGSVTDlvkgFLKRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEG----GVKL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 170 IDFGLAHEIEDGVEFKNI-FGTPEFVAPEIVNYE-----PLGLEADMWSIGvITYILLSGASPFLGD------------T 231
Cdd:cd06638   166 VDFGVSAQLTSTRLRRNTsVGTPFWMAPEVIACEqqldsTYDARCDVWSLG-ITAIELGDGDPPLADlhpmralfkiprN 244
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2056392213 232 KQETLANITAVSYDFDeeffsqtselakDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd06638   245 PPPTLHQPELWSNEFN------------DFIRKCLTKDYEKRPTVSDLLQHVFI 286
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
29-289 9.61e-25

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: 103.94  E-value: 9.61e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSrASRRGVSREEIEREvsILRQVLHHNVITLHDVYENRTDVVLILELVSG 108
Cdd:cd05598     9 IGVGAFGEVSLVRKKDTNALYAMKTLRKKDV-LKRNQVAHVKAERD--ILAEADNEWVVKLYYSFQDKENLYFVMDYIPG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 109 GELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGL-------------- 174
Cdd:cd05598    86 GDLMSLLIKKGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNI-LIDRD---GHIKLTDFGLctgfrwthdskyyl 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 175 AHeiedgvefkNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQT 254
Cdd:cd05598   162 AH---------SLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFLAQTPAETQLKVINWRTTLKIPHEANL 232
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2056392213 255 SELAKDFIRKLLVKETRK--RLTIQEALRHPWITPVD 289
Cdd:cd05598   233 SPEAKDLILRLCCDAEDRlgRNGADEIKAHPFFAGID 269
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
4-289 1.09e-24

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 103.91  E-value: 1.09e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213   4 ASMRSPNMEpfKQQKVEDFYDIgEELGSGQFAIVKKCREKSTglEYAAKFIKKRQSRASRRGVSREEIEREVSILRQVLH 83
Cdd:PTZ00426   16 DSTKEPKRK--NKMKYEDFNFI-RTLGTGSFGRVILATYKNE--DFPPVAIKRFEKSKIIKQKQVDHVFSERKILNYINH 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  84 HNVITLHDVYENRTDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENiMLLDKNip 163
Cdd:PTZ00426   91 PFCVNLYGSFKDESYLYLVLEFVIGGEFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPEN-LLLDKD-- 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 164 iPHIKLIDFGLAHEIEdgVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTK----QETLANI 239
Cdd:PTZ00426  168 -GFIKMTDFGFAKVVD--TRTYTLCGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPFYANEPlliyQKILEGI 244
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2056392213 240 TAVSYDFDEEffsqtselAKDFIRKLLVKETRKRL-----TIQEALRHPWITPVD 289
Cdd:PTZ00426  245 IYFPKFLDNN--------CKHLMKKLLSHDLTKRYgnlkkGAQNVKEHPWFGNID 291
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
27-285 1.36e-24

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: 102.88  E-value: 1.36e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRasrrgvSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELV 106
Cdd:cd06656    25 EKIGQGASGTVYTAIDIATGQEVAIKQMNLQQQP------KKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 107 SGGELFDFLAQKeSLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIML-LDKNIpiphiKLIDFGLAHEIE-DGVEF 184
Cdd:cd06656    99 AGGSLTDVVTET-CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLgMDGSV-----KLTDFGFCAQITpEQSKR 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 185 KNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLAnITAVSYDFDEEFFSQTSELAKDFIRK 264
Cdd:cd06656   173 STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALY-LIATNGTPELQNPERLSAVFRDFLNR 251
                         250       260
                  ....*....|....*....|.
gi 2056392213 265 LLVKETRKRLTIQEALRHPWI 285
Cdd:cd06656   252 CLEMDVDRRGSAKELLQHPFL 272
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
23-285 1.41e-24

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: 101.96  E-value: 1.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRqsRASRRG-VSREEIEREVSILRQV--LHHNVITLHDVYEnRTDV 99
Cdd:cd14102     2 YQVGSVLGSGGFGTVYAGSRIADGLPVAVKHVVKE--RVTEWGtLNGVMVPLEIVLLKKVgsGFRGVIKLLDWYE-RPDG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 100 VLIL----ELVSggELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipiPHIKLIDFGLA 175
Cdd:cd14102    79 FLIVmerpEPVK--DLFDFITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDLRT---GELKLIDFGSG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 176 HEIEDGVeFKNIFGTPEFVAPEIVNYEPL-GLEADMWSIGVITYILLSGASPFLGDtkQETLANITAvsydfdeeFFSQT 254
Cdd:cd14102   154 ALLKDTV-YTDFDGTRVYSPPEWIRYHRYhGRSATVWSLGVLLYDMVCGDIPFEQD--EEILRGRLY--------FRRRV 222
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2056392213 255 SELAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14102   223 SPECQQLIKWCLSLRPSDRPTLEQIFDHPWM 253
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
68-227 1.48e-24

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: 101.42  E-value: 1.48e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  68 REEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAH 147
Cdd:cd14059    25 RDEKETDIKHLRKLNHPNIIKFKGVCTQAPCYCILMEYCPYGQLYEVLRAGREITPSLLVDWSKQIASGMNYLHLHKIIH 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 148 FDLKPENIMLLDKNIpiphIKLIDFGLAHEIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPF 227
Cdd:cd14059   105 RDLKSPNVLVTYNDV----LKISDFGTSKELSEKSTKMSFAGTVAWMAPEVIRNEPCSEKVDIWSFGVVLWELLTGEIPY 180
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
26-286 2.34e-24

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: 101.35  E-value: 2.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  26 GEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVSREEIEREVSILRQVLHHNVI-----TLHDVYENrtdvv 100
Cdd:cd06630     5 GPLLGTGAFSSCYQARDVKTGTLMAVKQVSFCRNSSSEQEEVVEAIREEIRMMARLNHPNIVrmlgaTQHKSHFN----- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 101 LILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipIPHIKLIDFG----LAH 176
Cdd:cd06630    80 IFVEWMAGGSVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANL-LVDST--GQRLRIADFGaaarLAS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 177 EIEDGVEFK-NIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANI----TAVSYDFDEEFF 251
Cdd:cd06630   157 KGTGAGEFQgQLLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPWNAEKISNHLALIfkiaSATTPPPIPEHL 236
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2056392213 252 SQTSelaKDFIRKLLVKETRKRLTIQEALRHPWIT 286
Cdd:cd06630   237 SPGL---RDVTLRCLELQPEDRPPARELLKHPVFT 268
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
21-284 2.55e-24

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: 101.73  E-value: 2.55e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  21 DFYDIgEELGSGQFAIVKKCREKSTGlEYAAkfIKKRQSRASRRGVSREEIeREVSILRQVLHHNVITLHDVYENRTDVV 100
Cdd:cd07861     1 DYTKI-EKIGEGTYGVVYKGRNKKTG-QIVA--MKKIRLESEEEGVPSTAI-REISLLKELQHPNIVCLEDVLMQENRLY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 101 LILELVSGG--ELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEi 178
Cdd:cd07861    76 LVFEFLSMDlkKYLDSLPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGV----IKLADFGLARA- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 179 edgvefkniFGTP------EFV-----APEIVNYEPL-GLEADMWSIGVITYILLSGASPFLGDTKQETLANITAV---- 242
Cdd:cd07861   151 ---------FGIPvrvythEVVtlwyrAPEVLLGSPRySTPVDIWSIGTIFAEMATKKPLFHGDSEIDQLFRIFRIlgtp 221
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2056392213 243 ---------------------SYDFDEEFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd07861   222 tediwpgvtslpdykntfpkwKKGSLRTAVKNLDEDGLDLLEKMLIYDPAKRISAKKALVHPY 284
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
29-287 2.83e-24

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: 102.83  E-value: 2.83e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIkkrqSRASRRGVSREEIEREVSILRQVLHHNVITLHDVY-----ENRTDVVLIL 103
Cdd:cd07858    13 IGRGAYGIVCSAKNSETNEKVAIKKI----ANAFDNRIDAKRTLREIKLLRHLDHENVIAIKDIMppphrEAFNDVYIVY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 104 ELVSGgELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENiMLLDKNIpipHIKLIDFGLAHEIEDGVE 183
Cdd:cd07858    89 ELMDT-DLHQIIRSSQTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSN-LLLNANC---DLKICDFGLARTTSEKGD 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 184 FKNifgtpEFV------APE-IVNYEPLGLEADMWSIGVITYILLSGASPF---------------LGDTKQETLANIT- 240
Cdd:cd07858   164 FMT-----EYVvtrwyrAPElLLNCSEYTTAIDVWSVGCIFAELLGRKPLFpgkdyvhqlklitelLGSPSEEDLGFIRn 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2056392213 241 --AVSY----------DFdEEFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWITP 287
Cdd:cd07858   239 ekARRYirslpytprqSF-ARLFPHANPLAIDLLEKMLVFDPSKRITVEEALAHPYLAS 296
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
19-289 3.44e-24

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: 103.21  E-value: 3.44e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  19 VEDFYDIgEELGSGQFAIVKKCREKSTGLEYAAKFIKKrQSRASRRGVSREEIEREvsILRQVLHHNVITLHDVYENRTD 98
Cdd:cd05627     1 LDDFESL-KVIGRGAFGEVRLVQKKDTGHIYAMKILRK-ADMLEKEQVAHIRAERD--ILVEADGAWVVKMFYSFQDKRN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  99 VVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGL---- 174
Cdd:cd05627    77 LYLIMEFLPGGDMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKG----HVKLSDFGLctgl 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 175 --AHEIE----------DGVEFKNI--------------------FGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLS 222
Cdd:cd05627   153 kkAHRTEfyrnlthnppSDFSFQNMnskrkaetwkknrrqlaystVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLI 232
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2056392213 223 GASPFLGDTKQETLANIT--AVSYDFDEEFfsQTSELAKDFIRKLLVkETRKRL---TIQEALRHPWITPVD 289
Cdd:cd05627   233 GYPPFCSETPQETYRKVMnwKETLVFPPEV--PISEKAKDLILRFCT-DAENRIgsnGVEEIKSHPFFEGVD 301
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
21-285 3.98e-24

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: 100.95  E-value: 3.98e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  21 DFYDIGEE--LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASrrgvsrEEIEREVSILRQVLHHNVIT-LHDVYENrt 97
Cdd:cd06624     6 EYDESGERvvLGKGTFGVVYAARDLSTQVRIAIKEIPERDSREV------QPLHEEIALHSRLSHKNIVQyLGSVSED-- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  98 DVVLI-LELVSGGELFDFLAQK-ESLSEEEAT--SFIKQILDGVNYLHTKKIAHFDLKPENIMLldkNIPIPHIKLIDFG 173
Cdd:cd06624    78 GFFKIfMEQVPGGSLSALLRSKwGPLKDNENTigYYTKQILEGLKYLHDNKIVHRDIKGDNVLV---NTYSGVVKISDFG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 174 LAHEIEdGVE-----FKnifGTPEFVAPEIVNYEPLGL--EADMWSIGVITYILLSGASPF--LGDTKqetlANITAVS- 243
Cdd:cd06624   155 TSKRLA-GINpctetFT---GTLQYMAPEVIDKGQRGYgpPADIWSLGCTIIEMATGKPPFieLGEPQ----AAMFKVGm 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2056392213 244 YDFDEEFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd06624   227 FKIHPEIPESLSEEAKSFILRCFEPDPDKRATASDLLQDPFL 268
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
29-269 4.11e-24

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: 100.81  E-value: 4.11e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCReKSTGLEYAAKFIKKRqsrasRRGVSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSG 108
Cdd:cd14066     1 IGSGGFGTVYKGV-LENGTVVAVKRLNEM-----NCAASKKEFLTELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 109 GELFDFL-AQKES--LSEEEATSFIKQILDGVNYLHT---KKIAHFDLKPENImLLDKNiPIPhiKLIDFGLA---HEIE 179
Cdd:cd14066    75 GSLEDRLhCHKGSppLPWPQRLKIAKGIARGLEYLHEecpPPIIHGDIKSSNI-LLDED-FEP--KLTDFGLArliPPSE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 180 DGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITavsydfdEEFFSQTSELAK 259
Cdd:cd14066   151 SVSKTSAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVDENRENASRKDLV-------EWVESKGKEELE 223
                         250
                  ....*....|
gi 2056392213 260 DFIRKLLVKE 269
Cdd:cd14066   224 DILDKRLVDD 233
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
29-227 4.37e-24

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: 102.11  E-value: 4.37e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQsrasrrgVSREE----IEREVSILRQVLHHN-VITLHDVYENRTDVVLIL 103
Cdd:cd05588     3 IGRGSYAKVLMVELKKTKRIYAMKVIKKEL-------VNDDEdidwVQTEKHVFETASNHPfLVGLHSCFQTESRLFFVI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 104 ELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAHE-IEDGV 182
Cdd:cd05588    76 EFVNGGDLMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNV-LLDSE---GHIKLTDYGMCKEgLRPGD 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2056392213 183 EFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPF 227
Cdd:cd05588   152 TTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPF 196
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
23-285 4.62e-24

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: 100.87  E-value: 4.62e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQsrasrrGVSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd06646    11 YELIQRVGSGTYGDVYKARNLHTGELAAVKIIKLEP------GDDFSLIQQEIFMVKECKHCNIVAYFGSYLSREKLWIC 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIEDGV 182
Cdd:cd06646    85 MEYCGGGSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNG----DVKLADFGVAAKITATI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 183 -EFKNIFGTPEFVAPEIVNYEPLG---LEADMWSIGvITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQT--SE 256
Cdd:cd06646   161 aKRKSFIGTPYWMAPEVAAVEKNGgynQLCDIWAVG-ITAIELAELQPPMFDLHPMRALFLMSKSNFQPPKLKDKTkwSS 239
                         250       260
                  ....*....|....*....|....*....
gi 2056392213 257 LAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd06646   240 TFHNFVKISLTKNPKKRPTAERLLTHLFV 268
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
20-285 5.22e-24

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: 100.92  E-value: 5.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  20 EDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRrgvsrEEIEREVSILRQVLHHNVITLHDVYENRTDV 99
Cdd:cd06641     3 EELFTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEAEDEI-----EDIQQEITVLSQCDSPYVTKYYGSYLKDTKL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 100 VLILELVSGGELFDFLaQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIE 179
Cdd:cd06641    78 WIIMEYLGGGSALDLL-EPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHG----EVKLADFGVAGQLT 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 180 DGVEFKNIF-GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTselA 258
Cdd:cd06641   153 DTQIKRN*FvGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSELHPMKVLFLIPKNNPPTLEGNYSKP---L 229
                         250       260
                  ....*....|....*....|....*..
gi 2056392213 259 KDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd06641   230 KEFVEACLNKEPSFRPTAKELLKHKFI 256
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
27-285 6.21e-24

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


Pssm-ID: 132986 [Multi-domain]  Cd Length: 296  Bit Score: 100.95  E-value: 6.21e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFAIVKKCREKSTGLEYAAKFIK-KRQSRasrrgvsREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILEL 105
Cdd:cd06655    25 EKIGQGASGTVFTAIDVATGQEVAIKQINlQKQPK-------KELIINEILVMKELKNPNIVNFLDSFLVGDELFVVMEY 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 106 VSGGELFDFLAQKeSLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIE-DGVEF 184
Cdd:cd06655    98 LAGGSLTDVVTET-CMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDG----SVKLTDFGFCAQITpEQSKR 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 185 KNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLAnITAVSYDFDEEFFSQTSELAKDFIRK 264
Cdd:cd06655   173 STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALY-LIATNGTPELQNPEKLSPIFRDFLNR 251
                         250       260
                  ....*....|....*....|.
gi 2056392213 265 LLVKETRKRLTIQEALRHPWI 285
Cdd:cd06655   252 CLEMDVEKRGSAKELLQHPFL 272
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
18-283 6.35e-24

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: 102.07  E-value: 6.35e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  18 KVEDFyDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRqsrasrrgvsrEEIEREVSIL----RQVLHHN----VITL 89
Cdd:cd05596    24 NAEDF-DVIKVIGRGAFGEVQLVRHKSTKKVYAMKLLSKF-----------EMIKRSDSAFfweeRDIMAHAnsewIVQL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  90 HDVYENRTDVVLILELVSGGELFDFLAQKEsLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENiMLLDKNipiPHIKL 169
Cdd:cd05596    92 HYAFQDDKYLYMVMDYMPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDN-MLLDAS---GHLKL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 170 IDFGLAHEI-EDG-VEFKNIFGTPEFVAPEIVNYEP----LGLEADMWSIGVITYILLSGASPFLGDTKQETLANI---- 239
Cdd:cd05596   167 ADFGTCMKMdKDGlVRSDTAVGTPDYISPEVLKSQGgdgvYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYGKImnhk 246
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2056392213 240 TAVSYDFDEEFfsqtSELAKDFIRKLLVKETRK--RLTIQEALRHP 283
Cdd:cd05596   247 NSLQFPDDVEI----SKDAKSLICAFLTDREVRlgRNGIEEIKAHP 288
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
29-287 6.59e-24

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: 100.90  E-value: 6.59e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGlEYAAkfIKKRQSRASRRGVSREEIE----REVSILRQVLHHNVITLHDVYENRTDV-VLIL 103
Cdd:cd14040    14 LGRGGFSEVYKAFDLYEQ-RYAA--VKIHQLNKSWRDEKKENYHkhacREYRIHKELDHPRIVKLYDYFSLDTDTfCTVL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 104 ELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKK--IAHFDLKPENIMLLDkNIPIPHIKLIDFGLAHEIED- 180
Cdd:cd14040    91 EYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVD-GTACGEIKITDFGLSKIMDDd 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 181 --GVEFKNIF----GTPEFVAPE--IVNYEP--LGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEF 250
Cdd:cd14040   170 syGVDGMDLTsqgaGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQENTILKATEVQF 249
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2056392213 251 FSQ--TSELAKDFIRKLLVKETRKRLTIQEALRHPWITP 287
Cdd:cd14040   250 PVKpvVSNEAKAFIRRCLAYRKEDRFDVHQLASDPYLLP 288
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
29-274 7.79e-24

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: 101.22  E-value: 7.79e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSrasrrgVSREEIE------REVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd05589     7 LGRGHFGKVLLAEYKPTGELFAIKALKKGDI------IARDEVEslmcekRIFETVNSARHPFLVNLFACFQTPEHVCFV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQkESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENiMLLDKNipiPHIKLIDFGLAHEiedGV 182
Cdd:cd05589    81 MEYAAGGDLMMHIHE-DVFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDN-LLLDTE---GYVKIADFGLCKE---GM 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 183 EFK---NIF-GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANIT--AVSYdfdEEFFSqtSE 256
Cdd:cd05589   153 GFGdrtSTFcGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVndEVRY---PRFLS--TE 227
                         250
                  ....*....|....*...
gi 2056392213 257 lAKDFIRKLLVKETRKRL 274
Cdd:cd05589   228 -AISIMRRLLRKNPERRL 244
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
19-287 8.59e-24

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: 100.90  E-value: 8.59e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  19 VEDFYDIGEELGSGQFAIVKKCREKsTGLEYAAkfIKKRQSRASRRGVSREEIE----REVSILRQVLHHNVITLHDVYE 94
Cdd:cd14041     4 LNDRYLLLHLLGRGGFSEVYKAFDL-TEQRYVA--VKIHQLNKNWRDEKKENYHkhacREYRIHKELDHPRIVKLYDYFS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  95 NRTD-VVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKK--IAHFDLKPENIMLLDkNIPIPHIKLID 171
Cdd:cd14041    81 LDTDsFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEIKppIIHYDLKPGNILLVN-GTACGEIKITD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 172 FGLAHEIE-------DGVEFKNI-FGTPEFVAPE--IVNYEP--LGLEADMWSIGVITYILLSGASPFLGDTKQETLANI 239
Cdd:cd14041   160 FGLSKIMDddsynsvDGMELTSQgAGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFYQCLYGRKPFGHNQSQQDILQE 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2056392213 240 TAVSYDFDEEFFSQ--TSELAKDFIRKLLVKETRKRLTIQEALRHPWITP 287
Cdd:cd14041   240 NTILKATEVQFPPKpvVTPEAKAFIRRCLAYRKEDRIDVQQLACDPYLLP 289
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
27-285 1.04e-23

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: 100.57  E-value: 1.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRasrrgvSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELV 106
Cdd:cd06654    26 EKIGQGASGTVYTAMDVATGQEVAIRQMNLQQQP------KKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 107 SGGELFDFLAQKeSLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIML-LDKNIpiphiKLIDFGLAHEIE-DGVEF 184
Cdd:cd06654   100 AGGSLTDVVTET-CMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLgMDGSV-----KLTDFGFCAQITpEQSKR 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 185 KNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLAnITAVSYDFDEEFFSQTSELAKDFIRK 264
Cdd:cd06654   174 STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALY-LIATNGTPELQNPEKLSAIFRDFLNR 252
                         250       260
                  ....*....|....*....|.
gi 2056392213 265 LLVKETRKRLTIQEALRHPWI 285
Cdd:cd06654   253 CLEMDVEKRGSAKELLQHQFL 273
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
19-227 1.07e-23

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: 101.65  E-value: 1.07e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  19 VEDFyDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQsrasrrgVSREE----IEREVSILRQVLHHN-VITLHDVY 93
Cdd:cd05618    19 LQDF-DLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKKEL-------VNDDEdidwVQTEKHVFEQASNHPfLVGLHSCF 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  94 ENRTDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFG 173
Cdd:cd05618    91 QTESRLFFVIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEG----HIKLTDYG 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2056392213 174 LAHE-IEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPF 227
Cdd:cd05618   167 MCKEgLRPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPF 221
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
23-283 1.24e-23

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: 99.22  E-value: 1.24e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAK---FIKKRQSRASrrgvSREEIEREVSILrQVL--HHNVITLHDVYENRT 97
Cdd:cd14019     3 YRIIEKIGEGTFSSVYKAEDKLHDLYDRNKgrlVALKHIYPTS----SPSRILNELECL-ERLggSNNVSGLITAFRNED 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  98 DVVLILELVSGGELFDFLaqkESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLldkNIPIPHIKLIDFGLAHE 177
Cdd:cd14019    78 QVVAVLPYIEHDDFRDFY---RKMSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLY---NRETGKGVLVDFGLAQR 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 178 IEDGVEFK-NIFGTPEFVAPEIV-NYEPLGLEADMWSIGVITYILLSGA-SPFLGDTKQETLANITAVsydfdeefFSqt 254
Cdd:cd14019   152 EEDRPEQRaPRAGTRGFRAPEVLfKCPHQTTAIDIWSAGVILLSILSGRfPFFFSSDDIDALAEIATI--------FG-- 221
                         250       260
                  ....*....|....*....|....*....
gi 2056392213 255 SELAKDFIRKLLVKETRKRLTIQEALRHP 283
Cdd:cd14019   222 SDEAYDLLDKLLELDPSKRITAEEALKHP 250
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
26-280 1.39e-23

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: 99.38  E-value: 1.39e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  26 GEELGSGQFAIVKKCREKstGLEYAAKFIKK-RQSRASRRGVSREeieREVSILRqvlHHNVITLHDVyENRTDV----V 100
Cdd:cd13979     8 QEPLGSGGFGSVYKATYK--GETVAVKIVRRrRKNRASRQSFWAE---LNAARLR---HENIVRVLAA-ETGTDFaslgL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 101 LILELVSGGELFDFLAQ-KESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPiphiKLIDFGLAHEIE 179
Cdd:cd13979    79 IIMEYCGNGTLQQLIYEgSEPLPLAHRILISLDIARALRFCHSHGIVHLDVKPANILISEQGVC----KLCDFGCSVKLG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 180 DGVEF----KNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDtKQETLANITA-----VSYDFDEEF 250
Cdd:cd13979   155 EGNEVgtprSHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPYAGL-RQHVLYAVVAkdlrpDLSGLEDSE 233
                         250       260       270
                  ....*....|....*....|....*....|
gi 2056392213 251 FSQTselAKDFIRKLLVKETRKRLTIQEAL 280
Cdd:cd13979   234 FGQR---LRSLISRCWSAQPAERPNADESL 260
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
29-287 1.50e-23

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: 100.72  E-value: 1.50e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRAsrrgVSREEIEREVSILRQVLHHNVITLHDVY-ENRTDVVLILELVs 107
Cdd:cd07856    18 VGMGAFGLVCSARDQLTGQNVAVKKIMKPFSTP----VLAKRTYRELKLLKHLRHENIISLSDIFiSPLEDIYFVTELL- 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 108 GGELFDFLAQKEsLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNIpipHIKLIDFGLAhEIEDGvEFKNI 187
Cdd:cd07856    93 GTDLHRLLTSRP-LEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNI-LVNENC---DLKICDFGLA-RIQDP-QMTGY 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 188 FGTPEFVAPEI-VNYEPLGLEADMWSIGVITYILLSGASPF---------------LGDTKQETLANITAV-SYDFDE-- 248
Cdd:cd07856   166 VSTRYYRAPEImLTWQKYDVEVDIWSAGCIFAEMLEGKPLFpgkdhvnqfsiitelLGTPPDDVINTICSEnTLRFVQsl 245
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2056392213 249 ---------EFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWITP 287
Cdd:cd07856   246 pkrervpfsEKFKNADPDAIDLLEKMLVFDPKKRISAAEALAHPYLAP 293
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
23-227 1.69e-23

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: 100.87  E-value: 1.69e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRrgvSREEIEREVSILRQVLHHN-VITLHDVYENRTDVVL 101
Cdd:cd05617    17 FDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDE---DIDWVQTEKHVFEQASSNPfLVGLHSCFQTTSRLFL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 102 ILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAHE-IED 180
Cdd:cd05617    94 VIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNV-LLDAD---GHIKLTDYGMCKEgLGP 169
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2056392213 181 GVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPF 227
Cdd:cd05617   170 GDTTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPF 216
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
20-286 1.78e-23

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: 99.35  E-value: 1.78e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  20 EDFyDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQsrasrrGVSREEIEREVSILRQVLHHNVITLHDVYENRTDV 99
Cdd:cd06645    11 EDF-ELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLEP------GEDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 100 VLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIE 179
Cdd:cd06645    84 WICMEFCGGGSLQDIYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNG----HVKLADFGVSAQIT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 180 DGV-EFKNIFGTPEFVAPEIVNYEPLG---LEADMWSIGvITYILLSGASPFLGDTkQETLANITAVSYDFDEEFFSQTS 255
Cdd:cd06645   160 ATIaKRKSFIGTPYWMAPEVAAVERKGgynQLCDIWAVG-ITAIELAELQPPMFDL-HPMRALFLMTKSNFQPPKLKDKM 237
                         250       260       270
                  ....*....|....*....|....*....|....
gi 2056392213 256 ELAKD---FIRKLLVKETRKRLTIQEALRHPWIT 286
Cdd:cd06645   238 KWSNSfhhFVKMALTKNPKKRPTAEKLLQHPFVT 271
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
20-265 2.40e-23

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: 100.88  E-value: 2.40e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  20 EDFYDIgEELGSGQFAIVKKCREKSTGLEYAAKFIKKrQSRASRRGVSREEIEREVSILRQVLHhnVITLHDVYENRTDV 99
Cdd:cd05628     1 EDFESL-KVIGRGAFGEVRLVQKKDTGHVYAMKILRK-ADMLEKEQVGHIRAERDILVEADSLW--VVKMFYSFQDKLNL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 100 VLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLA---- 175
Cdd:cd05628    77 YLIMEFLPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKG----HVKLSDFGLCtglk 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 176 ------------HEIEDGVEFKNI--------------------FGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSG 223
Cdd:cd05628   153 kahrtefyrnlnHSLPSDFTFQNMnskrkaetwkrnrrqlafstVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIG 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2056392213 224 ASPFLGDTKQETLANIT--AVSYDFDEEFfsQTSELAKDFIRKL 265
Cdd:cd05628   233 YPPFCSETPQETYKKVMnwKETLIFPPEV--PISEKAKDLILRF 274
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
21-282 2.73e-23

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: 98.60  E-value: 2.73e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  21 DFYDIgEELGSGQFAIVKKCREKSTGLEYAAKFIKKR-QSRASRRgvsreeIEREVSILRQVLHHNVITLHDVYENRTDV 99
Cdd:cd14046     7 DFEEL-QVLGKGAFGQVVKVRNKLDGRYYAIKKIKLRsESKNNSR------ILREVMLLSRLNHQHVVRYYQAWIERANL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 100 VLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAHEIE 179
Cdd:cd14046    80 YIQMEYCEKSTLRDLIDSGLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNI-FLDSN---GNVKIGDFGLATSNK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 180 DGVEFKNI-------------------FGTPEFVAPEI-----VNYEPlglEADMWSIGVityILLSGASPFlgDTKQE- 234
Cdd:cd14046   156 LNVELATQdinkstsaalgssgdltgnVGTALYVAPEVqsgtkSTYNE---KVDMYSLGI---IFFEMCYPF--STGMEr 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2056392213 235 --TLANITAVSYDFDEEFFSQTSELAKDFIRKLLVKETRKRLTIQEALRH 282
Cdd:cd14046   228 vqILTALRSVSIEFPPDFDDNKHSKQAKLIRWLLNHDPAKRPSAQELLKS 277
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
22-283 3.18e-23

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: 98.44  E-value: 3.18e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  22 FYDIGEELGSGQFAIVKKCREkSTGLEYAAKfikkrqsRASRRGVSREEIE---REVSILRQVLHH-NVITL--HDVYEN 95
Cdd:cd14131     2 PYEILKQLGKGGSSKVYKVLN-PKKKIYALK-------RVDLEGADEQTLQsykNEIELLKKLKGSdRIIQLydYEVTDE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  96 RTDVVLILELvsgGE--LFDFLAQKES--LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipiphIKLID 171
Cdd:cd14131    74 DDYLYMVMEC---GEidLATILKKKRPkpIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLVKGR-----LKLID 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 172 FGLAHEIEDGVefKNI-----FGTPEFVAPEIV-------NYEP---LGLEADMWSIGVITYILLSGASPFLGDTKQetL 236
Cdd:cd14131   146 FGIAKAIQNDT--TSIvrdsqVGTLNYMSPEAIkdtsasgEGKPkskIGRPSDVWSLGCILYQMVYGKTPFQHITNP--I 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2056392213 237 ANITA-VSYDFDEEFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHP 283
Cdd:cd14131   222 AKLQAiIDPNHEIEFPDIPNPDLIDVMKRCLQRDPKKRPSIPELLNHP 269
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
23-292 4.18e-23

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: 98.64  E-value: 4.18e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIkkrqsraSRRGVSREEIEREVSILRQVLHH-NVITLHDVYENRT---- 97
Cdd:cd06637     8 FELVELVGNGTYGQVYKGRHVKTGQLAAIKVM-------DVTGDEEEEIKQEINMLKKYSHHrNIATYYGAFIKKNppgm 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  98 --DVVLILELVSGGELFDFL--AQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKnipiPHIKLIDFG 173
Cdd:cd06637    81 ddQLWLVMEFCGAGSVTDLIknTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTEN----AEVKLVDFG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 174 LAHEIEDGVEFKNIF-GTPEFVAPEIVNYE-----PLGLEADMWSIGVITYILLSGASPFlgdTKQETLANITAVSYDFD 247
Cdd:cd06637   157 VSAQLDRTVGRRNTFiGTPYWMAPEVIACDenpdaTYDFKSDLWSLGITAIEMAEGAPPL---CDMHPMRALFLIPRNPA 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2056392213 248 EEFFSQT-SELAKDFIRKLLVKETRKRLTIQEALRHPWITPVDNQQ 292
Cdd:cd06637   234 PRLKSKKwSKKFQSFIESCLVKNHSQRPSTEQLMKHPFIRDQPNER 279
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
29-227 4.21e-23

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: 97.97  E-value: 4.21e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRAsrrgvsreeieREVSILRQVLHHNVITLHDVYENRTDVVLILELVSG 108
Cdd:cd13991    14 IGRGSFGEVHRMEDKQTGFQCAVKKVRLEVFRA-----------EELMACAGLTSPRVVPLYGAVREGPWVNIFMDLKEG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 109 GELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipiPHIKLIDFGLAHEIEDGVEFKNIF 188
Cdd:cd13991    83 GSLGQLIKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDG---SDAFLCDFGHAECLDPDGLGKSLF 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2056392213 189 ------GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPF 227
Cdd:cd13991   160 tgdyipGTETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGCHPW 204
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
29-283 4.25e-23

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: 98.53  E-value: 4.25e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGlEYAAkfIKKRQSRASRRGVsREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSG 108
Cdd:cd07848     9 VGEGAYGVVLKCRHKETK-EIVA--IKKFKDSEENEEV-KETTLRELKMLRTLKQENIVELKEAFRRRGKLYLVFEYVEK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 109 GELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIEDGVE--FKN 186
Cdd:cd07848    85 NMLELLEEMPNGVPPEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDV----LKLCDFGFARNLSEGSNanYTE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 187 IFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEE----FFS---------- 252
Cdd:cd07848   161 YVATRWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQPLFPGESEIDQLFTIQKVLGPLPAEqmklFYSnprfhglrfp 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2056392213 253 -----QTSE---------LAKDFIRKLLVKETRKRLTIQEALRHP 283
Cdd:cd07848   241 avnhpQSLErrylgilsgVLLDLMKNLLKLNPTDRYLTEQCLNHP 285
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
18-284 5.30e-23

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: 99.26  E-value: 5.30e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  18 KVEDFYDIGEELGSGQFAIVKKCREKSTGleyaAKFIKKRQSRASRRGVSREEIEREVSILRQVLHHNVITLHDVY---- 93
Cdd:cd07880    12 EVPDRYRDLKQVGSGAYGTVCSALDRRTG----AKVAIKKLYRPFQSELFAKRAYRELRLLKHMKHENVIGLLDVFtpdl 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  94 --ENRTDVVLILELVsgGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLID 171
Cdd:cd07880    88 slDRFHDFYLVMPFM--GTDLGKLMKHEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDC----ELKILD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 172 FGLAHEIEDgvEFKNIFGTPEFVAPE-IVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEF 250
Cdd:cd07880   162 FGLARQTDS--EMTGYVVTRWYRAPEvILNWMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDHLDQLMEIMKVTGTPSKEF 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2056392213 251 FSQ-TSELAKDFIRKL--------------------------LVKETRKRLTIQEALRHPW 284
Cdd:cd07880   240 VQKlQSEDAKNYVKKLprfrkkdfrsllpnanplavnvlekmLVLDAESRITAAEALAHPY 300
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
28-291 5.63e-23

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: 97.90  E-value: 5.63e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  28 ELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRgvsreEIEREVSILRQVLHHNVITLHDVYENRT-DVVLILELV 106
Cdd:cd06620    12 DLGAGNGGSVSKVLHIPTGTIMAKKVIHIDAKSSVRK-----QILRELQILHECHSPYIVSFYGAFLNENnNIIICMEYM 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 107 SGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTK-KIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIEDGVefK 185
Cdd:cd06620    87 DCGSLDKILKKKGPFPEEVLGKIAVAVLEGLTYLYNVhRIIHRDIKPSNILVNSKG----QIKLCDFGVSGELINSI--A 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 186 NIF-GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDF--------------DEEF 250
Cdd:cd06620   161 DTFvGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPFAGSNDDDDGYNGPMGILDLlqrivneppprlpkDRIF 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2056392213 251 fsqtSELAKDFIRKLLVKETRKRLTIQEALRH-PWI-----TPVDNQ 291
Cdd:cd06620   241 ----PKDLRDFVDRCLLKDPRERPSPQLLLDHdPFIqavraSDVDLR 283
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
23-284 6.58e-23

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: 98.54  E-value: 6.58e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAakfIKKRQSRASRRGVSREEIeREVSILRQVLHHNVITLHD-VYE---NRTD 98
Cdd:cd07866    10 YEILGKLGEGTFGEVYKARQIKTGRVVA---LKKILMHNEKDGFPITAL-REIKILKKLKHPNVVPLIDmAVErpdKSKR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  99 VVLILELVSGGELFDF--LAQKES--LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGL 174
Cdd:cd07866    86 KRGSVYMVTPYMDHDLsgLLENPSvkLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGI----LKIADFGL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 175 AHEIED------------GVEFKNIFGTPEFVAPEIV----NYEPlglEADMWSIGVITYILLSGASPFLGDTK------ 232
Cdd:cd07866   162 ARPYDGpppnpkggggggTRKYTNLVVTRWYRPPELLlgerRYTT---AVDIWGIGCVFAEMFTRRPILQGKSDidqlhl 238
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2056392213 233 ---------QETLANITAV-----SYDF-------DEEFFSQTSELAkDFIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd07866   239 ifklcgtptEETWPGWRSLpgcegVHSFtnyprtlEERFGKLGPEGL-DLLSKLLSLDPYKRLTASDALEHPY 310
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
16-284 9.41e-23

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: 99.30  E-value: 9.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  16 QQKVEDfYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRqsrasrrgvsrEEIEREVSIL----RQVLHHN----VI 87
Cdd:cd05621    48 QMKAED-YDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKF-----------EMIKRSDSAFfweeRDIMAFAnspwVV 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  88 TLHDVYENRTDVVLILELVSGGELFDFLAQKEsLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENiMLLDKNipiPHI 167
Cdd:cd05621   116 QLFCAFQDDKYLYMVMEYMPGGDLVNLMSNYD-VPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDN-MLLDKY---GHL 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 168 KLIDFGLAHEIEDG--VEFKNIFGTPEFVAPEIVNYEP----LGLEADMWSIGVITYILLSGASPFLGDTKQETLANIT- 240
Cdd:cd05621   191 KLADFGTCMKMDETgmVHCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMd 270
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2056392213 241 -AVSYDFDEEffSQTSELAKDFIRKLLV-KETR-KRLTIQEALRHPW 284
Cdd:cd05621   271 hKNSLNFPDD--VEISKHAKNLICAFLTdREVRlGRNGVEEIKQHPF 315
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
21-284 1.09e-22

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: 97.06  E-value: 1.09e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  21 DFYDIGEELGSGQFAIVKKCREKSTGLEYAAK-FIKKRQSRASRRgvsreeIE-REVSILRQVLHHNVITLHDVYENRTD 98
Cdd:cd07847     1 EKYEKLSKIGEGSYGVVFKCRNRETGQIVAIKkFVESEDDPVIKK------IAlREIRMLKQLKHPNLVNLIEVFRRKRK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  99 VVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEI 178
Cdd:cd07847    75 LHLVFEYCDHTVLNELEKNPRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQ----IKLCDFGFARIL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 179 E-DGVEFKNIFGTPEFVAPE-IVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFD--------- 247
Cdd:cd07847   151 TgPGDDYTDYVATRWYRAPElLVGDTQYGPPVDVWAIGCVFAELLTGQPLWPGKSDVDQLYLIRKTLGDLIprhqqifst 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2056392213 248 ------------------EEFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd07847   231 nqffkglsipepetreplESKFPNISSPALSFLKGCLQMDPTERLSCEELLEHPY 285
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
59-285 1.79e-22

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: 95.96  E-value: 1.79e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  59 SRASRRgvSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSGGELFDFLAQKES--LSEEEATSFIKQILDG 136
Cdd:cd08221    36 SRLSEK--ERRDALNEIDILSLLNHDNIITYYNHFLDGESLFIEMEYCNGGNLHDKIAQQKNqlFPEEVVLWYLYQIVSA 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 137 VNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIE-DGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGV 215
Cdd:cd08221   114 VSHIHKAGILHRDIKTLNIFLTKADL----VKLGDFGISKVLDsESSMAESIVGTPYYMSPELVQGVKYNFKSDIWAVGC 189
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 216 ITYILLSGASPFLGDTKQETLANITAVSYdfdEEFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd08221   190 VLYELLTLKRTFDATNPLRLAVKIVQGEY---EDIDEQYSEEIIQLVHDCLHQDPEDRPTAEELLERPLL 256
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
23-285 2.43e-22

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: 96.23  E-value: 2.43e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRasrrgvsREEIEREVSILRQVLHH-NVITLHDVYENRT---- 97
Cdd:cd06636    18 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDE-------EEEIKLEINMLKKYSHHrNIATYYGAFIKKSppgh 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  98 --DVVLILELVSGGELFDFLAQKE--SLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKnipiPHIKLIDFG 173
Cdd:cd06636    91 ddQLWLVMEFCGAGSVTDLVKNTKgnALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTEN----AEVKLVDFG 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 174 LAHEIEDGVEFKNIF-GTPEFVAPEIVNYE-----PLGLEADMWSIGVITYILLSGASPFLGDTKQETLANI------TA 241
Cdd:cd06636   167 VSAQLDRTVGRRNTFiGTPYWMAPEVIACDenpdaTYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIprnpppKL 246
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2056392213 242 VSYDFDEEFFsqtselakDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd06636   247 KSKKWSKKFI--------DFIEGCLVKNYLSRPSTEQLLKHPFI 282
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
20-285 3.35e-22

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: 95.89  E-value: 3.35e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  20 EDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRrgvsrEEIEREVSILRQVLHHNVITLHDVYENRTDV 99
Cdd:cd06640     3 EELFTKLERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEEAEDEI-----EDIQQEITVLSQCDSPYVTKYYGSYLKGTKL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 100 VLILELVSGGELFDFLaQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIE 179
Cdd:cd06640    78 WIIMEYLGGGSALDLL-RAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQG----DVKLADFGVAGQLT 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 180 DGVEFKNIF-GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANI-----TAVSYDFDEEFfsq 253
Cdd:cd06640   153 DTQIKRNTFvGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPPNSDMHPMRVLFLIpknnpPTLVGDFSKPF--- 229
                         250       260       270
                  ....*....|....*....|....*....|..
gi 2056392213 254 tselaKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd06640   230 -----KEFIDACLNKDPSFRPTAKELLKHKFI 256
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
12-282 3.63e-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: 95.25  E-value: 3.63e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  12 EPFKQQkvedfYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKkrqsrasrrgVSREEIEREVSILRQVLHHNVITLHD 91
Cdd:cd14047     2 ERFRQD-----FKEIELIGSGGFGQVFKAKHRIDGKTYAIKRVK----------LNNEKAEREVKALAKLDHPNIVRYNG 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  92 VYE---------------NRTDVVLI-LELVSGGELFDFLAQ--KESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPE 153
Cdd:cd14047    67 CWDgfdydpetsssnssrSKTKCLFIqMEFCEKGTLESWIEKrnGEKLDKVLALEIFEQITKGVEYIHSKKLIHRDLKPS 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 154 NIMLLDKNipipHIKLIDFGLAHEIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQ 233
Cdd:cd14047   147 NIFLVDTG----KVKIGDFGLVTSLKNDGKRTKSKGTLSYMSPEQISSQDYGKEVDIYALGLILFELLHVCDSAFEKSKF 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2056392213 234 ETLANITAVSYDFDEEFFSQtselaKDFIRKLLVKETRKRLTIQEALRH 282
Cdd:cd14047   223 WTDLRNGILPDIFDKRYKIE-----KTIIKKMLSKKPEDRPNASEILRT 266
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
19-285 3.70e-22

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: 95.75  E-value: 3.70e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  19 VEDF---YDIGEelgsGQFAIVKKCREKSTGLEYAAKFIKkrqsrasrrgvSREEIE-------REVSILRQVLHHNVIT 88
Cdd:cd07843     4 VDEYeklNRIEE----GTYGVVYRARDKKTGEIVALKKLK-----------MEKEKEgfpitslREINILLKLQHPNIVT 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  89 LHDVY--ENRTDVVLILELVSGgELFDFLAQ-KESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpip 165
Cdd:cd07843    69 VKEVVvgSNLDKIYMVMEYVEH-DLKSLMETmKQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGI--- 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 166 hIKLIDFGLAHEIedGVEFKNIfgTPEFV-----APEIVNYEPL-GLEADMWSIGVITYILLSGASPFLGDTKQETLANI 239
Cdd:cd07843   145 -LKICDFGLAREY--GSPLKPY--TQLVVtlwyrAPELLLGAKEySTAIDMWSVGCIFAELLTKKPLFPGKSEIDQLNKI 219
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2056392213 240 -------------------TAVSYDFDEEFFSQ---------TSELAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd07843   220 fkllgtptekiwpgfselpGAKKKTFTKYPYNQlrkkfpalsLSDNGFDLLNRLLTYDPAKRISAEDALKHPYF 293
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
20-289 4.94e-22

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: 96.84  E-value: 4.94e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  20 EDFYDIgEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQsRASRRGVSREEIEREVsiLRQVLHHNVITLHDVYENRTDV 99
Cdd:cd05629     1 EDFHTV-KVIGKGAFGEVRLVQKKDTGKIYAMKTLLKSE-MFKKDQLAHVKAERDV--LAESDSPWVVSLYYSFQDAQYL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 100 VLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLA---H 176
Cdd:cd05629    77 YLIMEFLPGGDLMTMLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNI-LIDRG---GHIKLSDFGLStgfH 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 177 EIEDGVEFKNIF---------------------------------------------GTPEFVAPEIVNYEPLGLEADMW 211
Cdd:cd05629   153 KQHDSAYYQKLLqgksnknridnrnsvavdsinltmsskdqiatwkknrrlmaystvGTPDYIAPEIFLQQGYGQECDWW 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 212 SIGVITYILLSGASPFLGDTKQETLANITAV--SYDFDEEFfsQTSELAKDFIRKLLVKETRK--RLTIQEALRHPWITP 287
Cdd:cd05629   233 SLGAIMFECLIGWPPFCSENSHETYRKIINWreTLYFPDDI--HLSVEAEDLIRRLITNAENRlgRGGAHEIKSHPFFRG 310

                  ..
gi 2056392213 288 VD 289
Cdd:cd05629   311 VD 312
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
27-283 5.34e-22

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: 95.18  E-value: 5.34e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFAIVKKCREKS-TGLEYAAKFIKKRQSRASrrgvSREEIEREVSILRQVL---HHNVITLHDVYENRTDVVLI 102
Cdd:cd14052     6 ELIGSGEFSQVYKVSERVpTGKVYAVKKLKPNYAGAK----DRLRRLEEVSILRELTldgHDNIVQLIDSWEYHGHLYIQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLA---QKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHE-- 177
Cdd:cd14052    82 TELCENGSLDVFLSelgLLGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGT----LKIGDFGMATVwp 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 178 IEDGVEFKnifGTPEFVAPEIVNYEPLGLEADMWSIGVItyILLSGASPFLGDTKQE-------TLANITAVSYDFDEEF 250
Cdd:cd14052   158 LIRGIERE---GDREYIAPEILSEHMYDKPADIFSLGLI--LLEAAANVVLPDNGDAwqklrsgDLSDAPRLSSTDLHSA 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2056392213 251 FSQTSELAKDF-------------IRKLLVKETRKRLTIQEALRHP 283
Cdd:cd14052   233 SSPSSNPPPDPpnmpilsgsldrvVRWMLSPEPDRRPTADDVLATP 278
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
23-285 5.63e-22

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: 94.43  E-value: 5.63e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRqsRASRRgvSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd08223     2 YQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLK--NASKR--ERKAAEQEAKLLSKLKHPNIVSYKESFEGEDGFLYI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 -LELVSGGELFDFLAQKES--LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIE 179
Cdd:cd08223    78 vMGFCEGGDLYTRLKEQKGvlLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNI----IKVGDLGIARVLE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 180 DGVEF-KNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFlgdtkqeTLANITAVSYDFDE----EFFSQT 254
Cdd:cd08223   154 SSSDMaTTLIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAF-------NAKDMNSLVYKILEgklpPMPKQY 226
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2056392213 255 SELAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd08223   227 SPELGELIKAMLHQDPEKRPSVKRILRQPYI 257
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
23-284 6.19e-22

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: 95.14  E-value: 6.19e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRasrrGVSREEIeREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd07844     2 YKKLDKLGEGSYATVYKGRSKLTGQLVALKEIRLEHEE----GAPFTAI-REASLLKDLKHANIVTLHDIIHTKKTLTLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGgELFDFLAQKES-LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEiedg 181
Cdd:cd07844    77 FEYLDT-DLKQYMDDCGGgLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERG----ELKLADFGLARA---- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 182 vefKNIfgtP-EFVAPEIVN--YEP----LG-----LEADMWSIGVITYILLSGASPF----------------LGDTKQ 233
Cdd:cd07844   148 ---KSV---PsKTYSNEVVTlwYRPpdvlLGsteysTSLDMWGVGCIFYEMATGRPLFpgstdvedqlhkifrvLGTPTE 221
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2056392213 234 ETLANITA----VSYDF----DEEFFSQTSEL-----AKDFIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd07844   222 ETWPGVSSnpefKPYSFpfypPRPLINHAPRLdriphGEELALKFLQYEPKKRISAAEAMKHPY 285
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
22-284 6.65e-22

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: 95.43  E-value: 6.65e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  22 FYDIGEELGSGQFAIVKKCREK--STGLEYAAKFIKkrQSRASRRGVSREEIeREVSILRQVLHHNVITLHDVYENRTD- 98
Cdd:cd07842     1 KYEIEGCIGRGTYGRVYKAKRKngKDGKEYAIKKFK--GDKEQYTGISQSAC-REIALLRELKHENVVSLVEVFLEHADk 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  99 -VVLILELVSggelFDFL--------AQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKL 169
Cdd:cd07842    78 sVYLLFDYAE----HDLWqiikfhrqAKRVSIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANILVMGEGPERGVVKI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 170 IDFGLAHEI---------EDGVEFknifgTPEFVAPEIV----NYEPlglEADMWSIGVITYILLSGASPFLGDTKQ--- 233
Cdd:cd07842   154 GDLGLARLFnaplkpladLDPVVV-----TIWYRAPELLlgarHYTK---AIDIWAIGCIFAELLTLEPIFKGREAKikk 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 234 ------ETLANI----------------------TAVSYDFDEEF-----------FSQTSELAKDFIRKLLVKETRKRL 274
Cdd:cd07842   226 snpfqrDQLERIfevlgtptekdwpdikkmpeydTLKSDTKASTYpnsllakwmhkHKKPDSQGFDLLRKLLEYDPTKRI 305
                         330
                  ....*....|
gi 2056392213 275 TIQEALRHPW 284
Cdd:cd07842   306 TAEEALEHPY 315
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
27-285 7.55e-22

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: 94.85  E-value: 7.55e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFAIVKKCREKSTGLEYAAKFIKkrqsrASRRGVSREEIEREVSILRQVLH---HNVITLHDVYENRTDVVLIL 103
Cdd:cd06917     7 ELVGRGSYGAVYRGYHVKTGRVVALKVLN-----LDTDDDDVSDIQKEVALLSQLKLgqpKNIIKYYGSYLKGPSLWIIM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 104 ELVSGGELFDfLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIEDGVE 183
Cdd:cd06917    82 DYCEGGSIRT-LMRAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTG----NVKLCDFGVAASLNQNSS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 184 FKNIF-GTPEFVAPEIV----NYEplgLEADMWSIGVITYILLSGASPFlgdTKQETLANITAVSYDF-----DEEFfsq 253
Cdd:cd06917   157 KRSTFvGTPYWMAPEVItegkYYD---TKADIWSLGITTYEMATGNPPY---SDVDALRAVMLIPKSKpprleGNGY--- 227
                         250       260       270
                  ....*....|....*....|....*....|..
gi 2056392213 254 tSELAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd06917   228 -SPLLKEFVAACLDEEPKDRLSADELLKSKWI 258
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
23-241 7.62e-22

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: 94.42  E-value: 7.62e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTgLEYAAKFIKkrqsraSRRGVSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd05148     8 FTLERKLGSGYFGEVWEGLWKNR-VRVAIKILK------SDDLLKQQDFQKEVQALKRLRHKHLISLFAVCSVGEPVYII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQKE--SLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIED 180
Cdd:cd05148    81 TELMEKGSLLAFLRSPEgqVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLV----CKVADFGLARLIKE 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2056392213 181 GVEFKNIFGTP-EFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPFLGDTKQETLANITA 241
Cdd:cd05148   157 DVYLSSDKKIPyKWTAPEAASHGTFSTKSDVWSFGILLYEMFTyGQVPYPGMNNHEVYDQITA 219
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
27-235 8.07e-22

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: 94.05  E-value: 8.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVSREEierevSILRQVLHHNVITLHDVYENRTDVVLILELV 106
Cdd:cd05041     1 EKIGRGNFGDVYRGVLKPDNTEVAVKTCRETLPPDLKRKFLQEA-----RILKQYDHPNIVKLIGVCVQKQPIMIVMELV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 107 SGGELFDFL-AQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIEDGV--- 182
Cdd:cd05041    76 PGGSLLTFLrKKGARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNV----LKISDFGMSREEEDGEytv 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2056392213 183 --EFKNIfgtP-EFVAPEIVNYEPLGLEADMWSIGVITY-ILLSGASPFLGDTKQET 235
Cdd:cd05041   152 sdGLKQI---PiKWTAPEALNYGRYTSESDVWSFGILLWeIFSLGATPYPGMSNQQT 205
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
20-286 9.43e-22

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 95.60  E-value: 9.43e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  20 EDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIK----KRQSRASRRGVSREEIE----REVSILRQVLHHNVITLHD 91
Cdd:PTZ00024    8 ERYIQKGAHLGEGTYGKVEKAYDTLTGKIVAIKKVKiieiSNDVTKDRQLVGMCGIHfttlRELKIMNEIKHENIMGLVD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  92 VYENRTDVVLILELVSGgELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLID 171
Cdd:PTZ00024   88 VYVEGDFINLVMDIMAS-DLKKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGI----CKIAD 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 172 FGLAHEIEDGVEFKNIFG----------TPEFV-----APEIVnyepLGLEA-----DMWSIGVITYILLSGASPFLGDT 231
Cdd:PTZ00024  163 FGLARRYGYPPYSDTLSKdetmqrreemTSKVVtlwyrAPELL----MGAEKyhfavDMWSVGCIFAELLTGKPLFPGEN 238
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2056392213 232 KQETLANI-------------TAVSYDFDEEF-----------FSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWIT 286
Cdd:PTZ00024  239 EIDQLGRIfellgtpnednwpQAKKLPLYTEFtprkpkdlktiFPNASDDAIDLLQSLLKLNPLERISAKEALKHEYFK 317
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
23-240 1.14e-21

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: 94.41  E-value: 1.14e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAK-FIKKRQSRASRRGVSREeiereVSILRQVLHHNVITLHDVYENRTDVVL 101
Cdd:cd07846     3 YENLGLVGEGSYGMVMKCRHKETGQIVAIKkFLESEDDKMVKKIAMRE-----IKMLKQLRHENLVNLIEVFRRKKRWYL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 102 ILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIEDG 181
Cdd:cd07846    78 VFEFVDHTVLDDLEKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGV----VKLCDFGFARTLAAP 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2056392213 182 VE-FKNIFGTPEFVAPEIVNYEP-LGLEADMWSIGVITYILLSGASPFLGDTKQETLANIT 240
Cdd:cd07846   154 GEvYTDYVATRWYRAPELLVGDTkYGKAVDVWAVGCLVTEMLTGEPLFPGDSDIDQLYHII 214
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
25-282 1.42e-21

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: 93.89  E-value: 1.42e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  25 IGEELGSGQFAIVKKCREKSTGLEYAAKfikkRQSRASRRGVsrEEIEREVSILRQVL-HHNVITLHDVYENRT-----D 98
Cdd:cd14037     7 IEKYLAEGGFAHVYLVKTSNGGNRAALK----RVYVNDEHDL--NVCKREIEIMKRLSgHKNIVGYIDSSANRSgngvyE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  99 VVLILELVSGGELFDFLAQKES--LSEEEATSFIKQILDGVNYLHTKK--IAHFDLKPENIMLLDKNipipHIKLIDFGL 174
Cdd:cd14037    81 VLLLMEYCKGGGVIDLMNQRLQtgLTESEILKIFCDVCEAVAAMHYLKppLIHRDLKVENVLISDSG----NYKLCDFGS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 175 AHEI------EDGVEF--KNI--FGTPEFVAPEIVNY---EPLGLEADMWSIGVITYILLSGASPFlGDTKQetLAnITA 241
Cdd:cd14037   157 ATTKilppqtKQGVTYveEDIkkYTTLQYRAPEMIDLyrgKPITEKSDIWALGCLLYKLCFYTTPF-EESGQ--LA-ILN 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2056392213 242 VSYDFDEefFSQTSELAKDFIRKLLVKETRKRLTIQEALRH 282
Cdd:cd14037   233 GNFTFPD--NSRYSKRLHKLIRYMLEEDPEKRPNIYQVSYE 271
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
69-283 1.70e-21

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: 93.19  E-value: 1.70e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  69 EEIEREVSILRQVLHHNVITLHDV-YENRTD-----VVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHT 142
Cdd:cd14012    43 QLLEKELESLKKLRHPNLVSYLAFsIERRGRsdgwkVYLLTEYAPGGSLSELLDSVGSVPLDTARRWTLQLLEALEYLHR 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 143 KKIAHFDLKPENIMlLDKNIPIPHIKLIDFGLAHEIED--GVEFKNIFGTPEFVAPEIVN-YEPLGLEADMWSIGVITYI 219
Cdd:cd14012   123 NGVVHKSLHAGNVL-LDRDAGTGIVKLTDYSLGKTLLDmcSRGSLDEFKQTYWLPPELAQgSKSPTRKTDVWDLGLLFLQ 201
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2056392213 220 LLSGAspflgDTKQE-TLANITAVSYDFDEEFFsqtselakDFIRKLLVKETRKRLTIQEALRHP 283
Cdd:cd14012   202 MLFGL-----DVLEKyTSPNPVLVSLDLSASLQ--------DFLSKCLSLDPKKRPTALELLPHE 253
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
16-284 2.05e-21

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: 95.46  E-value: 2.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  16 QQKVEDfYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQsrASRRGVSREEIErEVSILRQVLHHNVITLHDVYEN 95
Cdd:cd05622    69 RMKAED-YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFE--MIKRSDSAFFWE-ERDIMAFANSPWVVQLFYAFQD 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  96 RTDVVLILELVSGGELFDFLAQKEsLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENiMLLDKNipiPHIKLIDFGLA 175
Cdd:cd05622   145 DRYLYMVMEYMPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDN-MLLDKS---GHLKLADFGTC 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 176 HEI--EDGVEFKNIFGTPEFVAPEIVNYEP----LGLEADMWSIGVITYILLSGASPFLGDTKQETLANIT--AVSYDFD 247
Cdd:cd05622   220 MKMnkEGMVRCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMnhKNSLTFP 299
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2056392213 248 EEffSQTSELAKDFIRKLLV-KETR-KRLTIQEALRHPW 284
Cdd:cd05622   300 DD--NDISKEAKNLICAFLTdREVRlGRNGVEEIKRHLF 336
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
26-235 2.31e-21

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: 92.69  E-value: 2.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  26 GEELGSGQFA--------------IVKKCREkSTGLEYAAKFIKkrqsrasrrgvsreeierEVSILRQVLHHNVITLHD 91
Cdd:cd05084     1 GERIGRGNFGevfsgrlradntpvAVKSCRE-TLPPDLKAKFLQ------------------EARILKQYSHPNIVRLIG 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  92 VYENRTDVVLILELVSGGELFDFL-AQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLI 170
Cdd:cd05084    62 VCTQKQPIYIVMELVQGGDFLTFLrTEGPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNV----LKIS 137
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2056392213 171 DFGLAHEIEDGVE-----FKNIfgTPEFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPFLGDTKQET 235
Cdd:cd05084   138 DFGMSREEEDGVYaatggMKQI--PVKWTAPEALNYGRYSSESDVWSFGILLWETFSlGAVPYANLSNQQT 206
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
29-240 3.29e-21

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: 92.83  E-value: 3.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCR----EKSTGLEYAAKfikkrQSRASRRGVSREEIEREVSILRQVLHHNVITLHDVYE--NRTDVVLI 102
Cdd:cd05038    12 LGEGHFGSVELCRydplGDNTGEQVAVK-----SLQPSGEEQHMSDFKREIEILRTLDHEYIVKYKGVCEspGRRSLRLI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLA-QKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAHEIEDG 181
Cdd:cd05038    87 MEYLPSGSLRDYLQrHRDQIDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNI-LVESE---DLVKISDFGLAKVLPED 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2056392213 182 VEF---KNIFGTPEF-VAPEIVNYEPLGLEADMWSIGVITYILLSgaspfLGDTKQETLANIT 240
Cdd:cd05038   163 KEYyyvKEPGESPIFwYAPECLRESRFSSASDVWSFGVTLYELFT-----YGDPSQSPPALFL 220
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
23-285 3.85e-21

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: 93.10  E-value: 3.85e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGleyaaKFIKKRQSRA--SRRGVSREEIeREVSILR---QVLHHNVITLHDVYEN-R 96
Cdd:cd07863     2 YEPVAEIGVGAYGTVYKARDPHSG-----HFVALKSVRVqtNEDGLPLSTV-REVALLKrleAFDHPNIVRLMDVCATsR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  97 TD----VVLILELVSGgELFDFL--AQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLI 170
Cdd:cd07863    76 TDretkVTLVFEHVDQ-DLRTYLdkVPPPGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGG----QVKLA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 171 DFGLAHEIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAV-------S 243
Cdd:cd07863   151 DFGLARIYSCQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLiglppedD 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2056392213 244 YDFD----------------EEFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd07863   231 WPRDvtlprgafsprgprpvQSVVPEIEESGAQLLLEMLTFNPHKRISAFRALQHPFF 288
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
117-282 3.86e-21

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: 92.85  E-value: 3.86e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 117 QKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENiMLLDKNIPipHIKLIDFGLA-HEIEDGVEFKNIFGTPEFVA 195
Cdd:cd13974   125 REKRLSEREALVIFYDVVRVVEALHKKNIVHRDLKLGN-MVLNKRTR--KITITNFCLGkHLVSEDDLLKDQRGSPAYIS 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 196 PEIVNYEP-LGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEffSQTSELAKDFIRKLLVKETRKRL 274
Cdd:cd13974   202 PDVLSGKPyLGKPSDMWALGVVLFTMLYGQFPFYDSIPQELFRKIKAAEYTIPED--GRVSENTVCLIRKLLVLNPQKRL 279

                  ....*...
gi 2056392213 275 TIQEALRH 282
Cdd:cd13974   280 TASEVLDS 287
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
29-284 3.99e-21

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: 93.20  E-value: 3.99e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGlEYAAkfIKKRQSRASRRGVSREEIeREVSILRQVLHHNVITLHDVYENR--TDVVLILELV 106
Cdd:cd07845    15 IGEGTYGIVYRARDTTSG-EIVA--LKKVRMDNERDGIPISSL-REITLLLNLRHPNIVELKEVVVGKhlDSIFLVMEYC 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 107 SG--GELFDFLAQkeSLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIEDGVEF 184
Cdd:cd07845    91 EQdlASLLDNMPT--PFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKG----CLKIADFGLARTYGLPAKP 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 185 KnifgTPEFV-----APEIVnyepLGLEA-----DMWSIGVITYILLSGASPFLGDTKQETLANITAV------------ 242
Cdd:cd07845   165 M----TPKVVtlwyrAPELL----LGCTTyttaiDMWAVGCILAELLAHKPLLPGKSEIEQLDLIIQLlgtpnesiwpgf 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2056392213 243 --------------SYDFDEEFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd07845   237 sdlplvgkftlpkqPYNNLKHKFPWLSEAGLRLLNFLLMYDPKKRATAEEALESSY 292
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
23-285 4.10e-21

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: 92.10  E-value: 4.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKkRQSRASRRGVSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd08222     2 YRVVRKLGSGNFGTVYLVSDLKATADEELKVLK-EISVGELQPDETVDANREAKLLSKLDHPAIVKFHDSFVEKESFCIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELfDFLAQ-----KESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNIpiphIKLIDFGLAHE 177
Cdd:cd08222    81 TEYCEGGDL-DDKISeykksGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNI-FLKNNV----IKVGDFGISRI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 178 IEDGVEFKNIF-GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGdtkqetlANITAVSYDFDE-------E 249
Cdd:cd08222   155 LMGTSDLATTFtGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAFDG-------QNLLSVMYKIVEgetpslpD 227
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2056392213 250 FFSqtSELaKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd08222   228 KYS--KEL-NAIYSRMLNKDPALRPSAAEILKIPFI 260
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
22-286 4.90e-21

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: 92.13  E-value: 4.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  22 FYDIgEELGSGQFAIVKKCREKSTGlEYAAkfIKKrQSRASRRGVSR-EEIEREVSILRQVLHHNVITLHDVYENRTDVV 100
Cdd:cd06607     3 FEDL-REIGHGSFGAVYYARNKRTS-EVVA--IKK-MSYSGKQSTEKwQDIIKEVKFLRQLRHPNTIEYKGCYLREHTAW 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 101 LILE--LVSGGELFDflAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEI 178
Cdd:cd06607    78 LVMEycLGSASDIVE--VHKKPLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGT----VKLADFGSASLV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 179 EDGVEFkniFGTPEFVAPEIV------NYEPlglEADMWSIGvITYILLSGASPflgdtkqeTLANITAVS--Y------ 244
Cdd:cd06607   152 CPANSF---VGTPYWMAPEVIlamdegQYDG---KVDVWSLG-ITCIELAERKP--------PLFNMNAMSalYhiaqnd 216
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2056392213 245 -------DFDEEFFSqtselakdFIRKLLVKETRKRLTIQEALRHPWIT 286
Cdd:cd06607   217 sptlssgEWSDDFRN--------FVDSCLQKIPQDRPSAEDLLKHPFVT 257
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
23-230 5.02e-21

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: 92.01  E-value: 5.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCrekSTGLEYAAKFIKKRQSRASRRGVSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd08228     4 FQIEKKIGRGQFSEVYRA---TCLLDRKPVALKKVQIFEMMDAKARQDCVKEIDLLKQLNHPNVIKYLDSFIEDNELNIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFD----FLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEI 178
Cdd:cd08228    81 LELADAGDLSQmikyFKKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGV----VKLGDLGLGRFF 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2056392213 179 E-DGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGD 230
Cdd:cd08228   157 SsKTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGD 209
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
72-283 5.41e-21

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: 91.95  E-value: 5.41e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  72 EREVSILRQV-LHHNVITLHDVYENRTDVVLILELVSGgELFDFLAQKESLSEE-----EATSFIKQILDGVNYLHTKKI 145
Cdd:cd13982    42 DREVQLLRESdEHPNVIRYFCTEKDRQFLYIALELCAA-SLQDLVESPRESKLFlrpglEPVRLLRQIASGLAHLHSLNI 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 146 AHFDLKPENImLLDKNIPIPHIKLI--DFGLAHEIEDGV----EFKNIFGTPEFVAPEIVNyEPLGLEA----DMWSIG- 214
Cdd:cd13982   121 VHRDLKPQNI-LISTPNAHGNVRAMisDFGLCKKLDVGRssfsRRSGVAGTSGWIAPEMLS-GSTKRRQtravDIFSLGc 198
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 215 VITYILLSGASPFlGDtKQETLANITAVSYDFDE-EFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHP 283
Cdd:cd13982   199 VFYYVLSGGSHPF-GD-KLEREANILKGKYSLDKlLSLGEHGPEAQDLIERMIDFDPEKRPSAEEVLNHP 266
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
23-285 7.04e-21

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: 92.85  E-value: 7.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVkkCREKSTGLEYAAKFIKKRQSRASRRGVSREEIEREVSILRQVL-HHNVITLHDV----YENRT 97
Cdd:cd07857     2 YELIKELGQGAYGIV--CSARNAETSEEETVAIKKITNVFSKKILAKRALRELKLLRHFRgHKNITCLYDMdivfPGNFN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  98 DVVLILELVSGgELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNIpipHIKLIDFGLAHE 177
Cdd:cd07857    80 ELYLYEELMEA-DLHQIIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNL-LVNADC---ELKICDFGLARG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 178 IEDGVEFKNIFGTpEFV------APEI-VNYEPLGLEADMWSIGVITYILLSGASPF---------------LGDTKQET 235
Cdd:cd07857   155 FSENPGENAGFMT-EYVatrwyrAPEImLSFQSYTKAIDVWSVGCILAELLGRKPVFkgkdyvdqlnqilqvLGTPDEET 233
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2056392213 236 LANI-TAVSYDFDEEF-----------FSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd07857   234 LSRIgSPKAQNYIRSLpnipkkpfesiFPNANPLALDLLEKLLAFDPTKRISVEEALEHPYL 295
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
19-289 7.41e-21

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: 93.02  E-value: 7.41e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  19 VEDFYdIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQsRASRRGVSREEIEREVSILRQvlHHNVITLHDVYENRTD 98
Cdd:cd05610     3 IEEFV-IVKPISRGAFGKVYLGRKKNNSKLYAVKVVKKAD-MINKNMVHQVQAERDALALSK--SPFIVHLYYSLQSANN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  99 VVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLA--- 175
Cdd:cd05610    79 VYLVMEYLIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEG----HIKLTDFGLSkvt 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 176 --HEIE-------------------------------------------------DGVEFKNIFGTPEFVAPEIVNYEPL 204
Cdd:cd05610   155 lnRELNmmdilttpsmakpkndysrtpgqvlslisslgfntptpyrtpksvrrgaARVEGERILGTPDYLAPELLLGKPH 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 205 GLEADMWSIGVITYILLSGASPFLGDTKQETLANITA--VSYDFDEEFFSQTSELAkdfIRKLLVKETRKRLTIQEALRH 282
Cdd:cd05610   235 GPAVDWWALGVCLFEFLTGIPPFNDETPQQVFQNILNrdIPWPEGEEELSVNAQNA---IEILLTMDPTKRAGLKELKQH 311

                  ....*..
gi 2056392213 283 PWITPVD 289
Cdd:cd05610   312 PLFHGVD 318
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
23-244 9.98e-21

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: 91.19  E-value: 9.98e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRrgvsrEEIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd08219     2 YNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIRLPKSSSAV-----EDSRKEAVLLAKMKHPNIVAFKESFEADGHLYIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLAQKES--LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIED 180
Cdd:cd08219    77 MEYCDGGDLMQKIKLQRGklFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNG----KVKLGDFGSARLLTS 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2056392213 181 GVEFKNIF-GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSY 244
Cdd:cd08219   153 PGAYACTYvGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGSY 217
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
29-287 1.04e-20

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: 92.66  E-value: 1.04e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAakfIKKrQSRASRRGVSREEIEREVSILRQVLHHNVITLHDVYENRTdvvlilelvSG 108
Cdd:cd07879    23 VGSGAYGSVCSAIDKRTGEKVA---IKK-LSRPFQSEIFAKRAYRELTLLKHMQHENVIGLLDVFTSAV---------SG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 109 GELFDFLA---------QK---ESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAH 176
Cdd:cd07879    90 DEFQDFYLvmpymqtdlQKimgHPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDC----ELKILDFGLAR 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 177 EIEdgVEFKNIFGTPEFVAPE-IVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEF----- 250
Cdd:cd07879   166 HAD--AEMTGYVVTRWYRAPEvILNWMHYNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDQLTQILKVTGVPGPEFvqkle 243
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2056392213 251 ----------------------FSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWITP 287
Cdd:cd07879   244 dkaaksyikslpkyprkdfstlFPKASPQAVDLLEKMLELDVDKRLTATEALEHPYFDS 302
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
29-227 1.42e-20

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: 90.57  E-value: 1.42e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKStgLEYAAKFIKKRQSRasrrgvsrEEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSG 108
Cdd:cd14058     1 VGRGSFGVVCKARWRN--QIVAVKIIESESEK--------KAFEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEG 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 109 GELFDFLAQKESLSE---EEATSFIKQILDGVNYLHT---KKIAHFDLKPENIMLLDKNipiPHIKLIDFGLAHEIEdgV 182
Cdd:cd14058    71 GSLYNVLHGKEPKPIytaAHAMSWALQCAKGVAYLHSmkpKALIHRDLKPPNLLLTNGG---TVLKICDFGTACDIS--T 145
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2056392213 183 EFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPF 227
Cdd:cd14058   146 HMTNNKGSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPF 190
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
23-283 1.47e-20

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: 90.45  E-value: 1.47e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVSREEIEREVSILRqvlHHNVITLHDVYENRTDVVLI 102
Cdd:cd14050     3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKRSRSRFRGEKDRKRKLEEVERHEKLGE---HPNCVRFIKAWEEKGILYIQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGgELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIeDGV 182
Cdd:cd14050    80 TELCDT-SLQQYCEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGV----CKLGDFGLVVEL-DKE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 183 EFKNIF-GTPEFVAPEIVNYEPlGLEADMWSIG-----VITYILLsgasPFLGDTKQEtLANitavsYDFDEEFFSQTSE 256
Cdd:cd14050   154 DIHDAQeGDPRYMAPELLQGSF-TKAADIFSLGitileLACNLEL----PSGGDGWHQ-LRQ-----GYLPEEFTAGLSP 222
                         250       260
                  ....*....|....*....|....*..
gi 2056392213 257 LAKDFIRKLLVKETRKRLTIQEALRHP 283
Cdd:cd14050   223 ELRSIIKLMMDPDPERRPTAEDLLALP 249
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
26-234 1.86e-20

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: 90.07  E-value: 1.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  26 GEELGSGQFA-------------IVKKCREKSTGlEYAAKFIKkrqsrasrrgvsreeierEVSILRQVLHHNVITLHDV 92
Cdd:cd05085     1 GELLGKGNFGevykgtlkdktpvAVKTCKEDLPQ-ELKIKFLS------------------EARILKQYDHPNIVKLIGV 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  93 YENRTDVVLILELVSGGELFDFL-AQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLID 171
Cdd:cd05085    62 CTQRQPIYIVMELVPGGDFLSFLrKKKDELKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNA----LKISD 137
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2056392213 172 FGLAHEIEDGVE----FKNIfgTPEFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPFLGDTKQE 234
Cdd:cd05085   138 FGMSRQEDDGVYsssgLKQI--PIKWTAPEALNYGRYSSESDVWSFGILLWETFSlGVCPYPGMTNQQ 203
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
29-239 2.67e-20

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: 91.01  E-value: 2.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSrasrrgVSREEIE---REVSILRQVLHHNVIT-LHDVYENRTDVVLILE 104
Cdd:cd05591     3 LGKGSFGKVMLAERKGTDEVYAIKVLKKDVI------LQDDDVDctmTEKRILALAAKHPFLTaLHSCFQTKDRLFFVME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 105 LVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAHE-IEDGVE 183
Cdd:cd05591    77 YVNGGDLMFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNI-LLDAE---GHCKLADFGMCKEgILNGKT 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2056392213 184 FKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANI 239
Cdd:cd05591   153 TTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESI 208
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
21-284 2.70e-20

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 90.65  E-value: 2.70e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  21 DFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRasrRGVSREEIeREVSILRQVLHHNVITLHDVYENRTDVV 100
Cdd:PLN00009    2 DQYEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQED---EGVPSTAI-REISLLKEMQHGNIVRLQDVVHSEKRLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 101 LILELVSGgELFDFLAQKESLSEEE--ATSFIKQILDGVNYLHTKKIAHFDLKPENiMLLDKNIPIphIKLIDFGLAHEI 178
Cdd:PLN00009   78 LVFEYLDL-DLKKHMDSSPDFAKNPrlIKTYLYQILRGIAYCHSHRVLHRDLKPQN-LLIDRRTNA--LKLADFGLARAF 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 179 EDGVE-FKNIFGTPEFVAPEIVnyepLGLE-----ADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFS 252
Cdd:PLN00009  154 GIPVRtFTHEVVTLWYRAPEIL----LGSRhystpVDIWSVGCIFAEMVNQKPLFPGDSEIDELFKIFRILGTPNEETWP 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2056392213 253 QTSELAK-------------------------DFIRKLLVKETRKRLTIQEALRHPW 284
Cdd:PLN00009  230 GVTSLPDyksafpkwppkdlatvvptlepagvDLLSKMLRLDPSKRITARAALEHEY 286
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
13-284 2.83e-20

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: 90.89  E-value: 2.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  13 PFKQQ--KVEDFYDIGEelgsGQFAIVKKCREKSTGLEYAAKFIKKRQSRasrRGVSREEIeREVSILRQVLHHNVITLH 90
Cdd:cd07865     6 PFCDEvsKYEKLAKIGQ----GTFGEVFKARHRKTGQIVALKKVLMENEK---EGFPITAL-REIKILQLLKHENVVNLI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  91 DVYEN--------RTDVVLILELVSGgELFDFLAQKE-SLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKN 161
Cdd:cd07865    78 EICRTkatpynryKGSIYLVFEFCEH-DLAGLLSNKNvKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 162 IpiphIKLIDFGLAH-----EIEDGVEFKNIFGTPEFVAPEIV----NYEPlglEADMWSIGVITYILLSgASPFL-GDT 231
Cdd:cd07865   157 V----LKLADFGLARafslaKNSQPNRYTNRVVTLWYRPPELLlgerDYGP---PIDMWGAGCIMAEMWT-RSPIMqGNT 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 232 KQETLANIT--------AVSYDFDEEFFSQTSEL--------------------AKDFIRKLLVKETRKRLTIQEALRHP 283
Cdd:cd07865   229 EQHQLTLISqlcgsitpEVWPGVDKLELFKKMELpqgqkrkvkerlkpyvkdpyALDLIDKLLVLDPAKRIDADTALNHD 308

                  .
gi 2056392213 284 W 284
Cdd:cd07865   309 F 309
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
29-297 2.90e-20

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: 90.19  E-value: 2.90e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRAsRRGVSREEIERevsILRQVLHHN-----VITLHDVYENRTDVVLIL 103
Cdd:cd05606     2 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKM-KQGETLALNER---IMLSLVSTGgdcpfIVCMTYAFQTPDKLCFIL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 104 ELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAHEIEDGVE 183
Cdd:cd05606    78 DLMNGGDLHYHLSQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANI-LLDEH---GHVRISDLGLACDFSKKKP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 184 FKNIfGTPEFVAPEI----VNYEplgLEADMWSIGVITYILLSGASPFLgDTKQETLANITAVSYDFDEEFFSQTSELAK 259
Cdd:cd05606   154 HASV-GTHGYMAPEVlqkgVAYD---SSADWFSLGCMLYKLLKGHSPFR-QHKTKDKHEIDRMTLTMNVELPDSFSPELK 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 2056392213 260 DFIRKLLVKETRKRL-----TIQEALRHPWITPVDNQQAMVRR 297
Cdd:cd05606   229 SLLEGLLQRDVSKRLgclgrGATEVKEHPFFKGVDWQQVYLQK 271
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
26-285 3.63e-20

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: 89.75  E-value: 3.63e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  26 GEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQsRASRRGVSR-----EEIEREVSILRQVLHHNVITLHDvYENRTDVV 100
Cdd:cd06629     6 GELIGKGTYGRVYLAMNATTGEMLAVKQVELPK-TSSDRADSRqktvvDALKSEIDTLKDLDHPNIVQYLG-FEETEDYF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 101 LI-LELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGL---AH 176
Cdd:cd06629    84 SIfLEYVPGGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGI----CKISDFGIskkSD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 177 EIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEA--DMWSIGVITYILLSGASPFLGDT------KQETLANITAVSYDFde 248
Cdd:cd06629   160 DIYGNNGATSMQGSVFWMAPEVIHSQGQGYSAkvDIWSLGCVVLEMLAGRRPWSDDEaiaamfKLGNKRSAPPVPEDV-- 237
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2056392213 249 effsQTSELAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd06629   238 ----NLSPEALDFLNACFAIDPRDRPTAAELLSHPFL 270
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
18-284 5.27e-20

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: 90.05  E-value: 5.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  18 KVEDFYDIgEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQsrasRRGVSREEIeREVSILRQVLHHNVITLHDVYENRT 97
Cdd:cd07872     4 KMETYIKL-EKLGEGTYATVFKGRSKLTENLVALKEIRLEH----EEGAPCTAI-REVSLLKDLKHANIVTLHDIVHTDK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  98 DVVLILELVSGgELFDFLAQKES-LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAH 176
Cdd:cd07872    78 SLTLVFEYLDK-DLKQYMDDCGNiMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERG----ELKLADFGLAR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 177 EIEDGVE-FKNIFGTPEFVAPEI-VNYEPLGLEADMWSIGVITYILLSGASPF---------------LGDTKQETLANI 239
Cdd:cd07872   153 AKSVPTKtYSNEVVTLWYRPPDVlLGSSEYSTQIDMWGVGCIFFEMASGRPLFpgstvedelhlifrlLGTPTEETWPGI 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2056392213 240 TAV----SYDF----DEEFFSQTSELAK---DFIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd07872   233 SSNdefkNYNFpkykPQPLINHAPRLDTegiELLTKFLQYESKKRISAEEAMKHAY 288
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
21-285 8.55e-20

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: 89.28  E-value: 8.55e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  21 DFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSrasrrgvSREEIEREVSILRQVLHH-NVITLHDVYENRTDV 99
Cdd:cd06639    22 DTWDIIETIGKGTYGKVYKVTNKKDGSLAAVKILDPISD-------VDEEIEAEYNILRSLPNHpNVVKFYGMFYKADQY 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 100 V-----LILELVSGGELFDF----LAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLI 170
Cdd:cd06639    95 VggqlwLVLELCNGGSVTELvkglLKCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEG----GVKLV 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 171 DFGLAHEIEDGVEFKNI-FGTPEFVAPEIVNYE-----PLGLEADMWSIGvITYILLSGASPFLGDTKQ-ETLANI---- 239
Cdd:cd06639   171 DFGVSAQLTSARLRRNTsVGTPFWMAPEVIACEqqydySYDARCDVWSLG-ITAIELADGDPPLFDMHPvKALFKIprnp 249
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2056392213 240 --TAVSYDFDEEFFSQtselakdFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd06639   250 ppTLLNPEKWCRGFSH-------FISQCLIKDFEKRPSVTHLLEHPFI 290
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
23-284 1.02e-19

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: 88.94  E-value: 1.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAkfIKKRQSRASRRGVSREEIeREVSILRQVL---HHNVITLHDVYE-NRTD 98
Cdd:cd07862     3 YECVAEIGEGAYGKVFKARDLKNGGRFVA--LKRVRVQTGEEGMPLSTI-REVAVLRHLEtfeHPNVVRLFDVCTvSRTD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  99 ----VVLILELVSGgELFDFL--AQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDF 172
Cdd:cd07862    80 retkLTLVFEHVDQ-DLTTYLdkVPEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSG----QIKLADF 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 173 GLAHEIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANI---TAVSYDFD-- 247
Cdd:cd07862   155 GLARIYSFQMALTSVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKPLFRGSSDVDQLGKIldvIGLPGEEDwp 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2056392213 248 ------------------EEFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd07862   235 rdvalprqafhsksaqpiEKFVTDIDELGKDLLLKCLTFNPAKRISAYSALSHPY 289
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
27-222 1.08e-19

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: 88.53  E-value: 1.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFAIVKKCR----EKSTGLEYAAKFIKKRQSRASRrgvsreEIEREVSILRQVLHHNVITLHDV--YENRTDVV 100
Cdd:cd14205    10 QQLGKGNFGSVEMCRydplQDNTGEVVAVKKLQHSTEEHLR------DFEREIEILKSLQHDNIVKYKGVcySAGRRNLR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 101 LILELVSGGELFDFLAQ-KESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIE 179
Cdd:cd14205    84 LIMEYLPYGSLRDYLQKhKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENEN----RVKIGDFGLTKVLP 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2056392213 180 DGVEFKNIFGTPE----FVAPEIVNYEPLGLEADMWSIGVITYILLS 222
Cdd:cd14205   160 QDKEYYKVKEPGEspifWYAPESLTESKFSVASDVWSFGVVLYELFT 206
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
29-173 1.23e-19

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: 84.80  E-value: 1.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKkrqsraSRRGVSREEIEREVSILRQVLHH--NVITLHDVYENRTDVVLILELV 106
Cdd:cd13968     1 MGEGASAKVFWAEGECTTIGVAVKIGD------DVNNEEGEDLESEMDILRRLKGLelNIPKVLVTEDVDGPNILLMELV 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2056392213 107 SGGELFDFLaQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFG 173
Cdd:cd13968    75 KGGTLIAYT-QEEELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGN----VKLIDFG 136
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
29-229 2.32e-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: 87.40  E-value: 2.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKstGLEYAAKfiKKRQSRASRRGVSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSG 108
Cdd:cd14146     2 IGVGGFGKVYRATWK--GQEVAVK--AARQDPDEDIKATAESVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEFARG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 109 GELFDFLAQKESLSEEEATSFIK---------QILDGVNYLHTKK---IAHFDLKPENIMLLDK----NIPIPHIKLIDF 172
Cdd:cd14146    78 GTLNRALAAANAAPGPRRARRIPphilvnwavQIARGMLYLHEEAvvpILHRDLKSSNILLLEKiehdDICNKTLKITDF 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2056392213 173 GLAHEIEDGVEFKNIfGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLG 229
Cdd:cd14146   158 GLAREWHRTTKMSAA-GTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPYRG 213
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
83-284 2.43e-19

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: 86.64  E-value: 2.43e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  83 HHNVITLHDVYENRTDVVLILElVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNI 162
Cdd:cd14023    44 HRNITGIVEVILGDTKAYVFFE-KDFGDMHSYVRSCKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSDEER 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 163 PIPHIK-LIDFGLAHEIEDGVEFKNifGTPEFVAPEIVNYEPL--GLEADMWSIGVITYILLSGASPFLGDTKQETLANI 239
Cdd:cd14023   123 TQLRLEsLEDTHIMKGEDDALSDKH--GCPAYVSPEILNTTGTysGKSADVWSLGVMLYTLLVGRYPFHDSDPSALFSKI 200
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2056392213 240 TAVSYDFDEeffsQTSELAKDFIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd14023   201 RRGQFCIPD----HVSPKARCLIRSLLRREPSERLTAPEILLHPW 241
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
45-236 2.72e-19

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 90.67  E-value: 2.72e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213   45 TGLEYAAKFIKKRQSRASRRgvsREEIEREVSILRQVLHHNVITLHDVYENRTDVVL-ILELVSGGELFDFLAQKESLSE 123
Cdd:TIGR03903    2 TGHEVAIKLLRTDAPEEEHQ---RARFRRETALCARLYHPNIVALLDSGEAPPGLLFaVFEYVPGRTLREVLAADGALPA 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  124 EEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPiPHIKLIDFG---LAHEIEDGVEFK-----NIFGTPEFVA 195
Cdd:TIGR03903   79 GETGRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVR-PHAKVLDFGigtLLPGVRDADVATltrttEVLGTPTYCA 157
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2056392213  196 PEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETL 236
Cdd:TIGR03903  158 PEQLRGEPVTPNSDLYAWGLIFLECLTGQRVVQGASVAEIL 198
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
23-284 3.61e-19

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: 87.08  E-value: 3.61e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIgeELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVSREEIErevsILRQVLHHNVITLHDVYEN----RTD 98
Cdd:cd14031    14 FDI--ELGRGAFKTVYKGLDTETWVEVAWCELQDRKLTKAEQQRFKEEAE----MLKGLQHPNIVRFYDSWESvlkgKKC 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  99 VVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKK--IAHFDLKPENIMLLDkniPIPHIKLIDFGLAH 176
Cdd:cd14031    88 IVLVTELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITG---PTGSVKIGDLGLAT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 177 EIEDGVEfKNIFGTPEFVAPEIVNyEPLGLEADMWSIGVITYILLSGASPFlgdTKQETLANI-TAVSYDFDEEFFSQ-T 254
Cdd:cd14031   165 LMRTSFA-KSVIGTPEFMAPEMYE-EHYDESVDVYAFGMCMLEMATSEYPY---SECQNAAQIyRKVTSGIKPASFNKvT 239
                         250       260       270
                  ....*....|....*....|....*....|
gi 2056392213 255 SELAKDFIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd14031   240 DPEVKEIIEGCIRQNKSERLSIKDLLNHAF 269
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
23-271 4.59e-19

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: 87.78  E-value: 4.59e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRAsRRGvsreeiEREVSILRQVLH-----HNVITLHDVYENRT 97
Cdd:cd14229     2 YEVLDFLGRGTFGQVVKCWKRGTNEIVAVKILKNHPSYA-RQG------QIEVGILARLSNenadeFNFVRAYECFQHRN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  98 DVVLILELVSGgELFDFLAQKE--SLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLA 175
Cdd:cd14229    75 HTCLVFEMLEQ-NLYDFLKQNKfsPLPLKVIRPILQQVATALKKLKSLGLIHADLKPENIMLVDPVRQPYRVKVIDFGSA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 176 HEIEDGVeFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGdtkqetlanitAVSYDfDEEFFSQTS 255
Cdd:cd14229   154 SHVSKTV-CSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPG-----------ALEYD-QIRYISQTQ 220
                         250
                  ....*....|....*.
gi 2056392213 256 ELAKDFIRKLLVKETR 271
Cdd:cd14229   221 GLPGEQLLNVGTKTSR 236
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
25-239 4.67e-19

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: 86.71  E-value: 4.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  25 IGEELGSGQFAIVKK---CREKSTGLEYAAKFIKKRQSRASRrgvsrEEIEREVSILRQVLHHNVITLHDVYENRTdVVL 101
Cdd:cd05056    10 LGRCIGEGQFGDVYQgvyMSPENEKIAVAVKTCKNCTSPSVR-----EKFLQEAYIMRQFDHPHIVKLIGVITENP-VWI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 102 ILELVSGGELFDFLAQ-KESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDknipiPH-IKLIDFGLAHEIE 179
Cdd:cd05056    84 VMELAPLGELRSYLQVnKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSS-----PDcVKLGDFGLSRYME 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2056392213 180 DGVEFKNIFGT-P-EFVAPEIVNYEPLGLEADMWSIGVITY-ILLSGASPFLGDTKQETLANI 239
Cdd:cd05056   159 DESYYKASKGKlPiKWMAPESINFRRFTSASDVWMFGVCMWeILMLGVKPFQGVKNNDVIGRI 221
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
27-239 4.79e-19

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: 86.18  E-value: 4.79e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFAIVKKCREKSTgLEYAAKFIKKRQsrasrrgVSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELV 106
Cdd:cd05034     1 KKLGAGQFGEVWMGVWNGT-TKVAVKTLKPGT-------MSPEAFLQEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTELM 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 107 SGGELFDFLAQKE--SLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIEDGvEF 184
Cdd:cd05034    73 SKGSLLDYLRTGEgrALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNV----CKVADFGLARLIEDD-EY 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2056392213 185 KNIFGT--P-EFVAPEIVNYEPLGLEADMWSIGVITY-ILLSGASPFLGDTKQETLANI 239
Cdd:cd05034   148 TAREGAkfPiKWTAPEAALYGRFTIKSDVWSFGILLYeIVTYGRVPYPGMTNREVLEQV 206
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
16-283 4.98e-19

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: 87.21  E-value: 4.98e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  16 QQKVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKrqsrasrrgVSREEIEREVSILrQVL--HHNVITLHDV- 92
Cdd:cd14132    13 EWGSQDDYEIIRKIGRGKYSEVFEGINIGNNEKVVIKVLKP---------VKKKKIKREIKIL-QNLrgGPNIVKLLDVv 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  93 -YENRTDVVLILELVsggELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLldkNIPIPHIKLID 171
Cdd:cd14132    83 kDPQSKTPSLIFEYV---NNTDFKTLYPTLTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMI---DHEKRKLRLID 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 172 FGLAHEIEDGVEFKNIFGTPEFVAPEI-VNYEPLGLEADMWSIGVITYILLSGASPFL-GDTKQETLANITAV------- 242
Cdd:cd14132   157 WGLAEFYHPGQEYNVRVASRYYKGPELlVDYQYYDYSLDMWSLGCMLASMIFRKEPFFhGHDNYDQLVKIAKVlgtddly 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2056392213 243 ----SYD--FDEEFFSQTSELAK--------------------DFIRKLLVKETRKRLTIQEALRHP 283
Cdd:cd14132   237 ayldKYGieLPPRLNDILGRHSKkpwerfvnsenqhlvtpealDLLDKLLRYDHQERITAKEAMQHP 303
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
21-286 5.23e-19

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: 87.06  E-value: 5.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  21 DFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQsrasRRGVSREEIeREVSILRQVLHHNVITLHDVYENRTDVV 100
Cdd:cd07869     5 DSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQE----EEGTPFTAI-REASLLKGLKHANIVLLHDIIHTKETLT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 101 LILELVSGgELFDFLAQKES-LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIE 179
Cdd:cd07869    80 LVFEYVHT-DLCQYMDKHPGgLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTG----ELKLADFGLARAKS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 180 -DGVEFKNIFGTPEFVAPEI-VNYEPLGLEADMWSIGVITYILLSGASPF----------------LGDTKQETLANITA 241
Cdd:cd07869   155 vPSHTYSNEVVTLWYRPPDVlLGSTEYSTCLDMWGVGCIFVEMIQGVAAFpgmkdiqdqleriflvLGTPNEDTWPGVHS 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2056392213 242 VSYDFDEEFFSQTSE-------------LAKDFIRKLLVKETRKRLTIQEALRHPWIT 286
Cdd:cd07869   235 LPHFKPERFTLYSPKnlrqawnklsyvnHAEDLASKLLQCFPKNRLSAQAALSHEYFS 292
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
29-227 6.09e-19

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: 85.81  E-value: 6.09e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKstGLEYAAKfiKKRQSRASRRGVSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSG 108
Cdd:cd14148     2 IGVGGFGKVYKGLWR--GEEVAVK--AARQDPDEDIAVTAENVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVMEYARG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 109 GELFDFLAQKEsLSEEEATSFIKQILDGVNYLHTKK---IAHFDLKPENIMLLDK----NIPIPHIKLIDFGLAHEIEDG 181
Cdd:cd14148    78 GALNRALAGKK-VPPHVLVNWAVQIARGMNYLHNEAivpIIHRDLKSSNILILEPiendDLSGKTLKITDFGLAREWHKT 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2056392213 182 VEFkNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPF 227
Cdd:cd14148   157 TKM-SAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPY 201
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
29-289 7.02e-19

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: 87.76  E-value: 7.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSrASRRGVSREEIEREvsILRQVLHHNVITLHDVYENRTDVVLILELVSG 108
Cdd:cd05626     9 LGIGAFGEVCLACKVDTHALYAMKTLRKKDV-LNRNQVAHVKAERD--ILAEADNEWVVKLYYSFQDKDNLYFVMDYIPG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 109 GELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIML-LDKnipipHIKLIDFGL------------- 174
Cdd:cd05626    86 GDMMSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIdLDG-----HIKLTDFGLctgfrwthnskyy 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 175 ---AHEIEDGVEFKNIF--------------------------------GTPEFVAPEIVNYEPLGLEADMWSIGVITYI 219
Cdd:cd05626   161 qkgSHIRQDSMEPSDLWddvsncrcgdrlktleqratkqhqrclahslvGTPNYIAPEVLLRKGYTQLCDWWSVGVILFE 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2056392213 220 LLSGASPFLGDTKQETlaNITAVSYDFDEEFFSQT--SELAKDFIRKLLVKETRK--RLTIQEALRHPWITPVD 289
Cdd:cd05626   241 MLVGQPPFLAPTPTET--QLKVINWENTLHIPPQVklSPEAVDLITKLCCSAEERlgRNGADDIKAHPFFSEVD 312
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
27-239 7.03e-19

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: 85.86  E-value: 7.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFAIVKK--CREKSTG-LEYAAKFIKKRQSRASRRgvsreEIEREVSILRQVLHHNVITLHDVYENRTdVVLIL 103
Cdd:cd05060     1 KELGHGNFGSVRKgvYLMKSGKeVEVAVKTLKQEHEKAGKK-----EFLREASVMAQLDHPCIVRLIGVCKGEP-LMLVM 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 104 ELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIEDGVE 183
Cdd:cd05060    75 ELAPLGPLLKYLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRH----QAKISDFGMSRALGAGSD 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2056392213 184 FKNiFGT----P-EFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPFLGDTKQETLANI 239
Cdd:cd05060   151 YYR-ATTagrwPlKWYAPECINYGKFSSKSDVWSYGVTLWEAFSyGAKPYGEMKGPEVIAML 211
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
40-229 7.16e-19

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: 85.39  E-value: 7.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  40 CREKSTGLEYAAKFIKKRQSRASRRGVsreEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSGGELFDFLAQKE 119
Cdd:cd14060     1 CGGGSFGSVYRAIWVSQDKEVAVKKLL---KIEKEAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGSLFDYLNSNE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 120 S--LSEEEATSFIKQILDGVNYLHTK---KIAHFDLKPENIMLLDKNIpiphIKLIDFGlAHEIEDGVEFKNIFGTPEFV 194
Cdd:cd14060    78 SeeMDMDQIMTWATDIAKGMHYLHMEapvKVIHRDLKSRNVVIAADGV----LKICDFG-ASRFHSHTTHMSLVGTFPWM 152
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2056392213 195 APEIVNYEPLGLEADMWSIGVITYILLSGASPFLG 229
Cdd:cd14060   153 APEVIQSLPVSETCDTYSYGVVLWEMLTREVPFKG 187
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
23-283 9.69e-19

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 88.39  E-value: 9.69e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIkkrqsraSRRGVSREEIER---EVSILRQVLHHNVITLHDVY------ 93
Cdd:PTZ00283   34 YWISRVLGSGATGTVLCAKRVSDGEPFAVKVV-------DMEGMSEADKNRaqaEVCCLLNCDFFSIVKCHEDFakkdpr 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  94 --ENRTDVVLILELVSGGELFDFLAQK----ESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphI 167
Cdd:PTZ00283  107 npENVLMIALVLDYANAGDLRQEIKSRaktnRTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSNGL----V 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 168 KLIDFGL----AHEIEDGVEfKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVS 243
Cdd:PTZ00283  183 KLGDFGFskmyAATVSDDVG-RTFCGTPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPFDGENMEEVMHKTLAGR 261
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2056392213 244 YDfdeEFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHP 283
Cdd:PTZ00283  262 YD---PLPPSISPEMQEIVTALLSSDPKRRPSSSKLLNMP 298
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
29-273 1.01e-18

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: 86.02  E-value: 1.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRqsRASRRGVSReeIEREVSILRQVLHHNVITLHDVYENRTDVVLILEL-VS 107
Cdd:cd14049    14 LGKGGYGKVYKVRNKLDGQYYAIKKILIK--KVTKRDCMK--VLREVKVLAGLQHPNIVGYHTAWMEHVQLMLYIQMqLC 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 108 GGELFDFLAQKESLSEEE--------------ATSFIKQILDGVNYLHTKKIAHFDLKPENIMLldkNIPIPHIKLIDFG 173
Cdd:cd14049    90 ELSLWDWIVERNKRPCEEefksapytpvdvdvTTKILQQLLEGVTYIHSMGIVHRDLKPRNIFL---HGSDIHVRIGDFG 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 174 LA--HEIEDGVEFKNI-----------FGTPEFVAPEIVNYEPLGLEADMWSIGVityILLSGASPFlgDTKQETLANIT 240
Cdd:cd14049   167 LAcpDILQDGNDSTTMsrlnglthtsgVGTCLYAAPEQLEGSHYDFKSDMYSIGV---ILLELFQPF--GTEMERAEVLT 241
                         250       260       270
                  ....*....|....*....|....*....|....
gi 2056392213 241 AV-SYDFDEEFFSQTSELAKdFIRKLLVKETRKR 273
Cdd:cd14049   242 QLrNGQIPKSLCKRWPVQAK-YIKLLTSTEPSER 274
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
23-282 1.04e-18

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


Pssm-ID: 270888 [Multi-domain]  Cd Length: 282  Bit Score: 85.81  E-value: 1.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKrQSRASRrgvsrEEIEREVSILRQVLHHNVITLHD---VYENRTD- 98
Cdd:cd13986     2 YRIQRLLGEGGFSFVYLVEDLSTGRLYALKKILC-HSKEDV-----KEAMREIENYRLFNHPNILRLLDsqiVKEAGGKk 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  99 -VVLILELVSGGELFDFL----AQKESLSEEEATSFIKQILDGVNYLH---TKKIAHFDLKPENIMLLDKNIPIphikLI 170
Cdd:cd13986    76 eVYLLLPYYKRGSLQDEIerrlVKGTFFPEDRILHIFLGICRGLKAMHepeLVPYAHRDIKPGNVLLSEDDEPI----LM 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 171 DFG-------------LAHEIEDGVEFKnifGTPEFVAPEIVNYEP---LGLEADMWSIGVITYILLSGASPF-----LG 229
Cdd:cd13986   152 DLGsmnparieiegrrEALALQDWAAEH---CTMPYRAPELFDVKShctIDEKTDIWSLGCTLYALMYGESPFerifqKG 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2056392213 230 DTKQetLANITAVsYDFDEEffSQTSELAKDFIRKLLVKETRKRLTIQEALRH 282
Cdd:cd13986   229 DSLA--LAVLSGN-YSFPDN--SRYSEELHQLVKSMLVVNPAERPSIDDLLSR 276
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
23-284 1.19e-18

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: 85.56  E-value: 1.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGlEYAAkfIKKRQSRASRRGVSREEIeREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd07839     2 YEKLEKIGEGTYGTVFKAKNRETH-EIVA--LKRVRLDDDDEGVPSSAL-REICLLKELKHKNIVRLYDVLHSDKKLTLV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGG--ELFDFLAQKesLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAHEied 180
Cdd:cd07839    78 FEYCDQDlkKYFDSCNGD--IDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNL-LINKN---GELKLADFGLARA--- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 181 gvefkniFGTP--EFVApEIVN--YEP----LGLEA-----DMWSIGVITYILLSGASP-FLGDTKQETLANITAVSYDF 246
Cdd:cd07839   149 -------FGIPvrCYSA-EVVTlwYRPpdvlFGAKLystsiDMWSAGCIFAELANAGRPlFPGNDVDDQLKRIFRLLGTP 220
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2056392213 247 DEEFFSQTSELAK-------------------------DFIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd07839   221 TEESWPGVSKLPDykpypmypattslvnvvpklnstgrDLLQNLLVCNPVQRISAEEALQHPY 283
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
29-286 1.37e-18

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: 86.62  E-value: 1.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKfikkRQSRASRRGVSREEIEREVSILRQVLHHNVITLHDVY------ENRTDVVLI 102
Cdd:cd07876    29 IGSGAQGIVCAAFDTVLGINVAVK----KLSRPFQNQTHAKRAYRELVLLKCVNHKNIISLLNVFtpqkslEEFQDVYLV 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGelfdfLAQ--KESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIED 180
Cdd:cd07876   105 MELMDAN-----LCQviHMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCT----LKILDFGLARTACT 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 181 GVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLG----------------------DTKQETLAN 238
Cdd:cd07876   176 NFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELVKGSVIFQGtdhidqwnkvieqlgtpsaefmNRLQPTVRN 255
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2056392213 239 IT-------AVSYD--FDEEFFSQTSE-------LAKDFIRKLLVKETRKRLTIQEALRHPWIT 286
Cdd:cd07876   256 YVenrpqypGISFEelFPDWIFPSESErdklktsQARDLLSKMLVIDPDKRISVDEALRHPYIT 319
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
23-282 2.24e-18

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: 84.28  E-value: 2.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIgeELGSGQFAIVKKCREKSTGLEYAAKfikKRQSRASRRGvSREEIEREVSILRQVLHHNVITLHDVYENRTD---- 98
Cdd:cd14033     5 FNI--EIGRGSFKTVYRGLDTETTVEVAWC---ELQTRKLSKG-ERQRFSEEVEMLKGLQHPNIVRFYDSWKSTVRghkc 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  99 VVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTK--KIAHFDLKPENIMLLDkniPIPHIKLIDFGLAh 176
Cdd:cd14033    79 IILVTELMTSGTLKTYLKRFREMKLKLLQRWSRQILKGLHFLHSRcpPILHRDLKCDNIFITG---PTGSVKIGDLGLA- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 177 EIEDGVEFKNIFGTPEFVAPEIvnYEPLGLEA-DMWSIGVITYILLSGASPFlgdTKQETLANI-TAVSYDFDEEFFSQT 254
Cdd:cd14033   155 TLKRASFAKSVIGTPEFMAPEM--YEEKYDEAvDVYAFGMCILEMATSEYPY---SECQNAAQIyRKVTSGIKPDSFYKV 229
                         250       260       270
                  ....*....|....*....|....*....|
gi 2056392213 255 S--ELaKDFIRKLLVKETRKRLTIQEALRH 282
Cdd:cd14033   230 KvpEL-KEIIEGCIRTDKDERFTIQDLLEH 258
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
23-230 2.26e-18

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: 85.08  E-value: 2.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCrekSTGLEYAAKFIKKRQSRASRRGVSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:cd08229    26 FRIEKKIGRGQFSEVYRA---TCLLDGVPVALKKVQIFDLMDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIV 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFD----FLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEI 178
Cdd:cd08229   103 LELADAGDLSRmikhFKKQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGV----VKLGDLGLGRFF 178
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2056392213 179 EDGVEFK-NIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGD 230
Cdd:cd08229   179 SSKTTAAhSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGD 231
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
23-229 2.38e-18

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: 85.58  E-value: 2.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRAsRRGvsreeiEREVSILRQVLH-----HNVITLHDVYENRT 97
Cdd:cd14211     1 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYA-RQG------QIEVSILSRLSQenadeFNFVRAYECFQHKN 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  98 DVVLILELVSGgELFDFLAQKE--SLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLA 175
Cdd:cd14211    74 HTCLVFEMLEQ-NLYDFLKQNKfsPLPLKYIRPILQQVLTALLKLKSLGLIHADLKPENIMLVDPVRQPYRVKVIDFGSA 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2056392213 176 HEIEDGVefKNIFGTPEFV-APEIVnyepLGL---EA-DMWSIGVITyillsgASPFLG 229
Cdd:cd14211   153 SHVSKAV--CSTYLQSRYYrAPEII----LGLpfcEAiDMWSLGCVI------AELFLG 199
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
57-229 2.47e-18

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: 84.31  E-value: 2.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  57 RQSRASRRGVSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSGGELFDFLAQKEsLSEEEATSFIKQILDG 136
Cdd:cd14147    35 RQDPDEDISVTAESVRQEARLFAMLAHPNIIALKAVCLEEPNLCLVMEYAAGGPLSRALAGRR-VPPHVLVNWAVQIARG 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 137 VNYLHTKKIA---HFDLKPENIMLL----DKNIPIPHIKLIDFGLAHEIEDGVEFKNIfGTPEFVAPEIVNYEPLGLEAD 209
Cdd:cd14147   114 MHYLHCEALVpviHRDLKSNNILLLqpieNDDMEHKTLKITDFGLAREWHKTTQMSAA-GTYAWMAPEVIKASTFSKGSD 192
                         170       180
                  ....*....|....*....|
gi 2056392213 210 MWSIGVITYILLSGASPFLG 229
Cdd:cd14147   193 VWSFGVLLWELLTGEVPYRG 212
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
14-285 2.56e-18

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: 85.09  E-value: 2.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  14 FKQQKVEDFYDIgEELGSGQFAIVKKCREKSTGlEYAAkfIKKRQSRASRRGVSREEIEREVSILRQVLHHNVITLHDVY 93
Cdd:cd06633    15 YKDDPEEIFVDL-HEIGHGSFGAVYFATNSHTN-EVVA--IKKMSYSGKQTNEKWQDIIKEVKFLQQLKHPNTIEYKGCY 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  94 ENRTDVVLILE--LVSGGELFDflAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLID 171
Cdd:cd06633    91 LKDHTAWLVMEycLGSASDLLE--VHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPG----QVKLAD 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 172 FGLAHEIEDGVEFkniFGTPEFVAPEIV------NYEPlglEADMWSIGvITYILLSGASPflgdtkqeTLANITAVSYD 245
Cdd:cd06633   165 FGSASIASPANSF---VGTPYWMAPEVIlamdegQYDG---KVDIWSLG-ITCIELAERKP--------PLFNMNAMSAL 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2056392213 246 F----DEEFFSQTSELA---KDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd06633   230 YhiaqNDSPTLQSNEWTdsfRGFVDYCLQKIPQERPSSAELLRHDFV 276
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
28-227 2.95e-18

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: 84.23  E-value: 2.95e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  28 ELGSGQFAIVKK--CREKSTGLEYAAKFIKKRQSRASRrgvsrEEIEREVSILRQVLHHNVITLHDVYENRTdVVLILEL 105
Cdd:cd05115    11 ELGSGNFGCVKKgvYKMRKKQIDVAIKVLKQGNEKAVR-----DEMMREAQIMHQLDNPYIVRMIGVCEAEA-LMLVMEM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 106 VSGGELFDFL-AQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEI--EDGV 182
Cdd:cd05115    85 ASGGPLNKFLsGKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQH----YAKISDFGLSKALgaDDSY 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2056392213 183 EFKNIFGT-P-EFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPF 227
Cdd:cd05115   161 YKARSAGKwPlKWYAPECINFRKFSSRSDVWSYGVTMWEAFSyGQKPY 208
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
29-286 3.57e-18

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: 85.16  E-value: 3.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAakfIKKrQSRASRRGVSREEIEREVSILRQVLHHNVITLHDVY------ENRTDVVLI 102
Cdd:cd07850     8 IGSGAQGIVCAAYDTVTGQNVA---IKK-LSRPFQNVTHAKRAYRELVLMKLVNHKNIIGLLNVFtpqkslEEFQDVYLV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGelfdfLAQ--KESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIed 180
Cdd:cd07850    84 MELMDAN-----LCQviQMDLDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCT----LKILDFGLARTA-- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 181 GVEFKNifgTPEFV-----APEIVnyepLGL----EADMWSIGVITYILLSGASPFLGD------TK------------- 232
Cdd:cd07850   153 GTSFMM---TPYVVtryyrAPEVI----LGMgykeNVDIWSVGCIMGEMIRGTVLFPGTdhidqwNKiieqlgtpsdefm 225
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2056392213 233 ---QETLANITA-----VSYDFDEEF----FSQTSEL--------AKDFIRKLLVKETRKRLTIQEALRHPWIT 286
Cdd:cd07850   226 srlQPTVRNYVEnrpkyAGYSFEELFpdvlFPPDSEEhnklkasqARDLLSKMLVIDPEKRISVDDALQHPYIN 299
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
28-222 3.58e-18

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: 84.21  E-value: 3.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  28 ELGSGQFAIVKKCREK----STGLEYAAKFIKKRQsrasrRGVSREEIEREVSILRQVLHHNVITLHDVYENRTD--VVL 101
Cdd:cd05079    11 DLGEGHFGKVELCRYDpegdNTGEQVAVKSLKPES-----GGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGngIKL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 102 ILELVSGGELFDFLAQ-KESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIED 180
Cdd:cd05079    86 IMEFLPSGSLKEYLPRnKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQ----VKIGDFGLTKAIET 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2056392213 181 GVEF---KNIFGTPEF-VAPEIVNYEPLGLEADMWSIGVITYILLS 222
Cdd:cd05079   162 DKEYytvKDDLDSPVFwYAPECLIQSKFYIASDVWSFGVTLYELLT 207
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
23-229 4.10e-18

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: 84.99  E-value: 4.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRaSRRGVSreeierEVSILRqVL--------HHNVITLHDVYE 94
Cdd:cd14212     1 YLVLDLLGQGTFGQVVKCQDLKTNKLVAVKVLKNKPAY-FRQAML------EIAILT-LLntkydpedKHHIVRLLDHFM 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  95 NRTDVVLILELVsGGELFDFLAQKE--SLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIphIKLIDF 172
Cdd:cd14212    73 HHGHLCIVFELL-GVNLYELLKQNQfrGLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVNLDSPE--IKLIDF 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 173 GLAHEiEDGVEFKNI---FgtpeFVAPEIVNYEPLGLEADMWSIGVITyillsgASPFLG 229
Cdd:cd14212   150 GSACF-ENYTLYTYIqsrF----YRSPEVLLGLPYSTAIDMWSLGCIA------AELFLG 198
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
29-289 4.93e-18

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: 85.48  E-value: 4.93e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRAsRRGVSREEIEREvsILRQVLHHNVITLHDVYENRTDVVLILELVSG 108
Cdd:cd05625     9 LGIGAFGEVCLARKVDTKALYATKTLRKKDVLL-RNQVAHVKAERD--ILAEADNEWVVRLYYSFQDKDNLYFVMDYIPG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 109 GELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLA------------- 175
Cdd:cd05625    86 GDMMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNI-LIDRD---GHIKLTDFGLCtgfrwthdskyyq 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 176 ---HEIEDGVEFKN--------------------------------IFGTPEFVAPEIVNYEPLGLEADMWSIGVITYIL 220
Cdd:cd05625   162 sgdHLRQDSMDFSNewgdpencrcgdrlkplerraarqhqrclahsLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEM 241
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2056392213 221 LSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSELAKDFIRKlLVKETRKRL---TIQEALRHPWITPVD 289
Cdd:cd05625   242 LVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIK-LCRGPEDRLgknGADEIKAHPFFKTID 312
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
17-242 5.42e-18

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: 84.68  E-value: 5.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  17 QKVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSrasrrgvSREEIEREVSILRQVLHH------NVITLH 90
Cdd:cd14226     9 EKWMDRYEIDSLIGKGSFGQVVKAYDHVEQEWVAIKIIKNKKA-------FLNQAQIEVRLLELMNKHdtenkyYIVRLK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  91 DVYENRTDVVLILELVSgGELFDFLAQK--ESLSEEEATSFIKQILDGVNYLHTK--KIAHFDLKPENIMLldKNIPIPH 166
Cdd:cd14226    82 RHFMFRNHLCLVFELLS-YNLYDLLRNTnfRGVSLNLTRKFAQQLCTALLFLSTPelSIIHCDLKPENILL--CNPKRSA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 167 IKLIDFG----LAHEIedgveFKNI---FgtpeFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANI 239
Cdd:cd14226   159 IKIIDFGsscqLGQRI-----YQYIqsrF----YRSPEVLLGLPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKI 229

                  ...
gi 2056392213 240 TAV 242
Cdd:cd14226   230 VEV 232
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
23-285 5.99e-18

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: 84.37  E-value: 5.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQsRASRRGVSreeierEVSILRQVLH------HNVITLHDVYENR 96
Cdd:cd14225    45 YEILEVIGKGSFGQVVKALDHKTNEHVAIKIIRNKK-RFHHQALV------EVKILDALRRkdrdnsHNVIHMKEYFYFR 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  97 TDVVLILELVsGGELFDfLAQKES---LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPipHIKLIDFG 173
Cdd:cd14225   118 NHLCITFELL-GMNLYE-LIKKNNfqgFSLSLIRRFAISLLQCLRLLYRERIIHCDLKPENILLRQRGQS--SIKVIDFG 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 174 laheiEDGVEFKNIFGTPE---FVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAV----SYDF 246
Cdd:cd14225   194 -----SSCYEHQRVYTYIQsrfYRSPEVILGLPYSMAIDMWSLGCILAELYTGYPLFPGENEVEQLACIMEVlglpPPEL 268
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2056392213 247 DEE------FFSQ------------------TSELAK----------DFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14225   269 IENaqrrrlFFDSkgnprcitnskgkkrrpnSKDLASalktsdplflDFIRRCLEWDPSKRMTPDEALQHEWI 341
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
27-284 6.03e-18

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: 83.86  E-value: 6.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFAIVKKCREKSTGLEYAAKFIkkrqSRASRRGVSREEIeREVSILRQVLHHNVITLHDVYENRTDVVLILELV 106
Cdd:cd07870     6 EKLGEGSYATVYKGISRINGQLVALKVI----SMKTEEGVPFTAI-REASLLKGLKHANIVLLHDIIHTKETLTFVFEYM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 107 SGgELFDFLAQKES-LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDknipIPHIKLIDFGLAHEiedgvefK 185
Cdd:cd07870    81 HT-DLAQYMIQHPGgLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISY----LGELKLADFGLARA-------K 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 186 NIfgTPEFVAPEIVN--YEP----LGL-----EADMWSIGVITYILLSGASPFLGDTKQ-ETLANITAVSYDFDEEFFSQ 253
Cdd:cd07870   149 SI--PSQTYSSEVVTlwYRPpdvlLGAtdyssALDIWGAGCIFIEMLQGQPAFPGVSDVfEQLEKIWTVLGVPTEDTWPG 226
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2056392213 254 TSEL----------------------------AKDFIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd07870   227 VSKLpnykpewflpckpqqlrvvwkrlsrppkAEDLASQMLMMFPKDRISAQDALLHPY 285
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
27-239 6.53e-18

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: 83.17  E-value: 6.53e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFAIV-KKCREKSTglEYAAKFIKKRQsrasrrgVSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILEL 105
Cdd:cd05072    13 KKLGAGQFGEVwMGYYNNST--KVAVKTLKPGT-------MSVQAFLEEANLMKTLQHDKLVRLYAVVTKEEPIYIITEY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 106 VSGGELFDFLAQKES--LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIEDGvE 183
Cdd:cd05072    84 MAKGSLLDFLKSDEGgkVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLM----CKIADFGLARVIEDN-E 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 184 FKNIFGTP---EFVAPEIVNYEPLGLEADMWSIGVITY-ILLSGASPFLGDTKQETLANI 239
Cdd:cd05072   159 YTAREGAKfpiKWTAPEAINFGSFTIKSDVWSFGILLYeIVTYGKIPYPGMSNSDVMSAL 218
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
23-285 6.89e-18

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: 84.17  E-value: 6.89e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQsrasrrgVSREEIEREVSILRQVLHH--------NVITLHDVYE 94
Cdd:cd14136    12 YHVVRKLGWGHFSTVWLCWDLQNKRFVALKVVKSAQ-------HYTEAALDEIKLLKCVREAdpkdpgreHVVQLLDDFK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  95 ----NRTDVVLILElVSGGELFDFLAQKE--SLSEEEATSFIKQILDGVNYLHTK-KIAHFDLKPENIMLldkNIPIPHI 167
Cdd:cd14136    85 htgpNGTHVCMVFE-VLGPNLLKLIKRYNyrGIPLPLVKKIARQVLQGLDYLHTKcGIIHTDIKPENVLL---CISKIEV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 168 KLIDFGLAHEIEDgvEFKNIFGTPEFVAPEIVnyepLGLE----ADMWSIGVITYILLSGAspFLGDTKQ---------- 233
Cdd:cd14136   161 KIADLGNACWTDK--HFTEDIQTRQYRSPEVI----LGAGygtpADIWSTACMAFELATGD--YLFDPHSgedysrdedh 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 234 -----ETLANI---TAVSYDFDEEFFSQTSEL-------------------------AK---DFIRKLLVKETRKRLTIQ 277
Cdd:cd14136   233 laliiELLGRIprsIILSGKYSREFFNRKGELrhisklkpwpledvlvekykwskeeAKefaSFLLPMLEYDPEKRATAA 312

                  ....*...
gi 2056392213 278 EALRHPWI 285
Cdd:cd14136   313 QCLQHPWL 320
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
23-271 7.32e-18

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: 84.37  E-value: 7.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRAsRRGvsreeiEREVSILRQVL-----HHNVITLHDVYENRT 97
Cdd:cd14228    17 YEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYA-RQG------QIEVSILSRLSsenadEYNFVRSYECFQHKN 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  98 DVVLILELVSGgELFDFLAQKE--SLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLA 175
Cdd:cd14228    90 HTCLVFEMLEQ-NLYDFLKQNKfsPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPVRQPYRVKVIDFGSA 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 176 HEIEDGVeFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLanitavsydfdeEFFSQTS 255
Cdd:cd14228   169 SHVSKAV-CSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQI------------RYISQTQ 235
                         250
                  ....*....|....*.
gi 2056392213 256 ELAKDFIRKLLVKETR 271
Cdd:cd14228   236 GLPAEYLLSAGTKTSR 251
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
27-241 7.39e-18

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: 82.69  E-value: 7.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFaivkkcrekstGLEYAAKFIKKRQS--RASRRG-VSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLIL 103
Cdd:cd05112    10 QEIGSGQF-----------GLVHLGYWLNKDKVaiKTIREGaMSEEDFIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 104 ELVSGGELFDFL-AQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIEDGv 182
Cdd:cd05112    79 EFMEHGCLSDYLrTQRGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQV----VKVSDFGMTRFVLDD- 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2056392213 183 EFKNIFGTP---EFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPFLGDTKQETLANITA 241
Cdd:cd05112   154 QYTSSTGTKfpvKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSeGKIPYENRSNSEVVEDINA 216
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
18-286 8.15e-18

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: 83.58  E-value: 8.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  18 KVEDFYDIGEeLGSGQFAIVKKCREKSTGLEYAAKFIkkrqsrasRRGVSREEIEREVSILRQVLHHN----VITLHDVY 93
Cdd:cd06618    13 DLNDLENLGE-IGSGTCGQVYKMRHKKTGHVMAVKQM--------RRSGNKEENKRILMDLDVVLKSHdcpyIVKCYGYF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  94 ENRTDVVLILELVSggELFDFLAQ--KESLSEEEATSFIKQILDGVNYLHTKK-IAHFDLKPENImLLDKNipiPHIKLI 170
Cdd:cd06618    84 ITDSDVFICMELMS--TCLDKLLKriQGPIPEDILGKMTVSIVKALHYLKEKHgVIHRDVKPSNI-LLDES---GNVKLC 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 171 DFGLAHEIEDGVEFKNIFGTPEFVAPEIVNYEPLG---LEADMWSIGVITYILLSGASPFLG-DTKQETLANI---TAVS 243
Cdd:cd06618   158 DFGISGRLVDSKAKTRSAGCAAYMAPERIDPPDNPkydIRADVWSLGISLVELATGQFPYRNcKTEFEVLTKIlneEPPS 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 2056392213 244 YDFDEEFfsqtSELAKDFIRKLLVKETRKRLTIQEALRHPWIT 286
Cdd:cd06618   238 LPPNEGF----SPDFCSFVDLCLTKDHRYRPKYRELLQHPFIR 276
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
23-284 9.10e-18

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: 82.82  E-value: 9.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIgeELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRAsrrgVSREEIEREVSILRQVLHHNVITLHDVYENRTD---- 98
Cdd:cd14032     5 FDI--ELGRGSFKTVYKGLDTETWVEVAWCELQDRKLTK----VERQRFKEEAEMLKGLQHPNIVRFYDFWESCAKgkrc 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  99 VVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKK--IAHFDLKPENIMLLDkniPIPHIKLIDFGLAh 176
Cdd:cd14032    79 IVLVTELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFITG---PTGSVKIGDLGLA- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 177 EIEDGVEFKNIFGTPEFVAPEIVNyEPLGLEADMWSIGVITYILLSGASPFlgdTKQETLANI-TAVSYDFDEEFFSQTS 255
Cdd:cd14032   155 TLKRASFAKSVIGTPEFMAPEMYE-EHYDESVDVYAFGMCMLEMATSEYPY---SECQNAAQIyRKVTCGIKPASFEKVT 230
                         250       260       270
                  ....*....|....*....|....*....|
gi 2056392213 256 ELA-KDFIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd14032   231 DPEiKEIIGECICKNKEERYEIKDLLSHAF 260
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
69-229 9.28e-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: 82.78  E-value: 9.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  69 EEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSGGELFDFLAQKEsLSEEEATSFIKQILDGVNYLHTKKIA-- 146
Cdd:cd14145    50 ENVRQEAKLFAMLKHPNIIALRGVCLKEPNLCLVMEFARGGPLNRVLSGKR-IPPDILVNWAVQIARGMNYLHCEAIVpv 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 147 -HFDLKPENIMLLDK----NIPIPHIKLIDFGLAHEIEDGVEFkNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILL 221
Cdd:cd14145   129 iHRDLKSSNILILEKvengDLSNKILKITDFGLAREWHRTTKM-SAAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELL 207

                  ....*...
gi 2056392213 222 SGASPFLG 229
Cdd:cd14145   208 TGEVPFRG 215
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
23-271 9.42e-18

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: 83.99  E-value: 9.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRAsRRGvsreeiEREVSILRQVL-----HHNVITLHDVYENRT 97
Cdd:cd14227    17 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYA-RQG------QIEVSILARLStesadDYNFVRAYECFQHKN 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  98 DVVLILELVSGgELFDFLAQKE--SLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLA 175
Cdd:cd14227    90 HTCLVFEMLEQ-NLYDFLKQNKfsPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPSRQPYRVKVIDFGSA 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 176 HEIEDGVeFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLanitavsydfdeEFFSQTS 255
Cdd:cd14227   169 SHVSKAV-CSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQI------------RYISQTQ 235
                         250
                  ....*....|....*.
gi 2056392213 256 ELAKDFIRKLLVKETR 271
Cdd:cd14227   236 GLPAEYLLSAGTKTTR 251
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
29-297 1.06e-17

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: 83.96  E-value: 1.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRAsRRGVSREEIER-EVSILRQVLHHNVITLHDVYENRTDVVLILELVS 107
Cdd:cd05633    13 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKM-KQGETLALNERiMLSLVSTGDCPFIVCMTYAFHTPDKLCFILDLMN 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 108 GGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIEDGVEFKNI 187
Cdd:cd05633    92 GGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHG----HVRISDLGLACDFSKKKPHASV 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 188 fGTPEFVAPEIVNY-EPLGLEADMWSIGVITYILLSGASPFLgDTKQETLANITAVSYDFDEEFFSQTSELAKDFIRKLL 266
Cdd:cd05633   168 -GTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFR-QHKTKDKHEIDRMTLTVNVELPDSFSPELKSLLEGLL 245
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2056392213 267 VKETRKRLTI-----QEALRHPWITPVDNQQAMVRR 297
Cdd:cd05633   246 QRDVSKRLGChgrgaQEVKEHSFFKGIDWQQVYLQK 281
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
29-283 1.13e-17

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: 82.66  E-value: 1.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKstGLEYAAKFIKK---------------RQSRASRRGVSREEIEREVSILRQVLHHNVITLhdVY 93
Cdd:cd14000     2 LGDGGFGSVYRASYK--GEPVAVKIFNKhtssnfanvpadtmlRHLRATDAMKNFRLLRQELTVLSHLHHPSIVYL--LG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  94 ENRTDVVLILELVSGGELfDFLAQKESLSEEEATSFIKQ-----ILDGVNYLHTKKIAHFDLKPENIML--LDKNIPIpH 166
Cdd:cd14000    78 IGIHPLMLVLELAPLGSL-DHLLQQDSRSFASLGRTLQQrialqVADGLRYLHSAMIIYRDLKSHNVLVwtLYPNSAI-I 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 167 IKLIDFGLA----HEIEDGVEfknifGTPEFVAPEIVNYEPLGLE-ADMWSIGVITYILLSGASPFLGDTKQETLANITA 241
Cdd:cd14000   156 IKIADYGISrqccRMGAKGSE-----GTPGFRAPEIARGNVIYNEkVDVFSFGMLLYEILSGGAPMVGHLKFPNEFDIHG 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2056392213 242 VSYDFDEEFFSQTSELAKDFIRKLLVKETRKR---LTIQEALRHP 283
Cdd:cd14000   231 GLRPPLKQYECAPWPEVEVLMKKCWKENPQQRptaVTVVSILNSP 275
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
27-291 1.89e-17

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


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 82.20  E-value: 1.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGvsreeIEREVSILRQVLHHNVITLHDVYENRTDVVLILELV 106
Cdd:cd06622     7 DELGKGNYGSVYKVLHRPTGVTMAMKEIRLELDESKFNQ-----IIMELDILHKAVSPYIVDFYGAFFIEGAVYMCMEYM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 107 SGG---ELFDFLAQKESLSEEEATSFIKQILDGVNYLHTK-KIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIEDGV 182
Cdd:cd06622    82 DAGsldKLYAGGVATEGIPEDVLRRITYAVVKGLKFLKEEhNIIHRDVKPTNVLVNGNG----QVKLCDFGVSGNLVASL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 183 EFKNIfGTPEFVAPEIVNYE-PLG-----LEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSE 256
Cdd:cd06622   158 AKTNI-GCQSYMAPERIKSGgPNQnptytVQSDVWSLGLSILEMALGRYPYPPETYANIFAQLSAIVDGDPPTLPSGYSD 236
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2056392213 257 LAKDFIRKLLVKETRKRLTIQEALRHPWITPVDNQ 291
Cdd:cd06622   237 DAQDFVAKCLNKIPNRRPTYAQLLEHPWLVKYKNA 271
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
29-216 2.57e-17

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: 81.00  E-value: 2.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKkrqsrasrRGVSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSG 108
Cdd:cd14065     1 LGKGFFGEVYKVTHRETGKVMVMKELK--------RFDEQRSFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 109 GELFDFLAQ-KESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIkLIDFGLAHEIEDGVEFK-- 185
Cdd:cd14065    73 GTLEELLKSmDEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVREANRGRNAV-VADFGLAREMPDEKTKKpd 151
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2056392213 186 -----NIFGTPEFVAPEIVNYEPLGLEADMWSIGVI 216
Cdd:cd14065   152 rkkrlTVVGSPYWMAPEMLRGESYDEKVDVFSFGIV 187
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
23-287 3.10e-17

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: 82.52  E-value: 3.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEE------LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVsreeieREVSILRQVLHHNVITLHDV---- 92
Cdd:cd07854     1 FDLGSRymdlrpLGCGSNGLVFSAVDSDCDKRVAVKKIVLTDPQSVKHAL------REIKIIRRLDHDNIVKVYEVlgps 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  93 -YENRTDVVLILELVS---GGELFDF----LAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLldkNIPI 164
Cdd:cd07854    75 gSDLTEDVGSLTELNSvyiVQEYMETdlanVLEQGPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFI---NTED 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 165 PHIKLIDFGLAHEIEDGVEFKNIFG----TPEFVAPEIV----NYEPlglEADMWSIGVITYILLSGASPFLGDTKQETL 236
Cdd:cd07854   152 LVLKIGDFGLARIVDPHYSHKGYLSeglvTKWYRSPRLLlspnNYTK---AIDMWAAGCIFAEMLTGKPLFAGAHELEQM 228
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2056392213 237 ANI---TAVSYDFDE-----------------------EFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWITP 287
Cdd:cd07854   229 QLIlesVPVVREEDRnellnvipsfvrndggeprrplrDLLPGVNPEALDFLEQILTFNPMDRLTAEEALMHPYMSC 305
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
26-241 3.92e-17

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: 80.57  E-value: 3.92e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  26 GEELGSGQFAIVKKCREKSTgLEYAAKFIKKrqsrasrrGVSREE--IErEVSILRQVLHHNVITLHDVYENRTDVVLIL 103
Cdd:cd05059     9 LKELGSGQFGVVHLGKWRGK-IDVAIKMIKE--------GSMSEDdfIE-EAKVMMKLSHPKLVQLYGVCTKQRPIFIVT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 104 ELVSGGELFDFL-AQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIEDGv 182
Cdd:cd05059    79 EYMANGCLLNYLrERRGKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNV----VKVSDFGLARYVLDD- 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2056392213 183 EFKNIFGTP---EFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPFLGDTKQETLANITA 241
Cdd:cd05059   154 EYTSSVGTKfpvKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSeGKMPYERFSNSEVVEHISQ 216
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
83-284 4.04e-17

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: 80.47  E-value: 4.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  83 HHNVITLHDVYENRTDVVLILELvSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNI 162
Cdd:cd14022    44 HSNINQITEIILGETKAYVFFER-SYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVFKDEER 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 163 PIPHIK-LIDFGLAHEIEDGVEFKNifGTPEFVAPEIVN----YEplGLEADMWSIGVITYILLSGASPFLGDTKQETLA 237
Cdd:cd14022   123 TRVKLEsLEDAYILRGHDDSLSDKH--GCPAYVSPEILNtsgsYS--GKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFS 198
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2056392213 238 NITAVSYDFDEEFfsqtSELAKDFIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd14022   199 KIRRGQFNIPETL----SPKAKCLIRSILRREPSERLTSQEILDHPW 241
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
28-239 6.36e-17

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: 80.01  E-value: 6.36e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  28 ELGSGQFAIVKK--CREKSTGLEYAAKFIKKRQSRASrrgvSREEIEREVSILRQVLHHNVITLHDVYENRTdVVLILEL 105
Cdd:cd05116     2 ELGSGNFGTVKKgyYQMKKVVKTVAVKILKNEANDPA----LKDELLREANVMQQLDNPYIVRMIGICEAES-WMLVMEM 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 106 VSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIEDGVEFK 185
Cdd:cd05116    77 AELGPLNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQH----YAKISDFGLSKALRADENYY 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2056392213 186 NIFGT---P-EFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPFLGDTKQETLANI 239
Cdd:cd05116   153 KAQTHgkwPvKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSyGQKPYKGMKGNEVTQMI 211
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
27-228 6.63e-17

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: 80.71  E-value: 6.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFAIVKKCR----EKSTGLEYAAKFIKKRQSRASRRGvsreeIEREVSILRQVLHHNVITLHDVYENRTD--VV 100
Cdd:cd05080    10 RDLGEGHFGKVSLYCydptNDGTGEMVAVKALKADCGPQHRSG-----WKQEIDILKTLYHENIVKYKGCCSEQGGksLQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 101 LILELVSGGELFDFLAqKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIED 180
Cdd:cd05080    85 LIMEYVPLGSLRDYLP-KHSIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRL----VKIGDFGLAKAVPE 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2056392213 181 GVEFKNIF---GTPEF-VAPEIVNYEPLGLEADMWSIGVITYILLSGASPFL 228
Cdd:cd05080   160 GHEYYRVRedgDSPVFwYAPECLKEYKFYYASDVWSFGVTLYELLTHCDSSQ 211
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
23-314 8.47e-17

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: 80.98  E-value: 8.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIK---KRQSRASRrgvsreeIEREVSILRQVLHHNVITLHDVY---ENR 96
Cdd:cd07859     2 YKIQEVIGKGSYGVVCSAIDTHTGEKVAIKKINdvfEHVSDATR-------ILREIKLLRLLRHPDIVEIKHIMlppSRR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  97 T--DVVLILELVsGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNIpipHIKLIDFGL 174
Cdd:cd07859    75 EfkDIYVVFELM-ESDLHQVIKANDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNI-LANADC---KLKICDFGL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 175 A----HEIEDGVEFKNIFGTPEFVAPEIV-----NYEPlglEADMWSIGVITYILLSGASPF---------------LGD 230
Cdd:cd07859   150 ArvafNDTPTAIFWTDYVATRWYRAPELCgsffsKYTP---AIDIWSIGCIFAEVLTGKPLFpgknvvhqldlitdlLGT 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 231 TKQETLA---NITAVSY----------DFDEEfFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWITPVDNQQAMVRR 297
Cdd:cd07859   227 PSPETISrvrNEKARRYlssmrkkqpvPFSQK-FPNADPLALRLLERLLAFDPKDRPTAEEALADPYFKGLAKVEREPSA 305
                         330
                  ....*....|....*..
gi 2056392213 298 ESVVNLEnFrkQYVRRR 314
Cdd:cd07859   306 QPITKLE-F--EFERRR 319
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
29-216 9.71e-17

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: 79.49  E-value: 9.71e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRqsrasrrgVSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSG 108
Cdd:cd14156     1 IGSGFFSKVYKVTHGATGKVMVVKIYKND--------VDQHKIVREISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 109 GELFDFLAQKE-SLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIkLIDFGLAHEI-----EDGV 182
Cdd:cd14156    73 GCLEELLAREElPLSWREKVELACDISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGREAV-VTDFGLAREVgempaNDPE 151
                         170       180       190
                  ....*....|....*....|....*....|....
gi 2056392213 183 EFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVI 216
Cdd:cd14156   152 RKLSLVGSAFWMAPEMLRGEPYDRKVDVFSFGIV 185
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
27-296 1.68e-16

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: 79.39  E-value: 1.68e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFAIVKKCREKSTGLEYAAKFIkkrqsRASRRGVSREEIEREVSI-LRQVLHHNVITLHDVYENRTDVVLILEL 105
Cdd:cd06617     7 EELGRGAYGVVDKMRHVPTGTIMAVKRI-----RATVNSQEQKRLLMDLDIsMRSVDCPYTVTFYGALFREGDVWICMEV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 106 VSGgELFDFLAQ---KESLSEEEATSFIK-QILDGVNYLHTK-KIAHFDLKPENImLLDKNipiPHIKLIDFGLAHEIED 180
Cdd:cd06617    82 MDT-SLDKFYKKvydKGLTIPEDILGKIAvSIVKALEYLHSKlSVIHRDVKPSNV-LINRN---GQVKLCDFGISGYLVD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 181 GVEFKNIFGTPEFVAPEIVNYE--PLG--LEADMWSIGvITYI-LLSGASPFlgDTKQETLANITAV----SYDFDEEFF 251
Cdd:cd06617   157 SVAKTIDAGCKPYMAPERINPElnQKGydVKSDVWSLG-ITMIeLATGRFPY--DSWKTPFQQLKQVveepSPQLPAEKF 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2056392213 252 SQTSElakDFIRKLLVKETRKRLTIQEALRHPWITPVDNQQAMVR 296
Cdd:cd06617   234 SPEFQ---DFVNKCLKKNYKERPNYPELLQHPFFELHLSKNTDVA 275
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
29-297 1.88e-16

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: 79.71  E-value: 1.88e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRAsRRGVSREEIER-EVSILRQVLHHNVITLHDVYENRTDVVLILELVS 107
Cdd:cd14223     8 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKM-KQGETLALNERiMLSLVSTGDCPFIVCMSYAFHTPDKLSFILDLMN 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 108 GGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIEDGVEFKNI 187
Cdd:cd14223    87 GGDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFG----HVRISDLGLACDFSKKKPHASV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 188 fGTPEFVAPEI----VNYEPlglEADMWSIGVITYILLSGASPFLgDTKQETLANITAVSYDFDEEFFSQTSELAKDFIR 263
Cdd:cd14223   163 -GTHGYMAPEVlqkgVAYDS---SADWFSLGCMLFKLLRGHSPFR-QHKTKDKHEIDRMTLTMAVELPDSFSPELRSLLE 237
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2056392213 264 KLLVKETRKRLTI-----QEALRHPWITPVDNQQAMVRR 297
Cdd:cd14223   238 GLLQRDVNRRLGCmgrgaQEVKEEPFFRGLDWQMVFLQK 276
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
32-228 2.02e-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: 78.51  E-value: 2.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  32 GQFAIVKKCREKSTGLEYAAKFIKKRQSRASrrgvsreeierEVSILRQVLHHNVITLHDVYENRTDVVLILELVSGGEL 111
Cdd:cd13995    15 GAFGKVYLAQDTKTKKRMACKLIPVEQFKPS-----------DVEIQACFRHENIAELYGALLWEETVHLFMEAGEGGSV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 112 FDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipiphIKLIDFGLAHEIEDGVEF-KNIFGT 190
Cdd:cd13995    84 LEKLESCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTK-----AVLVDFGLSVQMTEDVYVpKDLRGT 158
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2056392213 191 PEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFL 228
Cdd:cd13995   159 EIYMSPEVILCRGHNTKADIYSLGATIIHMQTGSPPWV 196
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
4-313 2.03e-16

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: 79.71  E-value: 2.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213   4 ASMRSPNM-EPFKQQKVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAakfIKKRQSRASRRGVSREEIEREVSILRQVL 82
Cdd:cd06635     7 GSLKDPDIaELFFKEDPEKLFSDLREIGHGSFGAVYFARDVRTSEVVA---IKKMSYSGKQSNEKWQDIIKEVKFLQRIK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  83 HHNVITLHDVYENRTDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNi 162
Cdd:cd06635    84 HPNSIEYKGCYLREHTAWLVMEYCLGSASDLLEVHKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPG- 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 163 pipHIKLIDFGLAHEIEDGVEFkniFGTPEFVAPEIVNYEPLGL---EADMWSIGVITYILLSGASPFLGDTKQETLANI 239
Cdd:cd06635   163 ---QVKLADFGSASIASPANSF---VGTPYWMAPEVILAMDEGQydgKVDVWSLGITCIELAERKPPLFNMNAMSALYHI 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 240 TAvsydfDEEFFSQTSELA---KDFIRKLLVKETRKRLTIQEALRHPWITPVDNQQAMV-----RRESVVNLENFRKQYV 311
Cdd:cd06635   237 AQ-----NESPTLQSNEWSdyfRNFVDSCLQKIPQDRPTSEELLKHMFVLRERPETVLIdliqrTKDAVRELDNLQYRKM 311

                  ..
gi 2056392213 312 RR 313
Cdd:cd06635   312 KK 313
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
27-239 2.03e-16

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: 78.78  E-value: 2.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFAIVKKCREKSTgLEYAAKFIKKRQsrasrrgVSREEIEREVSILRQVLHHNVITLHDVYeNRTDVVLILELV 106
Cdd:cd05067    13 ERLGAGQFGEVWMGYYNGH-TKVAIKSLKQGS-------MSPDAFLAEANLMKQLQHQRLVRLYAVV-TQEPIYIITEYM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 107 SGGELFDFLAQKE--SLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKnipiPHIKLIDFGLAHEIEDGvEF 184
Cdd:cd05067    84 ENGSLVDFLKTPSgiKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDT----LSCKIADFGLARLIEDN-EY 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2056392213 185 KNIFGTP---EFVAPEIVNYEPLGLEADMWSIGV-ITYILLSGASPFLGDTKQETLANI 239
Cdd:cd05067   159 TAREGAKfpiKWTAPEAINYGTFTIKSDVWSFGIlLTEIVTHGRIPYPGMTNPEVIQNL 217
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
66-285 2.18e-16

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: 80.17  E-value: 2.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  66 VSREEIEREVSILRQVLHHNVITLHDV--------YEnrtDVVLILELVSGgELFDFLAQKESLSEEEATSFIKQILDGV 137
Cdd:cd07853    41 VSCKRVFRELKMLCFFKHDNVLSALDIlqpphidpFE---EIYVVTELMQS-DLHKIIVSPQPLSSDHVKVFLYQILRGL 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 138 NYLHTKKIAHFDLKPENImLLDKNIpipHIKLIDFGLAhEIEDGVEFKNIfgTPEFV-----APEIVNYEP-LGLEADMW 211
Cdd:cd07853   117 KYLHSAGILHRDIKPGNL-LVNSNC---VLKICDFGLA-RVEEPDESKHM--TQEVVtqyyrAPEILMGSRhYTSAVDIW 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 212 SIGVITYILLSG------ASP---------FLGDTKQETL--ANITAVSY---------DFDEEFF--SQTSELAKDFIR 263
Cdd:cd07853   190 SVGCIFAELLGRrilfqaQSPiqqldlitdLLGTPSLEAMrsACEGARAHilrgphkppSLPVLYTlsSQATHEAVHLLC 269
                         250       260
                  ....*....|....*....|..
gi 2056392213 264 KLLVKETRKRLTIQEALRHPWI 285
Cdd:cd07853   270 RMLVFDPDKRISAADALAHPYL 291
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
27-239 2.54e-16

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror2 plays important roles in skeletal and heart formation. Ror2-deficient mice show widespread bone abnormalities, ventricular defects in the heart, and respiratory dysfunction. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Ror2 is also implicated in neural development. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 78.91  E-value: 2.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFAIVKKCREKST--GLEYAAKFIKKRQSRAsrRGVSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILE 104
Cdd:cd05091    12 EELGEDRFGKVYKGHLFGTapGEQTQAVAIKTLKDKA--EGPLREEFRHEAMLRSRLQHPNIVCLLGVVTKEQPMSMIFS 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 105 LVSGGELFDFLAQ----------------KESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKnipiPHIK 168
Cdd:cd05091    90 YCSHGDLHEFLVMrsphsdvgstdddktvKSTLEPADFLHIVTQIAAGMEYLSSHHVVHKDLATRNVLVFDK----LNVK 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2056392213 169 LIDFGLAHEIEDGVEFKNIFGTP---EFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPFLGDTKQETLANI 239
Cdd:cd05091   166 ISDLGLFREVYAADYYKLMGNSLlpiRWMSPEAIMYGKFSIDSDIWSYGVVLWEVFSyGLQPYCGYSNQDVIEMI 240
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
6-229 3.65e-16

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: 78.23  E-value: 3.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213   6 MRSPNMEPFKQQKVedfydigeeLGSGQFAIVKKCREKSTG----LEYAAKFIKKRQSRASRrgvsrEEIEREVSILRQV 81
Cdd:cd05057     1 LRIVKETELEKGKV---------LGSGAFGTVYKGVWIPEGekvkIPVAIKVLREETGPKAN-----EEILDEAYVMASV 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  82 LHHNVITLHDVYENRTdVVLILELVSGGELFDFLAQ-KESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDK 160
Cdd:cd05057    67 DHPHLVRLLGICLSSQ-VQLITQLMPLGCLLDYVRNhRDNIGSQLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTP 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2056392213 161 NipipHIKLIDFGLAHEIE-DGVEFKNIFG-TP-EFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPFLG 229
Cdd:cd05057   146 N----HVKITDFGLAKLLDvDEKEYHAEGGkVPiKWMALESIQYRIYTHKSDVWSYGVTVWELMTfGAKPYEG 214
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
29-239 3.68e-16

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: 78.22  E-value: 3.68e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTgLEYAAKFIKKRQsrasrrgVSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSG 108
Cdd:cd05068    16 LGSGQFGEVWEGLWNNT-TPVAVKTLKPGT-------MDPEDFLREAQIMKKLRHPKLIQLYAVCTLEEPIYIITELMKH 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 109 GELFDFL-AQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIEDGVEFKNI 187
Cdd:cd05068    88 GSLLEYLqGKGRSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVGENNI----CKVADFGLARVIKVEDEYEAR 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2056392213 188 FGTP---EFVAPEIVNYEPLGLEADMWSIGV-ITYILLSGASPFLGDTKQETLANI 239
Cdd:cd05068   164 EGAKfpiKWTAPEAANYNRFSIKSDVWSFGIlLTEIVTYGRIPYPGMTNAEVLQQV 219
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
23-227 3.69e-16

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: 78.55  E-value: 3.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIgeELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRgvsrEEIEREVSILRQVLHHNVITLHDVYEN----RTD 98
Cdd:cd14030    29 FDI--EIGRGSFKTVYKGLDTETTVEVAWCELQDRKLSKSER----QRFKEEAGMLKGLQHPNIVRFYDSWEStvkgKKC 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  99 VVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKK--IAHFDLKPENIMLLDkniPIPHIKLIDFGLAh 176
Cdd:cd14030   103 IVLVTELMTSGTLKTYLKRFKVMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITG---PTGSVKIGDLGLA- 178
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2056392213 177 EIEDGVEFKNIFGTPEFVAPEIVNyEPLGLEADMWSIGVITYILLSGASPF 227
Cdd:cd14030   179 TLKRASFAKSVIGTPEFMAPEMYE-EKYDESVDVYAFGMCMLEMATSEYPY 228
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
23-227 4.86e-16

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 80.55  E-value: 4.86e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213   23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIkkrqsraSRRGVSREEIER---EVSILRQVLHHNVITLHDVYENRTD- 98
Cdd:PTZ00266    15 YEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAI-------SYRGLKEREKSQlviEVNVMRELKHKNIVRYIDRFLNKANq 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213   99 -VVLILELVSGGELFDFLaQK-----ESLSEEEATSFIKQILDGVNYLHT-------KKIAHFDLKPENIMLldkNIPIP 165
Cdd:PTZ00266    88 kLYILMEFCDAGDLSRNI-QKcykmfGKIEEHAIVDITRQLLHALAYCHNlkdgpngERVLHRDLKPQNIFL---STGIR 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  166 HI----------------KLIDFGLAHEIedGVE--FKNIFGTPEFVAPEIVNYEPLGLE--ADMWSIGVITYILLSGAS 225
Cdd:PTZ00266   164 HIgkitaqannlngrpiaKIGDFGLSKNI--GIEsmAHSCVGTPYYWSPELLLHETKSYDdkSDMWALGCIIYELCSGKT 241

                   ..
gi 2056392213  226 PF 227
Cdd:PTZ00266   242 PF 243
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
29-239 7.11e-16

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: 77.32  E-value: 7.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRgvSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSG 108
Cdd:cd05063    13 IGAGEFGEVFRGILKMPGRKEVAVAIKTLKPGYTEK--QRQDFLSEASIMGQFSHHNIIRLEGVVTKFKPAMIITEYMEN 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 109 GELFDFLAQKE-SLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNIpipHIKLIDFGLAHEIEDGVEfkNI 187
Cdd:cd05063    91 GALDKYLRDHDgEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNI-LVNSNL---ECKVSDFGLSRVLEDDPE--GT 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2056392213 188 FGTP------EFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPFLGDTKQETLANI 239
Cdd:cd05063   165 YTTSggkipiRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSfGERPYWDMSNHEVMKAI 223
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
18-226 8.91e-16

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


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 78.17  E-value: 8.91e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  18 KVEDFYDIGEeLGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRrgvsrEEIEREVSILRQVLHHNVITLHDVYENRT 97
Cdd:cd06649     3 KDDDFERISE-LGAGNGGVVTKVQHKPSGLIMARKLIHLEIKPAIR-----NQIIRELQVLHECNSPYIVGFYGAFYSDG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  98 DVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTK-KIAHFDLKPENIMLLDKNipipHIKLIDFGLAH 176
Cdd:cd06649    77 EISICMEHMDGGSLDQVLKEAKRIPEEILGKVSIAVLRGLAYLREKhQIMHRDVKPSNILVNSRG----EIKLCDFGVSG 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2056392213 177 EIEDGVEfKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASP 226
Cdd:cd06649   153 QLIDSMA-NSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVELAIGRYP 201
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
18-215 1.10e-15

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: 77.40  E-value: 1.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  18 KVEDFYDIgEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRrgvsrEEIEREVSILRQVLHHNVITLHDVYENRT 97
Cdd:cd06650     3 KDDDFEKI-SELGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPAIR-----NQIIRELQVLHECNSPYIVGFYGAFYSDG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  98 DVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTK-KIAHFDLKPENIMLLDKNipipHIKLIDFGLAH 176
Cdd:cd06650    77 EISICMEHMDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYLREKhKIMHRDVKPSNILVNSRG----EIKLCDFGVSG 152
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2056392213 177 EIEDGVEfKNIFGTPEFVAPEIVNYEPLGLEADMWSIGV 215
Cdd:cd06650   153 QLIDSMA-NSFVGTRSYMSPERLQGTHYSVQSDIWSMGL 190
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
22-246 1.14e-15

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: 76.83  E-value: 1.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  22 FYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRgvSREEIEREVSILRQVLHHNVITLHDVYENRTDVVL 101
Cdd:cd05065     5 CVKIEEVIGAGEFGEVCRGRLKLPGKREIFVAIKTLKSGYTEK--QRRDFLSEASIMGQFDHPNIIHLEGVVTKSRPVMI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 102 ILELVSGGELFDFLAQKE-SLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNIPiphIKLIDFGLAHEIED 180
Cdd:cd05065    83 ITEFMENGALDSFLRQNDgQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNI-LVNSNLV---CKVSDFGLSRFLED 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2056392213 181 GVE---FKNIFGTP---EFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPFLGDTKQETlanITAVSYDF 246
Cdd:cd05065   159 DTSdptYTSSLGGKipiRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSyGERPYWDMSNQDV---INAIEQDY 228
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
29-282 1.23e-15

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: 76.84  E-value: 1.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIkkrqsRASRRGVSREEIEREVSILRQVLHHNVITLHDVYENR--------TDVV 100
Cdd:cd14048    14 LGRGGFGVVFEAKNKVDDCNYAVKRI-----RLPNNELAREKVLREVRALAKLDHPGIVRYFNAWLERppegwqekMDEV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 101 ---LILELVSGGELFDFLAQKESLSEEE---ATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGL 174
Cdd:cd14048    89 ylyIQMQLCRKENLKDWMNRRCTMESRElfvCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDV----VKVGDFGL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 175 AHEIEDGVEFKNI-------------FGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASpflgdTKQETLANITA 241
Cdd:cd14048   165 VTAMDQGEPEQTVltpmpayakhtgqVGTRLYMSPEQIHGNQYSEKVDIFALGLILFELIYSFS-----TQMERIRTLTD 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2056392213 242 VSYDFDEEFFSQTSELAKDFIRKLLVKETRKRLTIQEALRH 282
Cdd:cd14048   240 VRKLKFPALFTNKYPEERDMVQQMLSPSPSERPEAHEVIEH 280
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
29-234 1.47e-15

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: 76.23  E-value: 1.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKfIKKRQSRASRRgvSREEIEREVSILRQVLHH-NVITLHDVYENRTDVVLILELVS 107
Cdd:cd05047     3 IGEGNFGQVLKARIKKDGLRMDAA-IKRMKEYASKD--DHRDFAGELEVLCKLGHHpNIINLLGACEHRGYLYLAIEYAP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 108 GGELFDFLAQKE----------------SLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPiphiKLID 171
Cdd:cd05047    80 HGNLLDFLRKSRvletdpafaianstasTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVA----KIAD 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2056392213 172 FGLAHEIEdgVEFKNIFG--TPEFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPFLGDTKQE 234
Cdd:cd05047   156 FGLSRGQE--VYVKKTMGrlPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAE 219
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
27-236 1.48e-15

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: 76.22  E-value: 1.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFAIV-KKCREKSTglEYAAKFIKKRQsrasrrgVSREEIEREVSILRQVLHHNVITLHDVYeNRTDVVLILEL 105
Cdd:cd05073    17 KKLGAGQFGEVwMATYNKHT--KVAVKTMKPGS-------MSVEAFLAEANVMKTLQHDKLVKLHAVV-TKEPIYIITEF 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 106 VSGGELFDFLAQKESLSEE--EATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIEDGvE 183
Cdd:cd05073    87 MAKGSLLDFLKSDEGSKQPlpKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLV----CKIADFGLARVIEDN-E 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2056392213 184 FKNIFGTP---EFVAPEIVNYEPLGLEADMWSIGV-ITYILLSGASPFLGDTKQETL 236
Cdd:cd05073   162 YTAREGAKfpiKWTAPEAINFGSFTIKSDVWSFGIlLMEIVTYGRIPYPGMSNPEVI 218
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
29-229 2.15e-15

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: 75.51  E-value: 2.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKstGLEYAAKfiKKRQSRASRRGVSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSG 108
Cdd:cd14061     2 IGVGGFGKVYRGIWR--GEEVAVK--AARQDPDEDISVTLENVRQEARLFWMLRHPNIIALRGVCLQPPNLCLVMEYARG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 109 GELFDFLAqKESLSEEEATSFIKQILDGVNYLHTKK---IAHFDLKPENIMLLDK----NIPIPHIKLIDFGLAHEIEDG 181
Cdd:cd14061    78 GALNRVLA-GRKIPPHVLVDWAIQIARGMNYLHNEApvpIIHRDLKSSNILILEAieneDLENKTLKITDFGLAREWHKT 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2056392213 182 VEFKNIfGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLG 229
Cdd:cd14061   157 TRMSAA-GTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPYKG 203
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
29-227 2.17e-15

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: 76.00  E-value: 2.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLeyaakFIKKRQSRASRRGVSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSG 108
Cdd:cd14027     1 LDSGGFGKVSLCFHRTQGL-----VVLKTVYTGPNCIEHNEALLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 109 GELFDFLaQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNIpipHIKLIDFGLA------------H 176
Cdd:cd14027    76 GNLMHVL-KKVSVPLSVKGRIILEIIEGMAYLHGKGVIHKDLKPENI-LVDNDF---HIKIADLGLAsfkmwskltkeeH 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2056392213 177 EIEDGVE--FKNIFGTPEFVAPE---IVNYEPLGlEADMWSIGVITYILLSGASPF 227
Cdd:cd14027   151 NEQREVDgtAKKNAGTLYYMAPEhlnDVNAKPTE-KSDVYSFAIVLWAIFANKEPY 205
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
29-216 2.55e-15

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: 75.20  E-value: 2.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASrrgvsreeIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSG 108
Cdd:cd14155     1 IGSGFFSEVYKVRHRTSGQVMALKMNTLSSNRAN--------MLREVQLMNRLSHPNILRFMGVCVHQGQLHALTEYING 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 109 GELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIkLIDFGLAHEI---EDGVEFK 185
Cdd:cd14155    73 GNLEQLLDSNEPLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIKRDENGYTAV-VGDFGLAEKIpdySDGKEKL 151
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2056392213 186 NIFGTPEFVAPEIVNYEPLGLEADMWSIGVI 216
Cdd:cd14155   152 AVVGSPYWMAPEVLRGEPYNEKADVFSYGII 182
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
25-227 3.14e-15

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: 75.48  E-value: 3.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  25 IGEELGSGQFAIVKKCREKStglEYAAKFIKKRQSRASRRgvsrEEIEREVSILRQVLHHNVItLHDVYENRTDVVLILE 104
Cdd:cd14151    12 VGQRIGSGSFGTVYKGKWHG---DVAVKMLNVTAPTPQQL----QAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQ 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 105 LVSGGELFDFLAQKESLSE-EEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLA---HEIED 180
Cdd:cd14151    84 WCEGSSLYHHLHIIETKFEmIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLT----VKIGDFGLAtvkSRWSG 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2056392213 181 GVEFKNIFGTPEFVAPEIVNYE---PLGLEADMWSIGVITYILLSGASPF 227
Cdd:cd14151   160 SHQFEQLSGSILWMAPEVIRMQdknPYSFQSDVYAFGIVLYELMTGQLPY 209
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
37-229 4.21e-15

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: 75.00  E-value: 4.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  37 VKKCREKSTGleYAAKFIKKRQSRASRRGVSreEIEREVSILRQVLHHNVITLHDVyeNRTDVVLILELVSGGELFDFLA 116
Cdd:cd14067    27 IKKCKKRTDG--SADTMLKHLRAADAMKNFS--EFRQEASMLHSLQHPCIVYLIGI--SIHPLCFALELAPLGSLNTVLE 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 117 QKEslseeEATSFIK-----------QILDGVNYLHTKKIAHFDLKPENIML--LDKNIPIpHIKLIDFGLA----HEIE 179
Cdd:cd14067   101 ENH-----KGSSFMPlghmltfkiayQIAAGLAYLHKKNIIFCDLKSDNILVwsLDVQEHI-NIKLSDYGISrqsfHEGA 174
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2056392213 180 DGVEfknifGTPEFVAPEI---VNYEPlglEADMWSIGVITYILLSGASPFLG 229
Cdd:cd14067   175 LGVE-----GTPGYQAPEIrprIVYDE---KVDMFSYGMVLYELLSGQRPSLG 219
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
26-227 4.57e-15

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: 75.23  E-value: 4.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  26 GEELGSGQFAIVKKCREKSTGLEyaakfIKKRqsrASRRGVSREEI----EREVSILRQVLHHNVITLHDVYENRTDVVL 101
Cdd:cd14158    20 GNKLGEGGFGVVFKGYINDKNVA-----VKKL---AAMVDISTEDLtkqfEQEIQVMAKCQHENLVELLGYSCDGPQLCL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 102 ILELVSGGELFDFLAQKE---SLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPiphiKLIDFGLAHEI 178
Cdd:cd14158    92 VYTYMPNGSLLDRLACLNdtpPLSWHMRCKIAQGTANGINYLHENNHIHRDIKSANILLDETFVP----KISDFGLARAS 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2056392213 179 EDG---VEFKNIFGTPEFVAPEIVNYEpLGLEADMWSIGVITYILLSGASPF 227
Cdd:cd14158   168 EKFsqtIMTERIVGTTAYMAPEALRGE-ITPKSDIFSFGVVLLEIITGLPPV 218
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
27-295 8.88e-15

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: 74.14  E-value: 8.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRgvsreEIEREVSILRQVLHHNVITLHDVY--ENRtdVVLILE 104
Cdd:cd06619     7 EILGHGNGGTVYKAYHLLTRRILAVKVIPLDITVELQK-----QIMSELEILYKCDSPYIIGFYGAFfvENR--ISICTE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 105 LVSGGELFDFLAQKESLSEEEATSFIKqildGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIEDGVEf 184
Cdd:cd06619    80 FMDGGSLDVYRKIPEHVLGRIAVAVVK----GLTYLWSLKILHRDVKPSNMLVNTRG----QVKLCDFGVSTQLVNSIA- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 185 KNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTK-QETLANITAVSYDFDEEF----FSQTSELAK 259
Cdd:cd06619   151 KTYVGTNAYMAPERISGEQYGIHSDVWSLGISFMELALGRFPYPQIQKnQGSLMPLQLLQCIVDEDPpvlpVGQFSEKFV 230
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2056392213 260 DFIRKLLVKETRKRLTIQEALRHPWITPVDNQQAMV 295
Cdd:cd06619   231 HFITQCMRKQPKERPAPENLMDHPFIVQYNDGNAEV 266
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
56-285 1.57e-14

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: 74.35  E-value: 1.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  56 KRQSRASRRGVSREEIEREVSILRQVLHHNVITLHDVY------ENRTDVVLILELVSGGelfdfLAQ--KESLSEEEAT 127
Cdd:cd07874    48 KKLSRPFQNQTHAKRAYRELVLMKCVNHKNIISLLNVFtpqkslEEFQDVYLVMELMDAN-----LCQviQMELDHERMS 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 128 SFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIEDGVEFKNIFGTPEFVAPEIVNYEPLGLE 207
Cdd:cd07874   123 YLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCT----LKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGYKEN 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 208 ADMWSIGVIT------YILLSG----------------ASPFLGDTKQETLAN-------ITAVSYD--FDEEFFSQTSE 256
Cdd:cd07874   199 VDIWSVGCIMgemvrhKILFPGrdyidqwnkvieqlgtPCPEFMKKLQPTVRNyvenrpkYAGLTFPklFPDSLFPADSE 278
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2056392213 257 -------LAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd07874   279 hnklkasQARDLLSKMLVIDPAKRISVDEALQHPYI 314
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
21-284 1.87e-14

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: 73.72  E-value: 1.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  21 DFYDIGEELGSGQFAIVKKCREKSTGLEYAakfIKKRQSRASRRGVSREEIeREVSILRQVLHHN-VITLHDVYENRTDV 99
Cdd:cd07837     1 DAYEKLEKIGEGTYGKVYKARDKNTGKLVA---LKKTRLEMEEEGVPSTAL-REVSLLQMLSQSIyIVRLLDVEHVEENG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 100 VLILELVsggelFDFLAQK-------------ESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENiMLLDKNIPIph 166
Cdd:cd07837    77 KPLLYLV-----FEYLDTDlkkfidsygrgphNPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQN-LLVDKQKGL-- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 167 IKLIDFGLAHEIEdgVEFKNIfgTPEFV-----APEIVnyepLG-----LEADMWSIGVITYILLSGASPFLGDTKQETL 236
Cdd:cd07837   149 LKIADLGLGRAFT--IPIKSY--THEIVtlwyrAPEVL----LGsthysTPVDMWSVGCIFAEMSRKQPLFPGDSELQQL 220
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2056392213 237 ANITAVSYDFDEEFFSQTSEL------------------------AKDFIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd07837   221 LHIFRLLGTPNEEVWPGVSKLrdwheypqwkpqdlsravpdlepeGVDLLTKMLAYDPAKRISAKAALQHPY 292
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
29-285 2.11e-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: 74.31  E-value: 2.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVkkCREKSTGLEYAAKFikKRQSRASRRGVSREEIEREVSILRQVLHHNVITLHDVY------ENRTDVVLI 102
Cdd:cd07875    32 IGSGAQGIV--CAAYDAILERNVAI--KKLSRPFQNQTHAKRAYRELVLMKCVNHKNIIGLLNVFtpqkslEEFQDVYIV 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGelfdfLAQ--KESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIED 180
Cdd:cd07875   108 MELMDAN-----LCQviQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCT----LKILDFGLARTAGT 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 181 GVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPF---------------LGDTKQETLANITAV--- 242
Cdd:cd07875   179 SFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIKGGVLFpgtdhidqwnkvieqLGTPCPEFMKKLQPTvrt 258
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2056392213 243 ---------SYDFDEEF----FSQTSE-------LAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd07875   259 yvenrpkyaGYSFEKLFpdvlFPADSEhnklkasQARDLLSKMLVIDASKRISVDEALQHPYI 321
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
74-263 2.12e-14

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 74.14  E-value: 2.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  74 EVSILRQVLHHNVITLHDVYENRTDVVLILELVSGgELFDFLAQKES-LSEEEATSFIKQILDGVNYLHTKKIAHFDLKP 152
Cdd:PHA03209  107 EAMLLQNVNHPSVIRMKDTLVSGAITCMVLPHYSS-DLYTYLTKRSRpLPIDQALIIEKQILEGLRYLHAQRIIHRDVKT 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 153 ENIMLLDknipIPHIKLIDFGLAHEIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGD-- 230
Cdd:PHA03209  186 ENIFIND----VDQVCIGDLGAAQFPVVAPAFLGLAGTVETNAPEVLARDKYNSKADIWSAGIVLFEMLAYPSTIFEDpp 261
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2056392213 231 -TKQETLAN--------ITAVSYDFDEEFFSQTSELAKDFIR 263
Cdd:PHA03209  262 sTPEEYVKSchshllkiISTLKVHPEEFPRDPGSRLVRGFIE 303
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
27-234 2.22e-14

Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Ror subfamily consists of Ror1, Ror2, and similar proteins. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. Ror kinases are expressed in many tissues during development. They play important roles in bone and heart formation. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Drosophila Ror is expressed only in the developing nervous system during neurite outgrowth and neuronal differentiation, suggesting a role for Drosophila Ror in neural development. More recently, mouse Ror1 and Ror2 have also been found to play an important role in regulating neurite growth in central neurons. Ror1 and Ror2 are believed to have some overlapping and redundant functions. The Ror subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 73.18  E-value: 2.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELV 106
Cdd:cd05048    11 EELGEGAFGKVYKGELLGPSSEESAISVAIKTLKENASPKTQQDFRREAELMSDLQHPNIVCLLGVCTKEQPQCMLFEYM 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 107 SGGELFDFLAQKESLSEEEATS-------------FIK---QILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLI 170
Cdd:cd05048    91 AHGDLHEFLVRHSPHSDVGVSSdddgtassldqsdFLHiaiQIAAGMEYLSSHHYVHRDLAARNCLVGDGL----TVKIS 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2056392213 171 DFGLAHEIEDGVEFKNIFGTP---EFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPFLGDTKQE 234
Cdd:cd05048   167 DFGLSRDIYSSDYYRVQSKSLlpvRWMPPEAILYGKFTTESDVWSFGVVLWEIFSyGLQPYYGYSNQE 234
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
20-285 2.62e-14

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: 73.17  E-value: 2.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  20 EDFYDIGEeLGSGQFAIVKKCREKSTGLEYAAKFIkkrqsRASRRGVSREEIEREV-SILRQVLHHNVITLHDVYENRTD 98
Cdd:cd06616     6 EDLKDLGE-IGRGAFGTVNKMLHKPSGTIMAVKRI-----RSTVDEKEQKRLLMDLdVVMRSSDCPYIVKFYGALFREGD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  99 VVLILEL--VSGGELFDF--LAQKESLSEEEATSFIKQILDGVNYLHTK-KIAHFDLKPENImLLDKNipiPHIKLIDFG 173
Cdd:cd06616    80 CWICMELmdISLDKFYKYvyEVLDSVIPEEILGKIAVATVKALNYLKEElKIIHRDVKPSNI-LLDRN---GNIKLCDFG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 174 LAHEIEDGVEFKNIFGTPEFVAPEIVN----YEPLGLEADMWSIGVITYILLSGASPFlgDTKQETLANITAVSY----- 244
Cdd:cd06616   156 ISGQLVDSIAKTRDAGCRPYMAPERIDpsasRDGYDVRSDVWSLGITLYEVATGKFPY--PKWNSVFDQLTQVVKgdppi 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2056392213 245 ---DFDEEFfsqtSELAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd06616   234 lsnSEEREF----SPSFVNFVNLCLIKDESKRPKYKELLKHPFI 273
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
83-285 3.26e-14

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: 72.08  E-value: 3.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  83 HHNVITLHDVYENRTDVVLILELVSGgELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNI 162
Cdd:cd13976    44 HPNISGVHEVIAGETKAYVFFERDHG-DLHSYVRSRKRLREPEAARLFRQIASAVAHCHRNGIVLRDLKLRKFVFADEER 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 163 PipHIKLIDFGLAHeIEDGVE--FKNIFGTPEFVAPEIVN----YEplGLEADMWSIGVITYILLSGASPFLGDTKQETL 236
Cdd:cd13976   123 T--KLRLESLEDAV-ILEGEDdsLSDKHGCPAYVSPEILNsgatYS--GKAADVWSLGVILYTMLVGRYPFHDSEPASLF 197
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2056392213 237 ANITAVSYDFDEEFfsqtSELAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd13976   198 AKIRRGQFAIPETL----SPRARCLIRSLLRREPSERLTAEDILLHPWL 242
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
72-229 3.37e-14

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 73.72  E-value: 3.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  72 EREVSILRQVLHHNVITLHDVYENRTDVVLILElVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLK 151
Cdd:PHA03207  134 GREIDILKTISHRAIINLIHAYRWKSTVCMVMP-KYKCDLFTYVDRSGPLPLEQAITIQRRLLEALAYLHGRGIIHRDVK 212
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 152 PENIMLLDKNIPIphikLIDFGLAHEIEDGVEFKNIF---GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFL 228
Cdd:PHA03207  213 TENIFLDEPENAV----LGDFGAACKLDAHPDTPQCYgwsGTLETNSPELLALDPYCAKTDIWSAGLVLFEMSVKNVTLF 288

                  .
gi 2056392213 229 G 229
Cdd:PHA03207  289 G 289
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
29-280 4.23e-14

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: 72.16  E-value: 4.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRrgvsreEIEREVSILRQVL-HHNVITL--------HDVYENRTDV 99
Cdd:cd14036     8 IAEGGFAFVYEAQDVGTGKEYALKRLLSNEEEKNK------AIIQEINFMKKLSgHPNIVQFcsaasigkEESDQGQAEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 100 VLILELVSGGeLFDFLAQKESLSEEEATSFIK---QILDGVNYLHTKK--IAHFDLKPENIMLLDKNIpiphIKLIDFG- 173
Cdd:cd14036    82 LLLTELCKGQ-LVDFVKKVEAPGPFSPDTVLKifyQTCRAVQHMHKQSppIIHRDLKIENLLIGNQGQ----IKLCDFGs 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 174 ---LAH------------EIEDGVEfKNIfgTPEFVAPEIV----NYePLGLEADMWSIGVITYILLSGASPFLGDTKQE 234
Cdd:cd14036   157 attEAHypdyswsaqkrsLVEDEIT-RNT--TPMYRTPEMIdlysNY-PIGEKQDIWALGCILYLLCFRKHPFEDGAKLR 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2056392213 235 TL-ANITAVSYDFDEEFFSqtselakDFIRKLLVKETRKRLTIQEAL 280
Cdd:cd14036   233 IInAKYTIPPNDTQYTVFH-------DLIRSTLKVNPEERLSITEIV 272
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
23-239 7.02e-14

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: 71.33  E-value: 7.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKfIKKRQSRASRrgvsreeIEREVSILRQV-LHHNVITLHDVYENRTDVVL 101
Cdd:cd14016     2 YKLVKKIGSGSFGEVYLGIDLKTGEEVAIK-IEKKDSKHPQ-------LEYEAKVYKLLqGGPGIPRLYWFGQEGDYNVM 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 102 ILELV--SGGELFDFLAQKesLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIML-LDKNIPIphIKLIDFGLAHEI 178
Cdd:cd14016    74 VMDLLgpSLEDLFNKCGRK--FSLKTVLMLADQMISRLEYLHSKGYIHRDIKPENFLMgLGKNSNK--VYLIDFGLAKKY 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2056392213 179 EDG--------VEFKNIFGTPEFVApeiVNYEpLGLEA----DMWSIGvitYIL---LSGASPFLG---DTKQETLANI 239
Cdd:cd14016   150 RDPrtgkhipyREGKSLTGTARYAS---INAH-LGIEQsrrdDLESLG---YVLiyfLKGSLPWQGlkaQSKKEKYEKI 221
PK_NRBP1_like cd13984
Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The ...
67-283 7.82e-14

Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. This subfamily is composed of NRBP1, also called MLF1-adaptor molecule (MADM), and MADML. NRBP1 was originally named based on the presence of nuclear binding and localization motifs prior to functional analyses. It is expressed ubiquitously and is found to localize in the cytoplasm, not the nucleus. NRBP1 is an adaptor protein that interacts with myeloid leukemia factor 1 (MLF1), an oncogene that enhances myeloid development of hematopoietic cells. It also interacts with the small GTPase Rac3. NRBP1 may also be involved in Golgi to ER trafficking. MADML (for MADM-Like) has been shown to be expressed throughout development in Xenopus laevis with highest expression found in the developing lens and retina. The NRBP1-like 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: 270886 [Multi-domain]  Cd Length: 256  Bit Score: 71.03  E-value: 7.82e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  67 SREEIEREV-SILRQVLHHNVITLH----DVYENRTDVVLILELVSGGELFDFLAQ----KESLSEEEATSFIKQILDGV 137
Cdd:cd13984    37 AQEEKIRAVfDNLIQLDHPNIVKFHrywtDVQEEKARVIFITEYMSSGSLKQFLKKtkknHKTMNEKSWKRWCTQILSAL 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 138 NYLHT--KKIAHFDLKPENIMlldknipIPHIKLIDFG------LAHEIEdgvEFKNIFGTPEFVAPEIVNYEPLGLEAD 209
Cdd:cd13984   117 SYLHScdPPIIHGNLTCDTIF-------IQHNGLIKIGsvapdaIHNHVK---TCREEHRNLHFFAPEYGYLEDVTTAVD 186
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2056392213 210 MWSIGVITyilLSGASPFLGDTKQETLANITAVSydfdEEFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHP 283
Cdd:cd13984   187 IYSFGMCA---LEMAALEIQSNGEKVSANEEAII----RAIFSLEDPLQKDFIRKCLSVAPQDRPSARDLLFHP 253
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
24-227 7.88e-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: 71.23  E-value: 7.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  24 DIGEELGSGQFAIVKKCREKStglEYAAKFIKKRqsrasrrGVSREEIE---REVSILRQVLHHNVITLHDVYENRTDVV 100
Cdd:cd14063     3 EIKEVIGKGRFGRVHRGRWHG---DVAIKLLNID-------YLNEEQLEafkEEVAAYKNTRHDNLVLFMGACMDPPHLA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 101 LILELVSGGELFDFL-AQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipipHIKLIDFGL--AHE 177
Cdd:cd14063    73 IVTSLCKGRTLYSLIhERKEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNI-FLENG----RVVITDFGLfsLSG 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2056392213 178 IEDGVEFKNIFGTPE----FVAPEIV----------NYEPLGLEADMWSIGVITYILLSGASPF 227
Cdd:cd14063   148 LLQPGRREDTLVIPNgwlcYLAPEIIralspdldfeESLPFTKASDVYAFGTVWYELLAGRWPF 211
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
23-284 8.54e-14

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 72.76  E-value: 8.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVkkcrekstgleYAAKFIKKRQSRASRRGVSREEIE-REVSILRQVLHHNVITLHDVY------EN 95
Cdd:PTZ00036   68 YKLGNIIGNGSFGVV-----------YEAICIDTSEKVAIKKVLQDPQYKnRELLIMKNLNHINIIFLKDYYytecfkKN 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  96 RTDVVL--ILELVSG---GELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENiMLLDkniPIPH-IKL 169
Cdd:PTZ00036  137 EKNIFLnvVMEFIPQtvhKYMKHYARNNHALPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQN-LLID---PNTHtLKL 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 170 IDFGLAHEIEDGVEFKNIFGTPEFVAPEIV----NYEPlglEADMWSIGVITYILLSGASPFLGDTKQETLANITAV--- 242
Cdd:PTZ00036  213 CDFGSAKNLLAGQRSVSYICSRFYRAPELMlgatNYTT---HIDLWSLGCIIAEMILGYPIFSGQSSVDQLVRIIQVlgt 289
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2056392213 243 ----------------------SYDFDEEFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPW 284
Cdd:PTZ00036  290 ptedqlkemnpnyadikfpdvkPKDLKKVFPKGTPDDAINFISQFLKYEPLKRLNPIEALADPF 353
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
19-284 8.93e-14

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: 71.97  E-value: 8.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  19 VEDFYDIGEELGSGQFAIVKKCRE-KSTGLEYAAKFIKKRQSRasrrgvsREEIEREVSILRQVLH------HNVITLHD 91
Cdd:cd14215    10 LQERYEIVSTLGEGTFGRVVQCIDhRRGGARVALKIIKNVEKY-------KEAARLEINVLEKINEkdpenkNLCVQMFD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  92 VYENRTDVVLILELVsGGELFDFLAQKESL--SEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPH--- 166
Cdd:cd14215    83 WFDYHGHMCISFELL-GLSTFDFLKENNYLpyPIHQVRHMAFQVCQAVKFLHDNKLTHTDLKPENILFVNSDYELTYnle 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 167 ------------IKLIDFGLAheIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQE 234
Cdd:cd14215   162 kkrdersvkstaIRVVDFGSA--TFDHEHHSTIVSTRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLFQTHDNRE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 235 TLANITAV---------------------SYDFDEE-----------------FFSQTSELAK--DFIRKLLVKETRKRL 274
Cdd:cd14215   240 HLAMMERIlgpipsrmirktrkqkyfyhgRLDWDENtsagryvrenckplrryLTSEAEEHHQlfDLIESMLEYEPSKRL 319
                         330
                  ....*....|
gi 2056392213 275 TIQEALRHPW 284
Cdd:cd14215   320 TLAAALKHPF 329
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
23-284 1.53e-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: 71.42  E-value: 1.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCRE-KSTGLEYAAKFIKKRqsrasrrGVSREEIEREVSILRQVLHHN------VITLHDVYEN 95
Cdd:cd14213    14 YEIVDTLGEGAFGKVVECIDhKMGGMHVAVKIVKNV-------DRYREAARSEIQVLEHLNTTDpnstfrCVQMLEWFDH 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  96 RTDVVLILELVsGGELFDFLAQKESL--SEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPI--------- 164
Cdd:cd14213    87 HGHVCIVFELL-GLSTYDFIKENSFLpfPIDHIRNMAYQICKSVNFLHHNKLTHTDLKPENILFVQSDYVVkynpkmkrd 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 165 ------PHIKLIDFGLAheIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLAN 238
Cdd:cd14213   166 ertlknPDIKVVDFGSA--TYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFQTHDSKEHLAM 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 239 ITAV---------------------SYDFDE----------------EFF-SQTSELAK--DFIRKLLVKETRKRLTIQE 278
Cdd:cd14213   244 MERIlgplpkhmiqktrkrkyfhhdQLDWDEhssagryvrrrckplkEFMlSQDVDHEQlfDLIQKMLEYDPAKRITLDE 323

                  ....*.
gi 2056392213 279 ALRHPW 284
Cdd:cd14213   324 ALKHPF 329
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
27-236 1.56e-13

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: 70.81  E-value: 1.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFAIVKKCREKSTGLEYAaKFIKKRQSRASRRGVSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELV 106
Cdd:cd05090    11 EELGECAFGKIYKGHLYLPGMDHA-QLVAIKTLKDYNNPQQWNEFQQEASLMTELHHPNIVCLLGVVTQEQPVCMLFEFM 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 107 SGGELFDFLAQKES------LSEEEAT--------SFIK---QILDGVNYLHTKKIAHFDLKPENIMLLDKnipiPHIKL 169
Cdd:cd05090    90 NQGDLHEFLIMRSPhsdvgcSSDEDGTvkssldhgDFLHiaiQIAAGMEYLSSHFFVHKDLAARNILVGEQ----LHVKI 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2056392213 170 IDFGLAHEIEDG----VEFKNIFGTpEFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPFLGDTKQETL 236
Cdd:cd05090   166 SDLGLSREIYSSdyyrVQNKSLLPI-RWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVI 236
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
83-231 1.67e-13

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 72.14  E-value: 1.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  83 HHNVITLHDVYENRTDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNI 162
Cdd:NF033483   66 HPNIVSVYDVGEDGGIPYIVMEYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGR 145
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2056392213 163 piphIKLIDFGLAHEI-EDGVEFKN-IFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDT 231
Cdd:NF033483  146 ----VKVTDFGIARALsSTTMTQTNsVLGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPFDGDS 212
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
23-285 1.98e-13

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: 70.71  E-value: 1.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTG-LEYAAKFIKKRQsrasrrgVSREEIEREVSILRQVLHHN------VITLHDVYEN 95
Cdd:cd14135     2 YRVYGYLGKGVFSNVVRARDLARGnQEVAIKIIRNNE-------LMHKAGLKELEILKKLNDADpddkkhCIRLLRHFEH 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  96 RTDVVLILELVSGgELFDFL---AQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIML-LDKNIpiphIKLID 171
Cdd:cd14135    75 KNHLCLVFESLSM-NLREVLkkyGKNVGLNIKAVRSYAQQLFLALKHLKKCNILHADIKPDNILVnEKKNT----LKLCD 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 172 FGLAHEIEDGvefkNIfgTPEFV-----APEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANI------- 239
Cdd:cd14135   150 FGSASDIGEN----EI--TPYLVsrfyrAPEIILGLPYDYPIDMWSVGCTLYELYTGKILFPGKTNNHMLKLMmdlkgkf 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 240 --------TAVSYDFDEE--FFSQ-----------------------TSELA----------------KDFIRKLLVKET 270
Cdd:cd14135   224 pkkmlrkgQFKDQHFDENlnFIYRevdkvtkkevrrvmsdikptkdlKTLLIgkqrlpdedrkkllqlKDLLDKCLMLDP 303
                         330
                  ....*....|....*
gi 2056392213 271 RKRLTIQEALRHPWI 285
Cdd:cd14135   304 EKRITPNEALQHPFI 318
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
27-241 2.19e-13

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: 69.89  E-value: 2.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFAIVKKCREKSTgLEYAAKFIKKRqsrasrrGVSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELV 106
Cdd:cd05114    10 KELGSGLFGVVRLGKWRAQ-YKVAIKAIREG-------AMSEEDFIEEAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 107 SGGELFDFLAQKES-LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIEDGvEFK 185
Cdd:cd05114    82 ENGCLLNYLRQRRGkLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGV----VKVSDFGMTRYVLDD-QYT 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 186 NIFGTP---EFVAPEIVNYEPLGLEADMWSIGVITY-ILLSGASPFLGDTKQETLANITA 241
Cdd:cd05114   157 SSSGAKfpvKWSPPEVFNYSKFSSKSDVWSFGVLMWeVFTEGKMPFESKSNYEVVEMVSR 216
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
66-239 2.45e-13

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: 70.10  E-value: 2.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  66 VSREEIEREVSILRQVLHHNVITLHDVYENRTdVVLILELVSGGELFDFLAQKES--LSEEEATSFIKQILDGVNYLHTK 143
Cdd:cd05069    49 MMPEAFLQEAQIMKKLRHDKLVPLYAVVSEEP-IYIVTEFMGKGSLLDFLKEGDGkyLKLPQLVDMAAQIADGMAYIERM 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 144 KIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIEDGvEFKNIFGTP---EFVAPEIVNYEPLGLEADMWSIGVI-TYI 219
Cdd:cd05069   128 NYIHRDLRAANILVGDNLV----CKIADFGLARLIEDN-EYTARQGAKfpiKWTAPEAALYGRFTIKSDVWSFGILlTEL 202
                         170       180
                  ....*....|....*....|
gi 2056392213 220 LLSGASPFLGDTKQETLANI 239
Cdd:cd05069   203 VTKGRVPYPGMVNREVLEQV 222
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
27-240 2.66e-13

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: 69.52  E-value: 2.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFAIVKKCREKSTgLEYAAKFIKKRQsrasrrgVSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELV 106
Cdd:cd05113    10 KELGTGQFGVVKYGKWRGQ-YDVAIKMIKEGS-------MSEDEFIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 107 SGGELFDFLAQ-KESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIEDGvEFK 185
Cdd:cd05113    82 ANGCLLNYLREmRKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGV----VKVSDFGLSRYVLDD-EYT 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2056392213 186 NIFGTP---EFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPFLGDTKQETLANIT 240
Cdd:cd05113   157 SSVGSKfpvRWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSlGKMPYERFTNSETVEHVS 215
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
126-275 2.99e-13

Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PINK1 contains an N-terminal mitochondrial targeting sequence, a catalytic domain, and a C-terminal regulatory region. It plays an important role in maintaining mitochondrial homeostasis. It protects cells against oxidative stress-induced apoptosis by phosphorylating the chaperone TNFR-associated protein 1 (TRAP1), also called Hsp75. Phosphorylated TRAP1 prevents cytochrome c release and peroxide-induced apoptosis. PINK1 interacts with Omi/HtrA2, a serine protease, and Parkin, an E3 ubiquitin ligase, in different pathways to promote mitochondrial health. The parkin gene is the most commonly mutated gene in autosomal recessive familial parkinsonism. Mutations within the catalytic domain of PINK1 are also associated with Parkinson's disease. The PINK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270920 [Multi-domain]  Cd Length: 313  Bit Score: 70.22  E-value: 2.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 126 ATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLA--------------HEIEDGvefknifGTP 191
Cdd:cd14018   140 ARVMILQLLEGVDHLVRHGIAHRDLKSDNILLELDFDGCPWLVIADFGCCladdsiglqlpfssWYVDRG-------GNA 212
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 192 EFVAPEI----------VNYEplglEADMWSIGVITYILLSGASPFLGdtkqetLANITAVSYDFDEEFFSQTSE----L 257
Cdd:cd14018   213 CLMAPEVstavpgpgvvINYS----KADAWAVGAIAYEIFGLSNPFYG------LGDTMLESRSYQESQLPALPSavppD 282
                         170
                  ....*....|....*...
gi 2056392213 258 AKDFIRKLLVKETRKRLT 275
Cdd:cd14018   283 VRQVVKDLLQRDPNKRVS 300
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
25-239 3.00e-13

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: 69.32  E-value: 3.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  25 IGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRgvSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILE 104
Cdd:cd05033     8 IEKVIGGGEFGEVCSGSLKLPGKKEIDVAIKTLKSGYSDK--QRLDFLTEASIMGQFDHPNVIRLEGVVTKSRPVMIVTE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 105 LVSGGELFDFLAQKES-LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNIpipHIKLIDFGLAHEIEDGVE 183
Cdd:cd05033    86 YMENGSLDKFLRENDGkFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNI-LVNSDL---VCKVSDFGLSRRLEDSEA 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 184 FKNIFG--TP-EFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPFLGDTKQETLANI 239
Cdd:cd05033   162 TYTTKGgkIPiRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSyGERPYWDMSNQDVIKAV 221
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
29-239 3.01e-13

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: 70.03  E-value: 3.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAA--KFIKKRQSRASRRgvsreEIEREVSILRQVLHH-NVITLHDVYENRTDVVLILEL 105
Cdd:cd05089    10 IGEGNFGQVIKAMIKKDGLKMNAaiKMLKEFASENDHR-----DFAGELEVLCKLGHHpNIINLLGACENRGYLYIAIEY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 106 VSGGELFDFLAQKE----------------SLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPiphiKL 169
Cdd:cd05089    85 APYGNLLDFLRKSRvletdpafakehgtasTLTSQQLLQFASDVAKGMQYLSEKQFIHRDLAARNVLVGENLVS----KI 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2056392213 170 IDFGLAHEIEdgVEFKNIFG--TPEFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPFLGDTKQETLANI 239
Cdd:cd05089   161 ADFGLSRGEE--VYVKKTMGrlPVRWMAIESLNYSVYTTKSDVWSFGVLLWEIVSlGGTPYCGMTCAELYEKL 231
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
14-285 3.06e-13

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: 70.05  E-value: 3.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  14 FKQQKVEDFYDIgEELGSGQFAIVKKCREKSTGLEYAakfIKKRQSRASRRGVSREEIEREVSILRQVLHHNVITLHDVY 93
Cdd:cd06634     9 FKDDPEKLFSDL-REIGHGSFGAVYFARDVRNNEVVA---IKKMSYSGKQSNEKWQDIIKEVKFLQKLRHPNTIEYRGCY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  94 ENRTDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFG 173
Cdd:cd06634    85 LREHTAWLVMEYCLGSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGL----VKLGDFG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 174 LAHEIEDGVEFkniFGTPEFVAPEIVNYEPLGL---EADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEf 250
Cdd:cd06634   161 SASIMAPANSF---VGTPYWMAPEVILAMDEGQydgKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNESPALQS- 236
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2056392213 251 fSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd06634   237 -GHWSEYFRNFVDSCLQKIPQDRPTSDVLLKHRFL 270
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
21-283 6.34e-13

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: 68.90  E-value: 6.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  21 DFYDIgEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRAsrrgVSREEIEREV---SILRQvlHHNVITLHDVYENRT 97
Cdd:cd14138     6 EFHEL-EKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGS----VDEQNALREVyahAVLGQ--HSHVVRYYSAWAEDD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  98 DVVLILELVSGGELFDFLAQK----ESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIP---------- 163
Cdd:cd14138    79 HMLIQNEYCNGGSLADAISENyrimSYFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFISRTSIPnaaseegded 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 164 ---IPHI--KLIDFGLAHEIED-GVEfkniFGTPEFVAPEIV--NYEPLGlEADMWSIGvITYILLSGASPFL--GDT-- 231
Cdd:cd14138   159 ewaSNKVifKIGDLGHVTRVSSpQVE----EGDSRFLANEVLqeNYTHLP-KADIFALA-LTVVCAAGAEPLPtnGDQwh 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2056392213 232 --KQETLANITAVsydFDEEFFsqtselakDFIRKLLVKETRKRLTIQEALRHP 283
Cdd:cd14138   233 eiRQGKLPRIPQV---LSQEFL--------DLLKVMIHPDPERRPSAVALVKHS 275
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
14-236 6.83e-13

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: 68.52  E-value: 6.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  14 FKQQKVEdfydIGEELGSGQFAIV-----KKCREKSTGLEYAakfIKKRQSRASRRgvSREEIEREVSILRQVLHHNVIT 88
Cdd:cd05032     3 LPREKIT----LIRELGQGSFGMVyeglaKGVVKGEPETRVA---IKTVNENASMR--ERIEFLNEASVMKEFNCHHVVR 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  89 LHDVYENRTDVVLILELVSGGELFDFLAQKES----------LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLL 158
Cdd:cd05032    74 LLGVVSTGQPTLVVMELMAKGDLKSYLRSRRPeaennpglgpPTLQKFIQMAAEIADGMAYLAAKKFVHRDLAARNCMVA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 159 DKNIpiphIKLIDFGLAHEIEDGVEFKNIFGT--P-EFVAPEIVNYEPLGLEADMWSIGVITY-ILLSGASPFLGDTKQE 234
Cdd:cd05032   154 EDLT----VKIGDFGMTRDIYETDYYRKGGKGllPvRWMAPESLKDGVFTTKSDVWSFGVVLWeMATLAEQPYQGLSNEE 229

                  ..
gi 2056392213 235 TL 236
Cdd:cd05032   230 VL 231
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
27-239 7.53e-13

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: 68.14  E-value: 7.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFAIVKK---CREKSTGLEYAAKFIKKrqSRASRRGVSrEEIEREVSILRQVLHHNVITLHDVYenRTD-VVLI 102
Cdd:cd05040     1 EKLGDGSFGVVRRgewTTPSGKVIQVAVKCLKS--DVLSQPNAM-DDFLKEVNAMHSLDHPNLIRLYGVV--LSSpLMMV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFL-AQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIEDG 181
Cdd:cd05040    76 TELAPLGSLLDRLrKDQGHFLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLASKDK----VKIGDFGLMRALPQN 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2056392213 182 vefKNIFGTPE-------FVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPFLGDTKQETLANI 239
Cdd:cd05040   152 ---EDHYVMQEhrkvpfaWCAPESLKTRKFSHASDVWMFGVTLWEMFTyGEEPWLGLNGSQILEKI 214
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
66-239 7.91e-13

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: 68.02  E-value: 7.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  66 VSREEIEREVSILRQVLHHNVITLHDVYENRTdVVLILELVSGGELFDFLAQKES--LSEEEATSFIKQILDGVNYLHTK 143
Cdd:cd14203    32 MSPEAFLEEAQIMKKLRHDKLVQLYAVVSEEP-IYIVTEFMSKGSLLDFLKDGEGkyLKLPQLVDMAAQIASGMAYIERM 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 144 KIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIEDGvEFKNIFGTP---EFVAPEIVNYEPLGLEADMWSIGV-ITYI 219
Cdd:cd14203   111 NYIHRDLRAANILVGDNLV----CKIADFGLARLIEDN-EYTARQGAKfpiKWTAPEAALYGRFTIKSDVWSFGIlLTEL 185
                         170       180
                  ....*....|....*....|
gi 2056392213 220 LLSGASPFLGDTKQETLANI 239
Cdd:cd14203   186 VTKGRVPYPGMNNREVLEQV 205
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
29-234 8.36e-13

Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie2 is a receptor PTK (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie2 is expressed mainly in endothelial cells and hematopoietic stem cells. It is also found in a subset of tumor-associated monocytes and eosinophils. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. Tie2 signaling plays key regulatory roles in vascular integrity and quiescence, and in inflammation. The Tie2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133219 [Multi-domain]  Cd Length: 303  Bit Score: 68.87  E-value: 8.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKfIKKRQSRASRRgvSREEIEREVSILRQVLHH-NVITLHDVYENRTDVVLILELVS 107
Cdd:cd05088    15 IGEGNFGQVLKARIKKDGLRMDAA-IKRMKEYASKD--DHRDFAGELEVLCKLGHHpNIINLLGACEHRGYLYLAIEYAP 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 108 GGELFDFLAQKE----------------SLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPiphiKLID 171
Cdd:cd05088    92 HGNLLDFLRKSRvletdpafaianstasTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVA----KIAD 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2056392213 172 FGLAHEIEdgVEFKNIFG--TPEFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPFLGDTKQE 234
Cdd:cd05088   168 FGLSRGQE--VYVKKTMGrlPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAE 231
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
29-216 9.03e-13

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK2 activation is induced by transforming growth factor-beta l (TGFb-l) and shares the same subcellular location as the cofilin family member twinfilin, which may be its biological substrate. LIMK2 plays a role in spermatogenesis, and may contribute to tumor progression and metastasis formation in some cancer cells. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 68.05  E-value: 9.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGleyaAKFIKKRQSRASRRgvSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSG 108
Cdd:cd14222     1 LGKGFFGQAIKVTHKATG----KVMVMKELIRCDEE--TQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 109 GELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIML-LDKNIPIPhikliDFGLAHEI-EDGVE--- 183
Cdd:cd14222    75 GTLKDFLRADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIkLDKTVVVA-----DFGLSRLIvEEKKKppp 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2056392213 184 ----------FKN-------IFGTPEFVAPEIVNYEPLGLEADMWSIGVI 216
Cdd:cd14222   150 dkpttkkrtlRKNdrkkrytVVGNPYWMAPEMLNGKSYDEKVDIFSFGIV 199
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
25-278 9.43e-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: 68.45  E-value: 9.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  25 IGEELGSGQFA-IVKKCREKSTGL----EYAAKFIKKRQSRASRRgvsreEIEREVSILRQVLHHNVITLHDVYENRTDV 99
Cdd:cd05045     4 LGKTLGEGEFGkVVKATAFRLKGRagytTVAVKMLKENASSSELR-----DLLSEFNLLKQVNHPHVIKLYGACSQDGPL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 100 VLILELVSGGELFDFLAQ------------------------KESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENI 155
Cdd:cd05045    79 LLIVEYAKYGSLRSFLREsrkvgpsylgsdgnrnssyldnpdERALTMGDLISFAWQISRGMQYLAEMKLVHRDLAARNV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 156 MLLDKNIpiphIKLIDFGLAHEI-EDGVEFKNIFG-TP-EFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPFLGdT 231
Cdd:cd05045   159 LVAEGRK----MKISDFGLSRDVyEEDSYVKRSKGrIPvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPG-I 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2056392213 232 KQETLANITAVSYDFDEEffSQTSELAKDFIRKLLVKETRKRLTIQE 278
Cdd:cd05045   234 APERLFNLLKTGYRMERP--ENCSEEMYNLMLTCWKQEPDKRPTFAD 278
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
29-227 1.38e-12

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: 67.42  E-value: 1.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTgleYAAKFIKKRQSRASRRgvsrEEIEREVSILRQVLHHNVItLHDVYENRTDVVLILELVSG 108
Cdd:cd14062     1 IGSGSFGTVYKGRWHGD---VAVKKLNVTDPTPSQL----QAFKNEVAVLRKTRHVNIL-LFMGYMTKPQLAIVTQWCEG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 109 GELFDFLAQKESLSEEEATSFI-KQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLA---HEIEDGVEF 184
Cdd:cd14062    73 SSLYKHLHVLETKFEMLQLIDIaRQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLT----VKIGDFGLAtvkTRWSGSQQF 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2056392213 185 KNIFGTPEFVAPEIV---NYEPLGLEADMWSIGVITYILLSGASPF 227
Cdd:cd14062   149 EQPTGSILWMAPEVIrmqDENPYSFQSDVYAFGIVLYELLTGQLPY 194
pknD PRK13184
serine/threonine-protein kinase PknD;
23-227 1.67e-12

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 69.41  E-value: 1.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRgvsREEIEREVSILRQVLHHNVITLHDVYENRTDVVLI 102
Cdd:PRK13184    4 YDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDLSENPLL---KKRFLREAKIAADLIHPGIVPVYSICSDGDPVYYT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 103 LELVSGGELFDFLA---QKESLSEE--EATS-------FIKqILDGVNYLHTKKIAHFDLKPENIML-LDKNIPIphikl 169
Cdd:PRK13184   81 MPYIEGYTLKSLLKsvwQKESLSKElaEKTSvgaflsiFHK-ICATIEYVHSKGVLHRDLKPDNILLgLFGEVVI----- 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2056392213 170 IDFGLAHEIE-------------DGVEFKN------IFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPF 227
Cdd:PRK13184  155 LDWGAAIFKKleeedlldidvdeRNICYSSmtipgkIVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPY 231
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
23-285 1.84e-12

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: 68.23  E-value: 1.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIkkrqsRASRRgVSREEIErEVSILRQVLH------HNVITLHDVYENR 96
Cdd:cd14224    67 YEVLKVIGKGSFGQVVKAYDHKTHQHVALKMV-----RNEKR-FHRQAAE-EIRILEHLKKqdkdntMNVIHMLESFTFR 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  97 TDVVLILELVSGgELFDFLAQK--ESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLldKNIPIPHIKLIDFGl 174
Cdd:cd14224   140 NHICMTFELLSM-NLYELIKKNkfQGFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILL--KQQGRSGIKVIDFG- 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 175 aheiEDGVEFKNIFGTPE---FVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAV--------- 242
Cdd:cd14224   216 ----SSCYEHQRIYTYIQsrfYRAPEVILGARYGMPIDMWSFGCILAELLTGYPLFPGEDEGDQLACMIELlgmppqkll 291
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 243 -SYDFDEEFFSQT---------------------------------------------SELAKDFIRKLLVKETRKRLTI 276
Cdd:cd14224   292 eTSKRAKNFISSKgypryctvttlpdgsvvlnggrsrrgkmrgppgskdwvtalkgcdDPLFLDFLKRCLEWDPAARMTP 371

                  ....*....
gi 2056392213 277 QEALRHPWI 285
Cdd:cd14224   372 SQALRHPWL 380
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
27-229 2.72e-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: 66.75  E-value: 2.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASrrgvSREEIEREVSILRQVLHHNVITLHDVYenRTDVVLILELV 106
Cdd:cd14025     2 EKVGSGGFGQVYKVRHKHWKTWLAIKCPPSLHVDDS----ERMELLEEAKKMEMAKFRHILPVYGIC--SEPVGLVMEYM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 107 SGGELFDFLAQkESLSEEEATSFIKQILDGVNYLHTKK--IAHFDLKPENImLLDKNIpipHIKLIDFGLAHEIE----D 180
Cdd:cd14025    76 ETGSLEKLLAS-EPLPWELRFRIIHETAVGMNFLHCMKppLLHLDLKPANI-LLDAHY---HVKISDFGLAKWNGlshsH 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2056392213 181 GVEFKNIFGTPEFVAPEIV--NYEPLGLEADMWSIGVITYILLSGASPFLG 229
Cdd:cd14025   151 DLSRDGLRGTIAYLPPERFkeKNRCPDTKHDVYSFAIVIWGILTQKKPFAG 201
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
26-277 3.02e-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: 67.13  E-value: 3.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  26 GEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVSREEIEREVSILRQV-LHHNVITLHDVYENRTDVVLILE 104
Cdd:cd05055    40 GKTLGAGAFGKVVEATAYGLSKSDAVMKVAVKMLKPTAHSSEREALMSELKIMSHLgNHENIVNLLGACTIGGPILVITE 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 105 LVSGGELFDFLAQKES--LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEI---E 179
Cdd:cd05055   120 YCCYGDLLNFLRRKREsfLTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLLTHGKI----VKICDFGLARDImndS 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 180 DGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPFLGDTKQETLANITAVSYDFDEEFFSqtSELA 258
Cdd:cd05055   196 NYVVKGNARLPVKWMAPESIFNCVYTFESDVWSYGILLWEIFSlGSNPYPGMPVDSKFYKLIKEGYRMAQPEHA--PAEI 273
                         250
                  ....*....|....*....
gi 2056392213 259 KDFIRKLLVKETRKRLTIQ 277
Cdd:cd05055   274 YDIMKTCWDADPLKRPTFK 292
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
29-227 3.15e-12

Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes three leucine-rich repeat receptor-like kinases (LRR-RLKs): Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1), and Physcomitrella patens CLL1B clavata1-like receptor S/T protein kinase. BAK1 functions in various signaling pathways. It plays a role in BR (brassinosteroid)-regulated plant development as a co-receptor of BRASSINOSTEROID (BR) INSENSITIVE 1 (BRI1), the receptor for BRs, and is required for full activation of BR signaling. It also modulates pathways involved in plant resistance to pathogen infection (pattern-triggered immunity, PTI) and herbivore attack (wound- or herbivore feeding-induced accumulation of jasmonic acid (JA) and JA-isoleucine. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The STK_BAK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 66.36  E-value: 3.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCReKSTGLEYAAKFIKKRQSRASRRGvsreeIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSG 108
Cdd:cd14664     1 IGRGGAGTVYKGV-MPNGTLVAVKRLKGEGTQGGDHG-----FQAEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 109 GELFDFL----AQKESLSEEEATSFIKQILDGVNYLH---TKKIAHFDLKPENImLLDKNIPiPHIKliDFGLAHEIEDG 181
Cdd:cd14664    75 GSLGELLhsrpESQPPLDWETRQRIALGSARGLAYLHhdcSPLIIHRDVKSNNI-LLDEEFE-AHVA--DFGLAKLMDDK 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2056392213 182 VE--FKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPF 227
Cdd:cd14664   151 DShvMSSVAGSYGYIAPEYAYTGKVSEKSDVYSYGVVLLELITGKRPF 198
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
29-239 3.96e-12

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: 66.04  E-value: 3.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRgvSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSG 108
Cdd:cd05066    12 IGAGEFGEVCSGRLKLPGKREIPVAIKTLKAGYTEK--QRRDFLSEASIMGQFDHPNIIHLEGVVTRSKPVMIVTEYMEN 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 109 GELFDFLAQKES-LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNIPIphiKLIDFGLAHEIEDGVE--FK 185
Cdd:cd05066    90 GSLDAFLRKHDGqFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNI-LVNSNLVC---KVSDFGLSRVLEDDPEaaYT 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2056392213 186 NIFGT-P-EFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPFLGDTKQETLANI 239
Cdd:cd05066   166 TRGGKiPiRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSyGERPYWEMSNQDVIKAI 222
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
29-222 4.25e-12

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: 66.46  E-value: 4.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREK----STGLEYAAKFIKKRQSRASRrgvsreEIEREVSILRQvLHHNVITLHD---VYENRTDVVL 101
Cdd:cd05081    12 LGKGNFGSVELCRYDplgdNTGALVAVKQLQHSGPDQQR------DFQREIQILKA-LHSDFIVKYRgvsYGPGRRSLRL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 102 ILELVSGGELFDFLAQKES-LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIED 180
Cdd:cd05081    85 VMEYLPSGCLRDFLQRHRArLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEA----HVKIADFGLAKLLPL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2056392213 181 GVEF---KNIFGTPEF-VAPEIVNYEPLGLEADMWSIGVITYILLS 222
Cdd:cd05081   161 DKDYyvvREPGQSPIFwYAPESLSDNIFSRQSDVWSFGVVLYELFT 206
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
118-256 4.40e-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: 4.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 118 KESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIedgveFKNifgtPEFV--- 194
Cdd:cd14207   174 KRPLTMEDLISYSFQVARGMEFLSSRKCIHRDLAARNILLSENNV----VKICDFGLARDI-----YKN----PDYVrkg 240
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2056392213 195 ---------APEIVNYEPLGLEADMWSIGVITYILLS-GASPFLGdtkqetlanitavsYDFDEEFFSQTSE 256
Cdd:cd14207   241 darlplkwmAPESIFDKIYSTKSDVWSYGVLLWEIFSlGASPYPG--------------VQIDEDFCSKLKE 298
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
27-283 5.91e-12

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: 65.89  E-value: 5.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFAIVKKCREKSTGLEYAakfIKKrqSRASRRGVSREEierevSILRQVLHHNVITLHD----VY----ENrtD 98
Cdd:cd14051     6 EKIGSGEFGSVYKCINRLDGCVYA---IKK--SKKPVAGSVDEQ-----NALNEVYAHAVLGKHPhvvrYYsawaED--D 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  99 VVLIL-ELVSGGELFDFLAQKES----LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKniPIPHIKLIDFG 173
Cdd:cd14051    74 HMIIQnEYCNGGSLADAISENEKagerFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIFISRT--PNPVSSEEEEE 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 174 LAHEIEDGVEFKNIF-------------------GTPEFVAPEIV--NYEPLgLEADMWSIGvITYILLSGASPFL--GD 230
Cdd:cd14051   152 DFEGEEDNPESNEVTykigdlghvtsisnpqveeGDCRFLANEILqeNYSHL-PKADIFALA-LTVYEAAGGGPLPknGD 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2056392213 231 T----KQETLANITAVSYDFDEeffsqtselakdFIRKLLVKETRKRLTIQEALRHP 283
Cdd:cd14051   230 EwheiRQGNLPPLPQCSPEFNE------------LLRSMIHPDPEKRPSAAALLQHP 274
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
23-223 6.48e-12

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


Pssm-ID: 270883 [Multi-domain]  Cd Length: 298  Bit Score: 65.84  E-value: 6.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAaKFIKKRQSRASRRgvsreeierEVSILRQV--------LHHNVITLHDVYE 94
Cdd:cd13981     2 YVISKELGEGGYASVYLAKDDDEQSDGS-LVALKVEKPPSIW---------EFYICDQLhsrlknsrLRESISGAHSAHL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  95 NRTDVVLILELVSGGELFDFL-----AQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPH--- 166
Cdd:cd13981    72 FQDESILVMDYSSQGTLLDVVnkmknKTGGGMDEPLAMFFTIELLKVVEALHEVGIIHGDIKPDNFLLRLEICADWPgeg 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2056392213 167 --------IKLIDFGLA---HEIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSG 223
Cdd:cd13981   152 engwlskgLKLIDFGRSidmSLFPKNQSFKADWHTDSFDCIEMREGRPWTYQIDYFGIAATIHVMLFG 219
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
27-227 6.94e-12

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: 65.42  E-value: 6.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFAIVKKCREKStglEYAAKFIKKRQSRASRRgvsrEEIEREVSILRQVLHHNVItLHDVYENRTDVVLILELV 106
Cdd:cd14150     6 KRIGTGSFGTVFRGKWHG---DVAVKILKVTEPTPEQL----QAFKNEMQVLRKTRHVNIL-LFMGFMTRPNFAIITQWC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 107 SGGELFDFLAQKES-LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLA---HEIEDGV 182
Cdd:cd14150    78 EGSSLYRHLHVTETrFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLT----VKIGDFGLAtvkTRWSGSQ 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2056392213 183 EFKNIFGTPEFVAPEIVNYE---PLGLEADMWSIGVITYILLSGASPF 227
Cdd:cd14150   154 QVEQPSGSILWMAPEVIRMQdtnPYSFQSDVYAYGVVLYELMSGTLPY 201
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
28-236 8.01e-12

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: 65.76  E-value: 8.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  28 ELGSGQFAIVkkcrekstgLEYAAKFIKKRQ--SRASRRGVS-----REEIE--REVSILRQVLHHNVITLHDVYENRTD 98
Cdd:cd05061    13 ELGQGSFGMV---------YEGNARDIIKGEaeTRVAVKTVNesaslRERIEflNEASVMKGFTCHHVVRLLGVVSKGQP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  99 VVLILELVSGGELFDFLAQKESLSE----------EEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIK 168
Cdd:cd05061    84 TLVVMELMAHGDLKSYLRSLRPEAEnnpgrppptlQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFT----VK 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2056392213 169 LIDFGLAHEIEDGVEF----KNIFGTpEFVAPEIVNYEPLGLEADMWSIGVITYILLSGA-SPFLGDTKQETL 236
Cdd:cd05061   160 IGDFGMTRDIYETDYYrkggKGLLPV-RWMAPESLKDGVFTTSSDMWSFGVVLWEITSLAeQPYQGLSNEQVL 231
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
66-239 1.01e-11

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: 65.09  E-value: 1.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  66 VSREEIEREVSILRQVLHHNVITLHDVYENRTdVVLILELVSGGELFDFLAQKE--SLSEEEATSFIKQILDGVNYLHTK 143
Cdd:cd05070    46 MSPESFLEEAQIMKKLKHDKLVQLYAVVSEEP-IYIVTEYMSKGSLLDFLKDGEgrALKLPNLVDMAAQVAAGMAYIERM 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 144 KIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIEDGvEFKNIFGTP---EFVAPEIVNYEPLGLEADMWSIGV-ITYI 219
Cdd:cd05070   125 NYIHRDLRSANILVGNGLI----CKIADFGLARLIEDN-EYTARQGAKfpiKWTAPEAALYGRFTIKSDVWSFGIlLTEL 199
                         170       180
                  ....*....|....*....|
gi 2056392213 220 LLSGASPFLGDTKQETLANI 239
Cdd:cd05070   200 VTKGRVPYPGMNNREVLEQV 219
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
15-284 1.09e-11

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: 65.85  E-value: 1.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  15 KQQKVEDFYDI-GEELGSGQFAIVKKCREK--STGLEYAAKFIKKRqsrasrrGVSREEIeREVSILRQVLHHNVITLHD 91
Cdd:cd07868    10 ERERVEDLFEYeGCKVGRGTYGHVYKAKRKdgKDDKDYALKQIEGT-------GISMSAC-REIALLRELKHPNVISLQK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  92 VYENRTDVVLILelvsggeLFDFL---------------AQKE--SLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPEN 154
Cdd:cd07868    82 VFLSHADRKVWL-------LFDYAehdlwhiikfhraskANKKpvQLPRGMVKSLLYQILDGIHYLHANWVLHRDLKPAN 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 155 IMLLDKNIPIPHIKLIDFGLAH----EIEDGVEFKNIFGTPEFVAPEIVnyepLGLE-----ADMWSIGVITYILLSG-- 223
Cdd:cd07868   155 ILVMGEGPERGRVKIADMGFARlfnsPLKPLADLDPVVVTFWYRAPELL----LGARhytkaIDIWAIGCIFAELLTSep 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 224 -----------ASPFLGDtKQETLANITAVSYDFDEEFFSQTSE---LAKDF---------------------------- 261
Cdd:cd07868   231 ifhcrqediktSNPYHHD-QLDRIFNVMGFPADKDWEDIKKMPEhstLMKDFrrntytncslikymekhkvkpdskafhl 309
                         330       340
                  ....*....|....*....|...
gi 2056392213 262 IRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd07868   310 LQKLLTMDPIKRITSEQAMQDPY 332
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
66-239 1.29e-11

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: 64.71  E-value: 1.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  66 VSREEIEREVSILRQVLHHNVITLHDVYENRTdVVLILELVSGGELFDFLAQKES--LSEEEATSFIKQILDGVNYLHTK 143
Cdd:cd05071    46 MSPEAFLQEAQVMKKLRHEKLVQLYAVVSEEP-IYIVTEYMSKGSLLDFLKGEMGkyLRLPQLVDMAAQIASGMAYVERM 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 144 KIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIEDGvEFKNIFGTP---EFVAPEIVNYEPLGLEADMWSIGV-ITYI 219
Cdd:cd05071   125 NYVHRDLRAANILVGENLV----CKVADFGLARLIEDN-EYTARQGAKfpiKWTAPEAALYGRFTIKSDVWSFGIlLTEL 199
                         170       180
                  ....*....|....*....|
gi 2056392213 220 LLSGASPFLGDTKQETLANI 239
Cdd:cd05071   200 TTKGRVPYPGMVNREVLDQV 219
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
29-223 1.42e-11

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: 64.20  E-value: 1.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKkcREKSTGLEYAAKFIKKRQSRASRRgvsreeieREVSILRQVLHHNVITLhdVYENRTDVVLILELVSG 108
Cdd:cd14068     2 LGDGGFGSVY--RAVYRGEDVAVKIFNKHTSFRLLR--------QELVVLSHLHHPSLVAL--LAAGTAPRMLVMELAPK 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 109 GELfDFLAQKE--SLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHI-KLIDFGLA-HEIEDGVef 184
Cdd:cd14068    70 GSL-DALLQQDnaSLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLFTLYPNCAIIaKIADYGIAqYCCRMGI-- 146
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2056392213 185 KNIFGTPEFVAPEI----VNYEPlglEADMWSIGVITYILLSG 223
Cdd:cd14068   147 KTSEGTPGFRAPEVargnVIYNQ---QADVYSFGLLLYDILTC 186
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
26-284 1.43e-11

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: 65.09  E-value: 1.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  26 GEELGSGQFAIVKKCREKSTG--LEYAAKFIKKRqsrasrrGVSREEIeREVSILRQVLHHNVITLHDVYENRTDVVLIL 103
Cdd:cd07867     7 GCKVGRGTYGHVYKAKRKDGKdeKEYALKQIEGT-------GISMSAC-REIALLRELKHPNVIALQKVFLSHSDRKVWL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 104 elvsggeLFDFL---------------AQKE--SLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPH 166
Cdd:cd07867    79 -------LFDYAehdlwhiikfhraskANKKpmQLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEGPERGR 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 167 IKLIDFGLAH----EIEDGVEFKNIFGTPEFVAPEIVnyepLGLE-----ADMWSIGVITYILLSGASPFlgDTKQETLA 237
Cdd:cd07867   152 VKIADMGFARlfnsPLKPLADLDPVVVTFWYRAPELL----LGARhytkaIDIWAIGCIFAELLTSEPIF--HCRQEDIK 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 238 NITAVSYDFDEEFFS-----------------QTSELAKDF----------------------------IRKLLVKETRK 272
Cdd:cd07867   226 TSNPFHHDQLDRIFSvmgfpadkdwedirkmpEYPTLQKDFrrttyansslikymekhkvkpdskvfllLQKLLTMDPTK 305
                         330
                  ....*....|..
gi 2056392213 273 RLTIQEALRHPW 284
Cdd:cd07867   306 RITSEQALQDPY 317
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
25-234 1.59e-11

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: 65.03  E-value: 1.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  25 IGEELGSGQFAIVKKC------REKSTGLEYAAkfIKKRQSRASRRGVSreEIEREVSILRQV-LHHNVITLHDVYENRT 97
Cdd:cd05098    17 LGKPLGEGCFGQVVLAeaigldKDKPNRVTKVA--VKMLKSDATEKDLS--DLISEMEMMKMIgKHKNIINLLGACTQDG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  98 DVVLILELVSGGELFDFLAQK----------------ESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKN 161
Cdd:cd05098    93 PLYVIVEYASKGNLREYLQARrppgmeycynpshnpeEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDN 172
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2056392213 162 IpiphIKLIDFGLAHEIEDGVEFKNIFG---TPEFVAPEIVNYEPLGLEADMWSIGVITY-ILLSGASPFLGDTKQE 234
Cdd:cd05098   173 V----MKIADFGLARDIHHIDYYKKTTNgrlPVKWMAPEALFDRIYTHQSDVWSFGVLLWeIFTLGGSPYPGVPVEE 245
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
118-229 1.62e-11

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: 65.39  E-value: 1.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 118 KESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAheiedgvefKNIFGTPEFV--- 194
Cdd:cd05103   173 KDFLTLEDLICYSFQVAKGMEFLASRKCIHRDLAARNILLSENNV----VKICDFGLA---------RDIYKDPDYVrkg 239
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2056392213 195 ---------APEIVNYEPLGLEADMWSIGVITYILLS-GASPFLG 229
Cdd:cd05103   240 darlplkwmAPETIFDRVYTIQSDVWSFGVLLWEIFSlGASPYPG 284
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
66-227 1.92e-11

Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 64.33  E-value: 1.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  66 VSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSGGELFDFLAQKE-SLSEEEATSFIKQILDGVNYLHTKK 144
Cdd:cd13992    38 TEKRTILQELNQLKELVHDNLNKFIGICINPPNIAVVTEYCTRGSLQDVLLNREiKMDWMFKSSFIKDIVKGMNYLHSSS 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 145 I-AHFDLKPENImLLDKNIpipHIKLIDFGLAHEIED-GVEFKNIFGTPE---FVAPEIVNYEPLG----LEADMWSIGV 215
Cdd:cd13992   118 IgYHGRLKSSNC-LVDSRW---VVKLTDFGLRNLLEEqTNHQLDEDAQHKkllWTAPELLRGSLLEvrgtQKGDVYSFAI 193
                         170
                  ....*....|..
gi 2056392213 216 ITYILLSGASPF 227
Cdd:cd13992   194 ILYEILFRSDPF 205
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
24-227 2.45e-11

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: 63.52  E-value: 2.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  24 DIGEELGSGQFAIVKKCrekstglEYAAKFIKKRQSRasRRGVSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLIL 103
Cdd:cd05039     9 KLGELIGKGEFGDVMLG-------DYRGQKVAVKCLK--DDSTAAQAFLAEASVMTTLRHPNLVQLLGVVLEGNGLYIVT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 104 ELVSGGELFDFLAQKES--LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPiphiKLIDFGLAHEIEDG 181
Cdd:cd05039    80 EYMAKGSLVDYLRSRGRavITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVA----KVSDFGLAKEASSN 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2056392213 182 VEFKNIfgtP-EFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPF 227
Cdd:cd05039   156 QDGGKL---PiKWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPY 200
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
17-284 2.89e-11

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: 64.26  E-value: 2.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  17 QKVEDFYDIGEELGSGQFAIVKKCREKSTG-LEYAAKFIKKRqsrasrrGVSREEIEREVSILRQVLHHN------VITL 89
Cdd:cd14214     9 DWLQERYEIVGDLGEGTFGKVVECLDHARGkSQVALKIIRNV-------GKYREAARLEINVLKKIKEKDkenkflCVLM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  90 HDVYENRTDVVLILELVsGGELFDFlaQKESLSEEEATSFIK----QILDGVNYLHTKKIAHFDLKPENIMLL------- 158
Cdd:cd14214    82 SDWFNFHGHMCIAFELL-GKNTFEF--LKENNFQPYPLPHIRhmayQLCHALKFLHENQLTHTDLKPENILFVnsefdtl 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 159 --------DKNIPIPHIKLIDFGLA---HEiedgvEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPF 227
Cdd:cd14214   159 ynesksceEKSVKNTSIRVADFGSAtfdHE-----HHTTIVATRHYRPPEVILELGWAQPCDVWSLGCILFEYYRGFTLF 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 228 LGDTKQETLANITAV---------------------SYDFDEE----------------FFSQTS-ELAK--DFIRKLLV 267
Cdd:cd14214   234 QTHENREHLVMMEKIlgpipshmihrtrkqkyfykgSLVWDENssdgryvsenckplmsYMLGDSlEHTQlfDLLRRMLE 313
                         330
                  ....*....|....*..
gi 2056392213 268 KETRKRLTIQEALRHPW 284
Cdd:cd14214   314 FDPALRITLKEALLHPF 330
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
25-227 3.93e-11

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: 62.97  E-value: 3.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  25 IGEELGSGQFAIVkkCREKSTGLEYAAKFIKKrqsrasrrGVSREEIEREVSILRQVLHHNVITLHDVYEnRTDVVLILE 104
Cdd:cd05083    10 LGEIIGEGEFGAV--LQGEYMGQKVAVKNIKC--------DVTAQAFLEETAVMTKLQHKNLVRLLGVIL-HNGLYIVME 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 105 LVSGGELFDFLAQK--ESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPiphiKLIDFGLAHEIEDGV 182
Cdd:cd05083    79 LMSKGNLVNFLRSRgrALVPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVA----KISDFGLAKVGSMGV 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2056392213 183 EFKNIfgTPEFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPF 227
Cdd:cd05083   155 DNSRL--PVKWTAPEALKNKKFSSKSDVWSYGVLLWEVFSyGRAPY 198
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
83-285 4.11e-11

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: 62.97  E-value: 4.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  83 HHNVITLHDVYENrTDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDK-N 161
Cdd:cd14024    44 HEGVCSVLEVVIG-QDRAYAFFSRHYGDMHSHVRRRRRLSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTDElR 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 162 IPIPHIKLIDFGLAHEIEDGVEFKNifGTPEFVAPEIVN--YEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANI 239
Cdd:cd14024   123 TKLVLVNLEDSCPLNGDDDSLTDKH--GCPAYVGPEILSsrRSYSGKAADVWSLGVCLYTMLLGRYPFQDTEPAALFAKI 200
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2056392213 240 TAVSYDFDEEFfsqtSELAKDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14024   201 RRGAFSLPAWL----SPGARCLVSCMLRRSPAERLKASEILLHPWL 242
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
29-227 6.16e-11

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: 62.74  E-value: 6.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKStglEYAAKFIKKRQSRASRRGVSREEiereVSILRQVLHHNVItLHDVYENRTDVVLILELVSG 108
Cdd:cd14149    20 IGSGSFGTVYKGKWHG---DVAVKILKVVDPTPEQFQAFRNE----VAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 109 GELFDFL-AQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLA---HEIEDGVEF 184
Cdd:cd14149    92 SSLYKHLhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLT----VKIGDFGLAtvkSRWSGSQQV 167
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2056392213 185 KNIFGTPEFVAPEIVNYE---PLGLEADMWSIGVITYILLSGASPF 227
Cdd:cd14149   168 EQPTGSILWMAPEVIRMQdnnPFSFQSDVYSYGIVLYELMTGELPY 213
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
25-229 7.46e-11

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: 62.89  E-value: 7.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  25 IGEELGSGQFAIVKKCR----EKSTGLEYAAKFIKKRQSRASRRgvsrEEIEREVSILRQVLHH-NVITLHDV-YENRTD 98
Cdd:cd05054    11 LGKPLGRGAFGKVIQASafgiDKSATCRTVAVKMLKEGATASEH----KALMTELKILIHIGHHlNVVNLLGAcTKPGGP 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  99 VVLILELVSGGELFDFLAQK--------------------------ESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKP 152
Cdd:cd05054    87 LMVIVEFCKFGNLSNYLRSKreefvpyrdkgardveeeedddelykEPLTLEDLICYSFQVARGMEFLASRKCIHRDLAA 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 153 ENIMLLDKNIpiphIKLIDFGLAheiedgvefKNIFGTPEFV------------APEIVNYEPLGLEADMWSIGVITYIL 220
Cdd:cd05054   167 RNILLSENNV----VKICDFGLA---------RDIYKDPDYVrkgdarlplkwmAPESIFDKVYTTQSDVWSFGVLLWEI 233
                         250
                  ....*....|
gi 2056392213 221 LS-GASPFLG 229
Cdd:cd05054   234 FSlGASPYPG 243
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
24-239 1.01e-10

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


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 62.29  E-value: 1.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  24 DIGEELGSGQFAivKKCREKSTGlEYAAKFIKKRqsrasrrGVSREEIE---REVSILRQVLHHNVITLHDVYENRTDVV 100
Cdd:cd14152     3 ELGELIGQGRWG--KVHRGRWHG-EVAIRLLEID-------GNNQDHLKlfkKEVMNYRQTRHENVVLFMGACMHPPHLA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 101 LILELVSGGELFDFLAQ-KESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLidFGLAHEIE 179
Cdd:cd14152    73 IITSFCKGRTLYSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVVITDFGL--FGISGVVQ 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2056392213 180 DGV---EFKNIFGTPEFVAPEIV---------NYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANI 239
Cdd:cd14152   151 EGRrenELKLPHDWLCYLAPEIVremtpgkdeDCLPFSKAADVYAFGTIWYELQARDWPLKNQPAEALIWQI 222
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
14-239 1.20e-10

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: 62.35  E-value: 1.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  14 FKQQKVedfydigeeLGSGQFAIVKKCREKSTGlEYAAKFIKKRQSRASRRGVSREEIEREVSILRQVLHHNVITLHDVY 93
Cdd:cd05108     9 FKKIKV---------LGSGAFGTVYKGLWIPEG-EKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGIC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  94 ENRTdVVLILELVSGGELFDFLAQ-KESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDF 172
Cdd:cd05108    79 LTST-VQLITQLMPFGCLLDYVREhKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQ----HVKITDF 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2056392213 173 GLAHEI-EDGVEFKNIFG-TP-EFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPFLGDTKQEtLANI 239
Cdd:cd05108   154 GLAKLLgAEEKEYHAEGGkVPiKWMALESILHRIYTHQSDVWSYGVTVWELMTfGSKPYDGIPASE-ISSI 223
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
29-227 1.49e-10

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


Pssm-ID: 270966 [Multi-domain]  Cd Length: 254  Bit Score: 61.39  E-value: 1.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCRekstgleYAAKFIKKRQSRASRRGvSREEIE---REVSILRQVLHHNVIT-LHDVYENRTDVVLILE 104
Cdd:cd14064     1 IGSGSFGKVYKGR-------CRNKIVAIKRYRANTYC-SKSDVDmfcREVSILCRLNHPCVIQfVGACLDDPSQFAIVTQ 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 105 LVSGGELFDFL-AQKESLSEEEATSFIKQILDGVNYLH--TKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIEDg 181
Cdd:cd14064    73 YVSGGSLFSLLhEQKRVIDLQSKLIIAVDVAKGMEYLHnlTQPIIHRDLNSHNILLYEDG----HAVVADFGESRFLQS- 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2056392213 182 VEFKNIFGTP---EFVAPEIVN----YEplgLEADMWSIGVITYILLSGASPF 227
Cdd:cd14064   148 LDEDNMTKQPgnlRWMAPEVFTqctrYS---IKADVFSYALCLWELLTGEIPF 197
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
27-240 2.27e-10

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


Pssm-ID: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 60.94  E-value: 2.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFAIV--KKCREKSTGLEYAAKFIKKRQSRASRRgvSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILE 104
Cdd:cd05049    11 RELGEGAFGKVflGECYNLEPEQDKMLVAVKTLKDASSPD--ARKDFEREAELLTNLQHENIVKFYGVCTEGDPLLMVFE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 105 LVSGGELFDFL--------------AQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLI 170
Cdd:cd05049    89 YMEHGDLNKFLrshgpdaaflasedSAPGELTLSQLLHIAVQIASGMVYLASQHFVHRDLATRNCLVGTNLV----VKIG 164
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2056392213 171 DFGLAHEIEDgVEFKNIFGTP----EFVAPEIVNYEPLGLEADMWSIGVITY-ILLSGASPFLGDTKQETLANIT 240
Cdd:cd05049   165 DFGMSRDIYS-TDYYRVGGHTmlpiRWMPPESILYRKFTTESDVWSFGVVLWeIFTYGKQPWFQLSNTEVIECIT 238
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
54-258 2.29e-10

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


Pssm-ID: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 61.26  E-value: 2.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  54 IKKRQSRA--SRRGVSREEIEREVSILRQVLHHNVITLHDVYENrTDVVLILELVSGGE-LFDFLAQKESLSEE--EATS 128
Cdd:cd14001    33 VKKINSKCdkGQRSLYQERLKEEAKILKSLNHPNIVGFRAFTKS-EDGSLCLAMEYGGKsLNDLIEERYEAGLGpfPAAT 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 129 FIK---QILDGVNYLHT-KKIAHFDLKPENIMLldKNiPIPHIKLIDFGLAHEIEDGVEFK-----NIFGTPEFVAPEIV 199
Cdd:cd14001   112 ILKvalSIARALEYLHNeKKILHGDIKSGNVLI--KG-DFESVKLCDFGVSLPLTENLEVDsdpkaQYVGTEPWKAKEAL 188
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2056392213 200 NYE-PLGLEADMWSIGVITYILLSGASP--FLGDTKQETLANitavsyDFDEEFFSQTSELA 258
Cdd:cd14001   189 EEGgVITDKADIFAYGLVLWEMMTLSVPhlNLLDIEDDDEDE------SFDEDEEDEEAYYG 244
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
34-223 2.47e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 61.93  E-value: 2.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  34 FAIVKKCREKSTGLEYAAKFIKKRQSRASRRGvSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSGgELFD 113
Cdd:PHA03212   94 FSILETFTPGAEGFAFACIDNKTCEHVVIKAG-QRGGTATEAHILRAINHPSIIQLKGTFTYNKFTCLILPRYKT-DLYC 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 114 FLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLldkNIPiPHIKLIDFGLAHEIED--GVEFKNIFGTP 191
Cdd:PHA03212  172 YLAAKRNIAICDILAIERSVLRAIQYLHENRIIHRDIKAENIFI---NHP-GDVCLGDFGAACFPVDinANKYYGWAGTI 247
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2056392213 192 EFVAPEIVNYEPLGLEADMWSIGVITYILLSG 223
Cdd:PHA03212  248 ATNAPELLARDPYGPAVDIWSAGIVLFEMATC 279
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
29-229 2.69e-10

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: 60.51  E-value: 2.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRAsrrgvsrEEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSG 108
Cdd:cd05052    14 LGGGQYGEVYEGVWKKYNLTVAVKTLKEDTMEV-------EEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMPY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 109 GELFDFL--AQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIED------ 180
Cdd:cd05052    87 GNLLDYLreCNREELNAVVLLYMATQIASAMEYLEKKNFIHRDLAARNCLVGENHL----VKVADFGLSRLMTGdtytah 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2056392213 181 -GVEFknifgtP-EFVAPEIVNYEPLGLEADMWSIGVITY-ILLSGASPFLG 229
Cdd:cd05052   163 aGAKF------PiKWTAPESLAYNKFSIKSDVWAFGVLLWeIATYGMSPYPG 208
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
29-216 2.80e-10

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: 60.60  E-value: 2.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVsreeieREVSILRQVLHHNVITLHDV-YENRTdVVLILELVS 107
Cdd:cd14154     1 LGKGFFGQAIKVTHRETGEVMVMKELIRFDEEAQRNFL------KEVKVMRSLDHPNVLKFIGVlYKDKK-LNLITEYIP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 108 GGELFDFLAQKES-LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIML-LDKNIPIPhikliDFGLAHEIED----- 180
Cdd:cd14154    74 GGTLKDVLKDMARpLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVrEDKTVVVA-----DFGLARLIVEerlps 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2056392213 181 GVEFKN----------------IFGTPEFVAPEIVNYEPLGLEADMWSIGVI 216
Cdd:cd14154   149 GNMSPSetlrhlkspdrkkrytVVGNPYWMAPEMLNGRSYDEKVDIFSFGIV 200
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
128-284 2.99e-10

Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNT7 is a plant thylakoid-associated kinase that is essential in short- and long-term acclimation responses to cope with various light conditions in order to maintain photosynthetic redox poise for optimal photosynthetic performance. Short-term response involves state transitions over periods of minutes while the long-term response (LTR) occurs over hours to days and involves changing the relative amounts of photosystems I and II. SNT7 acts as a redox sensor and a signal transducer for both responses, which are triggered by the redox state of the plastoquinone (PQ) pool. It is positioned at the top of a phosphorylation cascade that induces state transitions by phosphorylating light-harvesting complex II (LHCII), and triggers the LTR through the phosphorylation of chloroplast proteins. The SNT7 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270915 [Multi-domain]  Cd Length: 318  Bit Score: 61.30  E-value: 2.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 128 SFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipiPHIKLIDFGLAHEIEDGVEF--KNIFGTPEFVAPE--IVNYE- 202
Cdd:cd14013   124 SIMRQILVALRKLHSTGIVHRDVKPQNIIVSEGD---GQFKIIDLGAAADLRIGINYipKEFLLDPRYAPPEqyIMSTQt 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 203 ----PLGLEA---------------DMWSIGVityILLSGASPFLGDTKQETLANITAVSYDFD------EEFFSQTSEL 257
Cdd:cd14013   201 psapPAPVAAalspvlwqmnlpdrfDMYSAGV---ILLQMAFPNLRSDSNLIAFNRQLKQCDYDlnawrmLVEPRASADL 277
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2056392213 258 AKDF-------------IRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd14013   278 REGFeildlddgagwdlVTKLIRYKPRGRLSASAALAHPY 317
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
73-286 3.06e-10

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


Pssm-ID: 270922 [Multi-domain]  Cd Length: 285  Bit Score: 60.72  E-value: 3.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  73 REVSILRQVL-HHNVITLHDVYENRTDV-----VLILEL--VSGGELFdFLAQKESLSEEEATSFIKQILDGVNYLHTKK 144
Cdd:cd14020    52 KERAALEQLQgHRNIVTLYGVFTNHYSAnvpsrCLLLELldVSVSELL-LRSSNQGCSMWMIQHCARDVLEALAFLHHEG 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 145 IAHFDLKPENIMLLDKNipiPHIKLIDFGLAHEiEDGVEFKNIfGTPEFVAPEIVNYEPL---GLEA--------DMWSI 213
Cdd:cd14020   131 YVHADLKPRNILWSAED---ECFKLIDFGLSFK-EGNQDVKYI-QTDGYRAPEAELQNCLaqaGLQSetectsavDLWSL 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 214 GVITYILLSGASpfLGDT--KQETLANITAVsydFDEEFFSQTSELA-------KDFIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd14020   206 GIVLLEMFSGMK--LKHTvrSQEWKDNSSAI---IDHIFASNAVVNPaipayhlRDLIKSMLHNDPGKRATAEAALCSPF 280

                  ..
gi 2056392213 285 IT 286
Cdd:cd14020   281 FS 282
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
21-234 4.02e-10

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: 60.80  E-value: 4.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  21 DFYDIGEELGSGQFAIVKKCR----EKSTGLEYAAKFIKKRQSRASRRGVSreEIEREVSILRQV-LHHNVITLHDVYEN 95
Cdd:cd05101    24 DKLTLGKPLGEGCFGQVVMAEavgiDKDKPKEAVTVAVKMLKDDATEKDLS--DLVSEMEMMKMIgKHKNIINLLGACTQ 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  96 RTDVVLILELVSGGELFDFLAQK----------------ESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLD 159
Cdd:cd05101   102 DGPLYVIVEYASKGNLREYLRARrppgmeysydinrvpeEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTE 181
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2056392213 160 KNIpiphIKLIDFGLAHEIEDGVEFKNIFG---TPEFVAPEIVNYEPLGLEADMWSIGVITY-ILLSGASPFLGDTKQE 234
Cdd:cd05101   182 NNV----MKIADFGLARDINNIDYYKKTTNgrlPVKWMAPEALFDRVYTHQSDVWSFGVLMWeIFTLGGSPYPGIPVEE 256
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
27-270 4.69e-10

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: 60.37  E-value: 4.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFAIVKKCR---------EKSTGLEYAAKFIKKRQSRASRRGVSREEIEREVSILRQVLHHNVITLHDVYENRT 97
Cdd:cd05097    11 EKLGEGQFGEVHLCEaeglaeflgEGAPEFDGQPVLVAVKMLRADVTKTARNDFLKEIKIMSRLKNPNIIRLLGVCVSDD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  98 DVVLILELVSGGELFDFLAQKE------------SLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNIPip 165
Cdd:cd05097    91 PLCMITEYMENGDLNQFLSQREiestfthannipSVSIANLLYMAVQIASGMKYLASLNFVHRDLATRNC-LVGNHYT-- 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 166 hIKLIDFGLAHEIEDGvEFKNIFGTP----EFVAPEIVNYEPLGLEADMWSIGVITYILLsgaspflgdtkqeTLANITA 241
Cdd:cd05097   168 -IKIADFGMSRNLYSG-DYYRIQGRAvlpiRWMAWESILLGKFTTASDVWAFGVTLWEMF-------------TLCKEQP 232
                         250       260
                  ....*....|....*....|....*....
gi 2056392213 242 VSYDFDEEFFSQTSELAKDFIRKLLVKET 270
Cdd:cd05097   233 YSLLSDEQVIENTGEFFRNQGRQIYLSQT 261
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
20-229 8.89e-10

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: 59.55  E-value: 8.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  20 EDFYDIGEELGSGQFAIVKKCREKS---TGLEYAAKFIKKRQSRASrrgvSREEIEREVSILRQVLHHNV-----ITLHD 91
Cdd:cd05074     8 EQQFTLGRMLGKGEFGSVREAQLKSedgSFQKVAVKMLKADIFSSS----DIEEFLREAACMKEFDHPNVikligVSLRS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  92 VYENRTDV-VLILELVSGGELFDFLAQKE------SLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMlLDKNIpi 164
Cdd:cd05074    84 RAKGRLPIpMVILPFMKHGDLHTFLLMSRigeepfTLPLQTLVRFMIDIASGMEYLSSKNFIHRDLAARNCM-LNENM-- 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2056392213 165 pHIKLIDFGLAHEIEDGVEFKNIFGTP---EFVAPEIVNYEPLGLEADMWSIGVITY-ILLSGASPFLG 229
Cdd:cd05074   161 -TVCVADFGLSKKIYSGDYYRQGCASKlpvKWLALESLADNVYTTHSDVWAFGVTMWeIMTRGQTPYAG 228
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
70-234 9.69e-10

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: 59.31  E-value: 9.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  70 EIEREVSILRQVLHHNVITLHDVYENRTdVVLILELVSGGELFDFLAQ-KESLSEEEATSFIKQILDGVNYLHTKKIAHF 148
Cdd:cd05110    55 EFMDEALIMASMDHPHLVRLLGVCLSPT-IQLVTQLMPHGCLLDYVHEhKDNIGSQLLLNWCVQIAKGMMYLEERRLVHR 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 149 DLKPENIMLLDKNipipHIKLIDFGLAHEIEDGVEFKNIFGTP---EFVAPEIVNYEPLGLEADMWSIGVITYILLS-GA 224
Cdd:cd05110   134 DLAARNVLVKSPN----HVKITDFGLARLLEGDEKEYNADGGKmpiKWMALECIHYRKFTHQSDVWSYGVTIWELMTfGG 209
                         170
                  ....*....|
gi 2056392213 225 SPFLGDTKQE 234
Cdd:cd05110   210 KPYDGIPTRE 219
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
83-229 1.00e-09

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: 59.35  E-value: 1.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  83 HHNVITLHDVYENRTDVVLILELVSGGELFDFLAQK----------------ESLSEEEATSFIKQILDGVNYLHTKKIA 146
Cdd:cd05053    76 HKNIINLLGACTQDGPLYVVVEYASKGNLREFLRARrppgeeaspddprvpeEQLTQKDLVSFAYQVARGMEYLASKKCI 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 147 HFDLKPENIMLLDKNIpiphIKLIDFGLAHEIEDgVEF--KNIFG-TP-EFVAPEIVNYEPLGLEADMWSIGVITY-ILL 221
Cdd:cd05053   156 HRDLAARNVLVTEDNV----MKIADFGLARDIHH-IDYyrKTTNGrLPvKWMAPEALFDRVYTHQSDVWSFGVLLWeIFT 230

                  ....*...
gi 2056392213 222 SGASPFLG 229
Cdd:cd05053   231 LGGSPYPG 238
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
28-239 1.09e-09

Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Musk is a receptor PTK (RTK) containing an extracellular region with four immunoglobulin-like domains and a cysteine-rich cluster, a transmembrane segment, and an intracellular catalytic domain. Musk is expressed and concentrated in the postsynaptic membrane in skeletal muscle. It is essential for the establishment of the neuromuscular junction (NMJ), a peripheral synapse that conveys signals from motor neurons to muscle cells. Agrin, a large proteoglycan released from motor neurons, stimulates Musk autophosphorylation and activation, leading to the clustering of acetylcholine receptors (AChRs). To date, there is no evidence to suggest that agrin binds directly to Musk. Mutations in AChR, Musk and other partners are responsible for diseases of the NMJ, such as the autoimmune syndrome myasthenia gravis. The Musk 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: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 59.08  E-value: 1.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  28 ELGSGQFAIVKKCRekSTGL-------EYAAKFIKKRQSRASRRgvsreEIEREVSILRQVLHHNVITLHDVYENRTDVV 100
Cdd:cd05050    12 DIGQGAFGRVFQAR--APGLlpyepftMVAVKMLKEEASADMQA-----DFQREAALMAEFDHPNIVKLLGVCAVGKPMC 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 101 LILELVSGGELFDFL----------------------AQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLL 158
Cdd:cd05050    85 LLFEYMAYGDLNEFLrhrspraqcslshstssarkcgLNPLPLSCTEQLCIAKQVAAGMAYLSERKFVHRDLATRNC-LV 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 159 DKNIpipHIKLIDFGLAHEIEDGVEFK---NIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPFLGDTKQE 234
Cdd:cd05050   164 GENM---VVKIADFGLSRNIYSADYYKaseNDAIPIRWMPPESIFYNRYTTESDVWAYGVVLWEIFSyGMQPYYGMAHEE 240

                  ....*
gi 2056392213 235 TLANI 239
Cdd:cd05050   241 VIYYV 245
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
29-229 1.23e-09

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: 58.88  E-value: 1.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTG----LEYAAKFIKKRQSRASRRgvsreEIEREVSILRQVLHHNVITLHDVYENRTdVVLILE 104
Cdd:cd05109    15 LGSGAFGTVYKGIWIPDGenvkIPVAIKVLRENTSPKANK-----EILDEAYVMAGVGSPYVCRLLGICLTST-VQLVTQ 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 105 LVSGGELFDFLAQ-KESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIE-DGV 182
Cdd:cd05109    89 LMPYGCLLDYVREnKDRIGSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPN----HVKITDFGLARLLDiDET 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2056392213 183 EFKNIFG-TP-EFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPFLG 229
Cdd:cd05109   165 EYHADGGkVPiKWMALESILHRRFTHQSDVWSYGVTVWELMTfGAKPYDG 214
STKc_SRPK3 cd14218
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs ...
23-285 1.44e-09

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK3 is highly expressed in the heart and skeletal muscles, and is controlled by a muscle-specific enhancer that is regulated by MEF2. It may play an important role in muscle development. 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. 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: 271120 [Multi-domain]  Cd Length: 365  Bit Score: 59.26  E-value: 1.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRAsrrgvsrEEIEREVSILRQVLHHN--------VITLHDVYE 94
Cdd:cd14218    12 YHVVRKLGWGHFSTVWLCWDIQRKRFVALKVVKSAVHYT-------ETAVDEIKLLKCVRDSDpsdpkretIVQLIDDFK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  95 ----NRTDVVLILElVSGGELFDFLAQK--ESLSEEEATSFIKQILDGVNYLHTK-KIAHFDLKPENIMLL--------- 158
Cdd:cd14218    85 isgvNGVHVCMVLE-VLGHQLLKWIIKSnyQGLPLPCVKSILRQVLQGLDYLHTKcKIIHTDIKPENILMCvdegyvrrl 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 159 --------DKNIPIPHIKLIDFGLAHEIEDGVEFKNI-----------------------FGTPEFVAPEIVNYEPLGLE 207
Cdd:cd14218   164 aaeatiwqQAGAPPPSGSSVSFGASDFLVNPLEPQNAdkirvkiadlgnacwvhkhftedIQTRQYRALEVLIGAEYGTP 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 208 ADMWSIGVITYILLSGA---SPFLGD--TKQET-LANIT----------AVSYDFDEEFFSQTSELA------------- 258
Cdd:cd14218   244 ADIWSTACMAFELATGDylfEPHSGEdyTRDEDhIAHIVellgdipphfALSGRYSREYFNRRGELRhiknlkhwglyev 323
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 2056392213 259 ---------------KDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14218   324 lvekyewpleqaaqfTDFLLPMMEFLPEKRATAAQCLQHPWL 365
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
25-234 1.48e-09

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: 59.26  E-value: 1.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  25 IGEELGSGQFAIVKKCREKSTGLEYAAK----FIKKRQSRASRRGVSreEIEREVSILRQV-LHHNVITLHDVYENRTDV 99
Cdd:cd05100    16 LGKPLGEGCFGQVVMAEAIGIDKDKPNKpvtvAVKMLKDDATDKDLS--DLVSEMEMMKMIgKHKNIINLLGACTQDGPL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 100 VLILELVSGGELFDFLAQK----------------ESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIp 163
Cdd:cd05100    94 YVLVEYASKGNLREYLRARrppgmdysfdtcklpeEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNV- 172
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2056392213 164 iphIKLIDFGLAHEIEDGVEFKNIFG---TPEFVAPEIVNYEPLGLEADMWSIGVITY-ILLSGASPFLGDTKQE 234
Cdd:cd05100   173 ---MKIADFGLARDVHNIDYYKKTTNgrlPVKWMAPEALFDRVYTHQSDVWSFGVLLWeIFTLGGSPYPGIPVEE 244
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
24-227 1.49e-09

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


Pssm-ID: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 58.48  E-value: 1.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  24 DIGEELGSGQFAIVKKCREKStglEYAAKFIKKRQSRASRRgvsrEEIEREVSILRQVLHHNVITLHDVYENRTDVVLIL 103
Cdd:cd14153     3 EIGELIGKGRFGQVYHGRWHG---EVAIRLIDIERDNEEQL----KAFKREVMAYRQTRHENVVLFMGACMSPPHLAIIT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 104 ELVSGGELFDFLAQKESLSEEEATSFIKQ-ILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIphiklIDFGL-------- 174
Cdd:cd14153    76 SLCKGRTLYSVVRDAKVVLDVNKTRQIAQeIVKGMGYLHAKGILHKDLKSKNVFYDNGKVVI-----TDFGLftisgvlq 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2056392213 175 AHEIEDGVEFKNifGTPEFVAPEIV---------NYEPLGLEADMWSIGVITYILLSGASPF 227
Cdd:cd14153   151 AGRREDKLRIQS--GWLCHLAPEIIrqlspeteeDKLPFSKHSDVFAFGTIWYELHAREWPF 210
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
29-281 1.56e-09

Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein 15; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Vps15 is a large protein consisting of an N-terminal kinase domain, a C-terminal WD-repeat containing domain, and an intermediate bridge domain that contain HEAT repeats. The kinase domain is necessary for the signaling functions of Vps15. Human Vps15 was previously called p150. It associates and regulates Vps34, also called Class III phosphoinositide 3-kinase (PI3K), which catalyzes the phosphorylation of D-myo-phosphatidylinositol (PtdIns). Vps34 is the only PI3K present in yeast. It plays an important role in the regulation of protein and vesicular trafficking and sorting, autophagy, trimeric G-protein signaling, and phagocytosis. The Vps15 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270882 [Multi-domain]  Cd Length: 278  Bit Score: 58.42  E-value: 1.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKStGLEYAAKFIKKRQSrasrrgVSREEIEREVSILRQVLHH--NVITLHDVYENRTDVVLILELV 106
Cdd:cd13980     8 LGSTRFLKVARARHDE-GLVVVKVFVKPDPA------LPLRSYKQRLEEIRDRLLElpNVLPFQKVIETDKAAYLIRQYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 107 sGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIphikLIDFG------LAHeiED 180
Cdd:cd13980    81 -KYNLYDRISTRPFLNLIEKKWIAFQLLHALNQCHKRGVCHGDIKTENVLVTSWNWVY----LTDFAsfkptyLPE--DN 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 181 GVEFKNIFGTPE----FVAPE------------IVNYEPLGLEADMWSIG-VITYILLSGASPFlgdtkqeTLANItavs 243
Cdd:cd13980   154 PADFSYFFDTSRrrtcYIAPErfvdaltldaesERRDGELTPAMDIFSLGcVIAELFTEGRPLF-------DLSQL---- 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2056392213 244 YDFDEEFFSQTSELAK---DFIRKL----LVKETRKRLTIQEALR 281
Cdd:cd13980   223 LAYRKGEFSPEQVLEKiedPNIRELilhmIQRDPSKRLSAEDYLK 267
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
29-216 2.42e-09

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: 58.04  E-value: 2.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  29 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVsreeieREVSILRQVLHHNVITLHDVYENRTDVVLILELVSG 108
Cdd:cd14221     1 LGKGCFGQAIKVTHRETGEVMVMKELIRFDEETQRTFL------KEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 109 GELFDFLAQKES-LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLL-DKNIPIPhikliDFGLAH-------EIE 179
Cdd:cd14221    75 GTLRGIIKSMDShYPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVReNKSVVVA-----DFGLARlmvdektQPE 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2056392213 180 DGVEFK--------NIFGTPEFVAPEIVNYEPLGLEADMWSIGVI 216
Cdd:cd14221   150 GLRSLKkpdrkkryTVVGNPYWMAPEMINGRSYDEKVDVFSFGIV 194
PTK_Jak3_rpt1 cd14208
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is ...
26-223 2.86e-09

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit, common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. Jaks are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271110 [Multi-domain]  Cd Length: 260  Bit Score: 57.61  E-value: 2.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  26 GEELGSGQFA-IVKKCREKSTGLEYAAKFIKKRQSRASRRGVSREEIErEVSILRQVLHHNVITLHDVYENRtDVVLILE 104
Cdd:cd14208     4 MESLGKGSFTkIYRGLRTDEEDDERCETEVLLKVMDPTHGNCQESFLE-AASIMSQISHKHLVLLHGVCVGK-DSIMVQE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 105 LVSGGELfDFLAQKESLSEEEATSF----IKQILDGVNYLHTKKIAHFDLKPENIMLL---DKNIPiPHIKLIDFGLAHE 177
Cdd:cd14208    82 FVCHGAL-DLYLKKQQQKGPVAISWklqvVKQLAYALNYLEDKQLVHGNVSAKKVLLSregDKGSP-PFIKLSDPGVSIK 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2056392213 178 IedgVEFKNIFGTPEFVAPEIVNyEP--LGLEADMWSIGVITYILLSG 223
Cdd:cd14208   160 V---LDEELLAERIPWVAPECLS-DPqnLALEADKWGFGATLWEIFSG 203
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
74-227 3.02e-09

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: 57.30  E-value: 3.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  74 EVSILRQVLHHNVITLHDV-YENRTDVVLILELVSGGELFDFLAQK--ESLSEEEATSFIKQILDGVNYLHTKKIAHFDL 150
Cdd:cd05082    49 EASVMTQLRHSNLVQLLGViVEEKGGLYIVTEYMAKGSLVDYLRSRgrSVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDL 128
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2056392213 151 KPENIMLLDKNIPiphiKLIDFGLAHEIEDGVEFKNIfgTPEFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPF 227
Cdd:cd05082   129 AARNVLVSEDNVA----KVSDFGLTKEASSTQDTGKL--PVKWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPY 200
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
25-234 4.80e-09

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: 56.94  E-value: 4.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  25 IGEELGSGQFAIVKK--CREKSTGLEYAAKFIKKRQsrasrrgVSREEIE---REVSILRQVLHHNVITLHDV------Y 93
Cdd:cd05075     4 LGKTLGEGEFGSVMEgqLNQDDSVLKVAVKTMKIAI-------CTRSEMEdflSEAVCMKEFDHPNVMRLIGVclqnteS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  94 ENRTDVVLILELVSGGELFDFLA------QKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMlLDKNIpipHI 167
Cdd:cd05075    77 EGYPSPVVILPFMKHGDLHSFLLysrlgdCPVYLPTQMLVKFMTDIASGMEYLSSKNFIHRDLAARNCM-LNENM---NV 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2056392213 168 KLIDFGLAHEIEDGVEFKN--IFGTP-EFVAPEIVNYEPLGLEADMWSIGVITY-ILLSGASPFLGDTKQE 234
Cdd:cd05075   153 CVADFGLSKKIYNGDYYRQgrISKMPvKWIAIESLADRVYTTKSDVWSFGVTMWeIATRGQTPYPGVENSE 223
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
23-236 5.54e-09

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: 57.18  E-value: 5.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKfiKKRQSRASRRGVSREEIEREVSILRQvlHHNVITLHDVYENRTDVV-- 100
Cdd:cd13977     2 YSLIREVGRGSYGVVYEAVVRRTGARVAVK--KIRCNAPENVELALREFWALSSIQRQ--HPNVIQLEECVLQRDGLAqr 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 101 ---------LILELVS-------------------------GGELFDFLAQKeSLSEEEATSFIKQILDGVNYLHTKKIA 146
Cdd:cd13977    78 mshgssksdLYLLLVEtslkgercfdprsacylwfvmefcdGGDMNEYLLSR-RPDRQTNTSFMLQLSSALAFLHRNQIV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 147 HFDLKPENImLLDKNIPIPHIKLIDFGL-------AHEIEDGVEFKNIF-----GTPEFVAPEIV--NYEPlglEADMWS 212
Cdd:cd13977   157 HRDLKPDNI-LISHKRGEPILKVADFGLskvcsgsGLNPEEPANVNKHFlssacGSDFYMAPEVWegHYTA---KADIFA 232
                         250       260
                  ....*....|....*....|....
gi 2056392213 213 IGVITYILLSGASPFLGDTKQETL 236
Cdd:cd13977   233 LGIIIWAMVERITFRDGETKKELL 256
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
27-227 6.34e-09

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


Pssm-ID: 271041 [Multi-domain]  Cd Length: 274  Bit Score: 56.86  E-value: 6.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFAIVKKCREKSTGLEYAAKfikkrQSRASRRGVSREEIE-REVSILRQVLHH-NVITLHDVYENRTDVVLILE 104
Cdd:cd14139     6 EKIGVGEFGSVYKCIKRLDGCVYAIK-----RSMRPFAGSSNEQLAlHEVYAHAVLGHHpHVVRYYSAWAEDDHMIIQNE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 105 LVSGGELFDFLAQK----ESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMlldknipIPHIKLIDFGLAHEIED 180
Cdd:cd14139    81 YCNGGSLQDAISENtksgNHFEEPELKDILLQVSMGLKYIHNSGLVHLDIKPSNIF-------ICHKMQSSSGVGEEVSN 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 181 --------GVEFK--------NIF------GTPEFVAPEIVNYEPLGL-EADMWSIGvITYILLSGASPF 227
Cdd:cd14139   154 eedeflsaNVVYKigdlghvtSINkpqveeGDSRFLANEILQEDYRHLpKADIFALG-LTVALAAGAEPL 222
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
27-278 7.11e-09

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: 56.92  E-value: 7.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  27 EELGSGQFAIVKKCR----EKSTGLEYAAK-------FIKKRQSRASRRGVSREEIEREVSILRQVLHHNVITLHDVYEN 95
Cdd:cd05095    11 EKLGEGQFGEVHLCEaegmEKFMDKDFALEvsenqpvLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIRLLAVCIT 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  96 RTDVVLILELVSGGELFDFLAQKE---SLSEEEATSFIK---------QILDGVNYLHTKKIAHFDLKPENImLLDKNIP 163
Cdd:cd05095    91 DDPLCMITEYMENGDLNQFLSRQQpegQLALPSNALTVSysdlrfmaaQIASGMKYLSSLNFVHRDLATRNC-LVGKNYT 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 164 iphIKLIDFGLAHEIEDGvEFKNIFGTPefVAP-EIVNYEPLGL-----EADMWSIGVITYILLS--GASPFLGDTKQET 235
Cdd:cd05095   170 ---IKIADFGMSRNLYSG-DYYRIQGRA--VLPiRWMSWESILLgkfttASDVWAFGVTLWETLTfcREQPYSQLSDEQV 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2056392213 236 LANITAVSYDFDEEFFSQTSELAKDFIRKLLV----KETRKRLTIQE 278
Cdd:cd05095   244 IENTGEFFRDQGRQTYLPQPALCPDSVYKLMLscwrRDTKDRPSFQE 290
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
15-250 7.64e-09

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 57.40  E-value: 7.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  15 KQQKVEDF---YDIGEELGSGQFAIVKKCR-EKSTGLEYAAKFIKKRQSRASR---------RGVSREEI--EREVSILR 79
Cdd:PHA03210  139 KLKHDDEFlahFRVIDDLPAGAFGKIFICAlRASTEEAEARRGVNSTNQGKPKcerliakrvKAGSRAAIqlENEILALG 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  80 QVLHHNVITLHDVYENRTDVVLILELVSGgELFDF-----LAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPEN 154
Cdd:PHA03210  219 RLNHENILKIEEILRSEANTYMITQKYDF-DLYSFmydeaFDWKDRPLLKQTRAIMKQLLCAVEYIHDKKLIHRDIKLEN 297
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 155 IMLLDKNipipHIKLIDFGLAHEIEDGVEFKNI--FGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGA-SPFLGDT 231
Cdd:PHA03210  298 IFLNCDG----KIVLGDFGTAMPFEKEREAFDYgwVGTVATNSPEILAGDGYCEITDIWSCGLILLDMLSHDfCPIGDGG 373
                         250       260
                  ....*....|....*....|..
gi 2056392213 232 K---QETLANITAVSYdFDEEF 250
Cdd:PHA03210  374 GkpgKQLLKIIDSLSV-CDEEF 394
STKc_SRPK1 cd14216
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs ...
23-285 8.11e-09

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK1 binds with high affinity the alternative splicing factor, SRSF1 (serine/arginine-rich splicing factor 1), and regiospecifically phosphorylates 10-12 serines in its RS domain. It plays a role in the regulation of pre-mRNA splicing, chromatin structure, and germ cell development. 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. 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: 271118 [Multi-domain]  Cd Length: 349  Bit Score: 56.96  E-value: 8.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  23 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRAsrrgvsrEEIEREVSILRQVLHHN--------VITLHDVYE 94
Cdd:cd14216    12 YHVIRKLGWGHFSTVWLSWDIQGKRFVAMKVVKSAEHYT-------ETALDEIKLLKSVRNSDpndpnremVVQLLDDFK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  95 ----NRTDVVLILElVSGGELFDFLAQK--ESLSEEEATSFIKQILDGVNYLHTK-KIAHFDLKPENIML---------- 157
Cdd:cd14216    85 isgvNGTHICMVFE-VLGHHLLKWIIKSnyQGLPLPCVKKIIRQVLQGLDYLHTKcRIIHTDIKPENILLsvneqyirrl 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 158 ---------------LD-KNIPIPHIKLIDFGLAHEIEDgvEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILL 221
Cdd:cd14216   164 aaeatewqrnflvnpLEpKNAEKLKVKIADLGNACWVHK--HFTEDIQTRQYRSLEVLIGSGYNTPADIWSTACMAFELA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 222 SGA---SPFLGDTKQ----------ETLANIT---AVSYDFDEEFFSQTSELA--------------------------- 258
Cdd:cd14216   242 TGDylfEPHSGEDYSrdedhialiiELLGKVPrklIVAGKYSKEFFTKKGDLKhitklkpwglfevlvekyewsqeeaag 321
                         330       340
                  ....*....|....*....|....*...
gi 2056392213 259 -KDFIRKLLVKETRKRLTIQEALRHPWI 285
Cdd:cd14216   322 fTDFLLPMLELIPEKRATAAECLRHPWL 349
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
118-229 9.00e-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: 56.91  E-value: 9.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 118 KESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEI---EDGVEFKNIFGTPEFV 194
Cdd:cd05102   166 QSPLTMEDLICYSFQVARGMEFLASRKCIHRDLAARNILLSENNV----VKICDFGLARDIykdPDYVRKGSARLPLKWM 241
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2056392213 195 APEIVNYEPLGLEADMWSIGVITYILLS-GASPFLG 229
Cdd:cd05102   242 APESIFDKVYTTQSDVWSFGVLLWEIFSlGASPYPG 277
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
70-222 9.17e-09

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


Pssm-ID: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 56.18  E-value: 9.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  70 EIEREVSILRQVLHHNVITLHDVyENRTDVV-----LILELVSGGELFDFLAQKeSLSEEEATSFIKQILDGVNYLHT-- 142
Cdd:cd14053    35 LTEREIYSLPGMKHENILQFIGA-EKHGESLeaeywLITEFHERGSLCDYLKGN-VISWNELCKIAESMARGLAYLHEdi 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 143 --------KKIAHFDLKPENIMLldKNIPIPHIKliDFGLAHEIEDGVEFKNIF---GTPEFVAPEI----VNYEPLG-L 206
Cdd:cd14053   113 patngghkPSIAHRDFKSKNVLL--KSDLTACIA--DFGLALKFEPGKSCGDTHgqvGTRRYMAPEVlegaINFTRDAfL 188
                         170
                  ....*....|....*.
gi 2056392213 207 EADMWSIGVITYILLS 222
Cdd:cd14053   189 RIDMYAMGLVLWELLS 204
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
41-284 9.35e-09

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: 56.18  E-value: 9.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  41 REKSTGLEyAAKFI--KKRQSRASRRgvSREEI----EREVSILRQVLHHNVITLHDVYENRTD--------------VV 100
Cdd:cd14011    16 SKKSTKQE-VSVFVfeKKQLEEYSKR--DREQIlellKRGVKQLTRLRHPRILTVQHPLEESREslafatepvfaslaNV 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 101 LIlELVSGGELFDFLAQKEsLSEEEATSFIKQILDGVNYLH-TKKIAHFDLKPENIMLlDKNipiPHIKLIDFGLAHEIE 179
Cdd:cd14011    93 LG-ERDNMPSPPPELQDYK-LYDVEIKYGLLQISEALSFLHnDVKLVHGNICPESVVI-NSN---GEWKLAGFDFCISSE 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 180 DGVEFKNIFG------------TPEFVAPEIVNYEPLGLEADMWSIGVITY-ILLSGASPFLGDTKQETLANITAVSYDF 246
Cdd:cd14011   167 QATDQFPYFReydpnlpplaqpNLNYLAPEYILSKTCDPASDMFSLGVLIYaIYNKGKPLFDCVNNLLSYKKNSNQLRQL 246
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2056392213 247 DEEFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPW 284
Cdd:cd14011   247 SLSLLEKVPEELRDHVKTLLNVTPEVRPDAEQLSKIPF 284
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
74-218 1.16e-08

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 56.82  E-value: 1.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  74 EVSILRQVLHHNVITLHDVYENRTDVVLILELVSGgELFDFLAQKES-LSEEEATSFIKQILDGVNYLHTKKIAHFDLKP 152
Cdd:PHA03211  210 EARLLRRLSHPAVLALLDVRVVGGLTCLVLPKYRS-DLYTYLGARLRpLGLAQVTAVARQLLSAIDYIHGEGIIHRDIKT 288
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2056392213 153 ENIMLldkNIPiPHIKLIDFGLAHEIEDGVE---FKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITY 218
Cdd:PHA03211  289 ENVLV---NGP-EDICLGDFGAACFARGSWStpfHYGIAGTVDTNAPEVLAGDPYTPSVDIWSAGLVIF 353
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
63-241 1.85e-08

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: 55.12  E-value: 1.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  63 RRGVSREEIE---REVSILRQVLHHNVITLHDVYENRTDVVLILELVSGGELFDFL-------AQKESLSEEEATSFIKQ 132
Cdd:cd05044    35 RKGATDQEKAeflKEAHLMSNFKHPNILKLLGVCLDNDPQYIILELMEGGDLLSYLraarptaFTPPLLTLKDLLSICVD 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 133 ILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLAHEIedgveFKNIFGTPE--------FVAPEIVNYEPL 204
Cdd:cd05044   115 VAKGCVYLEDMHFVHRDLAARNCLVSSKDYRERVVKIGDFGLARDI-----YKNDYYRKEgegllpvrWMAPESLVDGVF 189
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2056392213 205 GLEADMWSIGVITY-ILLSGASPFLGDTKQETLANITA 241
Cdd:cd05044   190 TTQSDVWAFGVLMWeILTLGQQPYPARNNLEVLHFVRA 227
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
67-216 2.28e-08

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: 54.97  E-value: 2.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  67 SREE--IEREVSILRQVL--HHNVITL--HDVYENR--TDVVLILELVSGGELFDFLaQKESLSEEEATSFIKQILDGVN 138
Cdd:cd14056    28 SRDEdsWFRETEIYQTVMlrHENILGFiaADIKSTGswTQLWLITEYHEHGSLYDYL-QRNTLDTEEALRLAYSAASGLA 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 139 YLHTK--------KIAHFDLKPENIMlldknipiphIK------LIDFGLA-------HEIEDGVEFKniFGTPEFVAPE 197
Cdd:cd14056   107 HLHTEivgtqgkpAIAHRDLKSKNIL----------VKrdgtccIADLGLAvrydsdtNTIDIPPNPR--VGTKRYMAPE 174
                         170       180
                  ....*....|....*....|....*
gi 2056392213 198 IVN--YEPLGLE----ADMWSIGVI 216
Cdd:cd14056   175 VLDdsINPKSFEsfkmADIYSFGLV 199
PTK_Jak1_rpt1 cd05077
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely ...
76-237 2.46e-08

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; 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 cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. The Jak1 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: 270662 [Multi-domain]  Cd Length: 266  Bit Score: 54.94  E-value: 2.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  76 SILRQVLHHNVITLHDVYENRTDVVLILELVSGGELFDFLAQK-ESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPEN 154
Cdd:cd05077    60 SMMRQVSHKHIVLLYGVCVRDVENIMVEEFVEFGPLDLFMHRKsDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKN 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 155 IMLLDKNIPI---PHIKLIDFGLAHEI---EDGVEfknifgTPEFVAPEIV-NYEPLGLEADMWSIGVITY-ILLSGASP 226
Cdd:cd05077   140 ILLAREGIDGecgPFIKLSDPGIPITVlsrQECVE------RIPWIAPECVeDSKNLSIAADKWSFGTTLWeICYNGEIP 213
                         170
                  ....*....|.
gi 2056392213 227 FlgdtKQETLA 237
Cdd:cd05077   214 L----KDKTLA 220
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
28-240 2.77e-08

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


Pssm-ID: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 55.05  E-value: 2.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213  28 ELGSGQFAIV--KKCREKSTGLEYAAKFIKKRQSrASRRGvsREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILEL 105
Cdd:cd05093    12 ELGEGAFGKVflAECYNLCPEQDKILVAVKTLKD-ASDNA--RKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392213 106 VSGGELFDFL-------------AQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDF 172
Cdd:cd05093    89 MKHGDLNKFLrahgpdavlmaegNRPAELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLL----VKIGDF 164
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2056392213 173 GLAHEIEDgVEFKNIFGTP----EFVAPEIVNYEPLGLEADMWSIGVITY-ILLSGASPFLGDTKQETLANIT 240
Cdd:cd05093   165 GMSRDVYS-TDYYRVGGHTmlpiRWMPPESIMYRKFTTESDVWSLGVVLWeIFTYGKQPWYQLSNNEVIECIT 236
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH