NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|32141327|ref|NP_733728|]
View 

Ser/Thr protein kinase, partial [Streptomyces coelicolor A3(2)]

Graphical summary

show options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
STKc_AGC cd05123
Catalytic domain of AGC family Protein Serine/Threonine Kinases; Serine/Threonine Kinases ...
96-254 3.17e-19

Catalytic domain of AGC family Protein Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), AGC (Protein Kinases A, G and C) family, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AGC 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 (PI3K). 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. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases.


:

Pssm-ID: 173660 [Multi-domain]  Cd Length: 250  Bit Score: 86.42  E-value: 3.17e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  96 VTEWVAGvplGDL---LDRRGAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLAgATLAPR 172
Cdd:cd05123  71 VLEYAPG---GELfshLSKEGRFSEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDADGHIKLTDFGLA-KELSSE 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 173 LTA-------PAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPFRDRGRpEATLKGVDRLPLRTPVRAGPLAQA-VT 244
Cdd:cd05123 147 GSRtntfcgtPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAEDR-KEIYEKILKDPLRFPEFLSPEARDlIS 225
                       170
                ....*....|
gi 32141327 245 GLLRKNSRER 254
Cdd:cd05123 226 GLLQKDPTKR 235
 
Name Accession Description Interval E-value
STKc_AGC cd05123
Catalytic domain of AGC family Protein Serine/Threonine Kinases; Serine/Threonine Kinases ...
96-254 3.17e-19

Catalytic domain of AGC family Protein Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), AGC (Protein Kinases A, G and C) family, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AGC 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 (PI3K). 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. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases.


Pssm-ID: 173660 [Multi-domain]  Cd Length: 250  Bit Score: 86.42  E-value: 3.17e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  96 VTEWVAGvplGDL---LDRRGAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLAgATLAPR 172
Cdd:cd05123  71 VLEYAPG---GELfshLSKEGRFSEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDADGHIKLTDFGLA-KELSSE 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 173 LTA-------PAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPFRDRGRpEATLKGVDRLPLRTPVRAGPLAQA-VT 244
Cdd:cd05123 147 GSRtntfcgtPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAEDR-KEIYEKILKDPLRFPEFLSPEARDlIS 225
                       170
                ....*....|
gi 32141327 245 GLLRKNSRER 254
Cdd:cd05123 226 GLLQKDPTKR 235
Kinase-like pfam14531
Kinase-like; This family includes the pseudokinases ROP2 and ROP8 from Toxoplasma gondii. ...
104-254 1.82e-07

Kinase-like; This family includes the pseudokinases ROP2 and ROP8 from Toxoplasma gondii. These proteins have a typical bilobed protein kinase fold, but lack catalytic actvity.


Pssm-ID: 258671  Cd Length: 289  Bit Score: 51.65  E-value: 1.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327   104 PLGDLLDRRG--AFGCARAARVGLELLAVLEAAHTH--GVTHGELSPGQVFVREEGSVLVTGFG---LAGATLAPRLTAP 176
Cdd:pfam14531 128 ILVKVLDSHStfHKSLEHAARLLLTLQLIRLAAGLQhrGLVHGDFRPDNFFLDQKGGVFLGGFTalvRAGTKVVVSEVDV 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327   177 AYASPE-QARDERIGPAA-------DLWTLGAILYTMVEGRPPFrDRGRPEATLKGVDRLPLRTPvraGPLAQAVTGLLR 248
Cdd:pfam14531 208 AFAPPElFASRGYTGKNTttmthktDAWQLGLVIYRIWCLRLPF-TLDTPEGGSEWKFGRCVNMP---EPVKALLAGFLN 283

                  ....*.
gi 32141327   249 KNSRER 254
Cdd:pfam14531 284 RSQEAR 289
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
103-211 3.23e-04

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


Pssm-ID: 214801  Cd Length: 176  Bit Score: 40.46  E-value: 3.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327    103 VPLGDLLDRRGA-FGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGfglaGATLAPrltAPAYASP 181
Cdd:smart00750   1 VSLADILEVRGRpLNEEEIWAVCLQCLGALRELHRQAKSGNILLTWDGLLKLDGSVAFKT----PEQSRP---DPYFMAP 73
                           90       100       110
                   ....*....|....*....|....*....|
gi 32141327    182 EQARDERIGPAADLWTLGAILYTMVEGRPP 211
Cdd:smart00750  74 EVIQGQSYTEKADIYSLGITLYEALDYELP 103
AarF COG0661
Predicted unusual protein kinase [General function prediction only]
96-166 1.32e-03

Predicted unusual protein kinase [General function prediction only]


Pssm-ID: 223733  Cd Length: 517  Bit Score: 39.99  E-value: 1.32e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32141327  96 VTEWVAGVPLGDL--LDRRGaFGCARAARVGLEllAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLAG 166
Cdd:COG0661 244 TMEWIDGIKISDIaaLKSAG-IDRKELAELLVR--AFLRQLLRDGFFHADPHPGNILVRSDGRIVLLDFGIVG 313
PRK14879 PRK14879
serine/threonine protein kinase; Provisional
96-166 1.76e-03

serine/threonine protein kinase; Provisional


Pssm-ID: 237847  Cd Length: 211  Bit Score: 38.73  E-value: 1.76e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32141327   96 VTEWVAGVPLGDLLDRRGAFGCARAARVGlELLAVLeaaHTHGVTHGELSPGQVFVREEGSVLVTgFGLAG 166
Cdd:PRK14879  77 VMEYIEGEPLKDLINSNGMEELELSREIG-RLVGKL---HSAGIIHGDLTTSNMILSGGKIYLID-FGLAE 142
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
83-256 1.07e-25

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 105.31  E-value: 1.07e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327     83 VLDAVVADGMLWTVTEWVAGVPLGDLLDRRGAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGF 162
Cdd:smart00220  62 LYDVFEDEDKLYLVMEYCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADF 141
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327    163 GLAGATLAPRLTA-----PAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPFRDRGRPEATLKGVDRLPLRTPVRAG 237
Cdd:smart00220 142 GLARQLDPGEKLTtfvgtPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEW 221
                          170       180
                   ....*....|....*....|...
gi 32141327    238 PLAQA----VTGLLRKNSRERPT 256
Cdd:smart00220 222 DISPEakdlIRKLLVKDPEKRLT 244
Pkinase pfam00069
Protein kinase domain;
72-256 5.31e-20

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 88.84  E-value: 5.31e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327    72 MASLCPGRIAPVLDAVVADGMLWTVTEWVAGVPLGDLLDRRGAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFV 151
Cdd:pfam00069  52 LRRLSHPNIVRLIDAFEDKDHLYLVMEYCEGGDLFDYLSRGGPLSEDEAKKIALQILRGLEYLHSNGIIHRDLKPENILL 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327   152 REEGSVLVTGFGLAGATLAPRLTA------PAYASPEQARDER-IGPAADLWTLGAILYTMVEGRPPFRDRGRP------ 218
Cdd:pfam00069 132 DENGVVKIADFGLAKKLTKSSSSLttfvgtPEYMAPEVLLGGNgYGPKVDVWSLGVILYELLTGKPPFSGESILdqlqli 211
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 32141327   219 EATLKGVDRLPLRTPVRAGPLAQA-VTGLLRKNSRERPT 256
Cdd:pfam00069 212 RRILGPPLEFDEPKSDSGSEEAKDlIKKCLNKDPSKRPT 250
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
64-256 6.01e-17

Serine/threonine protein kinase [General function prediction only / Signal transduction mechanisms / Transcription / DNA replication, recombination, and repair]


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 81.33  E-value: 6.01e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  64 RVIRTGETMASL-CPGRIAPVLDAVVADGMLWTVTEWVAGVPLGDLLDRRGAFGC---ARAARVGLELLAVLEAAHTHGV 139
Cdd:COG0515  43 RFLREIQILASLnHPPNIVKLYDFFQDEGSLYLVMEYVDGGSLEDLLKKIGRKGPlseSEALFILAQILSALEYLHSKGI 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 140 THGELSPGQVFVREEGSVLV-TGFGLAGATLAPRLTA------------PAYASPEQARD---ERIGPAADLWTLGAILY 203
Cdd:COG0515 123 IHRDIKPENILLDRDGRVVKlIDFGLAKLLPDPGSTSsipalpstsvgtPGYMAPEVLLGlslAYASSSSDIWSLGITLY 202
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32141327 204 TMVEGRPPFRDRGRPEATLKGVDRL-PLRTPVRAGP------------LAQAVTGLLRKNSRERPT 256
Cdd:COG0515 203 ELLTGLPPFEGEKNSSATSQTLKIIlELPTPSLASPlspsnpeliskaASDLLKKLLAKDPKNRLS 268
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
80-254 3.13e-12

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: 234389 [Multi-domain]  Cd Length: 1266  Bit Score: 67.95  E-value: 3.13e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327     80 IAPVLDAVVA-DGMLWTVTEWVAGVPLGDLLDRRGAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEG--- 155
Cdd:TIGR03903   40 IVALLDSGEApPGLLFAVFEYVPGRTLREVLAADGALPAGETGRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGvrp 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327    156 ---------SVLVTGFGLAGATLAPR----LTAPAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPFRDRGRPEATL 222
Cdd:TIGR03903  120 hakvldfgiGTLLPGVRDADVATLTRttevLGTPTYCAPEQLRGEPVTPNSDLYAWGLIFLECLTGQRVVQGASVAEILY 199
                          170       180       190
                   ....*....|....*....|....*....|....
gi 32141327    223 KGVDRLPLRTP--VRAGPLAQAVTGLLRKNSRER 254
Cdd:TIGR03903  200 QQLSPVDVSLPpwIAGHPLGQVLRKALNKDPRQR 233
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
90-214 6.73e-11

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 62.53  E-value: 6.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327   90 DGMLWTVTEWVAGVPLGDLLDRRGAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLAGATL 169
Cdd:PTZ00263  90 ENRVYFLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVP 169
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 32141327  170 APRLT---APAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPFRD 214
Cdd:PTZ00263 170 DRTFTlcgTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFD 217
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
127-258 9.08e-05

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 43.45  E-value: 9.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  127 LLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGlaGATLAPRLTAPAY---------ASPEQARDERIGPAADLWT 197
Cdd:PHA03212 191 VLRAIQYLHENRIIHRDIKAENIFINHPGDVCLGDFG--AACFPVDINANKYygwagtiatNAPELLARDPYGPAVDIWS 268
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32141327  198 LGAILYTMVEGRPPFRDRG------RPEATLKGVDRL----PLRTPVRA-GPLAQAVTGLLRKNSRERPTRP 258
Cdd:PHA03212 269 AGIVLFEMATCHDSLFEKDgldgdcDSDRQIKLIIRRsgthPNEFPIDAqANLDEIYIGLAKKSSRKPGSRP 340
pknD PRK13184
serine/threonine-protein kinase; Reviewed
129-254 1.82e-04

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 42.84  E-value: 1.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  129 AVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLAGA-----------------TLAPRLTAPA-------YASPEQA 184
Cdd:PRK13184 124 ATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGAAIFkkleeedlldidvdernICYSSMTIPGkivgtpdYMAPERL 203
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32141327  185 RDERIGPAADLWTLGAILYTMVEGRPPFR-DRGRpeatlKGVDRLPLRTPVRAGP-------LAQAVTGLLRKNSRER 254
Cdd:PRK13184 204 LGVPASESTDIYALGVILYQMLTLSFPYRrKKGR-----KISYRDVILSPIEVAPyreippfLSQIAMKALAVDPAER 276
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
15-229 3.46e-03

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 38.26  E-value: 3.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327   15 RYRLFEVVQRETNRVCWSGEDATTGRPCLVTRIELPEGRAGeaarrAPGRVIRTGETMASLCPGRIAPVLDAVVADGMLW 94
Cdd:PLN00009   3 QYEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQEDEG-----VPSTAIREISLLKEMQHGNIVRLQDVVHSEKRLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327   95 TVTEWVaGVPLGDLLDRRGAFgcARAARV----GLELLAVLEAAHTHGVTHGELSPGQVFV-REEGSVLVTGFGLAGA-- 167
Cdd:PLN00009  78 LVFEYL-DLDLKKHMDSSPDF--AKNPRLiktyLYQILRGIAYCHSHRVLHRDLKPQNLLIdRRTNALKLADFGLARAfg 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  168 ----TLAPRLTAPAYASPEQARDER-IGPAADLWTLGAILYTMVEGRP--P-----------FRDRGRP-EATLKGVDRL 228
Cdd:PLN00009 155 ipvrTFTHEVVTLWYRAPEILLGSRhYSTPVDIWSVGCIFAEMVNQKPlfPgdseidelfkiFRILGTPnEETWPGVTSL 234

                 .
gi 32141327  229 P 229
Cdd:PLN00009 235 P 235
 
Name Accession Description Interval E-value
STKc_AGC cd05123
Catalytic domain of AGC family Protein Serine/Threonine Kinases; Serine/Threonine Kinases ...
96-254 3.17e-19

Catalytic domain of AGC family Protein Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), AGC (Protein Kinases A, G and C) family, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AGC 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 (PI3K). 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. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases.


Pssm-ID: 173660 [Multi-domain]  Cd Length: 250  Bit Score: 86.42  E-value: 3.17e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  96 VTEWVAGvplGDL---LDRRGAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLAgATLAPR 172
Cdd:cd05123  71 VLEYAPG---GELfshLSKEGRFSEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDADGHIKLTDFGLA-KELSSE 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 173 LTA-------PAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPFRDRGRpEATLKGVDRLPLRTPVRAGPLAQA-VT 244
Cdd:cd05123 147 GSRtntfcgtPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAEDR-KEIYEKILKDPLRFPEFLSPEARDlIS 225
                       170
                ....*....|
gi 32141327 245 GLLRKNSRER 254
Cdd:cd05123 226 GLLQKDPTKR 235
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; Protein Kinases (PKs), STE family, catalytic ...
84-256 5.24e-18

Catalytic domain of STE family Protein Kinases; Protein Kinases (PKs), STE family, catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The STE family is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). 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), MAPK kinase kinases (MAPKKKs), or MAPK kinase kinase 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.


Pssm-ID: 173659 [Multi-domain]  Cd Length: 253  Bit Score: 83.03  E-value: 5.24e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  84 LDAVVADGMLWTVTEWVAGVPLGDLLD-RRGAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGF 162
Cdd:cd05122  63 YGSYLKKDELWIVMEFCSGGSLKDLLKsTNQTLTESQIAYVCKELLKGLEYLHSNGIIHRDIKAANILLTSDGEVKLIDF 142
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 163 GLAgATLAPRLT------APAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPFRDRGRPEATLKGVDRLP--LRTPV 234
Cdd:cd05122 143 GLS-AQLSDTKArntmvgTPYWMAPEVINGKPYDYKADIWSLGITAIELAEGKPPYSELPPMKALFKIATNGPpgLRNPE 221
                       170       180
                ....*....|....*....|...
gi 32141327 235 RAGPLAQA-VTGLLRKNSRERPT 256
Cdd:cd05122 222 KWSDEFKDfLKKCLQKNPEKRPT 244
STKc_PKB_beta cd05595
Catalytic domain of the Protein Serine/Threonine Kinase, Protein Kinase B beta; Serine ...
96-254 1.38e-16

Catalytic domain of the Protein Serine/Threonine Kinase, Protein Kinase B beta; Serine/Threonine Kinases (STKs), Protein Kinase B (PKB) or Akt subfamily, beta (or Akt2) isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. 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.


Pssm-ID: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 79.66  E-value: 1.38e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  96 VTEWVAGVPLGDLLDRRGAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLA------GATL 169
Cdd:cd05595  73 VMEYANGGELFFHLSRERVFTEERARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCkegisdGATM 152
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 170 APRLTAPAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPFRDRGRpEATLKGVDRLPLRTPVRAGPLAQA-VTGLLR 248
Cdd:cd05595 153 KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDH-ERLFELILMEEIRFPRTLSPEAKSlLAGLLK 231

                ....*.
gi 32141327 249 KNSRER 254
Cdd:cd05595 232 KDPKQR 237
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Protein Serine/Threonine Kinases; Serine ...
76-254 1.20e-15

Catalytic domain of Yeast Protein Kinase 1-like Protein Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), Yeast protein kinase 1 (YPK1)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The YPK1-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. 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.


Pssm-ID: 173676 [Multi-domain]  Cd Length: 312  Bit Score: 76.51  E-value: 1.20e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  76 CPgRIAPVLDAVVADGMLWTVTEWVAGVPLGDLLDRRGAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEG 155
Cdd:cd05585  52 CP-FIVPLKFSFQSPEKLYLVLAFINGGELFHHLQREGRFDLSRARFYTAELLCALENLHKFNVIYRDLKPENILLDYQG 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 156 SVLVTGFGLAGATLAPRLTA------PAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPFRDRGRPEATLKgVDRLP 229
Cdd:cd05585 131 HIALCDFGLCKLNMKDDDKTntfcgtPEYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYDENVNEMYRK-ILQEP 209
                       170       180
                ....*....|....*....|....*.
gi 32141327 230 LRTPVRAGPLAQA-VTGLLRKNSRER 254
Cdd:cd05585 210 LRFPDGFDRDAKDlLIGLLSRDPTRR 235
STKc_GRK6 cd05630
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; ...
113-254 1.20e-14

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; Serine/Threonine Kinases (STKs), G protein-coupled Receptor Kinase (GRK) subfamily, GRK6 isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. There are seven types of GRKs, named GRK1 to GRK7. GRK6 is widely expressed in many tissues. t 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.


Pssm-ID: 173719 [Multi-domain]  Cd Length: 285  Bit Score: 73.13  E-value: 1.20e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 113 GAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLA-----GATLAPRLTAPAYASPEQARDE 187
Cdd:cd05630  97 AGFEEGRAVFYAAEICCGLEDLHQERIVYRDLKPENILLDDHGHIRISDLGLAvhvpeGQTIKGRVGTVGYMAPEVVKNE 176
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32141327 188 RIGPAADLWTLGAILYTMVEGRPPFRDRGRP---EATLKGVDRLPLRTPVRAGPLAQAV-TGLLRKNSRER 254
Cdd:cd05630 177 RYTFSPDWWALGCLLYEMIAGQSPFQQRKKKikrEEVERLVKEVQEEYSEKFSPDARSLcKMLLCKDPKER 247
STKc_PAK2 cd06655
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 2; Serine ...
15-212 1.34e-14

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 2; Serine/threonine kinases (STKs), p21-activated kinase (PAK) 2, 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. PAK2 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). 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.


Pssm-ID: 132986 [Multi-domain]  Cd Length: 296  Bit Score: 73.22  E-value: 1.34e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  15 RYRLFEVVQRETNRVCWSGEDATTGRPCLVTRIELpegrageaaRRAPGRVIRTGE--TMASLCPGRIAPVLDAVVADGM 92
Cdd:cd06655  20 KYTRYEKIGQGASGTVFTAIDVATGQEVAIKQINL---------QKQPKKELIINEilVMKELKNPNIVNFLDSFLVGDE 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  93 LWTVTEWVAGVPLGDLLDRRgAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLAgATLAPR 172
Cdd:cd06655  91 LFVVMEYLAGGSLTDVVTET-CMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFC-AQITPE 168
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 32141327 173 LT-------APAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPF 212
Cdd:cd06655 169 QSkrstmvgTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPY 215
STKc_PAK1 cd06654
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 1; Serine ...
15-212 1.83e-14

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 1; Serine/threonine kinases (STKs), p21-activated kinase (PAK) 1, 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. PAK1 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). 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.


Pssm-ID: 132985 [Multi-domain]  Cd Length: 296  Bit Score: 72.83  E-value: 1.83e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  15 RYRLFEVVQRETNRVCWSGEDATTGRPCLVTRIELPEGRAGEAarrapgrVIRTGETMASLCPGRIAPVLDAVVADGMLW 94
Cdd:cd06654  21 KYTRFEKIGQGASGTVYTAMDVATGQEVAIRQMNLQQQPKKEL-------IINEILVMRENKNPNIVNYLDSYLVGDELW 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  95 TVTEWVAGVPLGDLLDRRgAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLAgATLAPRLT 174
Cdd:cd06654  94 VVMEYLAGGSLTDVVTET-CMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFC-AQITPEQS 171
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 32141327 175 -------APAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPF 212
Cdd:cd06654 172 krstmvgTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPY 216
STKc_SGK2 cd05603
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
93-254 2.48e-14

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; Serine/Threonine Kinases (STKs), Serum- and Glucocorticoid-induced Kinase (SGK) subfamily, SGK2 isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SGK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. There are three isoforms of SGK, named SGK1, SGK2, and SGK3. SGK2 shows a more restricted distribution that 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.


Pssm-ID: 173694 [Multi-domain]  Cd Length: 321  Bit Score: 72.70  E-value: 2.48e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  93 LWTVTEWVAGVPLGDLLDRRGAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLAGATLAPR 172
Cdd:cd05603  71 LYFVLDYVNGGELFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLCKEGVEPE 150
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 173 LTA------PAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPFRDRGRPEaTLKGVDRLPLRTP-VRAGPLAQAVTG 245
Cdd:cd05603 151 ETTstfcgtPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFYSRDVSQ-MYDNILHKPLQLPgGKTVAACDLLVG 229

                ....*....
gi 32141327 246 LLRKNSRER 254
Cdd:cd05603 230 LLHKDQRRR 238
STKc_PAK_I cd06647
Catalytic domain of the Protein Serine/Threonine Kinase, Group I p21-activated kinase; Serine ...
80-212 5.35e-14

Catalytic domain of the Protein Serine/Threonine Kinase, Group I p21-activated kinase; Serine/threonine kinases (STKs), p21-activated kinase (PAK) subfamily, Group I, 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 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. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. 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.


Pssm-ID: 132978 [Multi-domain]  Cd Length: 293  Bit Score: 71.47  E-value: 5.35e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  80 IAPVLDAVVADGMLWTVTEWVAGVPLGDLLDRRgAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLV 159
Cdd:cd06647  78 IVNYLDSYLVGDELWVVMEYLAGGSLTDVVTET-CMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKL 156
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 160 TGFGLAgATLAP----RLT---APAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPF 212
Cdd:cd06647 157 TDFGFC-AQITPeqskRSTmvgTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPY 215
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
15-212 6.49e-14

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: 71.29  E-value: 6.49e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  15 RYRLFEVVQRETNRVCWSGEDATTGRPCLVTRIELPEGRAGEAarrapgrVIRTGETMASLCPGRIAPVLDAVVADGMLW 94
Cdd:cd06656  20 KYTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKKEL-------IINEILVMRENKNPNIVNYLDSYLVGDELW 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  95 TVTEWVAGVPLGDLLDRRgAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLAgATLAPRLT 174
Cdd:cd06656  93 VVMEYLAGGSLTDVVTET-CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFC-AQITPEQS 170
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 32141327 175 -------APAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPF 212
Cdd:cd06656 171 krstmvgTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPY 215
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
70-214 2.25e-13

Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. 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. PKs make up a large family of serine/threonine kinases, protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation, about 95%, 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 550 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.


Pssm-ID: 173623 [Multi-domain]  Cd Length: 215  Bit Score: 68.42  E-value: 2.25e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  70 ETMASLCPGRIAPVLDAVVADGMLWTVTEWVAGVPLGDLLDRRGA-FGCARAARVGLELLAVLEAAHTHGVTHGELSPGQ 148
Cdd:cd00180  43 EILKKLNHPNIVKLYGVFEDENHLYLVMEYCEGGSLKDLLKENEGkLSEDEILRILLQILEGLEYLHSNGIIHRDLKPEN 122
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32141327 149 VFV-REEGSVLVTGFGLA------GATLAPRLTAPAYASPEQARDER-IGPAADLWTLGAILYTMvegrPPFRD 214
Cdd:cd00180 123 ILLdSDNGKVKLADFGLSklltsdKSLLKTIVGTPAYMAPEVLLGKGyYSEKSDIWSLGVILYEL----PELKD 192
STKc_MAPKKK cd06606
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein Kinase ...
98-222 3.40e-13

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; Serine/threonine kinases (STKs), mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173724 [Multi-domain]  Cd Length: 260  Bit Score: 68.35  E-value: 3.40e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  98 EWVAGVPLGDLLDRRGAFG---CARAARVGLELLAVLeaaHTHGVTHGELSPGQVFVREEGSVLVTGFGLA--------- 165
Cdd:cd06606  81 EYVSGGSLSSLLKKFGKLPepvIRKYTRQILEGLAYL---HSNGIVHRDIKGANILVDSDGVVKLADFGCAkrlgdietg 157
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 32141327 166 GATLAPRLTaPAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPFRDRGRPEATL 222
Cdd:cd06606 158 EGTGSVRGT-PYWMAPEVIRGEEYGRAADIWSLGCTVIEMATGKPPWSELGNPMAAL 213
STKc_PKB cd05571
Catalytic domain of the Protein Serine/Threonine Kinase, Protein Kinase B; Serine/Threonine ...
96-254 5.55e-13

Catalytic domain of the Protein Serine/Threonine Kinase, Protein Kinase B; Serine/Threonine Kinases (STKs), Protein Kinase B (PKB) or Akt subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKB subfamily is part of a 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). 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 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.


Pssm-ID: 173662 [Multi-domain]  Cd Length: 323  Bit Score: 68.68  E-value: 5.55e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  96 VTEWVAGVPLGDLLDRRGAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLA------GATL 169
Cdd:cd05571  73 VMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALGYLHSCDVVYRDLKLENLMLDKDGHIKITDFGLCkegisdGATM 152
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 170 APRLTAPAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPFRDRGRP---EATLKGVDRLPLRTPVRAGPLaqaVTGL 246
Cdd:cd05571 153 KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEklfELILMEEIRFPRTLSPEAKSL---LAGL 229

                ....*...
gi 32141327 247 LRKNSRER 254
Cdd:cd05571 230 LKKDPKQR 237
STKc_GRK5 cd05632
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; ...
119-215 6.83e-13

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; Serine/Threonine Kinases (STKs), G protein-coupled Receptor Kinase (GRK) subfamily, GRK5 isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. There are seven types of GRKs, named GRK1 to GRK7. 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.


Pssm-ID: 173721 [Multi-domain]  Cd Length: 285  Bit Score: 67.69  E-value: 6.83e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 119 RAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLA-----GATLAPRLTAPAYASPEQARDERIGPAA 193
Cdd:cd05632 103 RALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAvkipeGESIRGRVGTVGYMAPEVLNNQRYTLSP 182
                        90       100
                ....*....|....*....|..
gi 32141327 194 DLWTLGAILYTMVEGRPPFRDR 215
Cdd:cd05632 183 DYWGLGCLIYEMIEGQSPFRGR 204
STKc_SGK cd05575
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
93-254 9.00e-13

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; Serine/Threonine Kinases (STKs), Serum- and Glucocorticoid-induced Kinase (SGK) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SGK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. There are three isoforms of SGK, named SGK1, SGK2, and SGK3 (also called cytokine-independent survival kinase CISK). 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.


Pssm-ID: 173666 [Multi-domain]  Cd Length: 323  Bit Score: 67.89  E-value: 9.00e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  93 LWTVTEWVAGVPLGDLLDRRGAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLAGATLAPR 172
Cdd:cd05575  71 LYFVLDYVNGGELFFHLQRERSFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLCKEGIEHS 150
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 173 LTA------PAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPFRDRGRPEATLKGVDRlPLRTPVRAGPLAQAV-TG 245
Cdd:cd05575 151 KTTstfcgtPEYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRDTAEMYDNILNK-PLRLKPNISVSARHLlEG 229

                ....*....
gi 32141327 246 LLRKNSRER 254
Cdd:cd05575 230 LLQKDRTKR 238
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine kinase-like proteins; Serine ...
93-214 1.04e-12

Catalytic domain of Microtubule-associated serine/threonine kinase-like proteins; Serine/Threonine Kinases (STKs), Microtubule-associated serine/threonine (MAST) kinase subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. The MAST kinase subfamily includes MAST kinases, MAST-like (MASTL) kinases, 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 also contains an insert relative to MAST kinases like MASTL. 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. The fungal proteins Rim15 and cek1 are involved in the regulation of meiosis and mitosis, respectively.


Pssm-ID: 173670 [Multi-domain]  Cd Length: 265  Bit Score: 66.89  E-value: 1.04e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  93 LWTVTEWVAGVPLGDLLDRRGAFGcARAARVGL-ELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLAGATLAP 171
Cdd:cd05579  68 LYLVMEYLPGGDLASLLENVGSLD-EDVARIYIaEIVLALEYLHSNGIIHRDLKPDNILIDSNGHLKLTDFGLSKVGLVR 146
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 32141327 172 RLTA--------------PAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPFRD 214
Cdd:cd05579 147 RQINlnddekedkrivgtPDYIAPEVILGQGHSKTVDWWSLGCILYEFLVGIPPFHG 203
STKc_PKB_alpha cd05594
Catalytic domain of the Protein Serine/Threonine Kinase, Protein Kinase B alpha; Serine ...
96-254 1.16e-12

Catalytic domain of the Protein Serine/Threonine Kinase, Protein Kinase B alpha; Serine/Threonine Kinases (STKs), Protein Kinase B (PKB) or Akt subfamily, alpha (or Akt1) isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. 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.


Pssm-ID: 173685 [Multi-domain]  Cd Length: 325  Bit Score: 67.74  E-value: 1.16e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  96 VTEWVAGVPLGDLLDRRGAFGCARAARVGLELLAVLEAAHTH-GVTHGELSPGQVFVREEGSVLVTGFGLA------GAT 168
Cdd:cd05594  73 VMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEkNVVYRDLKLENLMLDKDGHIKITDFGLCkegikdGAT 152
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 169 LAPRLTAPAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPFRDRGRpEATLKGVDRLPLRTPVRAGPLAQA-VTGLL 247
Cdd:cd05594 153 MKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDH-EKLFELILMEEIRFPRTLSPEAKSlLSGLL 231

                ....*..
gi 32141327 248 RKNSRER 254
Cdd:cd05594 232 KKDPKQR 238
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
93-254 2.28e-12

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 1; Serine/Threonine Kinases (STKs), Serum- and Glucocorticoid-induced Kinase (SGK) subfamily, SGK1 isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SGK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. There are three isoforms of SGK, named SGK1, SGK2, and SGK3. 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.


Pssm-ID: 173693 [Multi-domain]  Cd Length: 325  Bit Score: 66.96  E-value: 2.28e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  93 LWTVTEWVAGVPLGDLLDRRGAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLAGATLAPR 172
Cdd:cd05602  71 LYFVLDYINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENIEHN 150
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 173 LTA------PAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPFRDRGRPEATLKGVDRlPLR-TPVRAGPLAQAVTG 245
Cdd:cd05602 151 GTTstfcgtPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNK-PLQlKPNITNSARHLLEG 229

                ....*....
gi 32141327 246 LLRKNSRER 254
Cdd:cd05602 230 LLQKDRTKR 238
STKc_nPKC_epsilon cd05591
Catalytic domain of the Protein Serine/Threonine Kinase, Novel Protein Kinase C epsilon; ...
93-212 2.44e-12

Catalytic domain of the Protein Serine/Threonine Kinase, Novel Protein Kinase C epsilon; Serine/Threonine Kinases (STKs), Novel Protein Kinase C (nPKC), epsilon isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The nPKC subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. 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.


Pssm-ID: 173682 [Multi-domain]  Cd Length: 321  Bit Score: 66.79  E-value: 2.44e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  93 LWTVTEWVAGvplGDLL---DRRGAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLAGATL 169
Cdd:cd05591  71 LFFVMEYVNG---GDLMfqiQRSRKFDEPRSRFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGI 147
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 32141327 170 APRLTA------PAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPF 212
Cdd:cd05591 148 LNGVTTttfcgtPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPF 196
STKc_PDK1 cd05581
Catalytic domain of the Protein Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; ...
93-256 2.55e-12

Catalytic domain of the Protein Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; Serine/Threonine Kinases (STKs), Phosphoinositide-dependent kinase 1 (PDK1) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PDK1 subfamily is part of a 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). 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. PDK1 is essential for normal embryo development and is important in regulating cell volume.


Pssm-ID: 173672 [Multi-domain]  Cd Length: 280  Bit Score: 66.06  E-value: 2.55e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  93 LWTVTEWVAGVPLGDLLDRRGAFG--CAR--AArvglELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLA--- 165
Cdd:cd05581  77 LYFVLEYAPNGELLQYIRKYGSLDekCTRfyAA----EILLALEYLHSKGIIHRDLKPENILLDKDMHIKITDFGTAkvl 152
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 166 ---------------GATLAPRLTA--------PAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPFRDRGRPEATL 222
Cdd:cd05581 153 dpnsspesnkgdatnIDSQIEKNRRrfasfvgtAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQ 232
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 32141327 223 KGVDR---LPLRTPVRAGPLaqaVTGLLRKNSRERPT 256
Cdd:cd05581 233 KILKLeysFPPNFPPDAKDL---IEKLLVLDPQDRLG 266
STKc_GRK cd05577
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase; ...
115-254 2.78e-12

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase; Serine/Threonine Kinases (STKs), G protein-coupled Receptor Kinase (GRK) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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 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. They 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. GRKs play important roles in the cardiovascular, immune, respiratory, skeletal, and nervous systems.


Pssm-ID: 173668 [Multi-domain]  Cd Length: 277  Bit Score: 65.98  E-value: 2.78e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 115 FGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLA-----GATLAPRLTAPAYASPEQARDERI 189
Cdd:cd05577  92 FPEARAIFYAAQIICGLEHLHQRRIVYRDLKPENVLLDDHGNVRISDLGLAvelkgGKKIKGRAGTPGYMAPEVLQGEVY 171
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 190 GPAADLWTLGAILYTMVEGRPPFRDRGRpEATLKGVDRLPLRTPV----RAGPLAQAV-TGLLRKNSRER 254
Cdd:cd05577 172 DFSVDWFALGCTLYEMIAGRSPFRQRKE-KVEKEELKRRTLEMAVeypdKFSPEAKDLcEALLQKDPEKR 240
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; Serine/Threonine Kinases (STKs) ...
93-214 5.99e-12

Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), cAMP-dependent protein kinase (PKA) subfamily, PRKX-like kinases, catalytic (c) subunit. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKA subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173703 [Multi-domain]  Cd Length: 291  Bit Score: 65.15  E-value: 5.99e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  93 LWTVTEWVAGVPLGDLLDRRGAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLAGATLAPR 172
Cdd:cd05612  76 LYMLMEYVPGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAKKLRDRT 155
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 32141327 173 LT---APAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPFRD 214
Cdd:cd05612 156 WTlcgTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFD 200
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Protein Serine/Threonine Kinases; ...
113-254 1.36e-11

Catalytic domain of G protein-coupled Receptor Kinase 4-like Protein Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), G protein-coupled Receptor Kinase (GRK) subfamily, GRK4-like group, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. There are seven types of GRKs, named GRK1 to GRK7. Members of the GRK4-like group include GRK4, GRK5, GRK6, and similar GRKs. GRKs in this group 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.


Pssm-ID: 173696 [Multi-domain]  Cd Length: 285  Bit Score: 64.08  E-value: 1.36e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 113 GAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLA-----GATLAPRLTAPAYASPEQARDE 187
Cdd:cd05605  97 PGFDEERAVFYAAEITCGLEDLHRERIVYRDLKPENILLDDYGHIRISDLGLAveipeGETIRGRVGTVGYMAPEVVKNE 176
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32141327 188 RIGPAADLWTLGAILYTMVEGRPPFRDRgRPEATLKGVDRLPLRTP----VRAGPLAQAV-TGLLRKNSRER 254
Cdd:cd05605 177 RYTFSPDWWGLGCLIYEMIEGKSPFRQR-KEKVKREEVERRVKEDQeeysEKFSEAARSIcRQLLTKDPGFR 247
STKc_p70S6K cd05584
Catalytic domain of the Protein Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; ...
80-254 2.01e-11

Catalytic domain of the Protein Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; Serine/Threonine Kinases (STKs), 70 kDa ribosomal protein S6 kinase (p70S6K) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. 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. 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).


Pssm-ID: 173675 [Multi-domain]  Cd Length: 323  Bit Score: 64.05  E-value: 2.01e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  80 IAPVLDAVVADGMLWTVTEWVAGVPLGDLLDRRGAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLV 159
Cdd:cd05584  62 IVDLIYAFQTGGKLYLILEYLSGGELFMHLEREGIFMEDTACFYLSEISLALEHLHQQGIIYRDLKPENILLDAQGHVKL 141
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 160 TGFGLA------GATLAPRLTAPAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPFRDRGRpEATLKGVDRLPLRTP 233
Cdd:cd05584 142 TDFGLCkesiheGTVTHTFCGTIEYMAPEILMRSGHGKAVDWWSLGALMYDMLTGAPPFTAENR-KKTIDKILKGKLNLP 220
                       170       180
                ....*....|....*....|..
gi 32141327 234 VRAGPLAQA-VTGLLRKNSRER 254
Cdd:cd05584 221 PYLTPEARDlLKKLLKRNPSSR 242
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
93-219 2.22e-11

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 3; Serine/Threonine Kinases (STKs), Serum- and Glucocorticoid-induced Kinase (SGK) subfamily, SGK3 isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SGK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. There are three isoforms of SGK, named SGK1, SGK2, and SGK3 (also called cytokine-independent survival kinase CISK). SGK3 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.


Pssm-ID: 173695 [Multi-domain]  Cd Length: 325  Bit Score: 63.87  E-value: 2.22e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  93 LWTVTEWVAGVPLGDLLDRRGAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLA--GATLA 170
Cdd:cd05604  71 LYFVLDFVNGGELFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHVVLTDFGLCkeGIAQS 150
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 32141327 171 PRLTA----PAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPFRDRGRPE 219
Cdd:cd05604 151 DTTTTfcgtPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAE 203
STKc_PKB_gamma cd05593
Catalytic domain of the Protein Serine/Threonine Kinase, Protein Kinase B gamma; Serine ...
96-215 2.50e-11

Catalytic domain of the Protein Serine/Threonine Kinase, Protein Kinase B gamma; Serine/Threonine Kinases (STKs), Protein Kinase B (PKB) or Akt subfamily, gamma (or Akt3) isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. 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.


Pssm-ID: 173684 [Multi-domain]  Cd Length: 328  Bit Score: 63.94  E-value: 2.50e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  96 VTEWVAGVPLGDLLDRRGAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLA------GATL 169
Cdd:cd05593  73 VMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCkegitdAATM 152
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 32141327 170 APRLTAPAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPFRDR 215
Cdd:cd05593 153 KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 198
STKc_PAK_II cd06648
Catalytic domain of the Protein Serine/Threonine Kinase, Group II p21-activated kinase; Serine ...
93-256 2.93e-11

Catalytic domain of the Protein Serine/Threonine Kinase, Group II p21-activated kinase; Serine/threonine kinases (STKs), p21-activated kinase (PAK) subfamily, Group II, 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. 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.


Pssm-ID: 132979 [Multi-domain]  Cd Length: 285  Bit Score: 62.85  E-value: 2.93e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  93 LWTVTEWVAGVPLGDLLDRrGAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLAGATL--A 170
Cdd:cd06648  91 LWVVMEFLEGGALTDIVTH-TRMNEEQIATVCLAVLKALSFLHAQGVIHRDIKSDSILLTSDGRVKLSDFGFCAQVSkeV 169
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 171 PR----LTAPAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPFRDRGRPEATLKGVDRLP--LRTPVRAGP-LAQAV 243
Cdd:cd06648 170 PRrkslVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIRDNLPpkLKNLHKVSPrLRSFL 249
                       170
                ....*....|...
gi 32141327 244 TGLLRKNSRERPT 256
Cdd:cd06648 250 DRMLVRDPAQRAT 262
STKc_Nek10 cd08528
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
93-255 3.85e-11

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related kinase 10; Serine/Threonine Kinases (STKs), Never In Mitosis gene A (NIMA)-related kinase 10 (Nek10) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek10 subfamily is one 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 protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173770 [Multi-domain]  Cd Length: 269  Bit Score: 62.52  E-value: 3.85e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  93 LWTVTEWVAGVPLGDLL----DRRGAFGCARAARVGLELLAVLEAAHTHG-VTHGELSPGQVFVREEGSVLVTGFGLA-- 165
Cdd:cd08528  84 LYIVMDLIEGAPLGEHFnslkEKKQRFTEERIWNIFVQMVLALRYLHKEKrIVHRDLTPNNIMLGEDDKVTITDFGLAkq 163
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 166 ---GATLAPRLTAPAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPFRDRGRPEATLKGVDrlPLRTPVRAGPLAQA 242
Cdd:cd08528 164 kqpESKLTSVVGTILYSCPEIVKNEPYGEKADVWAFGCILYQMCTLQPPFYSTNMLSLATKIVE--AVYEPLPEGMYSED 241
                       170
                ....*....|....*..
gi 32141327 243 VTGL----LRKNSRERP 255
Cdd:cd08528 242 VTDVitscLTPDAEARP 258
STKc_aPKC_zeta cd05617
Catalytic domain of the Protein Serine/Threonine Kinase, Atypical Protein Kinase C zeta; ...
93-254 4.37e-11

Catalytic domain of the Protein Serine/Threonine Kinase, Atypical Protein Kinase C zeta; Serine/Threonine Kinases (STKs), Atypical Protein Kinase C (aPKC) subfamily, zeta isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. There are two aPKC isoforms, zeta and iota. 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.


Pssm-ID: 173708 [Multi-domain]  Cd Length: 327  Bit Score: 63.13  E-value: 4.37e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  93 LWTVTEWVAGVPLGDLLDRRGAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLAGATLAPR 172
Cdd:cd05617  71 LFLVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPG 150
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 173 LTA------PAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPFR------DRGRPEATLKGVDRLPLRTP----VRA 236
Cdd:cd05617 151 DTTstfcgtPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDiitdnpDMNTEDYLFQVILEKPIRIPrflsVKA 230
                       170
                ....*....|....*...
gi 32141327 237 gplAQAVTGLLRKNSRER 254
Cdd:cd05617 231 ---SHVLKGFLNKDPKER 245
STKc_PKC cd05570
Catalytic domain of the Protein Serine/Threonine Kinase, Protein Kinase C; Serine/Threonine ...
93-212 4.78e-11

Catalytic domain of the Protein Serine/Threonine Kinase, Protein Kinase C; Serine/Threonine Kinases (STKs), Protein Kinase C (PKC) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKC subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173661 [Multi-domain]  Cd Length: 318  Bit Score: 62.78  E-value: 4.78e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  93 LWTVTEWVAGvplGDLL---DRRGAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLAGATL 169
Cdd:cd05570  71 LFFVMEYVNG---GDLMfhiQRSGRFDEPRARFYAAEIVLGLQFLHERGIIYRDLKLDNVLLDSEGHIKIADFGMCKEGI 147
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 32141327 170 APRLTA------PAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPF 212
Cdd:cd05570 148 LGGVTTstfcgtPDYIAPEILSYQPYGPAVDWWALGVLLYEMLAGQSPF 196
STKc_Nek2 cd08217
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
122-256 8.71e-11

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related kinase 2; Serine/Threonine Kinases (STKs), Never In Mitosis gene A (NIMA)-related kinase 2 (Nek2) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek2 subfamily is one 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 protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173757 [Multi-domain]  Cd Length: 265  Bit Score: 61.11  E-value: 8.71e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 122 RVGLELLAVLEAAHT-----HGVTHGELSPGQVFVREEGSVLVTGFGLA-----GATLAPR-LTAPAYASPEQARDERIG 190
Cdd:cd08217 109 RILTQLLLALYECHNrsdpgNTVLHRDLKPANIFLDANNNVKLGDFGLAkilghDSSFAKTyVGTPYYMSPEQLNHMSYD 188
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 191 PAADLWTLGAILYTMVEGRPPFRDRGRPEATLK---G-VDRLPLRtpvRAGPLAQAVTGLLRKNSRERPT 256
Cdd:cd08217 189 EKSDIWSLGCLIYELCALSPPFTARNQLQLASKikeGkFRRIPYR---YSSELNEVIKSMLNVDPDKRPS 255
STKc_CNK2-like cd08530
Catalytic domain of the Protein Serine/Threonine Kinase, Chlamydomonas reinhardtii CNK2, and ...
122-256 1.14e-10

Catalytic domain of the Protein Serine/Threonine Kinase, Chlamydomonas reinhardtii CNK2, and similar domains; Serine/Threonine Kinases (STKs), Chlamydomonas reinhardtii Never In Mitosis gene A (NIMA)-related kinase 1 (CNK2)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Chlamydomonas reinhardtii CNK2-like subfamily belongs to the (NIMA)-related kinase (Nek) family. The Nek family 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 protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173772 [Multi-domain]  Cd Length: 256  Bit Score: 60.92  E-value: 1.14e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 122 RVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLAGAtLAPRLT-----APAYASPEQARDERIGPAADLW 196
Cdd:cd08530 107 RIFIQLLRGLQALHEQKILHRDLKSANILLVANDLVKIGDLGISKV-LKKNMAktqigTPHYMAPEVWKGRPYSYKSDIW 185
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32141327 197 TLGAILYTMVEGRPPFRDRGRPEATLK----GVDRLPlrtPVRAGPLAQAVTGLLRKNSRERPT 256
Cdd:cd08530 186 SLGCLLYEMATFAPPFEARSMQDLRYKvqrgKYPPIP---PIYSQDLQNFIRSMLQVKPKLRPN 246
STKc_nPKC_eta cd05590
Catalytic domain of the Protein Serine/Threonine Kinase, Novel Protein Kinase C eta; Serine ...
93-212 1.21e-10

Catalytic domain of the Protein Serine/Threonine Kinase, Novel Protein Kinase C eta; Serine/Threonine Kinases (STKs), Novel Protein Kinase C (nPKC), eta isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The nPKC subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. 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.


Pssm-ID: 173681 [Multi-domain]  Cd Length: 320  Bit Score: 61.45  E-value: 1.21e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  93 LWTVTEWVAGvplGDLL-----DRRgaFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLA-- 165
Cdd:cd05590  71 LFFVMEFVNG---GDLMfhiqkSRR--FDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCke 145
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 32141327 166 ----GATLAPRLTAPAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPF 212
Cdd:cd05590 146 gifnGKTTSTFCGTPDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPF 196
STKc_PAK cd06614
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase; Serine ...
84-256 1.38e-10

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase; Serine/threonine kinases (STKs), p21-activated kinase (PAK) subfamily, 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 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.


Pssm-ID: 173728 [Multi-domain]  Cd Length: 286  Bit Score: 61.07  E-value: 1.38e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  84 LDAVVADGMLWTVTEWVAGVPLGDLLDR-RGAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGF 162
Cdd:cd06614  81 YDSYLVGDELWVVMEYMDGGSLTDIITQnFVRMNEPQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADF 160
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 163 GLAGatlapRLTA-----------PAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPFRD----RGRPEATLKGVDr 227
Cdd:cd06614 161 GFAA-----QLTKekskrnsvvgtPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPYLRepplRALFLITTKGIP- 234
                       170       180       190
                ....*....|....*....|....*....|
gi 32141327 228 lPLRTPVRAGPLAQA-VTGLLRKNSRERPT 256
Cdd:cd06614 235 -PLKNPEKWSPEFKDfLNKCLVKDPEKRPS 263
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; Serine/Threonine ...
93-227 1.66e-10

Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), Microtubule-associated serine/threonine (MAST) kinase subfamily, fungal Rim15-like kinases, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173702 [Multi-domain]  Cd Length: 260  Bit Score: 60.19  E-value: 1.66e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  93 LWTVTEWVAGVPLGDLLDRRGAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLAGATLAPR 172
Cdd:cd05611  72 LYLVMEYLNGGDCASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSRNGLENK 151
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 32141327 173 --LTAPAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPFrDRGRPEATLKGVDR 227
Cdd:cd05611 152 kfVGTPDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPF-HAETPDAVFDNILS 207
STKc_Sid2p_Dbf2p cd05600
Catalytic domain of Fungal Sid2p- and Dbf2p-like Protein Serine/Threonine Kinases; Serine ...
103-212 2.00e-10

Catalytic domain of Fungal Sid2p- and Dbf2p-like Protein Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), ROCK- and NDR-like subfamily, fungal Sid2p- and Dbf2p-like proteins, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Sid2p- and Dbf2p-like group is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173691 [Multi-domain]  Cd Length: 333  Bit Score: 60.88  E-value: 2.00e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 103 VPLGD---LLDRRGAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLAGATLA---PRLTAP 176
Cdd:cd05600  83 VPGGDfrtLLNNLGVLSEDHARFYMAEMFEAVDALHELGYIHRDLKPENFLIDASGHIKLTDFGLSKGIVTyanSVVGSP 162
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 32141327 177 AYASPEQARDERIGPAADLWTLGAILYTMVEGRPPF 212
Cdd:cd05600 163 DYMAPEVLRGKGYDFTVDYWSLGCMLYEFLCGFPPF 198
STKc_GRK4 cd05631
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; ...
115-215 2.23e-10

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; Serine/Threonine Kinases (STKs), G protein-coupled Receptor Kinase (GRK) subfamily, GRK4 isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. There are seven types of GRKs, named GRK1 to GRK7. 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. It 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.


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 60.39  E-value: 2.23e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 115 FGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLA-----GATLAPRLTAPAYASPEQARDERI 189
Cdd:cd05631  99 FDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAvqipeGETVRGRVGTVGYMAPEVINNEKY 178
                        90       100
                ....*....|....*....|....*.
gi 32141327 190 GPAADLWTLGAILYTMVEGRPPFRDR 215
Cdd:cd05631 179 TFSPDWWGLGCLIYEMIQGQSPFRKR 204
STKc_STK25-YSK1 cd06642
Catalytic domain of the Protein Serine/Threonine Kinase, STK25 or Yeast Sps1/Ste20-related ...
93-256 3.02e-10

Catalytic domain of the Protein Serine/Threonine Kinase, STK25 or Yeast Sps1/Ste20-related kinase 1; Serine/threonine kinases (STKs), STK25 subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The STK25 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. STK25 is also called Ste20/oxidant stress response kinase 1 (SOK1) or yeast Sps1/Ste20-related kinase 1 (YSK1). STK25 is localized in the Golgi apparatus through its interaction with the Golgi matrix protein GM130. It may play a role 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.


Pssm-ID: 132973 [Multi-domain]  Cd Length: 277  Bit Score: 60.06  E-value: 3.02e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  93 LWTVTEWVAGVPLGDLLdRRGAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLAGA---TL 169
Cdd:cd06642  77 LWIIMEYLGGGSALDLL-KPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQltdTQ 155
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 170 APRLT---APAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPFRDRgrpeATLKGVDRLPLRTP-----VRAGPLAQ 241
Cdd:cd06642 156 IKRNTfvgTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNSDL----HPMRVLFLIPKNSPptlegQYSKPFKE 231
                       170
                ....*....|....*
gi 32141327 242 AVTGLLRKNSRERPT 256
Cdd:cd06642 232 FVEACLNKDPRFRPT 246
STKc_aPKC_iota cd05618
Catalytic domain of the Protein Serine/Threonine Kinase, Atypical Protein Kinase C iota; ...
93-254 3.38e-10

Catalytic domain of the Protein Serine/Threonine Kinase, Atypical Protein Kinase C iota; Serine/Threonine Kinases (STKs), Atypical Protein Kinase C (aPKC) subfamily, iota isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. There are two aPKC isoforms, zeta and iota. 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.


Pssm-ID: 88519 [Multi-domain]  Cd Length: 329  Bit Score: 60.46  E-value: 3.38e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  93 LWTVTEWVAGVPLGDLLDRRGAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLAGATLAPR 172
Cdd:cd05618  71 LFFVIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPG 150
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 173 LTA------PAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPFRDRGRP------------EATLKGVDRLPLRTPV 234
Cdd:cd05618 151 DTTstfcgtPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDIVGSSdnpdqntedylfQVILEKQIRIPRSLSV 230
                       170       180
                ....*....|....*....|
gi 32141327 235 RAgplAQAVTGLLRKNSRER 254
Cdd:cd05618 231 KA---ASVLKSFLNKDPKER 247
STKc_MST3 cd06641
Catalytic domain of the Protein Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; ...
88-256 4.78e-10

Catalytic domain of the Protein Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; Serine/threonine kinases (STKs), mammalian Ste20-like protein kinase 3 (MST3) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MST3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 132972 [Multi-domain]  Cd Length: 277  Bit Score: 59.32  E-value: 4.78e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  88 VADGMLWTVTEWVAGVPLGDLLDRrGAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLAGA 167
Cdd:cd06641  72 LKDTKLWIIMEYLGGGSALDLLEP-GPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQ 150
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 168 TLAPRLT------APAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPFRDRgrpeATLKGVDRLPLRTPVR-----A 236
Cdd:cd06641 151 LTDTQIKrntfvgTPFWMAPEVIKQSAYDSKADIWSLGITAIELAKGEPPHSEL----HPMKVLFLIPKNNPPTlegnyS 226
                       170       180
                ....*....|....*....|
gi 32141327 237 GPLAQAVTGLLRKNSRERPT 256
Cdd:cd06641 227 KPLKEFVEACLNKEPSFRPT 246
STKc_MST4 cd06640
Catalytic domain of the Protein Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; ...
93-256 5.91e-10

Catalytic domain of the Protein Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; Serine/threonine kinases (STKs), mammalian Ste20-like protein kinase 4 (MST4) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MST4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 58.91  E-value: 5.91e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  93 LWTVTEWVAGVPLGDLLdRRGAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLAGA---TL 169
Cdd:cd06640  77 LWIIMEYLGGGSALDLL-RAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQltdTQ 155
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 170 APRLT---APAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPFRDRgRPEATLKGVDRLPlrTPVRAGPLAQA---- 242
Cdd:cd06640 156 IKRNTfvgTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPPNSDM-HPMRVLFLIPKNN--PPTLTGEFSKPfkef 232
                       170
                ....*....|....
gi 32141327 243 VTGLLRKNSRERPT 256
Cdd:cd06640 233 IDACLNKDPSFRPT 246
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Protein Serine/Threonine Kinases; Serine/Threonine ...
96-254 9.14e-10

Catalytic domain of Phototropin-like Protein Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), Phototropin-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The phototropin-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. Included in this subfamily are plant phototropins and predominantly uncharacterized fungal STKs whose catalytic domains resemble the phototropin kinase domain. One protein from Neurospora crassa is called nrc-2. 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. Neurospora crassa nrc-2 plays a role in growth and development by controlling entry into the conidiation program.


Pssm-ID: 173665 [Multi-domain]  Cd Length: 316  Bit Score: 58.83  E-value: 9.14e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  96 VTEWVAGVPLGDLLDRR-GAFGCARAARVGL-ELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLA-GATLAPR 172
Cdd:cd05574  79 VMDYCPGGELFRLLQRQpGKCLSEEVARFYAaEVLLALEYLHLLGIVYRDLKPENILLHESGHIMLSDFDLSkQSDVEPP 158
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 173 LTAPAYASPEQAR------------------------DERIGP----------AADLWTLGAILYTMVEGRPPFRDRGRp 218
Cdd:cd05574 159 PVSKALRKGSRRSsvnsipsetfseepsfrsnsfvgtEEYIAPevisgdghgsAVDWWTLGILLYEMLYGTTPFKGSNR- 237
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 32141327 219 EATLKGVDRLPLRTPVRAGPLAQA---VTGLLRKNSRER 254
Cdd:cd05574 238 DETFSNILKKEVTFPGSPPVSSSArdlIRKLLVKDPSKR 276
STKc_Nek cd08215
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
125-256 9.21e-10

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related kinase; Serine/Threonine Kinases (STKs), Never In Mitosis gene A (NIMA)-related kinase (Nek) family, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek 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. 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.


Pssm-ID: 173755 [Multi-domain]  Cd Length: 258  Bit Score: 57.89  E-value: 9.21e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 125 LELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLA---GATLAPRLTA---PAYASPEQARDERIGPAADLWTL 198
Cdd:cd08215 110 VQLCLALKYLHSRKILHRDIKPQNIFLTSNGLVKLGDFGISkvlSSTVDLAKTVvgtPYYLSPELCQNKPYNYKSDIWSL 189
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32141327 199 GAILYTMVEGRPPFRDRGRPE---ATLKG-VDRLPLRTPVRagpLAQAVTGLLRKNSRERPT 256
Cdd:cd08215 190 GCVLYELCTLKHPFEGENLLElalKILKGqYPPIPSQYSSE---LRNLVSSLLQKDPEERPS 248
STKc_Yank1 cd05578
Catalytic domain of the Protein Serine/Threonine Kinase, Yank1; Serine/Threonine Kinases (STKs) ...
93-217 1.01e-09

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


Pssm-ID: 173669 [Multi-domain]  Cd Length: 258  Bit Score: 58.10  E-value: 1.01e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  93 LWTVTEWVAGvplGDL---LDRRGAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLA---- 165
Cdd:cd05578  75 MYLVVDLLLG---GDLryhLSQKVKFSEEQVKFWICEIVLALEYLHSKGIIHRDIKPDNILLDEQGHVHITDFNIAtkvt 151
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 32141327 166 -GATLAPRLTAPAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPFRDRGR 217
Cdd:cd05578 152 pDTLTTSTSGTPGYMAPEVLCRQGYSVAVDWWSLGVTAYECLRGKRPYRGHSR 204
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Protein Serine/Threonine Kinase, Mitogen and ...
86-254 1.56e-09

N-terminal catalytic domain of the Protein Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; Serine/Threonine Kinases (STKs), Mitogen and stress-activated kinase (MSK) subfamily, MSK2, N-terminal catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. 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.


Pssm-ID: 173705 [Multi-domain]  Cd Length: 332  Bit Score: 58.42  E-value: 1.56e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  86 AVVADGMLWTVTEWVAGVPLGDLLDRRGAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLA 165
Cdd:cd05614  73 AFQTEAKLHLILDYVSGGEMFTHLYQRDNFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLS 152
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 166 GATLAPR-------LTAPAYASPEQARDER-IGPAADLWTLGAILYTMVEGRPPFRDRGRpEATLKGVDRLPLRT----P 233
Cdd:cd05614 153 KEFLSEEkertysfCGTIEYMAPEIIRGKGgHGKAVDWWSLGILIFELLTGASPFTLEGE-RNTQSEVSRRILKCdppfP 231
                       170       180
                ....*....|....*....|..
gi 32141327 234 VRAGPLAQ-AVTGLLRKNSRER 254
Cdd:cd05614 232 SFIGPEAQdLLHKLLRKDPKKR 253
STKc_aPKC cd05588
Catalytic domain of the Protein Serine/Threonine Kinase, Atypical Protein Kinase C; Serine ...
93-254 1.83e-09

Catalytic domain of the Protein Serine/Threonine Kinase, Atypical Protein Kinase C; Serine/Threonine Kinases (STKs), Atypical Protein Kinase C (aPKC) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. 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.


Pssm-ID: 173679 [Multi-domain]  Cd Length: 329  Bit Score: 57.91  E-value: 1.83e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  93 LWTVTEWVAGvplGDLL---DRRGAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLAGATL 169
Cdd:cd05588  71 LFFVIEFVSG---GDLMfhmQRQRKLPEEHARFYSAEISLALNFLHERGIIYRDLKLDNVLLDAEGHIKLTDYGMCKEGI 147
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 170 APRLTA------PAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPFR---DRGRPEAT---------LKGVDRLPLR 231
Cdd:cd05588 148 RPGDTTstfcgtPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDivgMSDNPDQNtedylfqviLEKQIRIPRS 227
                       170       180
                ....*....|....*....|...
gi 32141327 232 TPVRAgplAQAVTGLLRKNSRER 254
Cdd:cd05588 228 LSVKA---SSVLKGFLNKDPKER 247
STKc_PKA cd05580
Catalytic domain of the Protein Serine/Threonine Kinase, cAMP-dependent protein kinase; Serine ...
93-215 1.98e-09

Catalytic domain of the Protein Serine/Threonine Kinase, cAMP-dependent protein kinase; Serine/Threonine Kinases (STKs), cAMP-dependent protein kinase (PKA) subfamily, catalytic (c) subunit. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKA subfamily is part of a 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). This subfamily is composed of the cAMP-dependent proteins kinases, PKA and PRKX. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic (C) 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 C 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.


Pssm-ID: 173671 [Multi-domain]  Cd Length: 290  Bit Score: 57.56  E-value: 1.98e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  93 LWTVTEWVAGVPLGDLLDRRGAFG--CAR--AARVgleLLAvLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLAgAT 168
Cdd:cd05580  76 LYLVMEYVPGGELFSHLRKSGRFPepVARfyAAQV---VLA-LEYLHSLDIVYRDLKPENLLLDSDGYIKITDFGFA-KR 150
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 32141327 169 LAPRlT-----APAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPFRDR 215
Cdd:cd05580 151 VKGR-TytlcgTPEYLAPEIILSKGYGKAVDWWALGILIYEMLAGYPPFFDD 201
STKc_PAK4 cd06657
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 4; Serine ...
93-256 2.07e-09

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 4; Serine/threonine kinases (STKs), p21-activated kinase (PAK) 4, 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. PAK4 belongs to group II. Group II PAKs contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. 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.


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 57.73  E-value: 2.07e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  93 LWTVTEWVAGVPLGDLLDRRgAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLAG--ATLA 170
Cdd:cd06657  92 LWVVMEFLEGGALTDIVTHT-RMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAqvSKEV 170
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 171 PR----LTAPAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPFRDRGRPEATLKGVDRLP--LRTPVRAGPLAQA-V 243
Cdd:cd06657 171 PRrkslVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPpkLKNLHKVSPSLKGfL 250
                       170
                ....*....|...
gi 32141327 244 TGLLRKNSRERPT 256
Cdd:cd06657 251 DRLLVRDPAQRAT 263
STKc_PAK5 cd06658
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 5; Serine ...
93-231 2.34e-09

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 5; Serine/threonine kinases (STKs), p21-activated kinase (PAK) 5, 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. PAK5 belongs to group II. Group II PAKs contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. 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.


Pssm-ID: 132989 [Multi-domain]  Cd Length: 292  Bit Score: 57.36  E-value: 2.34e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  93 LWTVTEWVAGVPLGDLLDRRgAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLAG--ATLA 170
Cdd:cd06658  94 LWVVMEFLEGGALTDIVTHT-RMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAqvSKEV 172
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32141327 171 PR----LTAPAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPFRDRGRPEATLKGVDRLPLR 231
Cdd:cd06658 173 PKrkslVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIRDNLPPR 237
STKc_GRK1 cd05608
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; ...
119-254 2.88e-09

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; Serine/Threonine Kinases (STKs), G protein-coupled Receptor Kinase (GRK) subfamily, GRK1 isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. There are seven types of GRKs, named GRK1 to GRK7. 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.


Pssm-ID: 173699 [Multi-domain]  Cd Length: 280  Bit Score: 56.78  E-value: 2.88e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 119 RAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLAGATLAPRLTAPAYA------SPEQARDERIGPA 192
Cdd:cd05608  98 RACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDNDGNVRISDLGLAVELKDGQSKTKGYAgtpgfmAPELLQGEEYDFS 177
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32141327 193 ADLWTLGAILYTMVEGRPPFRDRGRPEATLKGVDRL---PLRTPVRAGPLAQAV-TGLLRKNSRER 254
Cdd:cd05608 178 VDYFALGVTLYEMIAARGPFRARGEKVENKELKQRIlndSVTYPDKFSPASKSFcEALLAKDPEKR 243
STKc_cPKC cd05587
Catalytic domain of the Protein Serine/Threonine Kinase, Classical Protein Kinase C; Serine ...
93-212 3.00e-09

Catalytic domain of the Protein Serine/Threonine Kinase, Classical Protein Kinase C; Serine/Threonine Kinases (STKs), Classical (or Conventional) Protein Kinase C (cPKC) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The cPKC subfamily is part of a 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). 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. cPKCs contain a calcium-binding C2 region in their regulatory domain. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. cPKCs are potent kinases for histones, myelin basic protein, and protamine. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia.


Pssm-ID: 173678 [Multi-domain]  Cd Length: 324  Bit Score: 57.48  E-value: 3.00e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  93 LWTVTEWVAGvplGDLL---DRRGAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLAGATL 169
Cdd:cd05587  76 LYFVMEYVNG---GDLMyhiQQVGKFKEPHAVFYAAEIAIGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCKENI 152
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 32141327 170 APRLTA------PAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPF 212
Cdd:cd05587 153 FGGKTTrtfcgtPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQPPF 201
STKc_Nek6_Nek7 cd08224
Catalytic domain of the Protein Serine/Threonine Kinases, Never In Mitosis gene A-related ...
84-212 3.21e-09

Catalytic domain of the Protein Serine/Threonine Kinases, Never In Mitosis gene A-related kinase 6 and 7; Serine/Threonine Kinases (STKs), Never In Mitosis gene A (NIMA)-related kinase 6 (Nek6) and Nek7 subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek6/7 subfamily 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 protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173764 [Multi-domain]  Cd Length: 267  Bit Score: 56.67  E-value: 3.21e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  84 LDAVVADGMLWTVTEWVagvPLGDL-------------LDRRGAFgcaraaRVGLELLAVLEAAHTHGVTHGELSPGQVF 150
Cdd:cd08224  68 LASFIENNELNIVLELA---DAGDLsrmikhfkkqkrlIPERTIW------KYFVQLCSALEHMHSKRIMHRDIKPANVF 138
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32141327 151 VREEGSVLVTGFGLaGATLAPRLTA-------PAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPF 212
Cdd:cd08224 139 ITATGVVKLGDLGL-GRFFSSKTTAahslvgtPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPF 206
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, MAP/ERK kinase kinase 1; Serine ...
30-212 3.79e-09

Catalytic domain of the Protein Serine/Threonine Kinase, MAP/ERK kinase kinase 1; Serine/threonine kinases (STKs), MAP/ERK kinase kinase 1 (MEKK1) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. MEKK1 is a mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK or MKKK or MAP3K), that 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. MEKK1 activates the extracellular signal-regulated kinase 1/2 (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.


Pssm-ID: 132961 [Multi-domain]  Cd Length: 268  Bit Score: 56.41  E-value: 3.79e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  30 CWSGEDATTGRPCLVTRIELPEGRAGEAARRAPGrVIRTGETMASLCPGRIAPVLDAVVADGMLWTVTEWVAGVPLGDLL 109
Cdd:cd06630  16 CYQARDVKTGTLMAVKQVTYVRNTSSEQEEVVEA-LRKEIRLMARLNHPHIIRMLGATCEDSHFNLFVEWMAGGSVSHLL 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 110 DRRGAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVL-VTGFGlAGATLAPRLTAP-----------A 177
Cdd:cd06630  95 SKYGAFKEAVIINYTEQLLRGLSYLHENQIIHRDVKGANLLIDSTGQRLrIADFG-AAARLAAKGTGAgefqgqllgtiA 173
                       170       180       190
                ....*....|....*....|....*....|....*
gi 32141327 178 YASPEQARDERIGPAADLWTLGAILYTMVEGRPPF 212
Cdd:cd06630 174 FMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPW 208
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Protein Serine ...
93-254 4.16e-09

Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Protein Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), Fission yeast Suppressor of loss of cAMP-dependent protein kinase (Sck1)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Sck1-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. This subfamily is composed of fungal proteins with similarity to the Schizosaccharomyces pombe STK Sck1. 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.


Pssm-ID: 173677 [Multi-domain]  Cd Length: 330  Bit Score: 56.87  E-value: 4.16e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  93 LWTVTEWVAGVPLGDLLDRRGAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLAGATLAPR 172
Cdd:cd05586  71 LYLVTDYMSGGELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKYDIVYRDLKPENILLDATGHIALCDFGLSKANLTDN 150
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 173 LT------APAYASPEQARDER-IGPAADLWTLGAILYTMVEGRPPFRDRGRPEATLK---GVDRLPLRTPVRAGplAQA 242
Cdd:cd05586 151 KTtntfcgTTEYLAPEVLLDEKgYTKHVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNiafGKVRFPKNVLSDEG--RQF 228
                       170
                ....*....|..
gi 32141327 243 VTGLLRKNSRER 254
Cdd:cd05586 229 VKGLLNRNPQHR 240
STKc_cPKC_alpha cd05615
Catalytic domain of the Protein Serine/Threonine Kinase, Classical Protein Kinase C alpha; ...
93-212 5.19e-09

Catalytic domain of the Protein Serine/Threonine Kinase, Classical Protein Kinase C alpha; Serine/Threonine Kinases (STKs), Classical Protein Kinase C (cPKC) subfamily, alpha isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The cPKC subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. 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.


Pssm-ID: 173706 [Multi-domain]  Cd Length: 323  Bit Score: 56.54  E-value: 5.19e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  93 LWTVTEWVAGvplGDLL---DRRGAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLAGATL 169
Cdd:cd05615  76 LYFVMEYVNG---GDLMyhiQQVGKFKEPQAVFYAAEISVGLFFLHRRGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHM 152
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 32141327 170 APRLTA------PAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPF 212
Cdd:cd05615 153 VDGVTTrtfcgtPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPF 201
STKc_FA2-like cd08529
Catalytic domain of the Protein Serine/Threonine Kinase, Chlamydomonas reinhardtii FA2 and ...
57-255 6.46e-09

Catalytic domain of the Protein Serine/Threonine Kinase, Chlamydomonas reinhardtii FA2 and similar domains; Serine/Threonine Kinases (STKs), Chlamydomonas reinhardtii FA2-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Chlamydomonas reinhardtii FA2-like subfamily belongs to the (NIMA)-related kinase (Nek) family. The Nek family includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily includes FA2 and CNK4. The Nek 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. 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.


Pssm-ID: 173771 [Multi-domain]  Cd Length: 256  Bit Score: 55.59  E-value: 6.46e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  57 AARRAPGRVIRTGETMASLCPGRIAPVLDAVVADGMLWTVTEWVAGvplGDLLDRRGAFGCARAA-----RVGLELLAVL 131
Cdd:cd08529  38 MNRREREEAIDEARVLAKLDSSYIIRYYESFLDKGKLNIVMEYAEN---GDLHKLLKMQRGRPLPedqvwRFFIQILLGL 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 132 EAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLAGATLAPRLTA------PAYASPEQARDERIGPAADLWTLGAILYTM 205
Cdd:cd08529 115 AHLHSKKILHRDIKSLNLFLDAYDNVKIGDLGVAKLLSDNTNFAntivgtPYYLSPELCEDKPYNEKSDVWALGVVLYEC 194
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 32141327 206 VEGRPPFRDRGRPEATLK---GVDRlPLRTPVRAGpLAQAVTGLLRKNSRERP 255
Cdd:cd08529 195 CTGKHPFDANNQGALILKiirGVFP-PVSQMYSQQ-LAQLIDQCLTKDYRQRP 245
STKc_cPKC_beta cd05616
Catalytic domain of the Protein Serine/Threonine Kinase, Classical Protein Kinase C beta; ...
93-212 7.66e-09

Catalytic domain of the Protein Serine/Threonine Kinase, Classical Protein Kinase C beta; Serine/Threonine Kinases (STKs), Classical Protein Kinase C (cPKC) subfamily, beta isoforms, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The cPKC subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG 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.


Pssm-ID: 173707 [Multi-domain]  Cd Length: 323  Bit Score: 56.16  E-value: 7.66e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  93 LWTVTEWVAGvplGDLL---DRRGAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLA---- 165
Cdd:cd05616  76 LYFVMEYVNG---GDLMyqiQQVGRFKEPHAVFYAAEIAIGLFFLHSKGIIYRDLKLDNVMLDSEGHIKIADFGMCkenm 152
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 32141327 166 --GATLAPRLTAPAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPF 212
Cdd:cd05616 153 wdGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPF 201
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; Serine/Threonine Kinases ...
46-223 8.29e-09

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; Serine/Threonine Kinases (STKs), PCTAIRE-3 subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PCTAIRE-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. 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. 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 (NFTs). In human glioma cells, PCTAIRE-3 induces cell cycle arrest and cell death.


Pssm-ID: 143376 [Multi-domain]  Cd Length: 288  Bit Score: 55.80  E-value: 8.29e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  46 RIELPEGrageaarrAPGRVIRTGETMASLCPGRIAPVLDAVVADGMLWTVTEWVAGvPLGDLLDRRGAFGCARAARVGL 125
Cdd:cd07871  39 RLEHEEG--------APCTAIREVSLLKNLKHANIVTLHDIIHTERCLTLVFEYLDS-DLKQYLDNCGNLMSMHNVKIFM 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 126 -ELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLAGATLAPRLTAPA------YASPE--QARDERIGPAaDLW 196
Cdd:cd07871 110 fQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLARAKSVPTKTYSNevvtlwYRPPDvlLGSTEYSTPI-DMW 188
                       170       180
                ....*....|....*....|....*..
gi 32141327 197 TLGAILYTMVEGRPPFrdrgrPEATLK 223
Cdd:cd07871 189 GVGCILYEMATGRPMF-----PGSTVK 210
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; Protein Tyrosine ...
72-225 9.17e-09

Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; Protein Tyrosine Kinase (PTK) family; C-terminal Src kinase (Csk); 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. The Csk subfamily kinases are cytoplasmic (or nonreceptor) tyr kinases 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 is 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. 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. 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.


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 54.99  E-value: 9.17e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  72 MASLCPGRIAPVLDAVVAD-GMLWTVTEWVAGVPLGDLLDRRG--AFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQ 148
Cdd:cd05082  53 MTQLRHSNLVQLLGVIVEEkGGLYIVTEYMAKGSLVDYLRSRGrsVLGGDCLLKFSLDVCEAMEYLEANNFVHRDLAARN 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 149 VFVREEGSVLVTGFGLAGATLAPRLTAP---AYASPEQARDERIGPAADLWTLGAILYTMVE-GRPPFrdrgrPEATLKG 224
Cdd:cd05082 133 VLVSEDNVAKVSDFGLTKEASSTQDTGKlpvKWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPY-----PRIPLKD 207

                .
gi 32141327 225 V 225
Cdd:cd05082 208 V 208
STKc_nPKC_theta_delta cd05592
Catalytic domain of the Protein Serine/Threonine Kinases, Novel Protein Kinase C theta and ...
93-219 1.27e-08

Catalytic domain of the Protein Serine/Threonine Kinases, Novel Protein Kinase C theta and delta; Serine/Threonine Kinases (STKs), Novel Protein Kinase C (nPKC), theta and delta-like isoforms, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The nPKC subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. 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.


Pssm-ID: 173683 [Multi-domain]  Cd Length: 316  Bit Score: 55.18  E-value: 1.27e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  93 LWTVTEWVAGvplGDLL---DRRGAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLAGATL 169
Cdd:cd05592  71 LFFVMEYLNG---GDLMfhiQSSGRFDEARARFYAAEIICGLQFLHKKGIIYRDLKLDNVLLDKDGHIKIADFGMCKENM 147
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 32141327 170 APRLTA------PAYASPEQARDERIGPAADLWTLGAILYTMVEGRPPFRDRGRPE 219
Cdd:cd05592 148 NGEGKAstfcgtPDYIAPEILKGQKYNESVDWWSFGVLLYEMLIGQSPFHGEDEDE 203
STKc_Nek6 cd08228
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
125-212 2.14e-08

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related kinase 6; Serine/Threonine Kinases (STKs), Never In Mitosis gene A (NIMA)-related kinase 6 (Nek6) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek6 subfamily is one 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 protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173768 [Multi-domain]  Cd Length: 267  Bit Score: 54.26  E-value: 2.14e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 125 LELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLaGATLAPRLTA-------PAYASPEQARDERIGPAADLWT 197
Cdd:cd08228 113 VQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGL-GRFFSSKTTAahslvgtPYYMSPERIHENGYNFKSDIWS 191
                        90
                ....*....|....*
gi 32141327 198 LGAILYTMVEGRPPF 212
Cdd:cd08228 192 LGCLLYEMAALQSPF 206
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, MAP/ERK kinase kinase 4; Serine ...
125-212 2.45e-08

Catalytic domain of the Protein Serine/Threonine Kinase, MAP/ERK kinase kinase 4; Serine/threonine kinases (STKs), MAP/ERK kinase kinase 4 (MEKK4) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MEKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. MEKK4 is a mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK or MKKK or MAP3K), that 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. MEKK4 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.


Pssm-ID: 132957 [Multi-domain]  Cd Length: 264  Bit Score: 53.88  E-value: 2.45e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 125 LELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLA-----GATLAPRLTA-----PAYASPE-QARDERIGP-- 191
Cdd:cd06626 106 LQLLEGLAYLHSHGIVHRDIKPANIFLDHNGVIKLGDFGCAvklknNTTTMGEEVQslagtPAYMAPEvITGGKGKGHgr 185
                        90       100
                ....*....|....*....|.
gi 32141327 192 AADLWTLGAILYTMVEGRPPF 212
Cdd:cd06626 186 AADIWSLGCVVLEMATGKRPW 206
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Protein Serine/Threonine Kinases; Serine/threonine ...
93-235 2.49e-08

Catalytic domain of Fungal Nak1-like Protein Serine/Threonine Kinases; Serine/threonine kinases (STKs), Nak1 subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nak1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This subfamily is composed of Schizosaccharomyces pombe Nak1, Saccharomyces cerevisiae Kic1p (kinase that interacts with Cdc31p) and related proteins. Nak1 (also known as 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.


Pssm-ID: 132991 [Multi-domain]  Cd Length: 277  Bit Score: 53.98  E-value: 2.49e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  93 LWTVTEWVAGVPLGDLLdRRGAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLAgATLA-- 170
Cdd:cd06917  77 LWIIMEYAEGGSVRTLM-KAGPIAEKYISVIIREVLVALKYIHKVGVIHRDIKAANILVTNTGNVKLCDFGVA-ALLNqn 154
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32141327 171 --PRLT---APAYASPEQARDERIGPA-ADLWTLGAILYTMVEGRPPFRDrgrpEATLKGVDRLPLRTPVR 235
Cdd:cd06917 155 ssKRSTfvgTPYWMAPEVITEGKYYDTkADIWSLGITIYEMATGNPPYSD----VDAFRAMMLIPKSKPPR 221
STKc_MAPKKK_Byr2_like cd06628
Catalytic domain of fungal Byr2-like MAP Kinase Kinase Kinases; Serine/threonine kinases (STKs) ...
33-223 2.49e-08

Catalytic domain of fungal Byr2-like MAP Kinase Kinase Kinases; Serine/threonine kinases (STKs), mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK) subfamily, fungal Byr2-like proteins, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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 (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. 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.


Pssm-ID: 173732 [Multi-domain]  Cd Length: 267  Bit Score: 54.08  E-value: 2.49e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327  33 GEDATTGRPCLVTRIELPEGRAGEAARRAP--GRVIRTGETMASLCPGRIAPVLDAVVADGMLWTVTEWVAGVPLGDLLD 110
Cdd:cd06628  19 GMNASSGELMAVKQVELPSVSASSKDRKRSmlDALAREIALLKELQHENIVQYLGSSLDADHLNIFLEYVPGGSVAALLN 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32141327 111 RRGAFGCARAARVGLELLAVLEAAHTHGVTHGELSPGQVFVREEGSVLVTGFGLAGATLA-----------PRLTAPAY- 178
Cdd:cd06628  99 NYGAFEETLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISKKLEAnslstktngarPSLQGSVFw 178
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 32141327 179 ASPEQARDERIGPAADLWTLGAILYTMVEGRPPFRDRGRPEATLK