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Conserved domains on  [gi|125848675|ref|XP_689783|]
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PREDICTED: G protein-coupled receptor kinase 6 [Danio rerio]

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
185-469 0e+00

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


:

Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 603.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 185 TFRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGESMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLT 264
Cdd:cd05630    1 TFRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 265 LMNGGDLKFHIYHMGEAGFDEKRAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVPEGQTIKG 344
Cdd:cd05630   81 LMNGGDLKFHIYHMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVPEGQTIKG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 345 RVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIEGQSPFQQRKKKIKREEVERLVKEVEEEYSSKFSEDAKSLCKMLL 424
Cdd:cd05630  161 RVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKREEVERLVKEVPEEYSEKFSPQARSLCSMLL 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 125848675 425 AKDPSERLGCQGGGASEVKAHLIFRSINFKRLAAGMLEAPFIPDP 469
Cdd:cd05630  241 CKDPAERLGCRGGGAREVKEHPLFKKLNFKRLGAGMLEPPFKPDP 285
RGS_GRK6 cd08751
Regulator of G protein signaling domain (RGS) found in G protein-coupled receptor kinase 6 ...
35-179 2.94e-104

Regulator of G protein signaling domain (RGS) found in G protein-coupled receptor kinase 6 (GRK6); The RGS domain is an essential part of the GRK6 (G protein-coupled receptor kinase 6) protein which plays an important role in the regulating of dopamine, opioids, M3 muscarinic, and chemokine receptor signaling. GRK6 is a member of the GRK kinase family which includes three major subfamilies: the GRK4 subfamily (GRK4, GRK5 and GRK6), the rhodopsin kinase or visual GRK subfamily (GRK1 and GRK7), and the beta-adrenergic receptor kinases subfamily (GRK2/GRK3). The RGS domain of the GRKs has very little sequence similarity with the canonical RGS domain of the RGS proteins and therefore is often refered to as the RH (RGS Homology) domain. The RH domain of GRK6 does not have structural determinants that are required for binding G-alpha subunit, in contrast to GRK2 and many other RGS proteins. GRK6 is an important target for treatment of addiction and Parkinson disease. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development.


:

Pssm-ID: 188705  Cd Length: 145  Bit Score: 313.06  E-value: 2.94e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675  35 QFPHISLCEELRQTIEKDYNSLCERQPIGRLLFRQFCDTRPELRRCVRFLDAVAEYEVTPDEKRKECGQELLDKYLNTKS 114
Cdd:cd08751    1 QFPHISLCEELRQSLERDYHSLCERQPIGRLLFRQFCATRPELSRCVAFLDAVAEYEVTPDEKRKECGQNLTQKYLSHKS 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 125848675 115 EDYIPEVTEEMVTKCADRLQQEACKELFMECTKLIHDYLSVAPFADYLDSMYYSRFLQWKWLERQ 179
Cdd:cd08751   81 EDYIPEVPRQLVTNCTQRLEQEPCKELFQELTKLIHDYLSVAPFADYLDSIYFNRFLQWKWLERQ 145
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
186-445 2.58e-82

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


:

Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 260.15  E-value: 2.58e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675   186 FRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRkgESMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTL 265
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKD--RERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675   266 MNGGDLKFHIYHMGeaGFDEKRAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVPEGQTIKGR 345
Cdd:smart00220  79 CEGGDLFDLLKKRG--RLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKLTTF 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675   346 VGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIEGQSPFQQRKKKIKREEVERLVKEVEEEYSSKFSEDAKSLCKMLLA 425
Cdd:smart00220 157 VGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDLIRKLLV 236
                          250       260
                   ....*....|....*....|
gi 125848675   426 KDPSERLgcqggGASEVKAH 445
Cdd:smart00220 237 KDPEKRL-----TAEEALQH 251
 
Name Accession Description Interval E-value
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
185-469 0e+00

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


Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 603.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 185 TFRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGESMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLT 264
Cdd:cd05630    1 TFRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 265 LMNGGDLKFHIYHMGEAGFDEKRAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVPEGQTIKG 344
Cdd:cd05630   81 LMNGGDLKFHIYHMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVPEGQTIKG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 345 RVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIEGQSPFQQRKKKIKREEVERLVKEVEEEYSSKFSEDAKSLCKMLL 424
Cdd:cd05630  161 RVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKREEVERLVKEVPEEYSEKFSPQARSLCSMLL 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 125848675 425 AKDPSERLGCQGGGASEVKAHLIFRSINFKRLAAGMLEAPFIPDP 469
Cdd:cd05630  241 CKDPAERLGCRGGGAREVKEHPLFKKLNFKRLGAGMLEPPFKPDP 285
RGS_GRK6 cd08751
Regulator of G protein signaling domain (RGS) found in G protein-coupled receptor kinase 6 ...
35-179 2.94e-104

Regulator of G protein signaling domain (RGS) found in G protein-coupled receptor kinase 6 (GRK6); The RGS domain is an essential part of the GRK6 (G protein-coupled receptor kinase 6) protein which plays an important role in the regulating of dopamine, opioids, M3 muscarinic, and chemokine receptor signaling. GRK6 is a member of the GRK kinase family which includes three major subfamilies: the GRK4 subfamily (GRK4, GRK5 and GRK6), the rhodopsin kinase or visual GRK subfamily (GRK1 and GRK7), and the beta-adrenergic receptor kinases subfamily (GRK2/GRK3). The RGS domain of the GRKs has very little sequence similarity with the canonical RGS domain of the RGS proteins and therefore is often refered to as the RH (RGS Homology) domain. The RH domain of GRK6 does not have structural determinants that are required for binding G-alpha subunit, in contrast to GRK2 and many other RGS proteins. GRK6 is an important target for treatment of addiction and Parkinson disease. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development.


Pssm-ID: 188705  Cd Length: 145  Bit Score: 313.06  E-value: 2.94e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675  35 QFPHISLCEELRQTIEKDYNSLCERQPIGRLLFRQFCDTRPELRRCVRFLDAVAEYEVTPDEKRKECGQELLDKYLNTKS 114
Cdd:cd08751    1 QFPHISLCEELRQSLERDYHSLCERQPIGRLLFRQFCATRPELSRCVAFLDAVAEYEVTPDEKRKECGQNLTQKYLSHKS 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 125848675 115 EDYIPEVTEEMVTKCADRLQQEACKELFMECTKLIHDYLSVAPFADYLDSMYYSRFLQWKWLERQ 179
Cdd:cd08751   81 EDYIPEVPRQLVTNCTQRLEQEPCKELFQELTKLIHDYLSVAPFADYLDSIYFNRFLQWKWLERQ 145
RGS smart00315
Regulator of G protein signalling domain; RGS family members are GTPase-activating proteins ...
52-170 3.84e-25

Regulator of G protein signalling domain; RGS family members are GTPase-activating proteins for heterotrimeric G-protein alpha-subunits.


Pssm-ID: 214613  Cd Length: 118  Bit Score: 100.81  E-value: 3.84e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675    52 DYNSLCeRQPIGRLLFRQFCDTRPELRrCVRFLDAVAEYEVTPD-EKRKECGQELLDKYLNTKSEDyIPEVTEEMVTKCA 130
Cdd:smart00315   1 SLESLL-SDPIGRLLFREFLESEFSEE-NLEFWLAVEEFKKAEDdEERIAKAREIYDKFLSPNAPK-EVNLDSDLREKIE 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 125848675   131 DRL-QQEACKELFMECTKLIHDYLSVAPFADYLDSMYYSRF 170
Cdd:smart00315  78 ENLeSEEPPPDLFDEAQREVYELLEKDSFPRFLESDYYLRF 118
RGS pfam00615
Regulator of G protein signaling domain; RGS family members are GTPase-activating proteins for ...
52-170 5.07e-22

Regulator of G protein signaling domain; RGS family members are GTPase-activating proteins for heterotrimeric G-protein alpha-subunits.


Pssm-ID: 249998  Cd Length: 117  Bit Score: 91.90  E-value: 5.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675   52 DYNSLCERQPiGRLLFRQFCDTR-PElrRCVRFLDAVAEYEVT-PDEKRKECGQELLDKYLNTKSEDYIpEVTEEMVTKC 129
Cdd:pfam00615   1 SFESLLSDQP-GRRLFREFLESEfSE--ENLEFWLACEEFKKAkSDEERLKKAREIYNKFLAPDSPSEI-NLDSATREKI 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 125848675  130 ADRLQQEACKELFMECTKLIHDYLSVAPFADYLDSMYYSRF 170
Cdd:pfam00615  77 EENLEKEPSPDLFDEAQEEVYDLLEKDSYPRFLKSPLYLRL 117
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
186-445 2.58e-82

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 260.15  E-value: 2.58e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675   186 FRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRkgESMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTL 265
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKD--RERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675   266 MNGGDLKFHIYHMGeaGFDEKRAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVPEGQTIKGR 345
Cdd:smart00220  79 CEGGDLFDLLKKRG--RLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKLTTF 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675   346 VGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIEGQSPFQQRKKKIKREEVERLVKEVEEEYSSKFSEDAKSLCKMLLA 425
Cdd:smart00220 157 VGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDLIRKLLV 236
                          250       260
                   ....*....|....*....|
gi 125848675   426 KDPSERLgcqggGASEVKAH 445
Cdd:smart00220 237 KDPEKRL-----TAEEALQH 251
Pkinase pfam00069
Protein kinase domain;
186-448 4.12e-67

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 220.58  E-value: 4.12e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675  186 FRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGESmALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTL 265
Cdd:pfam00069   1 YELLRKLGSGSFGTVYKAKHKGTGKIVAVKILKKRSEKSKKDQT-ARREIRILRRLSHPNIVRLIDAFEDKDHLYLVMEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675  266 MNGGDLKFHIYHMGeaGFDEKRAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVPEGQTI-KG 344
Cdd:pfam00069  80 CEGGDLFDYLSRGG--PLSEDEAKKIALQILRGLEYLHSNGIIHRDLKPENILLDENGVVKIADFGLAKKLTKSSSSlTT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675  345 RVGTVGYMAPEVVK-NERYTFSPDWWALGCLLYEMIEGQSPFQQRKKKIKREEVERLVK---EVEEEYSSKFSEDAKSLC 420
Cdd:pfam00069 158 FVGTPEYMAPEVLLgGNGYGPKVDVWSLGVILYELLTGKPPFSGESILDQLQLIRRILGpplEFDEPKSDSGSEEAKDLI 237
                         250       260
                  ....*....|....*....|....*...
gi 125848675  421 KMLLAKDPSERLgcqggGASEVKAHLIF 448
Cdd:pfam00069 238 KKCLNKDPSKRP-----TAEEILQHPWF 260
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
192-467 1.72e-49

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 175.39  E-value: 1.72e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 192 LGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGESMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTLMNGGDL 271
Cdd:PTZ00263  26 LGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFLLEFVVGGEL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 272 KFHIYHMGEagFDEKRAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVPEgQTIKgRVGTVGY 351
Cdd:PTZ00263 106 FTHLRKAGR--FPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVPD-RTFT-LCGTPEY 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 352 MAPEVVKNERYTFSPDWWALGCLLYEMIEGQSPF-QQRKKKIKREEVERLVKeveeeYSSKFSEDAKSLCKMLLAKDPSE 430
Cdd:PTZ00263 182 LAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFfDDTPFRIYEKILAGRLK-----FPNWFDGRARDLVKGLLQTDHTK 256
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 125848675 431 RLGCQGGGASEVKAHLIFRSINFKRLAAGMLEAPfIP 467
Cdd:PTZ00263 257 RLGTLKGGVADVKNHPYFHGANWDKLYARYYPAP-IP 292
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
186-457 1.06e-44

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: 163.37  E-value: 1.06e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 186 FRQYRVLGKGGFGEVCACQVRatgKMYACKKLEKKRIKKRKGESMALNEKQILEKVNS-RFVVSLAYAYETKDALCLVLT 264
Cdd:COG0515    2 YRILRKLGEGSFGEVYLARDR---KLVALKVLAKKLESKSKEVERFLREIQILASLNHpPNIVKLYDFFQDEGSLYLVME 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 265 LMNGGDLKFHIYHMGEAG-FDEKRAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGH-IRISDLGLA-------VH 335
Cdd:COG0515   79 YVDGGSLEDLLKKIGRKGpLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRvVKLIDFGLAkllpdpgST 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 336 VPEGQTIKGRVGTVGYMAPEVVK---NERYTFSPDWWALGCLLYEMIEGQSPFQ---------QRKKKIKREEVERLVKE 403
Cdd:COG0515  159 SSIPALPSTSVGTPGYMAPEVLLglsLAYASSSSDIWSLGITLYELLTGLPPFEgeknssatsQTLKIILELPTPSLASP 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 125848675 404 VEEEYSSKFSEDAKSLCKMLLAKDPSERLGCQGGGASEVKAHLIFRSINFKRLA 457
Cdd:COG0515  239 LSPSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESDLSDLL 292
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
195-423 1.87e-25

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 105.32  E-value: 1.87e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 195 GGFGEVCACQVRATGKMYACkklekkrikkrkgesmalneKQILEK-------------VNSRFVVSLAYAYETKDALCL 261
Cdd:PHA03390  27 GKFGKVSVLKHKPTQKLFVQ--------------------KIIKAKnfnaiepmvhqlmKDNPNFIKLYYSVTTLKGHVL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 262 VLTLMNGGDLkFHIYHMGEAgFDEKRAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDH-GHIRISDLGLAVHVpeGQ 340
Cdd:PHA03390  87 IMDYIKDGDL-FDLLKKEGK-LSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDRAkDRIYLCDYGLCKII--GT 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 341 TIKGRvGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIEGQSPFqqrkKKIKREEVErlVKEVEEEYSSKF------SE 414
Cdd:PHA03390 163 PSCYD-GTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPF----KEDEDEELD--LESLLKRQQKKLpfiknvSK 235
                        250
                 ....*....|
gi 125848675 415 DAKS-LCKML 423
Cdd:PHA03390 236 NANDfVQSML 245
pknD PRK13184
serine/threonine-protein kinase; Reviewed
295-431 3.62e-16

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 80.58  E-value: 3.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 295 ICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVPEGQ------------------TIKGR-VGTVGYMAPE 355
Cdd:PRK13184 122 ICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGAAIFKKLEEedlldidvdernicyssmTIPGKiVGTPDYMAPE 201
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 125848675 356 VVKNERYTFSPDWWALGCLLYEMIEGQSPFqqRKKKIKREEVERLVKEVEEeySSKFSEDAKSLCKML---LAKDPSER 431
Cdd:PRK13184 202 RLLGVPASESTDIYALGVILYQMLTLSFPY--RRKKGRKISYRDVILSPIE--VAPYREIPPFLSQIAmkaLAVDPAER 276
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
190-385 2.64e-15

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 76.40  E-value: 2.64e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 190 RVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEsmALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTLMNGG 269
Cdd:PLN00034  80 NRIGSGAGGTVYKVIHRPTGRLYALKVIYGNHEDTVRRQ--ICREIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGG 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 270 DLK-FHIYHmgeagfdEKRAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVpeGQTI---KGR 345
Cdd:PLN00034 158 SLEgTHIAD-------EQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRIL--AQTMdpcNSS 228
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 125848675 346 VGTVGYMAPEVVKNE----RYT-FSPDWWALGCLLYEMIEGQSPF 385
Cdd:PLN00034 229 VGTIAYMSPERINTDlnhgAYDgYAGDIWSLGVSILEFYLGRFPF 273
 
Name Accession Description Interval E-value
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
185-469 0e+00

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


Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 603.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 185 TFRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGESMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLT 264
Cdd:cd05630    1 TFRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 265 LMNGGDLKFHIYHMGEAGFDEKRAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVPEGQTIKG 344
Cdd:cd05630   81 LMNGGDLKFHIYHMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVPEGQTIKG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 345 RVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIEGQSPFQQRKKKIKREEVERLVKEVEEEYSSKFSEDAKSLCKMLL 424
Cdd:cd05630  161 RVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKREEVERLVKEVPEEYSEKFSPQARSLCSMLL 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 125848675 425 AKDPSERLGCQGGGASEVKAHLIFRSINFKRLAAGMLEAPFIPDP 469
Cdd:cd05630  241 CKDPAERLGCRGGGAREVKEHPLFKKLNFKRLGAGMLEPPFKPDP 285
RGS_GRK6 cd08751
Regulator of G protein signaling domain (RGS) found in G protein-coupled receptor kinase 6 ...
35-179 2.94e-104

Regulator of G protein signaling domain (RGS) found in G protein-coupled receptor kinase 6 (GRK6); The RGS domain is an essential part of the GRK6 (G protein-coupled receptor kinase 6) protein which plays an important role in the regulating of dopamine, opioids, M3 muscarinic, and chemokine receptor signaling. GRK6 is a member of the GRK kinase family which includes three major subfamilies: the GRK4 subfamily (GRK4, GRK5 and GRK6), the rhodopsin kinase or visual GRK subfamily (GRK1 and GRK7), and the beta-adrenergic receptor kinases subfamily (GRK2/GRK3). The RGS domain of the GRKs has very little sequence similarity with the canonical RGS domain of the RGS proteins and therefore is often refered to as the RH (RGS Homology) domain. The RH domain of GRK6 does not have structural determinants that are required for binding G-alpha subunit, in contrast to GRK2 and many other RGS proteins. GRK6 is an important target for treatment of addiction and Parkinson disease. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development.


Pssm-ID: 188705  Cd Length: 145  Bit Score: 313.06  E-value: 2.94e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675  35 QFPHISLCEELRQTIEKDYNSLCERQPIGRLLFRQFCDTRPELRRCVRFLDAVAEYEVTPDEKRKECGQELLDKYLNTKS 114
Cdd:cd08751    1 QFPHISLCEELRQSLERDYHSLCERQPIGRLLFRQFCATRPELSRCVAFLDAVAEYEVTPDEKRKECGQNLTQKYLSHKS 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 125848675 115 EDYIPEVTEEMVTKCADRLQQEACKELFMECTKLIHDYLSVAPFADYLDSMYYSRFLQWKWLERQ 179
Cdd:cd08751   81 EDYIPEVPRQLVTNCTQRLEQEPCKELFQELTKLIHDYLSVAPFADYLDSIYFNRFLQWKWLERQ 145
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
185-469 0e+00

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


Pssm-ID: 270756 [Multi-domain]  Cd Length: 285  Bit Score: 588.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 185 TFRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGESMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLT 264
Cdd:cd05605    1 TFRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 265 LMNGGDLKFHIYHMGEAGFDEKRAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVPEGQTIKG 344
Cdd:cd05605   81 IMNGGDLKFHIYNMGNPGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVEIPEGETIRG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 345 RVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIEGQSPFQQRKKKIKREEVERLVKEVEEEYSSKFSEDAKSLCKMLL 424
Cdd:cd05605  161 RVGTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFRARKEKVKREEVDRRVKEDQEEYSEKFSEEAKSICSQLL 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 125848675 425 AKDPSERLGCQGGGASEVKAHLIFRSINFKRLAAGMLEAPFIPDP 469
Cdd:cd05605  241 QKDPKTRLGCRGEGAEDVKSHPFFKSINFKRLEAGLLEPPFVPDP 285
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
185-469 0e+00

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


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 548.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 185 TFRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGESMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLT 264
Cdd:cd05631    1 TFRHYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKRILEKVNSRFVVSLAYAYETKDALCLVLT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 265 LMNGGDLKFHIYHMGEAGFDEKRAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVPEGQTIKG 344
Cdd:cd05631   81 IMNGGDLKFHIYNMGNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVQIPEGETVRG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 345 RVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIEGQSPFQQRKKKIKREEVERLVKEVEEEYSSKFSEDAKSLCKMLL 424
Cdd:cd05631  161 RVGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRKERVKREEVDRRVKEDQEEYSEKFSEDAKSICRMLL 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 125848675 425 AKDPSERLGCQGGGASEVKAHLIFRSINFKRLAAGMLEAPFIPDP 469
Cdd:cd05631  241 TKNPKERLGCRGNGAAGVKQHPIFKNINFKRLEANMLEPPFCPDP 285
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
183-495 0e+00

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


Pssm-ID: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 541.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 183 KNTFRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGESMALNEKQILEKVNSRFVVSLAYAYETKDALCLV 262
Cdd:cd05632    1 KNTFRQYRVLGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKGESMALNEKQILEKVNSQFVVNLAYAYETKDALCLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 263 LTLMNGGDLKFHIYHMGEAGFDEKRAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVPEGQTI 342
Cdd:cd05632   81 LTIMNGGDLKFHIYNMGNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVKIPEGESI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 343 KGRVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIEGQSPFQQRKKKIKREEVERLVKEVEEEYSSKFSEDAKSLCKM 422
Cdd:cd05632  161 RGRVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEKVKREEVDRRVLETEEVYSAKFSEEAKSICKM 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 125848675 423 LLAKDPSERLGCQGGGASEVKAHLIFRSINFKRLAAGMLEAPFIPDPQAIYCKDVLDIEQFSTVKGVELEPKD 495
Cdd:cd05632  241 LLTKDPKQRLGCQEEGAGEVKRHPFFRNMNFKRLEAGMLDPPFVPDPRAVYCKDVLDIEQFSTVKGVNLDQTD 313
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
192-468 1.47e-165

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


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 475.48  E-value: 1.47e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 192 LGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGESMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTLMNGGDL 271
Cdd:cd05577    1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIKKKKGETMALNEKIILEKVSSPFIVSLAYAFETKDKLCLVLTLMNGGDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 272 KFHIYHMGEAGFDEKRAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVPEGQTIKGRVGTVGY 351
Cdd:cd05577   81 KYHIYNVGTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAVEFKGGKKIKGRVGTHGY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 352 MAPEVVKNER-YTFSPDWWALGCLLYEMIEGQSPFQQRKKKIKREEVERLVKEVEEEYSSKFSEDAKSLCKMLLAKDPSE 430
Cdd:cd05577  161 MAPEVLQKEVaYDFSVDWFALGCMLYEMIAGRSPFRQRKEKVDKEELKRRTLEMAVEYPDSFSPEARSLCEGLLQKDPER 240
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 125848675 431 RLGCQGGGASEVKAHLIFRSINFKRLAAGMLEAPFIPD 468
Cdd:cd05577  241 RLGCRGGSADEVKEHPFFRSLNWQRLEAGMLEPPFVPD 278
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
186-468 2.02e-123

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


Pssm-ID: 270758 [Multi-domain]  Cd Length: 286  Bit Score: 368.08  E-value: 2.02e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 186 FRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGESMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTL 265
Cdd:cd05607    4 FYEFRVLGKGGFGEVCAVQVKNTGQMYACKKLDKKRLKKKSGEKMALLEKEILEKVNSPFIVSLAYAFETKTHLCLVMSL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 266 MNGGDLKFHIYHMGEAGFDEKRAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVPEGQTIKGR 345
Cdd:cd05607   84 MNGGDLKYHIYNVGERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVEVKEGKPITQR 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 346 VGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIEGQSPFQQRKKKIKREEVER--LVKEVEEEYSSkFSEDAKSLCKML 423
Cdd:cd05607  164 AGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFRDHKEKVSKEELKRrtLEDEVKFEHQN-FTEEAKDICRLF 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 125848675 424 LAKDPSERLGCQgGGASEVKAHLIFRSINFKRLAAGMLEAPFIPD 468
Cdd:cd05607  243 LAKKPENRLGSR-TNDDDPRKHEFFKSINFPRLEAGLIDPPFVPD 286
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
186-468 2.73e-121

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


Pssm-ID: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 362.66  E-value: 2.73e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 186 FRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGESMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTL 265
Cdd:cd05608    3 FLDFRVLGKGGFGEVSACQMRATGKLYACKKLNKKRLKKRKGYEGAMVEKRILAKVHSRFIVSLAYAFQTKTDLCLVMTI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 266 MNGGDLKFHIYHMGE--AGFDEKRAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVPEGQT-I 342
Cdd:cd05608   83 MNGGDLRYHIYNVDEenPGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAVELKDGQTkT 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 343 KGRVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIEGQSPFQQRKKKIKREEVERLVKEVEEEYSSKFSEDAKSLCKM 422
Cdd:cd05608  163 KGYAGTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFRARGEKVENKELKQRILNDSVTYSEKFSPASKSICEA 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 125848675 423 LLAKDPSERLGCQGGGASEVKAHLIFRSINFKRLAAGMLEAPFIPD 468
Cdd:cd05608  243 LLAKDPEKRLGFRDGNCDGLRTHPFFRDINWRKLEAGILPPPFVPD 288
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
192-448 3.61e-105

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


Pssm-ID: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 319.46  E-value: 3.61e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 192 LGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGESMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTLMNGGDL 271
Cdd:cd05123    1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIIKRKEVEHTLNERNILERVNHPFIVKLHYAFQTEEKLYLVLDYVPGGEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 272 KFHIYHMGeaGFDEKRAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVH-VPEGQTIKGRVGTVG 350
Cdd:cd05123   81 FSHLSKEG--RFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKElSSDGDRTYTFCGTPE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 351 YMAPEVVKNERYTFSPDWWALGCLLYEMIEGQSPFQQRkkkiKREEVERLVKEVEEEYSSKFSEDAKSLCKMLLAKDPSE 430
Cdd:cd05123  159 YLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAE----NRKEIYEKILKSPLKFPEYVSPEAKSLISGLLQKDPTK 234
                        250
                 ....*....|....*...
gi 125848675 431 RLGCqgGGASEVKAHLIF 448
Cdd:cd05123  235 RLGS--GGAEEIKAHPFF 250
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
191-467 5.83e-89

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


Pssm-ID: 270757 [Multi-domain]  Cd Length: 279  Bit Score: 278.55  E-value: 5.83e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 191 VLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGESMALNEKQILEKVN----SRFVVSLAYAYETKDALCLVLTLM 266
Cdd:cd05606    1 IIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVStggdCPFIVCMTYAFQTPDKLCFILDLM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 267 NGGDLKFHIYHMGEagFDEKRAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVPEGQTiKGRV 346
Cdd:cd05606   81 NGGDLHYHLSQHGV--FSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLACDFSKKKP-HASV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 347 GTVGYMAPEVV-KNERYTFSPDWWALGCLLYEMIEGQSPFQQRKKKIKReEVERLVKEVEEEYSSKFSEDAKSLCKMLLA 425
Cdd:cd05606  158 GTHGYMAPEVLqKGVAYDSSADWFSLGCMLYKLLKGHSPFRQHKTKDKH-EIDRMTLTMNVELPDSFSPELKSLLEGLLQ 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 125848675 426 KDPSERLGCQGGGASEVKAHLIFRSINFKRLAAGMLEAPFIP 467
Cdd:cd05606  237 RDVSKRLGCLGRGATEVKEHPFFKGVDWQQVYLQKYPPPLIP 278
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
181-518 8.65e-84

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


Pssm-ID: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 267.70  E-value: 8.65e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125848675 181 ITKNTFRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGESMALNEKQILEKVNS---RFVVSLAYAYETKD 257
Cdd:cd05633    2 LTMNDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTgdcPFIVCMTYAFHTPD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|