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Conserved domains on  [gi|17136724|ref|NP_476867.1|]
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G protein-coupled receptor kinase 2, isoform A [Drosophila melanogaster]

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List of domain hits

Name Accession Description Interval E-value
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
308-597 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: 595.87  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724 308 TFRMYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGESMVLIEKQILQKINSPFVVNLAYAYETKDALCLVLT 387
Cdd:cd05605   1 TFRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724 388 IMNGGDLKFHIYNMGgEPGFELERARFYAAEVACGLQHLHKQGIVYRDCKPENILLDDHGHVRISDLGLAVEIPEGEMVR 467
Cdd:cd05605  81 IMNGGDLKFHIYNMG-NPGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVEIPEGETIR 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724 468 GRVGTVGYMAPEVIDNEKYAFSPDWFSFGCLLYEMIEGQAPFRMRKEKVKREEVDRRVKEDPEKYSSKFNDEAKSMCQQL 547
Cdd:cd05605 160 GRVGTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFRARKEKVKREEVDRRVKEDQEEYSEKFSEEAKSICSQL 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 17136724 548 LAKSIKQRLGCRngRMGGQDVMAHPFFHStqLNWRRLEAGMLEPPFVPDP 597
Cdd:cd05605 240 LQKDPKTRLGCR--GEGAEDVKSHPFFKS--INFKRLEAGLLEPPFVPDP 285
RGS super family cl02565
Regulator of G protein signaling (RGS) domain superfamily; The RGS domain is an essential part ...
248-305 1.77e-14

Regulator of G protein signaling (RGS) domain superfamily; The RGS domain is an essential part of the Regulator of G-protein Signaling (RGS) protein family, a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins play critical regulatory roles as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. While inactive, G-alpha-subunits bind GDP, which is released and replaced by GTP upon agonist activation. GTP binding leads to dissociation of the alpha-subunit and the beta-gamma-dimer, allowing them to interact with effectors molecules and propagate signaling cascades associated with cellular growth, survival, migration, and invasion. Deactivation of the G-protein signaling controlled by the RGS domain accelerates GTPase activity of the alpha subunit by hydrolysis of GTP to GDP, which results in the reassociation of the alpha-subunit with the beta-gamma-dimer and thereby inhibition of downstream activity. As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. RGS proteins are also involved in apoptosis and cell proliferation, as well as modulation of cardiac development. Several RGS proteins can fine-tune immune responses, while others play important roles in neuronal signals modulation. Some RGS proteins are principal elements needed for proper vision.


The actual alignment was detected with superfamily member cd08750:

Pssm-ID: 261346  Cd Length: 132  Bit Score: 71.08  E-value: 1.77e-14
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17136724 248 DLIAQVRNKL-NSGGKDIFAQCVNAVKAFLAGEPFREFESSMYFHRYLQWKWLEAQPIT 305
Cdd:cd08750  73 DVVTECRLKLeENPSKELFEECTRVVHEYLSGEPFEAYQESMYFSRFLQWKWLERQPVT 131
RGS super family cl02565
Regulator of G protein signaling (RGS) domain superfamily; The RGS domain is an essential part ...
35-111 9.69e-14

Regulator of G protein signaling (RGS) domain superfamily; The RGS domain is an essential part of the Regulator of G-protein Signaling (RGS) protein family, a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins play critical regulatory roles as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. While inactive, G-alpha-subunits bind GDP, which is released and replaced by GTP upon agonist activation. GTP binding leads to dissociation of the alpha-subunit and the beta-gamma-dimer, allowing them to interact with effectors molecules and propagate signaling cascades associated with cellular growth, survival, migration, and invasion. Deactivation of the G-protein signaling controlled by the RGS domain accelerates GTPase activity of the alpha subunit by hydrolysis of GTP to GDP, which results in the reassociation of the alpha-subunit with the beta-gamma-dimer and thereby inhibition of downstream activity. As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. RGS proteins are also involved in apoptosis and cell proliferation, as well as modulation of cardiac development. Several RGS proteins can fine-tune immune responses, while others play important roles in neuronal signals modulation. Some RGS proteins are principal elements needed for proper vision.


The actual alignment was detected with superfamily member cd08751:

Pssm-ID: 261346  Cd Length: 145  Bit Score: 69.23  E-value: 9.69e-14
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17136724  35 QFPHISQCINLKDKLDISYGYVIDQQPIGRELFRLFCENkRPVYFRYITFLDEVVKYEIEYISNRIFIGHDIGRRFL 111
Cdd:cd08751   1 QFPHISLCEELRQSLERDYHSLCERQPIGRLLFRQFCAT-RPELSRCVAFLDAVAEYEVTPDEKRKECGQNLTQKYL 76
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
309-574 3.42e-81

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


:

Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 260.93  E-value: 3.42e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724    309 FRMYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRkgESMVLIEKQILQKINSPFVVNLAYAYETKDALCLVLTI 388
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKD--RERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724    389 MNGGDLKFHIYNMGGepgFELERARFYAAEVACGLQHLHKQGIVYRDCKPENILLDDHGHVRISDLGLAVEIPEGEMVRG 468
Cdd:smart00220  79 CEGGDLFDLLKKRGR---LSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKLTT 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724    469 RVGTVGYMAPEVIDNEKYAFSPDWFSFGCLLYEMIEGQAPFRMRKEKVKREEVDRRVKEDPEKYSSKFNDEAKSMCQQLL 548
Cdd:smart00220 156 FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDLIRKLL 235
                          250       260
                   ....*....|....*....|....*.
gi 17136724    549 AKSIKQRLGCRngrmggqDVMAHPFF 574
Cdd:smart00220 236 VKDPEKRLTAE-------EALQHPFF 254
 
Name Accession Description Interval E-value
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
308-597 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: 595.87  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724 308 TFRMYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGESMVLIEKQILQKINSPFVVNLAYAYETKDALCLVLT 387
Cdd:cd05605   1 TFRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724 388 IMNGGDLKFHIYNMGgEPGFELERARFYAAEVACGLQHLHKQGIVYRDCKPENILLDDHGHVRISDLGLAVEIPEGEMVR 467
Cdd:cd05605  81 IMNGGDLKFHIYNMG-NPGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVEIPEGETIR 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724 468 GRVGTVGYMAPEVIDNEKYAFSPDWFSFGCLLYEMIEGQAPFRMRKEKVKREEVDRRVKEDPEKYSSKFNDEAKSMCQQL 547
Cdd:cd05605 160 GRVGTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFRARKEKVKREEVDRRVKEDQEEYSEKFSEEAKSICSQL 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 17136724 548 LAKSIKQRLGCRngRMGGQDVMAHPFFHStqLNWRRLEAGMLEPPFVPDP 597
Cdd:cd05605 240 LQKDPKTRLGCR--GEGAEDVKSHPFFKS--INFKRLEAGLLEPPFVPDP 285
RGS_GRK4 cd08750
Regulator of G protein signaling domain (RGS) found in G protein-coupled receptor kinase 4 ...
248-305 1.77e-14

Regulator of G protein signaling domain (RGS) found in G protein-coupled receptor kinase 4 (GRK4); The RGS domain is an essential part of the GRK4 (G protein-coupled receptor kinase4) proteins, which are membrane-associated serine/threonine protein kinases that phosphorylate G protein-coupled receptors (GPCRs) upon agonist stimulation. This phosphorylation initiates beta-arrestin-mediated receptor desensitization, internalization, and signaling events. GRK4 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. GRK4 plays a key role in regulating dopaminergic-mediated natriuresis and is associated with essential hypertension and/or salt-sensitive hypertension. GRK4 exists in four splice variants involved in hyperphosphorylation, desensitization, and internalization of two dopamine receptors (D1R and D3R). GRK4 also increases the expression of a key receptor of the renin-angiotensin system, the AT1R (angiotensin type 1 receptor). 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: 188704  Cd Length: 132  Bit Score: 71.08  E-value: 1.77e-14
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17136724 248 DLIAQVRNKL-NSGGKDIFAQCVNAVKAFLAGEPFREFESSMYFHRYLQWKWLEAQPIT 305
Cdd:cd08750  73 DVVTECRLKLeENPSKELFEECTRVVHEYLSGEPFEAYQESMYFSRFLQWKWLERQPVT 131
RGS_GRK6 cd08751
Regulator of G protein signaling domain (RGS) found in G protein-coupled receptor kinase 6 ...
35-111 9.69e-14

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: 69.23  E-value: 9.69e-14
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17136724  35 QFPHISQCINLKDKLDISYGYVIDQQPIGRELFRLFCENkRPVYFRYITFLDEVVKYEIEYISNRIFIGHDIGRRFL 111
Cdd:cd08751   1 QFPHISLCEELRQSLERDYHSLCERQPIGRLLFRQFCAT-RPELSRCVAFLDAVAEYEVTPDEKRKECGQNLTQKYL 76
RGS smart00315
Regulator of G protein signalling domain; RGS family members are GTPase-activating proteins ...
59-149 1.56e-08

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: 53.04  E-value: 1.56e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724     59 QQPIGRELFRLFCENKRPVyfRYITFLDEVVKYE-IEYISNRIFIGHDIGRRFLDVEAQLELRngsggdaLDAETQEELL 137
Cdd:smart00315   7 SDPIGRLLFREFLESEFSE--ENLEFWLAVEEFKkAEDDEERIAKAREIYDKFLSPNAPKEVN-------LDSDLREKIE 77
                           90
                   ....*....|..
gi 17136724    138 LNSSNANPTETA 149
Cdd:smart00315  78 ENLESEEPPPDL 89
RGS smart00315
Regulator of G protein signalling domain; RGS family members are GTPase-activating proteins ...
245-293 1.09e-05

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: 44.57  E-value: 1.09e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 17136724    245 LNDDLIAQVRNKLNSGG--KDIFAQCVNAVKAFLAGEPFREFESSMYFHRY 293
Cdd:smart00315  68 LDSDLREKIEENLESEEppPDLFDEAQREVYELLEKDSFPRFLESDYYLRF 118
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
309-574 3.42e-81

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 260.93  E-value: 3.42e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724    309 FRMYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRkgESMVLIEKQILQKINSPFVVNLAYAYETKDALCLVLTI 388
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKD--RERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724    389 MNGGDLKFHIYNMGGepgFELERARFYAAEVACGLQHLHKQGIVYRDCKPENILLDDHGHVRISDLGLAVEIPEGEMVRG 468
Cdd:smart00220  79 CEGGDLFDLLKKRGR---LSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKLTT 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724    469 RVGTVGYMAPEVIDNEKYAFSPDWFSFGCLLYEMIEGQAPFRMRKEKVKREEVDRRVKEDPEKYSSKFNDEAKSMCQQLL 548
Cdd:smart00220 156 FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDLIRKLL 235
                          250       260
                   ....*....|....*....|....*.
gi 17136724    549 AKSIKQRLGCRngrmggqDVMAHPFF 574
Cdd:smart00220 236 VKDPEKRLTAE-------EALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
309-574 1.57e-60

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 205.17  E-value: 1.57e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724   309 FRMYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGESmVLIEKQILQKINSPFVVNLAYAYETKDALCLVLTI 388
Cdd:pfam00069   1 YELLRKLGSGSFGTVYKAKHKGTGKIVAVKILKKRSEKSKKDQT-ARREIRILRRLSHPNIVRLIDAFEDKDHLYLVMEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724   389 MNGGDLKFHIYNMGGepgFELERARFYAAEVACGLQHLHKQGIVYRDCKPENILLDDHGHVRISDLGLAVEIPE-GEMVR 467
Cdd:pfam00069  80 CEGGDLFDYLSRGGP---LSEDEAKKIALQILRGLEYLHSNGIIHRDLKPENILLDENGVVKIADFGLAKKLTKsSSSLT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724   468 GRVGTVGYMAPEVIDNEKYAFSP-DWFSFGCLLYEMIEGQAPFRMRKEKVKREEVDRRVKED---PEKYSSKFNDEAKSM 543
Cdd:pfam00069 157 TFVGTPEYMAPEVLLGGNGYGPKvDVWSLGVILYELLTGKPPFSGESILDQLQLIRRILGPPlefDEPKSDSGSEEAKDL 236
                         250       260       270
                  ....*....|....*....|....*....|.
gi 17136724   544 CQQLLAKSIKQRLGCRngrmggqDVMAHPFF 574
Cdd:pfam00069 237 IKKCLNKDPSKRPTAE-------EILQHPWF 260
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
309-592 5.71e-49

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 175.01  E-value: 5.71e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724  309 FRMYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGESMVLIEKQILQKINSPFVVNLAYAYETKDALCLVLTI 388
Cdd:PTZ00263  20 FEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFLLEF 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724  389 MNGGDLKFHIYNMGGEPGfelERARFYAAEVACGLQHLHKQGIVYRDCKPENILLDDHGHVRISDLGLAVEIPEGEMVrg 468
Cdd:PTZ00263 100 VVGGELFTHLRKAGRFPN---DVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVPDRTFT-- 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724  469 RVGTVGYMAPEVIDNEKYAFSPDWFSFGCLLYEMIEGQAPFrMRKEKVKREEvdrRVKEDPEKYSSKFNDEAKSMCQQLL 548
Cdd:PTZ00263 175 LCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPF-FDDTPFRIYE---KILAGRLKFPNWFDGRARDLVKGLL 250
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 17136724  549 AKSIKQRLGCRNGrmGGQDVMAHPFFHSTqlNWRRLEAGMLEPP 592
Cdd:PTZ00263 251 QTDHTKRLGTLKG--GVADVKNHPYFHGA--NWDKLYARYYPAP 290
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
309-580 2.64e-38

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 146.43  E-value: 2.64e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724 309 FRMYRVLGKGGFGEVCACQVRatgKMYACKKLEKKRIKKRKGESMVLIEKQILQKINSP-FVVNLAYAYETKDALCLVLT 387
Cdd:COG0515   2 YRILRKLGEGSFGEVYLARDR---KLVALKVLAKKLESKSKEVERFLREIQILASLNHPpNIVKLYDFFQDEGSLYLVME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724 388 IMNGGDLKFHIYNMGGEPGFELERARFYAAEVACGLQHLHKQGIVYRDCKPENILLDDHGH-VRISDLGLAVEIPEG--- 463
Cdd:COG0515  79 YVDGGSLEDLLKKIGRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRvVKLIDFGLAKLLPDPgst 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724 464 ----EMVRGRVGTVGYMAPEVI---DNEKYAFSPDWFSFGCLLYEMIEGQAPFRMRKEKVKREEVDRRVKEDP------- 529
Cdd:COG0515 159 ssipALPSTSVGTPGYMAPEVLlglSLAYASSSSDIWSLGITLYELLTGLPPFEGEKNSSATSQTLKIILELPtpslasp 238
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 17136724 530 --EKYSSKFNDEAKSMCQQLLAKSIKQRLGCRngrmggqDVMAHPFFHSTQLN 580
Cdd:COG0515 239 lsPSNPELISKAASDLLKKLLAKDPKNRLSSS-------SDLSHDLLAHLKLK 284
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
318-574 3.59e-19

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 87.60  E-value: 3.59e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724  318 GGFGEVCACQVRATGKMYACKKLEKKRIKKRkgESMVliekQILQKINSPFVvNLAYAYETKDALCLVLTIMNGGDLkFH 397
Cdd:PHA03390  27 GKFGKVSVLKHKPTQKLFVQKIIKAKNFNAI--EPMV----HQLMKDNPNFI-KLYYSVTTLKGHVLIMDYIKDGDL-FD 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724  398 IYNMggEPGFELERARFYAAEVACGLQHLHKQGIVYRDCKPENILLDDH-GHVRISDLGLAVEIPEGEMVRGrvgTVGYM 476
Cdd:PHA03390  99 LLKK--EGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDRAkDRIYLCDYGLCKIIGTPSCYDG---TLDYF 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724  477 APEVIDNEKYAFSPDWFSFGCLLYEMIEGQAPF-RMRKEKVKREEVDRRVKEDPEKYSSKfNDEAKSMCQQLLAKSIKQR 555
Cdd:PHA03390 174 SPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFkEDEDEELDLESLLKRQQKKLPFIKNV-SKNANDFVQSMLKYNINYR 252
                        250
                 ....*....|....*....
gi 17136724  556 LGCRNgrmggqDVMAHPFF 574
Cdd:PHA03390 253 LTNYN------EIIKHPFL 265
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
313-514 7.20e-16

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 78.33  E-value: 7.20e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724  313 RVLGKGGFGEVCACQVRATGKMYACKKLEKKRikkrkgESMVLI----EKQILQKINSPFVVNLAYAYETKDALCLVLTI 388
Cdd:PLN00034  80 NRIGSGAGGTVYKVIHRPTGRLYALKVIYGNH------EDTVRRqicrEIEILRDVNHPNVVKCHDMFDHNGEIQVLLEF 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724  389 MNGGDLK-FHIynmgGEPGFELERARfyaaEVACGLQHLHKQGIVYRDCKPENILLDDHGHVRISDLGLAvEIPEGEM-- 465
Cdd:PLN00034 154 MDGGSLEgTHI----ADEQFLADVAR----QILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVS-RILAQTMdp 224
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 17136724  466 VRGRVGTVGYMAPEVIDNE----KY-AFSPDWFSFGCLLYEMIEGQAPFRMRKE 514
Cdd:PLN00034 225 CNSSVGTIAYMSPERINTDlnhgAYdGYAGDIWSLGVSILEFYLGRFPFGVGRQ 278
pknD PRK13184
serine/threonine-protein kinase; Reviewed
419-530 4.21e-13

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 71.34  E-value: 4.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724  419 VACGLQHLHKQGIVYRDCKPENILLDDHGHVRISDLGLAV-----------------EIPEGEM-VRGR-VGTVGYMAPE 479
Cdd:PRK13184 122 ICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGAAIfkkleeedlldidvderNICYSSMtIPGKiVGTPDYMAPE 201
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 17136724  480 VIDNEKYAFSPDWFSFGCLLYEMIEGQAPFRMRKekvKREEVDRRVKEDPE 530
Cdd:PRK13184 202 RLLGVPASESTDIYALGVILYQMLTLSFPYRRKK---GRKISYRDVILSPI 249
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
357-506 5.07e-09

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


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 58.32  E-value: 5.07e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724    357 EKQILQKINSPFVVNLAYAYETKDALCL-VLTIMNGGDLKFHIYNMGGEPGFELERarfYAAEVACGLQHLHKQGIVYRD 435
Cdd:TIGR03903   28 ETALCARLYHPNIVALLDSGEAPPGLLFaVFEYVPGRTLREVLAADGALPAGETGR---LMLQVLDALACAHNQGIVHRD 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724    436 CKPENILL---DDHGHVRISDLGLAVEIP------------EGEMvrgrVGTVGYMAPEVIDNEKYAFSPDWFSFGCLLY 500
Cdd:TIGR03903  105 LKPQNIMVsqtGVRPHAKVLDFGIGTLLPgvrdadvatltrTTEV----LGTPTYCAPEQLRGEPVTPNSDLYAWGLIFL 180

                   ....*.
gi 17136724    501 EMIEGQ 506
Cdd:TIGR03903  181 ECLTGQ 186
 
Name Accession Description Interval E-value
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
308-597 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: 595.87  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724 308 TFRMYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGESMVLIEKQILQKINSPFVVNLAYAYETKDALCLVLT 387
Cdd:cd05605   1 TFRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724 388 IMNGGDLKFHIYNMGgEPGFELERARFYAAEVACGLQHLHKQGIVYRDCKPENILLDDHGHVRISDLGLAVEIPEGEMVR 467
Cdd:cd05605  81 IMNGGDLKFHIYNMG-NPGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVEIPEGETIR 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724 468 GRVGTVGYMAPEVIDNEKYAFSPDWFSFGCLLYEMIEGQAPFRMRKEKVKREEVDRRVKEDPEKYSSKFNDEAKSMCQQL 547
Cdd:cd05605 160 GRVGTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFRARKEKVKREEVDRRVKEDQEEYSEKFSEEAKSICSQL 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 17136724 548 LAKSIKQRLGCRngRMGGQDVMAHPFFHStqLNWRRLEAGMLEPPFVPDP 597
Cdd:cd05605 240 LQKDPKTRLGCR--GEGAEDVKSHPFFKS--INFKRLEAGLLEPPFVPDP 285
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
308-623 2.10e-176

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: 509.51  E-value: 2.10e-176
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724 308 TFRMYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGESMVLIEKQILQKINSPFVVNLAYAYETKDALCLVLT 387
Cdd:cd05632   3 TFRQYRVLGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKGESMALNEKQILEKVNSQFVVNLAYAYETKDALCLVLT 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724 388 IMNGGDLKFHIYNMGgEPGFELERARFYAAEVACGLQHLHKQGIVYRDCKPENILLDDHGHVRISDLGLAVEIPEGEMVR 467
Cdd:cd05632  83 IMNGGDLKFHIYNMG-NPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVKIPEGESIR 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724 468 GRVGTVGYMAPEVIDNEKYAFSPDWFSFGCLLYEMIEGQAPFRMRKEKVKREEVDRRVKEDPEKYSSKFNDEAKSMCQQL 547
Cdd:cd05632 162 GRVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEKVKREEVDRRVLETEEVYSAKFSEEAKSICKML 241
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17136724 548 LAKSIKQRLGCRngRMGGQDVMAHPFFHStqLNWRRLEAGMLEPPFVPDPHAVYAKDVLDIEQFSTVKGVNIDESD 623
Cdd:cd05632 242 LTKDPKQRLGCQ--EEGAGEVKRHPFFRN--MNFKRLEAGMLDPPFVPDPRAVYCKDVLDIEQFSTVKGVNLDQTD 313
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
308-597 4.65e-171

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: 494.90  E-value: 4.65e-171
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724 308 TFRMYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGESMVLIEKQILQKINSPFVVNLAYAYETKDALCLVLT 387
Cdd:cd05631   1 TFRHYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKRILEKVNSRFVVSLAYAYETKDALCLVLT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724 388 IMNGGDLKFHIYNMGgEPGFELERARFYAAEVACGLQHLHKQGIVYRDCKPENILLDDHGHVRISDLGLAVEIPEGEMVR 467
Cdd:cd05631  81 IMNGGDLKFHIYNMG-NPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVQIPEGETVR 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724 468 GRVGTVGYMAPEVIDNEKYAFSPDWFSFGCLLYEMIEGQAPFRMRKEKVKREEVDRRVKEDPEKYSSKFNDEAKSMCQQL 547
Cdd:cd05631 160 GRVGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRKERVKREEVDRRVKEDQEEYSEKFSEDAKSICRML 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 17136724 548 LAKSIKQRLGCRNGrmGGQDVMAHPFFHStqLNWRRLEAGMLEPPFVPDP 597
Cdd:cd05631 240 LTKNPKERLGCRGN--GAAGVKQHPIFKN--INFKRLEANMLEPPFCPDP 285
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
308-597 2.58e-167

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: 485.30  E-value: 2.58e-167
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724 308 TFRMYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGESMVLIEKQILQKINSPFVVNLAYAYETKDALCLVLT 387
Cdd:cd05630   1 TFRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724 388 IMNGGDLKFHIYNMGgEPGFELERARFYAAEVACGLQHLHKQGIVYRDCKPENILLDDHGHVRISDLGLAVEIPEGEMVR 467
Cdd:cd05630  81 LMNGGDLKFHIYHMG-QAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVPEGQTIK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724 468 GRVGTVGYMAPEVIDNEKYAFSPDWFSFGCLLYEMIEGQAPFRMRKEKVKREEVDRRVKEDPEKYSSKFNDEAKSMCQQL 547
Cdd:cd05630 160 GRVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKREEVERLVKEVPEEYSEKFSPQARSLCSML 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 17136724 548 LAKSIKQRLGCRNGrmGGQDVMAHPFFHstQLNWRRLEAGMLEPPFVPDP 597
Cdd:cd05630 240 LCKDPAERLGCRGG--GAREVKEHPLFK--KLNFKRLGAGMLEPPFKPDP 285
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
315-596 8.85e-149

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: 437.34  E-value: 8.85e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724 315 LGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGESMVLIEKQILQKINSPFVVNLAYAYETKDALCLVLTIMNGGDL 394
Cdd:cd05577   1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIKKKKGETMALNEKIILEKVSSPFIVSLAYAFETKDKLCLVLTLMNGGDL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724 395 KFHIYNMgGEPGFELERARFYAAEVACGLQHLHKQGIVYRDCKPENILLDDHGHVRISDLGLAVEIPEGEMVRGRVGTVG 474
Cdd:cd05577  81 KYHIYNV-GTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAVEFKGGKKIKGRVGTHG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724 475 YMAPEVIDNEK-YAFSPDWFSFGCLLYEMIEGQAPFRMRKEKVKREEVDRRVKEDPEKYSSKFNDEAKSMCQQLLAKSIK 553
Cdd:cd05577 160 YMAPEVLQKEVaYDFSVDWFALGCMLYEMIAGRSPFRQRKEKVDKEELKRRTLEMAVEYPDSFSPEARSLCEGLLQKDPE 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 17136724 554 QRLGCRNGrmGGQDVMAHPFFHStqLNWRRLEAGMLEPPFVPD 596
Cdd:cd05577 240 RRLGCRGG--SADEVKEHPFFRS--LNWQRLEAGMLEPPFVPD 278
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
307-596 2.41e-122

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: 369.62  E-value: 2.41e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724 307 KTFRMYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGESMVLIEKQILQKINSPFVVNLAYAYETKDALCLVL 386
Cdd:cd05607   2 KYFYEFRVLGKGGFGEVCAVQVKNTGQMYACKKLDKKRLKKKSGEKMALLEKEILEKVNSPFIVSLAYAFETKTHLCLVM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724 387 TIMNGGDLKFHIYNMGgEPGFELERARFYAAEVACGLQHLHKQGIVYRDCKPENILLDDHGHVRISDLGLAVEIPEGEMV 466
Cdd:cd05607  82 SLMNGGDLKYHIYNVG-ERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVEVKEGKPI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724 467 RGRVGTVGYMAPEVIDNEKYAFSPDWFSFGCLLYEMIEGQAPFRMRKEKVKREEVDRRVKEDPEKYS-SKFNDEAKSMCQ 545
Cdd:cd05607 161 TQRAGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFRDHKEKVSKEELKRRTLEDEVKFEhQNFTEEAKDICR 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 17136724 546 QLLAKSIKQRLGCRNgrmGGQDVMAHPFFHStqLNWRRLEAGMLEPPFVPD 596
Cdd:cd05607 241 LFLAKKPENRLGSRT---NDDDPRKHEFFKS--INFPRLEAGLIDPPFVPD 286
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
309-596 8.91e-120

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: 363.05  E-value: 8.91e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724 309 FRMYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGESMVLIEKQILQKINSPFVVNLAYAYETKDALCLVLTI 388
Cdd:cd05608   3 FLDFRVLGKGGFGEVSACQMRATGKLYACKKLNKKRLKKRKGYEGAMVEKRILAKVHSRFIVSLAYAFQTKTDLCLVMTI 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724 389 MNGGDLKFHIYNMGGE-PGFELERARFYAAEVACGLQHLHKQGIVYRDCKPENILLDDHGHVRISDLGLAVEIPEG-EMV 466
Cdd:cd05608  83 MNGGDLRYHIYNVDEEnPGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAVELKDGqTKT 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724 467 RGRVGTVGYMAPEVIDNEKYAFSPDWFSFGCLLYEMIEGQAPFRMRKEKVKREEVDRRVKEDPEKYSSKFNDEAKSMCQQ 546
Cdd:cd05608 163 KGYAGTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFRARGEKVENKELKQRILNDSVTYSEKFSPASKSICEA 242
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 17136724 547 LLAKSIKQRLGCRNGRMGGqdVMAHPFFhsTQLNWRRLEAGMLEPPFVPD 596
Cdd:cd05608 243 LLAKDPEKRLGFRDGNCDG--LRTHPFF--RDINWRKLEAGILPPPFVPD 288
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
315-574 3.84e-95

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: 297.51  E-value: 3.84e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724 315 LGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGESMVLIEKQILQKINSPFVVNLAYAYETKDALCLVLTIMNGGDL 394
Cdd:cd05123   1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIIKRKEVEHTLNERNILERVNHPFIVKLHYAFQTEEKLYLVLDYVPGGEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724 395 KFHIYNMGgepGFELERARFYAAEVACGLQHLHKQGIVYRDCKPENILLDDHGHVRISDLGLAVEIPEGEMV-RGRVGTV 473
Cdd:cd05123  81 FSHLSKEG---RFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELSSDGDRtYTFCGTP 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136724 474 GYMAPEVIDNEKYAFSPDWFSFGCLLYEMIEGQAPFRmrkeKVKREEVDRRVKEDPEKYSSKFNDEAKSMCQQLLAKSIK 553
Cdd:cd05123 158 EYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFY----AENRKEIYEKILKSPLKFPEYVSP