ID GRK1_CAEBR Reviewed; 640 AA.
AC Q622Z7; A8WRN1;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=G protein-coupled receptor kinase 1;
DE EC=2.7.11.16;
GN Name=grk-1; ORFNames=CBG01947;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Specifically phosphorylates the activated forms of G protein-
CC coupled receptors. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[G-protein-coupled receptor] + ATP = [G-protein-coupled
CC receptor]-phosphate + ADP + H(+); Xref=Rhea:RHEA:12008, Rhea:RHEA-
CC COMP:11260, Rhea:RHEA-COMP:11261, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546,
CC ChEBI:CHEBI:456216; EC=2.7.11.16;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. GPRK subfamily. {ECO:0000305}.
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DR EMBL; HE601451; CAP23139.3; -; Genomic_DNA.
DR RefSeq; XP_002643750.1; XM_002643704.1.
DR AlphaFoldDB; Q622Z7; -.
DR SMR; Q622Z7; -.
DR STRING; 6238.Q622Z7; -.
DR GeneID; 8585743; -.
DR KEGG; cbr:CBG_01947; -.
DR CTD; 8585743; -.
DR WormBase; CBG01947a; CBP30829; WBGene00025109; Cbr-grk-1.
DR eggNOG; KOG0986; Eukaryota.
DR HOGENOM; CLU_000288_63_41_1; -.
DR InParanoid; Q622Z7; -.
DR OMA; FTRCISE; -.
DR OrthoDB; 2906348at2759; -.
DR Proteomes; UP000008549; Chromosome X.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004703; F:G protein-coupled receptor kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009966; P:regulation of signal transduction; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR000239; GPCR_kinase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR044926; RGS_subdomain_2.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24355:SF28; G PROTEIN-COUPLED RECEPTOR KINASE 2; 1.
DR PANTHER; PTHR24355; G PROTEIN-COUPLED RECEPTOR KINASE/RIBOSOMAL PROTEIN S6 KINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00615; RGS; 1.
DR PRINTS; PR00717; GPCRKINASE.
DR SMART; SM00315; RGS; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50132; RGS; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..640
FT /note="G protein-coupled receptor kinase 1"
FT /id="PRO_0000226318"
FT DOMAIN 52..187
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT DOMAIN 202..469
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 479..544
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 1..201
FT /note="N-terminal"
FT /evidence="ECO:0000250"
FT REGION 610..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 327
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 208..216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 640 AA; 73412 MW; 40E5E4D8A78B8252 CRC64;
MEIENIVANT VYIKARESGG QKKGKSKKWK NYLQFPHYTE CIPQKKENGE PYAFVVEKQP
IGKLLFHEFC QATNPQYHQC CQFQTKVEEY ETSDDDGQSR RDLASAIVAL LSSKNDQDLS
SSIDEEVWCA FLSDEVISTC ISTADSATHD SEPRSDIFSE PYRLTREYLK QKPFAEFIQT
MYFHRFLQWK WLEKRPVDKH TFRLYRVLGK GGFGEVCACQ VRASGKMYAL KKLEKKRVKK
RHAETLSLNE KQILQKVNSP FVVSLAYAYE TKDALCLVLT LMNGGDLKFH LYNLMPGGFD
EKRVQFYAAE ITLGLQHLHL EHILYRDLKP ENILLDDFGH VRISDLGLAV ELKDNEPIKG
RVGTVGYMAP EIVKNERYTY GVDWWGVGCL IYEMIEGKAP FRQRKEKVKR EEVERRVRED
QEKYSEKFSE AARTLCRGLL HKEPGFRLGC RRVGKPEDGA EEIRAHPFFN TADTATGREP
VPWKKMEAGK VTPPFCPDPR AVYAKDVLDI EQFSTVKGVR LDATDTQFYG KFNTGCVSIP
WQSEMIETEC FAELNTFYEE DGSLVWNLRP DGINMEERRN GTSKPGFFSR LFRKKNIEVT
KSLHDLSRLG VDQQQPSTSA KPAAVRSSRA ASASGRTSMI
//
