ID H2KYN2_CAEEL Unreviewed; 617 AA.
AC H2KYN2;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=cGMP-dependent protein kinase {ECO:0000256|ARBA:ARBA00012428};
DE EC=2.7.11.12 {ECO:0000256|ARBA:ARBA00012428};
GN Name=pkg-2 {ECO:0000313|EMBL:CCD63997.1,
GN ECO:0000313|WormBase:C09G4.2c};
GN ORFNames=C09G4.2 {ECO:0000313|WormBase:C09G4.2c}, CELE_C09G4.2
GN {ECO:0000313|EMBL:CCD63997.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CCD63997.1, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CCD63997.1, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CCD63997.1,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.12;
CC Evidence={ECO:0000256|ARBA:ARBA00000962};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.12; Evidence={ECO:0000256|ARBA:ARBA00000555};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. cGMP subfamily. {ECO:0000256|ARBA:ARBA00006352}.
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DR EMBL; BX284604; CCD63997.1; -; Genomic_DNA.
DR RefSeq; NP_741467.1; NM_171401.6.
DR AlphaFoldDB; H2KYN2; -.
DR SMR; H2KYN2; -.
DR STRING; 6239.C09G4.2c.1; -.
DR EPD; H2KYN2; -.
DR PaxDb; 6239-C09G4-2c; -.
DR EnsemblMetazoa; C09G4.2c.1; C09G4.2c.1; WBGene00015650.
DR GeneID; 177659; -.
DR KEGG; cel:CELE_C09G4.2; -.
DR AGR; WB:WBGene00015650; -.
DR WormBase; C09G4.2c; CE31158; WBGene00015650; pkg-2.
DR eggNOG; KOG0614; Eukaryota.
DR InParanoid; H2KYN2; -.
DR OMA; FPAFDNF; -.
DR OrthoDB; 10768at2759; -.
DR PhylomeDB; H2KYN2; -.
DR Reactome; R-CEL-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
DR Reactome; R-CEL-9648002; RAS processing.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00015650; Expressed in larva and 3 other cell types or tissues.
DR ExpressionAtlas; H2KYN2; baseline and differential.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW.
DR GO; GO:0004692; F:cGMP-dependent protein kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00038; CAP_ED; 1.
DR CDD; cd05572; STKc_cGK; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR002374; cGMP_dep_kinase.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR035014; STKc_cGK.
DR PANTHER; PTHR24353:SF91; -; 1.
DR PANTHER; PTHR24353; CYCLIC NUCLEOTIDE-DEPENDENT PROTEIN KINASE; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF000559; cGMP-dep_kinase; 2.
DR SMART; SM00100; cNMP; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00888; CNMP_BINDING_1; 1.
DR PROSITE; PS00889; CNMP_BINDING_2; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000559-
KW 2}; cGMP {ECO:0000256|ARBA:ARBA00022535};
KW cGMP-binding {ECO:0000256|ARBA:ARBA00022992};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CCD63997.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000559-2};
KW Proteomics identification {ECO:0007829|EPD:H2KYN2};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 72..187
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 310..565
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 566..617
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT COILED 5..32
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 432
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000559-1"
FT BINDING 316..324
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000559-2"
FT BINDING 338
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000559-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 617 AA; 70852 MW; 0261DC699241D38A CRC64;
MDFTREALLA ELELKDDIIE QLRKELDEYR MMNTTRKTAI SSEPDIQVKR PIIGKSDAAF
ETIGNALRLN SFLRNLDATQ IEKISSAMYP VEVPAGAIII RQGDLGSIMY VIQEGKVQVV
KDNRFVRTME DGALFGELAI LHHCERTATV RAIESCHLWA IERNVFHAIM MESAREKTMS
FKRHLKYSAR FGGYPEEVLL RIAEFCTEMR YDAREELVVK PQYVYLVCRG SVLCDDQGEV
SKIVAGQDFE LRCGRKGRFE RFFVLEGPAH LIKMHVEQLC KALDTTDLDD EIRPRASSTI
EEADVELEDL QRVSTLGMGG FGRVELVRSA SSRTYALKIM NKAHIVETKQ ESHVVSERRI
LMQCDNDYIV RMYKTYRDSE KIYMLMEPCL GGEIWTILRK KGRFDNDLTR FYCAGAMEAL
EYLHRKNIVY RDLKPENMLL DRNGWPKLVD FGFAKKLKNG GRTWTFCGTA EYVAPEIVLN
KGHDLSVDIW ALGIFMCELL TGSPPFSSTD PMVTYNAILK GLEKWAWPRF VTKEAIDMML
SLCKYEPTER LGFGDIGEIR HHIWFDNFDF VGFRAHRIRP PFIPSVANDI DTSNFDTFPA
FDNFASGSDE SGWDIDF
//
