ID B2Y2Z7_9BILA Unreviewed; 777 AA.
AC B2Y2Z7;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=cGMP-dependent protein kinase {ECO:0000256|ARBA:ARBA00012428, ECO:0000256|PIRNR:PIRNR000559};
DE EC=2.7.11.12 {ECO:0000256|ARBA:ARBA00012428, ECO:0000256|PIRNR:PIRNR000559};
OS Pristionchus sp. 11 RH-2008.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Diplogasteromorpha; Diplogasteroidea; Neodiplogasteridae;
OC Pristionchus.
OX NCBI_TaxID=511822 {ECO:0000313|EMBL:ACB59339.1};
RN [1] {ECO:0000313|EMBL:ACB59339.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=RS5228 {ECO:0000313|EMBL:ACB59339.1};
RX PubMed=18509055; DOI=10.1073/pnas.0708406105;
RA Hong R.L., Witte H., Sommer R.J.;
RT "Natural variation in Pristionchus pacificus insect pheromone attraction
RT involves the protein kinase EGL-4.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:7779-7784(2008).
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 ECO:0000256|PIRNR:PIRNR000559};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. cGMP subfamily. {ECO:0000256|ARBA:ARBA00006352,
CC ECO:0000256|PIRNR:PIRNR000559}.
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DR EMBL; EU375880; ACB59339.1; -; mRNA.
DR AlphaFoldDB; B2Y2Z7; -.
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:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00038; CAP_ED; 2.
DR CDD; cd05572; STKc_cGK; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 2.
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; CYCLIC NUCLEOTIDE-DEPENDENT PROTEIN KINASE; 1.
DR PANTHER; PTHR24353:SF111; PROTEIN KINASE CGMP-DEPENDENT 1; 1.
DR Pfam; PF00027; cNMP_binding; 2.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF000559; cGMP-dep_kinase; 1.
DR PRINTS; PR00104; CGMPKINASE.
DR SMART; SM00100; cNMP; 2.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00888; CNMP_BINDING_1; 2.
DR PROSITE; PS00889; CNMP_BINDING_2; 2.
DR PROSITE; PS50042; CNMP_BINDING_3; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000559};
KW cGMP {ECO:0000256|ARBA:ARBA00022535, ECO:0000256|PIRNR:PIRNR000559};
KW cGMP-binding {ECO:0000256|ARBA:ARBA00022992,
KW ECO:0000256|PIRNR:PIRNR000559};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000559};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000559};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|PIRNR:PIRNR000559};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000559}.
FT DOMAIN 197..312
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 315..428
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 466..726
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 727..777
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 740..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 590
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000559-1"
FT BINDING 472..480
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000559-2"
FT BINDING 496
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000559-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 777 AA; 86863 MW; 212AB1B8272DB6BE CRC64;
MSNNGSASAR SASGNSGGGG GGGIRGFFSK LRKPSGEAGG GGSSPSQVQI GTKMYDAHEL
QKLIPQLEDA VQKRDQQIRQ QQTIVETHVK RIAELEAEVT SLQRECDKLR SVLEQKAQNV
ANSPGARSPS NGSPRNDQDK HDKEVHDKLL DAASRAKKLA VSAEPAKLDS KPATLQHHIK
NAAAKQLIRD AVHKNDFLKQ LAKEQIIELV ECMYEMRARS GQWVIQEGEP GDRLFVVAEG
DLTVSREGVA LGTMRPGTVM GELAILYNCT RTASVQALTD VQLWVLDRSV FQMITMRLGM
ERQQQLMSFL TKVSIFENLP EDRISKIADV MDQDYYAGGH HIIRQGEKGD TFFIINNGQV
KVTQQIEGET EPREIRVLNQ GDFFGERALL GDELRTANII AMNPGVEVLT LDRESFLKLI
GDIDAVKKDY GDSDRLSQST VPIIEPPSPT KVALQAEFDQ VTLRNLKRLA TLGVGGFGRV
ELVCINGDKA RTFALKALKK KHIVDTRQQE HIFAERNIML ETNTDWIVKL YKTFRDTKYV
YMMLEVCLGG ELWTTLRDRG HFDDYTARFY VACVLEGLEY LHRRNIVYRD LKPENCLLAN
SGYLKLVDFG FAKKLAPGRK TWTFCGTPEY VSPEIILNKG HEQSADYWAL GIYICELMLG
RPPFQAADPM KTYTLILKGV DALEIPNRRI GKTATALVKK LCRDNPGERL GSGSGGVNDI
RKHRWFMGFD WEGLRNHTLK PPIQPKVQNP ADVTNFDNYP ADPDVPPDEF SGWDEGF
//
