ID A0A3B3VJT9_9TELE Unreviewed; 642 AA.
AC A0A3B3VJT9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=cGMP-dependent protein kinase {ECO:0000256|ARBA:ARBA00012428};
DE EC=2.7.11.12 {ECO:0000256|ARBA:ARBA00012428};
OS Poecilia latipinna (sailfin molly).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000025313.1, ECO:0000313|Proteomes:UP000261500};
RN [1] {ECO:0000313|Ensembl:ENSPLAP00000025313.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 AlphaFoldDB; A0A3B3VJT9; -.
DR STRING; 48699.ENSPLAP00000025313; -.
DR Ensembl; ENSPLAT00000001200.1; ENSPLAP00000025313.1; ENSPLAG00000012238.1.
DR GeneTree; ENSGT00940000154704; -.
DR Proteomes; UP000261500; Unplaced.
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; 2.
DR CDD; cd12085; DD_cGKI-alpha; 1.
DR CDD; cd05572; STKc_cGK; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR Gene3D; 1.20.5.490; Single helix bin; 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; IPR031831; PKcGMP_CC.
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:SF151; -; 1.
DR PANTHER; PTHR24353; CYCLIC NUCLEOTIDE-DEPENDENT PROTEIN KINASE; 1.
DR Pfam; PF00027; cNMP_binding; 2.
DR Pfam; PF16808; PKcGMP_CC; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF000559; cGMP-dep_kinase; 2.
DR PRINTS; PR00103; CAMPKINASE.
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; 1.
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 3: Inferred from homology;
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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000559-2};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 100..215
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 212..313
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 331..590
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 591..642
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 618..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 12..46
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 622..642
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 455
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000559-1"
FT BINDING 337..345
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000559-2"
FT BINDING 361
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000559-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 642 AA; 73127 MW; 779E135DC277A824 CRC64;
MSELEDDFAK ILLLKEERIR DLERRLADRE DEIHELKRKL HKCQSVLPSA QLIGPRTRRA
QGISAEPQTH QDLSRQTFRK YPKSDWSKDL IKEAILDNDF MKNLELSQIQ EIVDCMYPVE
YGKDSCIIKE GDVGSLVYVM EDGKVEVTKE SLKLCTMGPG KVFGELAILY NCTRTATVKT
LTNVKLWAID RQCFQTIMMR TGLIKHTEYM EFLKSASFLC LQGARGDTFF IISKGKVNVT
REDLPNGEPV YLHSLGKGDW FGEKALQGED IRTANVIAAE AVTCLVIDRD SFKHLIGGLE
DVSNKGHEDA DAKAKYEAEN AFFFNLNLAD FNIIDTLGVG GFGRVELVQL KSDENKTFAM
KILKKRHIVD TRQQEHIRSE KLIMQEAHSD FIVRLYRTFK DSKYLYMLME ACLGGELWTI
LRDRGSFEDS TTRFYTACVV EAFAYLHSKG IIYRDLKPEN LILDHRGYAK LVDFGFAKKI
GFGKKTWTFC GTPEYVAPEI ILNKGHDISA DYWSLGILMF ELLTGSPPFS GPDPMKTYNI
ILRGIDMIEF PKKITKNAAN LIKKLCRDNP CERLGNLKNG VKDIQKHKWF EGFNWEGLKK
GTLTPPIIPN VTSAVDTSNF DSFPEDNEDP PPDDTSGWDV DF
//
