ID W5MJV8_LEPOC Unreviewed; 757 AA.
AC W5MJV8;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
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 Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000008667.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000008667.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 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; AHAT01014534; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01014535; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01014536; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5MJV8; -.
DR Ensembl; ENSLOCT00000008677.1; ENSLOCP00000008667.1; ENSLOCG00000007145.1.
DR GeneTree; ENSGT00940000159393; -.
DR HOGENOM; CLU_000288_73_2_1; -.
DR Proteomes; UP000018468; Linkage group LG2.
DR Bgee; ENSLOCG00000007145; Expressed in mesonephros and 2 other cell types or tissues.
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:SF24; PROTEIN KINASE CGMP-DEPENDENT 2; 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 3: Inferred from homology;
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}; Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000559};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000559};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
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 164..279
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 282..395
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 448..706
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 707..757
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT COILED 49..83
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 571
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000559-1"
FT BINDING 454..462
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000559-2"
FT BINDING 477
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000559-2"
FT BINDING 481
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 757 AA; 86959 MW; B8C79E3B1817B058 CRC64;
MGNGSVKPKQ IKQPDRTVGT SEILRFKVSD LEKESKRKDE ELRDKDYKIK GLQEQLVKQT
TVISELTEEL QNKCIQLNKL QDVVKTQGGQ SLHPSPLKVR FSQHVSDFFS HTLNKRKGAK
EGVSAEPTSA STSRFPKFSF EKVRVRKDSS VKKLITEALN KNQFLKRLET QQIRDMVECM
YERTYNQGEY VIKQGEPGNH LFVLAEGHLD VFQQSKLLTT ISMWTAFGEL AILYNCTRTA
SVRAVTNVKT WALDREVFQN ITRRTAQARH EQYRNFLRSV SLLANLPEDK LCKIVDCLEV
EYYDKGDYVI REGEEGSTFY IIAKGKVKVT QSTQDHVEPQ TIKTLQKGDY FGEKALISDD
VRSANIIADE NDVECLVIDR ETFNQTVGTY DELQKYLQGY VANLTRADEK RHAKRSACMH
WASALSLELI QLKEKVSSFS SSSPFENLEV IATLGVGGFG RVELVKVRNE DIAFALKCIK
KKHIVDTRQE EHIHSERKIL EETCCPFIVQ LYRTFKDTKC VYMLMEACLG GEIWSLLRDR
GSFDDHTAKF CTGCVTEAFD YLHQNSILYR DLKPENLMLD SEGYIKLVDF GFAKKIECGQ
KTWTFCGTPE YVAPEIILNK GHDFSVDFWS LGILVFELLT GNPPFCGSDQ MMTYNFILKG
IEKMDFPKKI TRRPEDLIRK LCKQNPTERL GNLKNGITDI KKHRWFNGFN WEGLKARSLM
SPLKRELKGP TDHSYFDNYP PDVDIPPDEL SGWDNDF
//
