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Database: UniProt
Entry: A0A3Q1EGS9_9TELE
LinkDB: A0A3Q1EGS9_9TELE
Original site: A0A3Q1EGS9_9TELE 
ID   A0A3Q1EGS9_9TELE        Unreviewed;       679 AA.
AC   A0A3Q1EGS9;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=cGMP-dependent protein kinase {ECO:0000256|PIRNR:PIRNR000559};
DE            EC=2.7.11.12 {ECO:0000256|PIRNR:PIRNR000559};
OS   Acanthochromis polyacanthus (spiny chromis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Acanthochromis.
OX   NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000002569.1, ECO:0000313|Proteomes:UP000257200};
RN   [1] {ECO:0000313|Ensembl:ENSAPOP00000002569.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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|PIRNR:PIRNR000559};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. cGMP subfamily. {ECO:0000256|PIRNR:PIRNR000559}.
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DR   AlphaFoldDB; A0A3Q1EGS9; -.
DR   STRING; 80966.ENSAPOP00000002569; -.
DR   Ensembl; ENSAPOT00000013225.1; ENSAPOP00000002569.1; ENSAPOG00000003968.1.
DR   GeneTree; ENSGT00940000165510; -.
DR   InParanoid; A0A3Q1EGS9; -.
DR   OrthoDB; 10768at2759; -.
DR   Proteomes; UP000257200; 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; 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; 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:SF118; PROTEIN KINASE CGMP-DEPENDENT 3; 1.
DR   Pfam; PF00027; cNMP_binding; 2.
DR   Pfam; PF00069; Pkinase; 1.
DR   PIRSF; PIRSF000559; cGMP-dep_kinase; 1.
DR   SMART; SM00100; cNMP; 2.
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; PS00888; CNMP_BINDING_1; 1.
DR   PROSITE; PS00889; CNMP_BINDING_2; 1.
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|PIRNR:PIRNR000559};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR000559};
KW   Reference proteome {ECO:0000313|Proteomes:UP000257200};
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          107..222
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          225..327
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          372..628
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   COILED          5..46
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        495
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000559-1"
FT   BINDING         378..386
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000559-2"
FT   BINDING         401
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000559-2"
FT   BINDING         411
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   679 AA;  78110 MW;  5399608C6369D7B3 CRC64;
     MEKQLEELKQ QLEKQCLINQ ELQRQNKDLQ QRLQEKEKLL QELHSQYHDL EFPSQSGNEI
     EPEVRKSRAA VIAPEPIPET LEITRTRVKK TVSETSLIVK AIQKNDFLSR LDDEQIAMMV
     DLLMVSNSKP GDEIIKEGSE GDTMYIVAAG ELLVTQAGRD LRTLTSGDIF GELAILYNCK
     RTATVKAKTA VHLWFMERQT YRTIITNKSK KKREQLMGFL KTSRTLKDLN DVQLSKIIDS
     MEEVKYQDKD VIVREGTEAD TFYIILKGEV LVTKNVNGHQ KQIRRMGKGE HFGEQALIRE
     VLRTATCAAD GPVTCFSIDK EVFEETIPIE HLELFDDSKV MQEAQAPEKS SPISTLRFKD
     LVPVLYQEGR YQGDPVTLGV GGFGRVELLT TVNHGKYYAM KRVSKKHIVA KRQEEHMLFE
     KKILKAIQCE FIVRLHGAFK DTRYIYMVME FCGGGEIWTK LKEVGRFDEN IAVFCTACVV
     EAYAYLHKKS IMYRDLKPEN LMLDVKGYIK LVDFGFAKEL VRGEKTYSFV GTPEYMAPEI
     IKNQGHDFAV DFWSLGILIF ELLVGSPPFS SSEPQKIYAK ILDGVLKYPP YLSEASKSII
     SKLCRNRPGQ RLGNTKNGIK DVRHHRWFSS INWHKLRMCQ LDAPTVRLIR KGPCYINFDR
     FPHDQTIADE DFSDWDRDF
//
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