ID H3H125_PHYRM Unreviewed; 761 AA.
AC H3H125;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=cGMP-dependent protein kinase {ECO:0000256|ARBA:ARBA00012428};
DE EC=2.7.11.12 {ECO:0000256|ARBA:ARBA00012428};
OS Phytophthora ramorum (Sudden oak death agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=164328 {ECO:0000313|EnsemblProtists:Phyra83909, ECO:0000313|Proteomes:UP000005238};
RN [1] {ECO:0000313|Proteomes:UP000005238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pr102 {ECO:0000313|Proteomes:UP000005238};
RX PubMed=16946064; DOI=10.1126/science.1128796;
RA Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H., Aerts A.,
RA Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA Damasceno C.M., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.K.,
RA McDonald W.H., Medina M., Meijer H.J., Nordberg E.K., Maclean D.J.,
RA Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA Rose J.K., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA Smith B.M., Sobral B.W., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT of pathogenesis.";
RL Science 313:1261-1266(2006).
RN [2] {ECO:0000313|EnsemblProtists:Phyra83909}
RP IDENTIFICATION.
RC STRAIN=Pr102 {ECO:0000313|EnsemblProtists:Phyra83909};
RG EnsemblProtists;
RL Submitted (JUN-2015) 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 EMBL; DS566096; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3H125; -.
DR STRING; 164328.H3H125; -.
DR EnsemblProtists; Phyra83909; Phyra83909; Phyra83909.
DR VEuPathDB; FungiDB:PSURA_83909; -.
DR eggNOG; KOG0614; Eukaryota.
DR HOGENOM; CLU_000288_73_3_1; -.
DR InParanoid; H3H125; -.
DR OMA; IMSEANC; -.
DR Proteomes; UP000005238; Unassembled WGS sequence.
DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004691; F:cAMP-dependent protein kinase activity; IBA:GO_Central.
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 GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd00038; CAP_ED; 2.
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 PANTHER; PTHR24353; CYCLIC NUCLEOTIDE-DEPENDENT PROTEIN KINASE; 1.
DR PANTHER; PTHR24353:SF152; UT01108P-RELATED; 1.
DR Pfam; PF00027; cNMP_binding; 2.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF000559; cGMP-dep_kinase; 1.
DR PRINTS; PR00103; CAMPKINASE.
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; 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; 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 Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000559-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000005238};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 184..304
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 307..428
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 457..711
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 712..761
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 36..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 580
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000559-1"
FT BINDING 463..471
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000559-2"
FT BINDING 486
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000559-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 761 AA; 86304 MW; D342EB1A9E768DDB CRC64;
MGGGVSKHEY ERIRKELMLK DQVIRALQER LANGGYIGPM HASPGGDSDE KVTPERAAAA
TMVAKVRGKE KDKESRVSNA EHTLQKGGSF SSRFTLLDEA KELLRDSIDH SDSDAKSRYN
STDENGGPDS SGHTAGSKGK LRRVEVSAEV MPSRKIMSTK ERVVYPKGDS SRELLLKVLQ
SNVLFKGQSY GELRDCLDAF FPMRVEPGHF VIKQGAQGDN FYAVESGQLE ILVSMGEAPP
IRYGYLGPGL GFGELALLYN MPRAATIRAV TEVELWALER NTFREILASH KLNRLHRTLE
VLEKVAILSK LTSSEKQQVA AAMDWEEFEG KAAIVRQGEV GEKFYIITKG EIVVTQLDAN
TSEENIIRRL KAGDHFGEMA LFKDEMRSAT CTAVTRVQCV TLVREHFIAM LGTLQELMDR
EPAQLEAKHL AHRRASAEEL VDPADYKYYM EIPREELEVL QTLGRGAFGR VRLVRHAASN
RAYALKCLIK SHIVENNLKE HVLNEKRVML ALDHPFILKL YTTFKDRTHL YFLVELALGG
ELFTYLRRRD HFEEPIARFY IASVVLVFQH MHSKSIVYRD LKPENILLDN EGFMKLADFG
LAKLVTDRTW TLCGTPDYLA PEIILNKGHD KAVDYWALGI LIFELMTGSA PFYAQDPMQI
YALIIQGNIK FPAYMGRASV DLVQKLLCQN PARRLGNMKH GIKDIINHRW FSSFQWESLR
NKSMRPPIVP QVRDDFDTSN FEDFRHEVED PGNECDWDPD F
//
