ID H3HDS7_PHYRM Unreviewed; 564 AA.
AC H3HDS7;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=AGC protein kinase {ECO:0008006|Google:ProtNLM};
OS Phytophthora ramorum (Sudden oak death agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=164328 {ECO:0000313|EnsemblProtists:Phyra96430, 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:Phyra96430}
RP IDENTIFICATION.
RC STRAIN=Pr102 {ECO:0000313|EnsemblProtists:Phyra96430};
RG EnsemblProtists;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00009903}.
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DR EMBL; DS566074; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3HDS7; -.
DR STRING; 164328.H3HDS7; -.
DR EnsemblProtists; Phyra96430; Phyra96430; Phyra96430.
DR VEuPathDB; FungiDB:PSURA_96430; -.
DR eggNOG; KOG0690; Eukaryota.
DR HOGENOM; CLU_000288_163_0_1; -.
DR InParanoid; H3HDS7; -.
DR OMA; EMFDSTT; -.
DR Proteomes; UP000005238; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06093; PX_domain; 1.
DR CDD; cd05123; STKc_AGC; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR045270; STKc_AGC.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR PANTHER; PTHR24351:SF234; SERINE/THREONINE-PROTEIN KINASE YPK2/YKR2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50195; PX; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000005238};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..114
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 202..460
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 461..548
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT BINDING 231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 564 AA; 63487 MW; E91F54B1536C7EE1 CRC64;
MATLSVLITG FGVARDGGQA DCVVFLGTVQ QGGGGPWTVY RPFEAFQRLG QQLAMIFGQA
VPACPPHTFD MRFPDSLEKA RVDLSMWMMQ LLQHPPIYQS HVFVDFVSAD ANVPPPGMQG
PAMGGRAANV VGDLDMDEMF DSTTDDDPRE LRDDDMFQFD YNTDMSGAGL DQQTLLEETQ
MQHNQQLQEK KKRSEKVTLE DFVMIKVIGK GSFGKVLLVR KRDTGLIYAM KVLRKENIIK
RNQVEHTRTE RHVLGYVRHP FIVGLNYAFQ TSEKLYFVLD YCAGGELFFH LGKVQRFPEH
RARFYAAEIT LAIEYVHNLD VIYRDLKPEN VLLDENGHIR LTDFGLSKEG IQDDFSGANS
FCGTPEYLAP EILNRSGHGR AVDWWSLGAL LYEMLTGLPP FYCRDRDRLF EKIRKGDLSF
PKYLSPNAKD LLKKLLERDP TQRLGTGPTD AGEIKNHPFF AEIKWDALAT GQLPPPWRPT
FSGALDTSQF DREFTDMPVV SPDNHVRGMA MAMGRRPANG AAYGSSLTGN DPFKGFTYTE
DSYLQDVLQA EEVAVCGTTT CDHK
//