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Database: UniProt
Entry: A0A0W8CA52_PHYNI
LinkDB: A0A0W8CA52_PHYNI
Original site: A0A0W8CA52_PHYNI 
ID   A0A0W8CA52_PHYNI        Unreviewed;       445 AA.
AC   A0A0W8CA52;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=AP-2 complex subunit alpha {ECO:0000313|EMBL:KUF92772.1};
DE   SubName: Full=Kinase 2 protein {ECO:0000313|EMBL:KUF80968.1};
GN   ORFNames=AM587_10008219 {ECO:0000313|EMBL:KUF80968.1}, AM588_10004038
GN   {ECO:0000313|EMBL:KUF92772.1};
OS   Phytophthora nicotianae (Buckeye rot agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4790 {ECO:0000313|EMBL:KUF80968.1, ECO:0000313|Proteomes:UP000052943};
RN   [1] {ECO:0000313|Proteomes:UP000052943, ECO:0000313|Proteomes:UP000054636}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 0 {ECO:0000313|Proteomes:UP000052943}, Race 0
RC   {ECO:0000313|EMBL:KUF80968.1}, Race 1 {ECO:0000313|EMBL:KUF92772.1},
RC   and race 1 {ECO:0000313|Proteomes:UP000054636};
RA   Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT   "Genomes and virulence difference between two physiological races of
RT   Phytophthora nicotianae.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily.
CC       {ECO:0000256|RuleBase:RU000304}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KUF80968.1}.
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DR   EMBL; LNFO01004476; KUF80968.1; -; Genomic_DNA.
DR   EMBL; LNFP01000443; KUF92772.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0W8CA52; -.
DR   STRING; 4790.A0A0W8CA52; -.
DR   EnsemblProtists; KUF80968; KUF80968; AM587_10008219.
DR   EnsemblProtists; KUF92772; KUF92772; AM588_10004038.
DR   OMA; CVIYDMM; -.
DR   OrthoDB; 3028764at2759; -.
DR   Proteomes; UP000052943; Unassembled WGS sequence.
DR   Proteomes; UP000054636; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd05123; STKc_AGC; 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; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR045270; STKc_AGC.
DR   PANTHER; PTHR24351:SF247; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KUF80968.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000052943};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|RuleBase:RU000304};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          109..369
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          370..443
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   REGION          1..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..72
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         138
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   445 AA;  49733 MW;  FA319A7003B53C9C CRC64;
     MGNKGSKGAK SLRPPIKSDS RGFKFGNYAN GGRDAGKSAP AAPSYPSNGP PPAPGQAQAQ
     QQQQQQQQQQ QTEEESDLED DDSGPIEQVA IEDMDGPARP QTKVNVEDFD LLKVLGKGSF
     GKVMMVRKKD TKMIYAMKTL RKAALVKRNQ LLHTKTERSI LQSIKHPYLT SLTYAFQTPD
     KLYLVMDYCG GGELFFWLKK DRRFSQQKAR LFAAEIILAL QELHKHDIIY RDLKPENILL
     DLEGHIRLTD FGLSKEAVTG AGATGGTKTF CGTPEYLAPE ILENKGHGKA VDWWSLGTLI
     YEMLTGLPPF YDQNMQRMYD KILNAPLRFP SFMSAEAKDL LTGLLTRKVA DRLGSGPTDA
     EEIKSHPFFK GIDWEAVLRK EVQPEFKPPN RLGSMDTSNF DVEFTAEKPV DSVVTTTMSE
     TQRNKAQFPG FTYNADTIDE DHKGN
//
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