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Database: UniProt
Entry: V9E645_PHYPR
LinkDB: V9E645_PHYPR
Original site: V9E645_PHYPR 
ID   V9E645_PHYPR            Unreviewed;      1074 AA.
AC   V9E645;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   ORFNames=F443_18954 {ECO:0000313|EMBL:ETI34565.1};
OS   Phytophthora parasitica P1569.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=1317065 {ECO:0000313|EMBL:ETI34565.1, ECO:0000313|Proteomes:UP000018721};
RN   [1] {ECO:0000313|EMBL:ETI34565.1, ECO:0000313|Proteomes:UP000018721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P1569 {ECO:0000313|EMBL:ETI34565.1,
RC   ECO:0000313|Proteomes:UP000018721};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica P1569.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001433};
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=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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:ETI34565.1}.
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DR   EMBL; ANIZ01003313; ETI34565.1; -; Genomic_DNA.
DR   AlphaFoldDB; V9E645; -.
DR   EnsemblProtists; ETI34565; ETI34565; F443_18954.
DR   OrthoDB; 65703at2759; -.
DR   Proteomes; UP000018721; Unassembled WGS sequence.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 4.
DR   Gene3D; 3.30.70.1390; ROC domain from the Parkinson's disease-associated leucine-rich repeat kinase 2; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR032171; COR.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020859; ROC_dom.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR24193:SF121; ANK_REP_REGION DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR24193; ANKYRIN REPEAT PROTEIN; 1.
DR   Pfam; PF12796; Ank_2; 3.
DR   Pfam; PF16095; COR; 1.
DR   Pfam; PF08477; Roc; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 9.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 8.
DR   PROSITE; PS50088; ANK_REPEAT; 8.
DR   PROSITE; PS51424; ROC; 1.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW   ProRule:PRU00023}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018721};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT   REPEAT          40..72
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          73..107
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          108..140
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          141..173
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          174..206
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          207..239
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          240..272
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          273..305
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          400..623
FT                   /note="Roc"
FT                   /evidence="ECO:0000259|PROSITE:PS51424"
SQ   SEQUENCE   1074 AA;  121368 MW;  1AD76CE0A6F48D5A CRC64;
     MKCKQEESLK RVWDKSDQEA AAAIITLLHQ GVDAKSPDGG AAIALQYALR NSRADVISLL
     LERGADVNSQ DEFGDTALHR AIEQYRGNTA VISLLLQRGA DAAVQNVDGQ NALHYAAAIA
     NSEAISLLLK QGIDIDAQDE TGQTVLHYAT VIANTEVMSL LLEQGADVGT QDEDGKTALH
     YAVTSHNTDV MSLLLERGAD LAARYEDDET ILHYAVRNGD VDVISLLLEK GADVAATDNN
     GEIALHYAAS FGHTERILLL LDRGSDVNAS DNDQLTVLHH AVTRCSPEAV LLLLNKGADA
     NALTKDGLNP LSHMILVKED DPDDDYLGVV RLLCSQEPKL KLPPSTQSLA INQLGMLACA
     QYWQDRYEKK QPLLEIPSEV VKGGENAVEM YLAELEKTDS SEVVHRQKIC VVGRTKWGKT
     SLVRSITEET SVLVPLEDRT IGIEVFPLRF TVDGDGNKMK ATHHDVTFWD FAGQGVYRVA
     HAVFFSKRTL YLVCVDLAAY NEILEQAKKE SKTQRDEVPQ RFFEKHILRW IVLILLRQPE
     AEFKLIGTKH DEVSDSSRSE ISHDIRDRLG QFLEKLDGSI QITGHAATAL KKEFEEGLVT
     TSVTNVESIQ KVKNSIKHTI TAKPHLSFKM PITYTRVINY ILEKRQSVVG ATNQDRMDKM
     IVSVRQLCKD LLKLPDFPQD TDCREILRVL HELGDVLWYK GIDEELEKWI ILDPSVVLDL
     VREVINHKYK EEVDEQYKVL SQNGILPHSL LMTFPSWKSL AAVEDKMVHL FKQLLHRLNL
     VYPVNDMEAI DKADILVPMY WKTRETPKAD LKLLATQKTI LTQDFGDSWH VATWRYWLPI
     VVSDAIFVNF VVKCYRPFVH RSARRAYFES SVRREFRAVV NHSANKTGQY NDILIEVAAP
     TEKLAWAEMM YFVTDMEKIL EKDYPGLTKH ARVKRFIVDD GEDRGVNDLM ENPEDGKRQR
     AKARWLPPDF SWFTQCAWKN GGVYEIHQLR HQLEAVKNIV VTSESCRLPR LWTLLYPRKG
     SHVELRIHSD VSDVSVLYFC PVSSLCSHPQ CRGCCRRESS FRSVEIGIKP KDHG
//
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