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Database: UniProt
Entry: W2QWB8_PHYPN
LinkDB: W2QWB8_PHYPN
Original site: W2QWB8_PHYPN 
ID   W2QWB8_PHYPN            Unreviewed;      1245 AA.
AC   W2QWB8;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 44.
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=PPTG_05075 {ECO:0000313|EMBL:ETN17216.1};
OS   Phytophthora parasitica (strain INRA-310).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=761204 {ECO:0000313|EMBL:ETN17216.1, ECO:0000313|Proteomes:UP000018817};
RN   [1] {ECO:0000313|Proteomes:UP000018817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=INRA-310 {ECO:0000313|Proteomes:UP000018817};
RG   The Broad Institute Genome Sequencing Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA   Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D.,
RA   Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ETN17216.1, ECO:0000313|Proteomes:UP000018817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=INRA-310 {ECO:0000313|EMBL:ETN17216.1,
RC   ECO:0000313|Proteomes:UP000018817};
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 INRA-310.";
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};
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DR   EMBL; KI669567; ETN17216.1; -; Genomic_DNA.
DR   RefSeq; XP_008896799.1; XM_008898551.1.
DR   AlphaFoldDB; W2QWB8; -.
DR   EnsemblProtists; ETN17216; ETN17216; PPTG_05075.
DR   GeneID; 20175140; -.
DR   VEuPathDB; FungiDB:PPTG_05075; -.
DR   OrthoDB; 65703at2759; -.
DR   Proteomes; UP000018817; 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; 2.
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; PTHR24189; MYOTROPHIN; 1.
DR   PANTHER; PTHR24189:SF50; MYOTROPHIN-RELATED; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF13857; Ank_5; 1.
DR   Pfam; PF16095; COR; 1.
DR   Pfam; PF08477; Roc; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 6.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 5.
DR   PROSITE; PS50088; ANK_REPEAT; 5.
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:UP000018817};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT   REPEAT          40..67
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          84..116
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          117..149
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          150..182
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          183..215
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          310..533
FT                   /note="Roc"
FT                   /evidence="ECO:0000259|PROSITE:PS51424"
SQ   SEQUENCE   1245 AA;  140073 MW;  7959CC44CCDD4A30 CRC64;
     MKCKQEESLK RVWDKSDQEA AAAIITLLHQ GVDAKSPDGG AAIALQYALR NSRADVISLL
     LERGADVMSL LLEQGADVGT QDEDGKTALH YAVTSHNTDV MSLLLERGAD LAARYEDDET
     ILHYAVRNGD VDVISLLLEK GADVAATDNN GEIALHYAAS FGHTERILLL LDRGSDVNAS
     DNDQLTVLHH AVTRCSPEAV LLLLNKGADA NALTKDGLNP LSHMILVKED DPDDDYLGVV
     RLLCSQEPKL KLPPSTQSLA INQLGMLACA QYWQDRYEKK QPLLEIPSEV VKGGENAVEV
     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 GWFTQCAWKN GGVYEIHQLR
     HQLEAVKNIV VTSESCRLPR LWTLLYPRKG SHVELRIHSD VSGKCEHKAL QIPVNDNILT
     RYPKMFQFCI SALSAASVAI PNAVAVAAVN QVLEASKSAL NQKITAKEVL DRANLGAGEE
     KSSHELGMGP AERRAFLLQL LALHDPSFNE DTIGRACQLQ RGATKEGYYI WLSDDEYSDL
     KHCVTLCDPE SGPPVIPILA TTSSPEPSIS LRIIGAEGTW KPLTKMYCAW ELLRDLKVVG
     NGSTSKTACT EIGTSWESTA VKLNFVDSHI KMLRDCTLVI RVKKARSFTC CFRSDKVIVQ
     GETQLCDHVN ANCSTTQLIN VPISVATGTL TRTVNCQIKI KFIGP
//
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