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Database: UniProt
Entry: W2QVH4_PHYPN
LinkDB: W2QVH4_PHYPN
Original site: W2QVH4_PHYPN 
ID   W2QVH4_PHYPN            Unreviewed;      1003 AA.
AC   W2QVH4;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
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:ETN17222.1};
OS   Phytophthora parasitica (strain INRA-310).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=761204 {ECO:0000313|EMBL:ETN17222.1, 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:ETN17222.1, ECO:0000313|Proteomes:UP000018817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=INRA-310 {ECO:0000313|EMBL:ETN17222.1,
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; ETN17222.1; -; Genomic_DNA.
DR   RefSeq; XP_008896805.1; XM_008898557.1.
DR   AlphaFoldDB; W2QVH4; -.
DR   EnsemblProtists; ETN17222; ETN17222; 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; 3.
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; PF13606; Ank_3; 1.
DR   Pfam; PF16095; COR; 1.
DR   Pfam; PF08477; Roc; 1.
DR   SMART; SM00248; ANK; 5.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 4.
DR   PROSITE; PS50088; ANK_REPEAT; 4.
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          92..119
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          136..168
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          169..201
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          202..234
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          329..552
FT                   /note="Roc"
FT                   /evidence="ECO:0000259|PROSITE:PS51424"
SQ   SEQUENCE   1003 AA;  114068 MW;  3E7939A2857B67DC CRC64;
     MDTNEMKAPL QAVIDRLVEE REHVLGEERI TLASHLILGG IQDVLKCLER ERISSDTEES
     LKRVWDKSDQ EAAAAIITLL HQGVDAKSPD GGAAIALQYA LRNSRADVIS LLLERGADVM
     SLLLERGADL AARYEDDETI LHYAVRNGDV DVISLLLEKG ADVAATDNNG EIALHYAASF
     GHTERILLLL DRGSDVNASD NDQLTVLHHA VTRCSPEAVL LLLNKGADAN ALTKDGLNPL
     SHMILVKEDD PDDDYLGVVR LLCSQEPKLK LPPSTQSLAI NQLGMLACAQ YWQDRYEKKQ
     PLLEIPSEVV KGGENAVEVY LAELEKTDSS EVVHRQKICV VGRTKWGKTS LVRSITEETS
     VLVPLEDRTI GIEVFPLRFT VDGDGNKMKA THHDVTFWDF AGQGVYRVAH AVFFSKRTLY
     LVCVDLAAYN EILEQAKKES KTQRDEVPQR FFEKHILRWI VLILLRQPEA EFKLIGTKHD
     EVSDSSRSEI SHDIRDRLGQ FLEKLDGSIQ ITGHAATALK KEFEEGLVTT SVTNVESIQK
     VKNSIKHTIT AKPHLSFKMP ITYTRVINYI LEKRQSVVGA TNQDRMDKMI VSVRQLCKDL
     LKLPDFPQDT DCREILRVLH ELGDVLWYKG IDEELEKWII LDPSVVLDLV REVINHKYKE
     EVDEQYKVLS QNGILPHSLL MTFPSWKSLA AVEDKMVHLF KQLLHRLNLV YPVNDMEAID
     KADILVPMYW KTRETPKADL KLLATQKTIL TQDFGDSWHV ATWRYWLPIV VSDAIFVNFV
     VKCYRPFVHR SARRAYFESS VRREFRAVVN HSANKTGQYN DILIEVAAPT EKLAWAEMMY
     FVTDMEKILE KDYPGLTKHA RVKRFIVDDG EDRGVNDLME NPEDGKRQRA KARWLPPDFG
     WFTQCAWKNG GVYEIHQLRH QLEAVKNIVV TSESCRLPRL WTLLYPRKGS HVELRIHSDV
     SDVSVLYFCP VSSLCSHPQC RGCCRRESSF RSVEIGIKPK DHG
//
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