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Database: UniProt/TrEMBL
Entry: D0NEA4_PHYIT
LinkDB: D0NEA4_PHYIT
Original site: D0NEA4_PHYIT 
ID   D0NEA4_PHYIT            Unreviewed;       767 AA.
AC   D0NEA4;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   24-JAN-2024, entry version 71.
DE   RecName: Full=Serine/threonine-protein kinase PLK {ECO:0000256|RuleBase:RU361162};
DE            EC=2.7.11.21 {ECO:0000256|RuleBase:RU361162};
DE   AltName: Full=Polo-like kinase {ECO:0000256|RuleBase:RU361162};
GN   ORFNames=PITG_10092 {ECO:0000313|EMBL:EEY56549.1};
OS   Phytophthora infestans (strain T30-4) (Potato late blight agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=403677 {ECO:0000313|EMBL:EEY56549.1, ECO:0000313|Proteomes:UP000006643};
RN   [1] {ECO:0000313|Proteomes:UP000006643}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T30-4 {ECO:0000313|Proteomes:UP000006643};
RX   PubMed=19741609; DOI=10.1038/nature08358;
RG   The Broad Institute Genome Sequencing Platform;
RA   Haas B.J., Kamoun S., Zody M.C., Jiang R.H., Handsaker R.E., Cano L.M.,
RA   Grabherr M., Kodira C.D., Raffaele S., Torto-Alalibo T., Bozkurt T.O.,
RA   Ah-Fong A.M., Alvarado L., Anderson V.L., Armstrong M.R., Avrova A.,
RA   Baxter L., Beynon J., Boevink P.C., Bollmann S.R., Bos J.I., Bulone V.,
RA   Cai G., Cakir C., Carrington J.C., Chawner M., Conti L., Costanzo S.,
RA   Ewan R., Fahlgren N., Fischbach M.A., Fugelstad J., Gilroy E.M., Gnerre S.,
RA   Green P.J., Grenville-Briggs L.J., Griffith J., Grunwald N.J., Horn K.,
RA   Horner N.R., Hu C.H., Huitema E., Jeong D.H., Jones A.M., Jones J.D.,
RA   Jones R.W., Karlsson E.K., Kunjeti S.G., Lamour K., Liu Z., Ma L.,
RA   Maclean D., Chibucos M.C., McDonald H., McWalters J., Meijer H.J.,
RA   Morgan W., Morris P.F., Munro C.A., O'Neill K., Ospina-Giraldo M.,
RA   Pinzon A., Pritchard L., Ramsahoye B., Ren Q., Restrepo S., Roy S.,
RA   Sadanandom A., Savidor A., Schornack S., Schwartz D.C., Schumann U.D.,
RA   Schwessinger B., Seyer L., Sharpe T., Silvar C., Song J., Studholme D.J.,
RA   Sykes S., Thines M., van de Vondervoort P.J., Phuntumart V., Wawra S.,
RA   Weide R., Win J., Young C., Zhou S., Fry W., Meyers B.C., van West P.,
RA   Ristaino J., Govers F., Birch P.R., Whisson S.C., Judelson H.S.,
RA   Nusbaum C.;
RT   "Genome sequence and analysis of the Irish potato famine pathogen
RT   Phytophthora infestans.";
RL   Nature 461:393-398(2009).
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=2.7.11.21; Evidence={ECO:0000256|RuleBase:RU361162};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. CDC5/Polo subfamily. {ECO:0000256|RuleBase:RU361162}.
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DR   EMBL; DS028134; EEY56549.1; -; Genomic_DNA.
DR   RefSeq; XP_002902623.1; XM_002902577.1.
DR   AlphaFoldDB; D0NEA4; -.
DR   STRING; 403677.D0NEA4; -.
DR   EnsemblProtists; PITG_10092T0; PITG_10092T0; PITG_10092.
DR   GeneID; 9461186; -.
DR   KEGG; pif:PITG_10092; -.
DR   VEuPathDB; FungiDB:PITG_10092; -.
DR   eggNOG; KOG0575; Eukaryota.
DR   HOGENOM; CLU_000288_46_1_1; -.
DR   InParanoid; D0NEA4; -.
DR   OMA; IQIHKSM; -.
DR   OrthoDB; 5471704at2759; -.
DR   Proteomes; UP000006643; Partially assembled 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; cd13118; POLO_box_1; 1.
DR   CDD; cd13117; POLO_box_2; 1.
DR   CDD; cd14099; STKc_PLK; 1.
DR   Gene3D; 3.30.1120.30; POLO box domain; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR033701; POLO_box_1.
DR   InterPro; IPR033695; POLO_box_2.
DR   InterPro; IPR000959; POLO_box_dom.
DR   InterPro; IPR036947; POLO_box_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24345; SERINE/THREONINE-PROTEIN KINASE PLK; 1.
DR   PANTHER; PTHR24345:SF0; SERINE/THREONINE-PROTEIN KINASE PLK1; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00659; POLO_box; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF82615; Polo-box domain; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50078; POLO_BOX; 2.
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:0000256|RuleBase:RU361162};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000006643};
KW   Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU361162};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361162}.
FT   DOMAIN          127..384
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          561..631
FT                   /note="POLO box"
FT                   /evidence="ECO:0000259|PROSITE:PS50078"
FT   DOMAIN          686..754
FT                   /note="POLO box"
FT                   /evidence="ECO:0000259|PROSITE:PS50078"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          55..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          400..492
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..36
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..74
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        471..492
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         160
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   767 AA;  85782 MW;  69E18A16D1D44BF3 CRC64;
     MTMQARDPTE VLTTENKENS AAGSNQTSAT MRAKLRNSSD ASRRVYDSDR FKLVQSRRGS
     GASSPGHALQ TSNQDENVEM DRLVDAVPPP APAAQKKKKE PTPQPVVPDQ ILEAYLDTKG
     YVKTRTYIKG KFLGKGGFAR CYEVKCDQTG KIYAGKVVAK SSLVKPKAKQ KFTSEIKIHK
     SLHHPQVVQF EHFFEDSDNA YILLELCRNQ SMSDLMRRRK RLSESEVRFY MRQLVDGLAY
     LHKNLVIHRD LKLGNLFLTS DMRLKIGDFG LATRLDNPED RKRTMCGTPN YIAPEILSGQ
     RGDGHSFEVD IWSTGVVMYT LLVGRPPFET DDVKATYKRI RANQYEFPDT VHVSRSAQSL
     IRGILRSDPG ARPSLEQILK HPFLADEFVP TALPRTALMV TPPSCKPPSF ASRHSDSERF
     VRSTGVKVPP PRAASKRYPL KTRDDNQRAS DPGTSPALAQ SLPPAYKRDG SGRTSGSSSS
     NRRTERSTAV ETSQTVLEAA YKSLSRFFYL QEHSRDGRLS ASSSAASIVA EAQKLKQIRD
     EAAEMQPLVA ASLWISQWVD YTTKYGIGYM LSNGGSGVYF NDSTKMISSA DGKVFEYIER
     QSSQTSGPEA HARYTVENYD PVLSKKVTLL GHFKGYLVDA RAENDEADTL ESQLARSFVL
     SSREVNTDTS SDDGASQSMV FVKKWVKTRH AVLFQLSNGT IQFNFFDKSK LMLSSNARVA
     TYLNREGDLT VFSSSMAILT SERPDLAKRL RYAKDMLQQM VRPPEHK
//
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