ID A0A061HKM5_BLUGR Unreviewed; 952 AA.
AC A0A061HKM5;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU361162};
DE EC=2.7.11.21 {ECO:0000256|RuleBase:RU361162};
GN ORFNames=BGT96224_1762 {ECO:0000313|EMBL:EPQ67296.1},
GN BGT96224V2_LOCUS115 {ECO:0000313|EMBL:SUZ07484.1};
OS Blumeria graminis f. sp. tritici 96224.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Blumeria.
OX NCBI_TaxID=1268274 {ECO:0000313|EMBL:SUZ07484.1};
RN [1] {ECO:0000313|Proteomes:UP000053110}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=96224 {ECO:0000313|Proteomes:UP000053110};
RX PubMed=23852167; DOI=10.1038/ng.2704;
RA Wicker T., Oberhaensli S., Parlange F., Buchmann J.P., Shatalina M.,
RA Roffler S., Ben-David R., Dolezel J., Simkova H., Schulze-Lefert P.,
RA Spanu P.D., Bruggmann R., Amselem J., Quesneville H.,
RA Ver Loren van Themaat E., Paape T., Shimizu K.K., Keller B.;
RT "The wheat powdery mildew genome shows the unique evolution of an obligate
RT biotroph.";
RL Nat. Genet. 45:1092-1096(2013).
RN [2] {ECO:0000313|EMBL:EPQ67296.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=96224 {ECO:0000313|EMBL:EPQ67296.1};
RA Oberhaensli S., Wicker T., Keller B.;
RT "The wheat powdery mildew genome reveals unique evolution of an obligate
RT biotroph.";
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SUZ07484.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=96224 {ECO:0000313|EMBL:SUZ07484.1};
RA Quirk P.G., Krulwich T.A.;
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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; KE373660; EPQ67296.1; -; Genomic_DNA.
DR EMBL; UIGY01000001; SUZ07484.1; -; Genomic_DNA.
DR HOGENOM; CLU_000288_46_0_1; -.
DR OrthoDB; 5471704at2759; -.
DR Proteomes; UP000053110; 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; cd13118; POLO_box_1; 1.
DR CDD; cd14099; STKc_PLK; 1.
DR Gene3D; 3.30.1120.30; POLO box domain; 1.
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; 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 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; 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|RuleBase:RU361162, ECO:0000313|EMBL:EPQ67296.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000053110};
KW Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU361162};
KW Transferase {ECO:0000256|RuleBase:RU361162}.
FT DOMAIN 61..323
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 608..627
FT /note="POLO box"
FT /evidence="ECO:0000259|PROSITE:PS50078"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 952 AA; 108572 MW; 69888A62B26E3472 CRC64;
MDALSPRDVN AHLRVKQTKH LVLKQPAVNV KTSQKQKDHP PPPPAEVREP PSFDRKDGII
YKTGQMLGRG GFAICYEAQN LNTQQIYALK IVKSHMPQKR MEQKFQTELQ IHSKMKHPNI
VEFHRAFSYL NCTYIVLELC PNGSLMDMVK RRKYITEPEA RYWTVQIAGA VKYMHGKGII
HRDLKMGNIF LDKNMDVKIG DFGLAALIMS GKDLQACRRT TLCGTPNYIA PEILSKEKGG
HDHAVDIWSL GIIIFAMLTG KPPFQSETAD EIYRRARERD YDWPSLDSTE NLISKDTKDL
VSKLLQPAHL RPDPDQIVQH SFFMCGWTPR QEEMSISLRE KHISPKKYFS EINFSANMTV
SNRNLKKLCV KCGVGPWTPA KKYTSTYREV AEEEKLGLTP AVPLAEDVVY HPFHAWLQDQ
VQSIQEHGEN AEAALKILEK IISPASKSKY TGIPTSRTPI QSFAAQQRAK DSKQSVSQRQ
AQINRIGGDK TYVDRPMPPI KTEMKIRDAM VDIEDRLAVD MLHKLKLNAH EENRDKFTQP
SIQRLKKISI FDEREKAELV PNTKPSHVLL RLCHLRTEIE RALKARSPAT EVKTPTKSPV
IVVKWVDYTN KFGLGYILSN GSVGTLFRAM PTSQHGSKKE SCPSTCVLIR DSEKHLINQS
NPDWAHYGQL VPLSGCKVEF FENRGDEGLF SASVDSENFK ATPGPNGEMF KLSASRDEFD
SRKKERVALW RKFGNYMTHY GRDTEYTQEE SHCHNSEQEH AIKNTVTFYQ RWGDVGCWGF
GDGQLQFNFP DHTKIILSSD GTWCDFYHLP LQAAHELSEK GIISAQALDE RQHLSYPLKT
MLNFKPKLTR SRSQRQAIID PLVQEIPSAN DFRRKIEFIF QCITEWTQNG GIGISDLTAK
GRLRWSGARQ SVNTKMPYKH VWVCVGGQAT DERKVAWFDP RNPDVVLPDI EG
//
