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Database: UniProt
Entry: W2LFZ8_PHYPR
LinkDB: W2LFZ8_PHYPR
Original site: W2LFZ8_PHYPR 
ID   W2LFZ8_PHYPR            Unreviewed;      1157 AA.
AC   W2LFZ8;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=BUB protein kinase {ECO:0000313|EMBL:ETL96372.1};
GN   ORFNames=L917_06112 {ECO:0000313|EMBL:ETL96372.1};
OS   Phytophthora parasitica (Potato buckeye rot agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4792 {ECO:0000313|EMBL:ETL96372.1};
RN   [1] {ECO:0000313|EMBL:ETL96372.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CHvinca01 {ECO:0000313|EMBL:ETL96372.1};
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 CHvinca01.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KI678920; ETL96372.1; -; Genomic_DNA.
DR   AlphaFoldDB; W2LFZ8; -.
DR   EnsemblProtists; ETL96372; ETL96372; L917_06112.
DR   VEuPathDB; FungiDB:PPTG_02534; -.
DR   Proteomes; UP000054423; Unassembled WGS sequence.
DR   GO; GO:0000776; C:kinetochore; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.40.430; -; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR015661; Bub1/Mad3.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR013212; Mad3/Bub1_I.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   PANTHER; PTHR14030:SF4; BUB1 KINASE, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR14030; MITOTIC CHECKPOINT SERINE/THREONINE-PROTEIN KINASE BUB1; 1.
DR   Pfam; PF08311; Mad3_BUB1_I; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00777; Mad3_BUB1_I; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51489; BUB1_N; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:ETL96372.1};
KW   Transferase {ECO:0000313|EMBL:ETL96372.1}.
FT   DOMAIN          127..284
FT                   /note="BUB1 N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51489"
FT   DOMAIN          840..1152
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          44..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          320..342
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          354..413
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          519..570
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        373..390
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        519..539
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        555..570
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1157 AA;  132142 MW;  39C977D9BDFDF621 CRC64;
     MNTALVVTRA RLQYVTVVRY LLSNLAGFQN FELEREVRTR SAHTIQNPSV VRDERDRQRS
     SQKPTPMTMD AALSDRKRKA DAFEWEASKE NVMPLKRGRN VADLNKALRA HDSFQTKLRL
     EDELKAKQDA VEAYNGDDPL AAWLEYIRWL EVKMPEDTRK KFTALEKCTR ELKDNPHYKN
     DMRYIRLWIQ YADLVSNPKD IFKYLYQNKI GERVSLFYIG WAYVLETMAN YPQAHKIYLK
     AGQKNAEPQD LLERKYKEFQ RRMSRQWLRM TEETGANGID ERQQLHQHRA SARVQRIQKA
     NAHKPVFVVY EDPVGHSVDP FDGNGGWKKL GTMQQQDKEN EMAPSAWNTL AARGESGAGA
     GRQSDRRSPP GRNSRPQDAS TLQVFVDEEF SVSESEQKRR TPLTHRSQTL RQRLDGVATE
     EEMLAQEPLK NFTASDKKAR AQKQVTKGRS EKSCYDVEQI TSSTGDAISF EEIRASAYQQ
     AVDRHRELEH RALHDVTHEV DSASNVTLSL SAATSSVTAS VASHRANPSA PTTTSSTSRE
     VESPERKPAP LATAAQTAAV STHNGEQEDM TINTRVALED INSMFCSPPR QPKPSVWDAK
     EGDPVERKLH FSVFEDSVDS VALNAQDQSQ RQDINESIPK QTFQVFKDDA SAEPLVGRKQ
     DFQIFSDGAP EEPRTGKAFQ VFSDDVPEEP RTGKTSWSQK RKPLGARDDL VCSVRLTNKD
     VLMRVQKDAA EKDSTESRWI QGTTKNLARE GSSRNITQPT PKSVTHLSTK VPVAALVLDP
     YTFENRQNLI LDRRVDWYLC SRPDAVKLHS QTLPRVPCTN PVKRKLPKPI VFKASTTLTV
     QLVGVLGSGS FAYVFSAKVV DTTINSTRNK AVKIEKERQN LAWEFYITNK IKKKLRIERG
     IPDEKIPVPT LTELHLFSNG ALLIMDKGHV GTLFDVLNCY KQWGTTFPEV LAVYYGIKML
     RCIELLHSAN VLHGDIKPDN WLMIPGNPSS ELELISQEPK LDKVYQAGDL YLIDYGRSID
     LSFYPDGTVF RGSCHAKGFQ CVEMLTQRPW TYQIDTFAFC GTMHCMLFGE YMEVKPKRNA
     KGATHWGIVR QFKRYWQVDM WENFFHVLLN VHSCTDQPSL LNLRRRMERY FVSDRSRQQE
     LFKQLSRQDS VLRKTTV
//
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