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Database: UniProt
Entry: A0A0F8B1I8_CERFI
LinkDB: A0A0F8B1I8_CERFI
Original site: A0A0F8B1I8_CERFI 
ID   A0A0F8B1I8_CERFI        Unreviewed;      1395 AA.
AC   A0A0F8B1I8;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   18-JUN-2025, entry version 35.
DE   SubName: Full=Checkpoint serine/threonine-protein kinase bub1 {ECO:0000313|EMBL:KKF95056.1};
DE            EC=2.7.11.1 {ECO:0000313|EMBL:KKF95056.1};
GN   Name=bub1 {ECO:0000313|EMBL:KKF95056.1};
GN   ORFNames=CFO_g2581 {ECO:0000313|EMBL:KKF95056.1};
OS   Ceratocystis fimbriata f. sp. platani.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Microascales; Ceratocystidaceae; Ceratocystis.
OX   NCBI_TaxID=88771 {ECO:0000313|EMBL:KKF95056.1, ECO:0000313|Proteomes:UP000034841};
RN   [1] {ECO:0000313|EMBL:KKF95056.1, ECO:0000313|Proteomes:UP000034841}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFO {ECO:0000313|EMBL:KKF95056.1,
RC   ECO:0000313|Proteomes:UP000034841};
RA   Belbahri L.;
RT   "Genome sequence of Ceratocystis platani, a major pathogen of plane
RT   trees.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore
CC       {ECO:0000256|ARBA:ARBA00004629}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKF95056.1}.
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DR   EMBL; LBBL01000123; KKF95056.1; -; Genomic_DNA.
DR   OrthoDB; 643121at147550; -.
DR   Proteomes; UP000034841; Unassembled WGS sequence.
DR   GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:TreeGrafter.
DR   GO; GO:0032991; C:protein-containing complex; IEA:UniProtKB-ARBA.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051754; P:meiotic sister chromatid cohesion, centromeric; IEA:TreeGrafter.
DR   GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IEA:InterPro.
DR   CDD; cd13981; STKc_Bub1_BubR1; 1.
DR   FunFam; 1.25.40.430:FF:000003; Checkpoint serine/threonine-protein kinase BUB1; 1.
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; IPR012572; Mad3/Bub1_II.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
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; PF08171; Mad3_BUB1_II; 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.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Centromere {ECO:0000256|ARBA:ARBA00023328};
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW   Kinase {ECO:0000313|EMBL:KKF95056.1};
KW   Kinetochore {ECO:0000256|ARBA:ARBA00022838};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034841};
KW   Transferase {ECO:0000313|EMBL:KKF95056.1}.
FT   DOMAIN          63..222
FT                   /note="BUB1 N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51489"
FT   DOMAIN          1014..1395
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          17..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          443..488
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          505..541
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          557..890
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        445..461
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        468..484
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        505..518
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        663..677
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        730..763
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        773..790
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        796..812
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        816..827
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        855..870
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        876..888
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1395 AA;  156838 MW;  F0BD9F57351EFC61 CRC64;
     MSDAQDPVDF EILEGQKENI QSLPGGRSAR KLAQLYSPNP LKPLSTPNPA DTQDAHSAKR
     AEFEQEVAAI DESDDPLDVY DRYVRWTLEA YPSAQATPQS QLDQLLERAT KSFVSSAQYR
     NDPRYLKMWV YYIQFFSDAP RETFLFLSRH GIGESLALFY EEYATWLEGQ SRWAQAEEVY
     KLGIECEARP QARLLRKFKE FEHRMSEQPA ESVRPTSPAI PPVRAALAAK VDPFAIAMLP
     DDPQVPRPSA GLPGYASPKA NKTKGKMAIF SDSNAKEPAM GERATAGSRG WDSIGSLSER
     KKENVIEPKP WAGETLKAGG KKPSGPKMAI FKDTSQKSKI HSSQPSQTVF DQLSQYKISS
     ASDQVVVNPR TGKMERILVD LEVIYPQPDV RGAELSFEEV WARNRGWLDR SWEEEEGEER
     EMTMVDVDES VSQYDESFIL QQQRLQHEEE QRRQQEQEQQ KKPVQRQKKL EMYHDDTSIS
     RDENSPIQGT SRLEHQNMAV CRDSPEGRPH KMQIHRDGVV PQKQKLSIHR DDEPVVPKKQ
     KMAIHRDEFV DEENRLVSSL SSPVARPPVQ KIPIHRDEPV DENGMVIQQQ QKPAKSKKKI
     MDYNETQIIK AKLDSPSRPK ISKRKSIAAD PTMTIHTKSA TDDIYDIFNA PLPSKTGDKG
     GSDDDEEYDS DEYESDGESM GTTRNVDLED SDDDDAKSDW SDYTVKKKAS GLDDLTCKTN
     PDFTVRGVID DEEEEEEEDD GDDDDDESDE EEEGETEAEE QSEISEMRGP DEGNQSSQFS
     EQEPSLQSVE NDLVAQTGQQ TQQQQSHTIT HTKFIPVPPE DYVPPTRPYR DPAEVANNRL
     PFMTPITERT EMSLDFQQTQ GKTPSRSRGT MHSMPEEDED EDEDEDEEKA YNPTTDLNEA
     MSSPLIDMGK SPISYNTKIA QPAFPKPTTK ALAPKGPIIK DLQINPMDEG IRSQILDKTR
     PPLATYVGFF DHRDQNYEKG NEIRRFARAM SKAKSSGDHL AGPVIRLPDS QGMYTVKKEL
     GAGAFAPVYL VENSAPYSSQ ADEAIVLLGP KAPLSRHRNH LEALKMETPP SLWEFFMMRL
     THNRLGPQDR AAASLSYAHE LHLYRDEGFL VLPYHPHGTL LDVVNHFRAE PSGVMDEQLA
     MFFSIELLRT VEALHSKAIM HGDLKADNCL LRIDAASSAS GPASALATFG SAGSPDPETT
     VLTSQYHIDG SGGWATRGVT LIDFGRGIDM RAFVADQVQF IADWKTTSQD CAEMREGRSW
     TWHIDYHGLA GIIHTLLFGK YIETVRMDQG PGTTGGISGT AVGGPLNIGI GSRKYRIRES
     LKRYWQTDIW AECFDLLLNP GHFVERDGEG GRMPVTRGLK RVRESMEEWL SANCERGAGL
     KTLVNKVEAF AKGRR
//
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