ID A0A0D2CX20_9EURO Unreviewed; 1377 AA.
AC A0A0D2CX20;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 02-APR-2025, entry version 39.
DE RecName: Full=BUB protein kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV07_02309 {ECO:0000313|EMBL:KIW35623.1};
OS Cladophialophora immunda.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW35623.1, ECO:0000313|Proteomes:UP000054466};
RN [1] {ECO:0000313|EMBL:KIW35623.1, ECO:0000313|Proteomes:UP000054466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW35623.1,
RC ECO:0000313|Proteomes:UP000054466};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora immunda CBS83496.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore
CC {ECO:0000256|ARBA:ARBA00004629}.
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DR EMBL; KN847040; KIW35623.1; -; Genomic_DNA.
DR RefSeq; XP_016255839.1; XM_016388911.1.
DR STRING; 569365.A0A0D2CX20; -.
DR GeneID; 27341503; -.
DR VEuPathDB; FungiDB:PV07_02309; -.
DR HOGENOM; CLU_002115_1_0_1; -.
DR OrthoDB; 248495at2759; -.
DR Proteomes; UP000054466; 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:0004672; F:protein kinase activity; IEA:InterPro.
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 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 Kinetochore {ECO:0000256|ARBA:ARBA00022838};
KW Reference proteome {ECO:0000313|Proteomes:UP000054466}.
FT DOMAIN 71..230
FT /note="BUB1 N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51489"
FT DOMAIN 1026..1377
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 242..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 859..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 992..1015
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1049..1074
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..571
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..620
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..656
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..870
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 899..915
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1049..1058
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1377 AA; 152525 MW; F86ACBD996E976DE CRC64;
MAAPVAADSD LINFDIIETH KENIQSLPGG RSVKQLASIL SPLPSSRTLG SGAPPTLEET
KTLNDAIRQE YEIELQSIAD SDDPLDIYDR YVKWTLNAYP SAQATPQSQL LPLLERATKA
FLTSTHYKND PRYLKLWLHY IRLFSDTPRE TFAFLARHGI GEGLGLFYEE FAAWLEAAGR
WVQADEVYKL GIEREARPTE RLARKYAQFQ QRFDARPQVD DEPSSPALPT VRPALAAKID
PFASAHRGDD PQVARQRNGL AGSSAPASRS GKPKMAIFSD VDSAQQQPLA ANNTKGWDSI
GSMKERKKEN TIEARSWAGE KLKAGGKVGS VPKMEIFKDP ASRTQGQPKR SLPTQDSQQP
HQVVNPRTGR AERVFVDLEA IYPADTDLEF SFEELRAMSR GWAQRDWRPQ EATPLRATAG
NTVANAKSKV TKSREPEDVE NLTKSFADKV DLNNGANSTL SVHDVSTQSM VGMPESDSQL
ATKPPKQKEK KLKIREVKQE TQTVKTRLES PTGKKLKRKN SSQEPTMTFH SKAATNEIYD
MFNQPLRRPT TARDDTQSGD ETDFTEGEVD DGYSTAGDAE STDTGRVSAP GSEYGDDTLA
SMRRNQTQSQ SQSESVSPWS DFTTSKHVPR LDSAQLASVK DKAPSVKNHR RVKHHKDRSE
DMTESMDSSS QNQTQSSGFG AFDTQAIAAI AEGNFDDLDT KAIAMMAGDI DEGVADAGDV
DIEQDVTVAT SINHTTPVDE KAQHLEASDN HAGADDEALA TPIDDEFAEH REISHKPRFI
PIPPVDYEPT PIRPYRDPAM LAQNKMPFMT PIAERTESSL APSTVFNVPG YFESKTPSRS
QYESPSKIGV EDLFLSSPQQ QITTPTSGSP AQKRKYGESG ATEEELITSS PQKKGPSRTD
LNSSPVAPSS TNNEAFKTPA LPSKPIIRSP LSKIHKGPII PDLQCNPCDD AVRQQILGSV
YPPLSTQKGY HDHSSVDFGR YSALKSYAEK QAKAKAKFSP RKSQNDKPPS KAVPPVLKFS
ETSRVYAVKR ELGEGAFAPV YLVDSYDPAE NEEADENDKE NKSPPSSHPA DASRQALEAL
KTESPPGTLV WEFHIVRLIK QRLGSAARSM QSIILAHECH LYRDEAYLVL SYSPQGTLLD
LVNMARAESV KAGKPAEGLD EVLAMWFSVE LLRTMEDLHR VGILHGDLKG DNCLVRFDTT
VDLTAPFDPE GNYGWQSRGL RLIDFGRGID TRMFKPNAQF IADWPSCPQD CTEIRECRPW
KWQIDYHGAA GVIHSLLFGK YIETVPAGGN GLAGPGQKKE WKLKENLKRY WEKDVWGDVF
ATLLNPGCLA DGEEMPIQGN LKRARVMMEQ WLVDEGERGG RDLRASLRRM ERLVCAK
//
