BBP1_YEASL
ID BBP1_YEASL Reviewed; 419 AA.
AC E7KV71;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 25-MAY-2022, entry version 28.
DE RecName: Full=Spindle pole component BBP1;
DE AltName: Full=BFR1-binding protein 1;
GN Name=BBP1; ORFNames=QA23_4725;
OS Saccharomyces cerevisiae (strain Lalvin QA23) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=764098;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lalvin QA23;
RX PubMed=21304888; DOI=10.1371/journal.pgen.1001287;
RA Borneman A.R., Desany B.A., Riches D., Affourtit J.P., Forgan A.H.,
RA Pretorius I.S., Egholm M., Chambers P.J.;
RT "Whole-genome comparison reveals novel genetic elements that characterize
RT the genome of industrial strains of Saccharomyces cerevisiae.";
RL PLoS Genet. 7:E1001287-E1001287(2011).
CC -!- FUNCTION: Component of the spindle pole body (SPB) required for
CC insertion of the nascent SPB into the nuclear envelope and for the
CC proper execution of spindle pole body (SPB) duplication. Connects the
CC central plaque of the SPB with the half-bridge. Required for proper
CC localization of CDC5 at the SPB and for proper M-phase progression (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with KAR1, MPS2 and SPC29. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, spindle pole body {ECO:0000250}. Note=Associates with the
CC periphary of the central plaque. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the BBP1 family. {ECO:0000305}.
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DR EMBL; ADVV01000082; EGA80363.1; -; Genomic_DNA.
DR AlphaFoldDB; E7KV71; -.
DR SMR; E7KV71; -.
DR EnsemblFungi; EGA80363; EGA80363; QA23_4725.
DR HOGENOM; CLU_711875_0_0_1; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005816; C:spindle pole body; IEA:UniProtKB-SubCell.
DR InterPro; IPR029330; Bbp1_C.
DR InterPro; IPR029328; Bbp1_N.
DR Pfam; PF15272; BBP1_C; 1.
DR Pfam; PF15271; BBP1_N; 1.
PE 3: Inferred from homology;
KW Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein.
FT CHAIN 1..419
FT /note="Spindle pole component BBP1"
FT /id="PRO_0000409181"
FT REGION 34..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 229..355
FT /evidence="ECO:0000255"
FT COMPBIAS 34..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12365"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12365"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12365"
SQ SEQUENCE 419 AA; 49446 MW; 52DF7318E27D338A CRC64;
MNQEDNTGGG GIFGLFKWTK DALFGTDISP SMKYKDQEER RDRSRYAQDD TNFSMKFGND
SNRRSTNLSR SNSWSGLDST LHRKYELLPE YNENGFNSIV NGDHHSKERI RSLRSPAPIV
PREPLRNEPT DTFGHRLHTK RRTINELSNS QIPFIPPQED DPLLSKLFNK DGVNEVRRSP
YKLSVKDIPG KFPSPLTKRD EIDNYYVRDE DACHKNREYK KAYFDLFAQM DLNSRDLEDL
CEDVREQREQ FHRNEQTYKQ AYEEMRAELV NELKKSKTLF ENYYSLGQKY KSLKKVLDQT
ISHEAELATS RERLYQEEDL KNFEIQTLKQ RLSDLELKYT NLQIEKDMQR DNYESEIHDL
LLQLSLRNNE RKDTSAGSNI FSTGQYDRTP FHNGNNSYDS NSHSWDTDYL KNIDGFIER