ID   BBP1_YEASZ              Reviewed;         419 AA.
AC   E7QLJ6;
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=VL3_4732;
OS   Saccharomyces cerevisiae (strain Zymaflore VL3) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=764100;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zymaflore VL3;
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; AEJS01000063; EGA84446.1; -; Genomic_DNA.
DR   AlphaFoldDB; E7QLJ6; -.
DR   SMR; E7QLJ6; -.
DR   EnsemblFungi; EGA84446; EGA84446; VL3_4732.
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_0000409183"
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