ID   IBD2_YEAS7              Reviewed;         351 AA.
AC   A6ZRR9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 43.
DE   RecName: Full=Protein IBD2;
DE   AltName: Full=Inhibition of bud division protein 2;
GN   Name=IBD2; ORFNames=SCY_4630;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC   -!- FUNCTION: Part of a checkpoint which monitors spindle integrity and
CC       prevents premature exit from mitosis. This cell-cycle arrest depends
CC       upon inhibition of the G-protein TEM1 by the BFA1/BUB2 complex (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with BFA1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle pole
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the IBD2 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AAFW02000067; EDN62651.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZRR9; -.
DR   EnsemblFungi; EDN62651; EDN62651; SCY_4630.
DR   HOGENOM; CLU_067888_0_0_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IEA:InterPro.
DR   InterPro; IPR026231; IBD2.
DR   PRINTS; PR02099; PROTEINIBD2.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Mitosis;
KW   Phosphoprotein.
FT   CHAIN           1..351
FT                   /note="Protein IBD2"
FT                   /id="PRO_0000333337"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          222..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        233..247
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         100
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P53892"
FT   MOD_RES         106
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P53892"
FT   MOD_RES         211
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P53892"
SQ   SEQUENCE   351 AA;  39988 MW;  9A416D52B29ED587 CRC64;
     MTPTNQSSGT TNASVEVLSE DGPMPINVMM QEGVKALTKI LSNQLQDRQA FQNAPHAMQF
     VIRNGGKALS NARLEELKDA LPKMDSLSLE DELAKIDGQS AYHIDSAEEK ETFESKIGQI
     ASRNSADFII EEDLQNILDD DLKDSELNLD GEEAEIIFDY ESQELDTPDG IGEKISQMIE
     SVLPGGFGSE EQGGLRTVTN VEDLDVAEEV TDIDHDTVDA ARLHGDGKHS ISSRKHSRSK
     NSKKNGHVRR HDFYDESRDH KSCCPHHHYE NLSKLRNYYY HDFEYISKTE NRVPDFSVLV
     NESSPMCLFC EYYMVFGEPP RNMIKWYNRT FGYNRMPNPP RDEQDSRKRN R