ID   SPC29_YEASL             Reviewed;         253 AA.
AC   E7KVI3;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   25-MAY-2022, entry version 33.
DE   RecName: Full=Spindle pole component 29;
GN   Name=SPC29; Synonyms=LPH3, NIP29; ORFNames=QA23_4843;
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 the
CC       proper execution of spindle pole body (SPB) duplication. Links the
CC       central plaque component SPC42 to the inner plaque component SPC110 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the SPC110 complex containing at least CMD1,
CC       SPC29, SPC42 and SCP110. Interacts with BBP1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton,
CC       microtubule organizing center, spindle pole body {ECO:0000250}.
CC   -!- PTM: MPS1-mediated phosphorylation at Thr-240 is required for spindle
CC       pole body duplication. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SPC29 family. {ECO:0000305}.
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DR   EMBL; ADVV01000082; EGA80463.1; -; Genomic_DNA.
DR   AlphaFoldDB; E7KVI3; -.
DR   SMR; E7KVI3; -.
DR   EnsemblFungi; EGA80463; EGA80463; QA23_4843.
DR   HOGENOM; CLU_1099229_0_0_1; -.
DR   GO; GO:0005823; C:central plaque of spindle pole body; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR   GO; GO:0030474; P:spindle pole body duplication; IEA:InterPro.
DR   InterPro; IPR031392; Spc29.
DR   Pfam; PF17082; Spc29; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Cytoskeleton; Nucleus; Phosphoprotein.
FT   CHAIN           1..253
FT                   /note="Spindle pole component 29"
FT                   /id="PRO_0000409195"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          31..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          210..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..89
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        215..231
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         18
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P33419"
FT   MOD_RES         65
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P33419"
FT   MOD_RES         240
FT                   /note="Phosphothreonine; by MPS1"
FT                   /evidence="ECO:0000250|UniProtKB:P33419"
SQ   SEQUENCE   253 AA;  29280 MW;  0730B17A86136621 CRC64;
     MDYSNFGNSA SKKFQDDTLN RVRKEHEEAL KKLREENFSS NTSELGNKKH YRAQERMSSP
     LHRLSPTGKS DDRKVKSPLD DKLRRQLREG NTRLPPPPFS SYGMPPTNRS NLDRIRRRTS
     SPVRTDKFAS QNVIDDQRLE IKYLERIVYD QGTVIDNLTS RITRLESFIL NSISDRGDKN
     FASLEHSRSF SGFPTNKTYG LQMGGLYEND MPYRRSSDNI NKEGAREDRS SQIHIENEST
     EDILKILSSS FHN