ID   SPC42_YEASA             Reviewed;         363 AA.
AC   E7KEZ1;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   25-MAY-2022, entry version 32.
DE   RecName: Full=Spindle pole body component SPC42;
GN   Name=SPC42; ORFNames=AWRI796_2915;
OS   Saccharomyces cerevisiae (strain AWRI796) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=764097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AWRI796;
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: Forms a polymeric layer at the periphery of the spindle pole
CC       body (SPB) central plaque which has an essential function during SPB
CC       duplication and may facilitate attachment of the SPB to the nuclear
CC       membrane. {ECO:0000250}.
CC   -!- SUBUNIT: Component of the SPC110 complex containing at least CMD1,
CC       SPC29, SPC42 and SCP110. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton,
CC       microtubule organizing center, spindle pole body {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SPC42 family. {ECO:0000305}.
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DR   EMBL; ADVS01000035; EGA74197.1; -; Genomic_DNA.
DR   AlphaFoldDB; E7KEZ1; -.
DR   SMR; E7KEZ1; -.
DR   HOGENOM; CLU_761996_0_0_1; -.
DR   OMA; HNHATHR; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005816; C:spindle pole body; IEA:UniProtKB-SubCell.
DR   InterPro; IPR021611; Spc42.
DR   Pfam; PF11544; Spc42p; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Nucleus; Phosphoprotein.
FT   CHAIN           1..363
FT                   /note="Spindle pole body component SPC42"
FT                   /id="PRO_0000409216"
FT   REGION          160..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          310..363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          62..136
FT                   /evidence="ECO:0000255"
FT   COILED          248..297
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        168..184
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        349..363
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         213
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P36094"
FT   MOD_RES         217
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P36094"
FT   MOD_RES         284
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P36094"
FT   MOD_RES         329
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P36094"
SQ   SEQUENCE   363 AA;  42245 MW;  E3B5731F219EA441 CRC64;
     MNGSPTPKRY SSKSSRLYDD YYNIPYQYSN PTPMNRDYND VGSRINADKL VPEEYKRNTE
     FINKAVQQNK ELNFKLREKQ NEIFELKKIA ETLRSKLEKY VDITKKLEDQ NLNLQIKISD
     LEKKLSDANS TFKEMRFPKV KDPMVDDDPV SENYDQINVP KHRAPDATGN PRTTNKVSNT
     SDQDSRLKAI ERTLSVLTNY VMRSEDGNND RMSPLPSPLN TISPINNRLN FQEPKRYNPT
     VKVNPSDDDI MMYESAELKR VEEEIEELKR KILVRKKHDL RKLSLNNQLQ ELQSMMDGDD
     NIKLDNVSKH NHATHRHSSQ SSRDYSPSSD ACLECSNDLY EKNRVKPENN MSETFATPTP
     NNR