ID   SP110_YEAS8             Reviewed;         944 AA.
AC   C8Z5R8;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=Spindle pole body component 110;
DE   AltName: Full=Extragenic suppressor of CMD1-1 mutant protein 1;
DE   AltName: Full=Nuclear filament-related protein 1;
DE   AltName: Full=Spindle pole body spacer protein SPC110;
GN   Name=SPC110; Synonyms=NUF1, XCM1; ORFNames=EC1118_1D0_6491g;
OS   Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's
OS   yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=643680;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lalvin EC1118 / Prise de mousse;
RX   PubMed=19805302; DOI=10.1073/pnas.0904673106;
RA   Novo M., Bigey F., Beyne E., Galeote V., Gavory F., Mallet S., Cambon B.,
RA   Legras J.-L., Wincker P., Casaregola S., Dequin S.;
RT   "Eukaryote-to-eukaryote gene transfer events revealed by the genome
RT   sequence of the wine yeast Saccharomyces cerevisiae EC1118.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:16333-16338(2009).
CC   -!- FUNCTION: Component of the spindle pole body (SPB) required for the
CC       proper execution of spindle pole body (SPB) duplication. Potential role
CC       in cross-linking filaments or anchoring other molecules. It is
CC       essential for growth (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Component of the SPC110 complex containing at least
CC       CMD1, SPC29 and SCP110. Interacts with SPC97 and SPC98. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton,
CC       microtubule organizing center, spindle pole body {ECO:0000250}.
CC       Note=Tightly associated with the nucleus. It is present in a granular
CC       pattern that excludes the nucleolus. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SPC110 family. {ECO:0000305}.
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DR   EMBL; FN393063; CAY78857.1; -; Genomic_DNA.
DR   AlphaFoldDB; C8Z5R8; -.
DR   SMR; C8Z5R8; -.
DR   PRIDE; C8Z5R8; -.
DR   TopDownProteomics; C8Z5R8; -.
DR   EnsemblFungi; CAY78857; CAY78857; EC1118_1D0_6491g.
DR   HOGENOM; CLU_329279_0_0_1; -.
DR   Proteomes; UP000000286; Chromosome IV, Scaffold EC1118_1D0.
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; IPR040593; Spc110_C.
DR   Pfam; PF18520; Spc110_C; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Nucleus; Phosphoprotein.
FT   CHAIN           1..944
FT                   /note="Spindle pole body component 110"
FT                   /id="PRO_0000409205"
FT   REGION          23..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          900..927
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000250"
FT   COILED          119..799
FT                   /evidence="ECO:0000255"
FT   MOTIF           54..59
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           726..731
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           742..747
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        23..45
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..66
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..110
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:P32380"
FT   MOD_RES         60
FT                   /note="Phosphoserine; by MPS1"
FT                   /evidence="ECO:0000250|UniProtKB:P32380"
FT   MOD_RES         64
FT                   /note="Phosphothreonine; by MPS1"
FT                   /evidence="ECO:0000250|UniProtKB:P32380"
FT   MOD_RES         68
FT                   /note="Phosphothreonine; by MPS1"
FT                   /evidence="ECO:0000250|UniProtKB:P32380"
FT   MOD_RES         80
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P32380"
FT   MOD_RES         529
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P32380"
SQ   SEQUENCE   944 AA;  111769 MW;  2A575DF072670A22 CRC64;
     MDEASHLPNG SLKNMEFTPV GFIKSKRNTT QTQVVSPTKV PNANNGDENE GPVKKRQRRS
     IDDTIDSTRL FSEASQFDDS FPEIKANIPP SPRSGNVDKS RKRNLIDDLK KDVPMSQPLK
     EQEVREHQMK KERFDRALES KLLGKRHITY ANSDISNKEL YINEIKSLKH EIKELRKEKN
     DTLNNYDTLE EETDDLKNRL QALEKELDAK NKIVNSRKVD DHSGCIEERE QMERKLAELE
     RKLKTVKDQV LELENNSDVQ SLKLRSKEDE LKNLMNELNE LKSNAEEKDT QLEFKKNELR
     KRTIELNELK IKSDEMDLQL KQKQNESKRL KDELNELETK FSENGSQSSA KENELKMLKN
     KIAELEEEIS TKNSQLIAKE GKLASLMAQL TQLESKLNQR DSQLGSREEE LKKTNDKLQK
     DIRIAREETV SKDERITDLQ KKVKQLENDL FVIKKTHSES KTITDNELES KDKLIKILEN
     DLKVAQEKYS KMEKELKERE FNYKISESKL EDEKTTLNEK ISNLAAENSQ LKNKIEDNST
     ATHHMKENYE KQLESLRKDI EEYKESAKDS EDKIEELKIR IAENSAKVSE KRSKDIKQKD
     EQISDLTQNL KLQEDEISSL KSIIDRYKKD FNQLKSEQSN IQHDLNLQIL NLENKLIESE
     DELKSLRDSQ KIEIENWKRK YNNLSLENDR LLTEKESASD KEREISILNR KLDEMDKEKW
     NLQESKEKYK RELQKVITAN DRLRREKEEL NENSNNIRIM EDKMTRIKKN YLSEITSLQE
     ENRRLEERLI LNERRKDNDS TMQLNDIISY YKLKYHSEVR HNNDLKVIND YLNKVLALGT
     RRLRLDTRKG EHSLNISLPD DDELDRDYYN SHVYTRYHDY EYPLRFNLNR RGPYFERRLS
     FKTVALLVLA CVRMKRIAFY RRSDDNRLRI LRDRIESSSG RISW