ID   SFH1_YARLI              Reviewed;         441 AA.
AC   Q6C9N2;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Chromatin structure-remodeling complex subunit SFH1;
DE   AltName: Full=RSC complex subunit SFH1;
DE   AltName: Full=SNF5 homolog 1;
GN   Name=SFH1; OrderedLocusNames=YALI0D09779g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Part of the chromatin structure-remodeling complex (RSC)
CC       which is involved in transcription regulation and nucleosome
CC       positioning. RSC is responsible for the transfer of a histone octamer
CC       from a nucleosome core particle to naked DNA. The reaction requires ATP
CC       and involves an activated RSC-nucleosome intermediate. Remodeling
CC       reaction also involves DNA translocation, DNA twist and conformational
CC       change. As a reconfigurer of centromeric and flanking nucleosomes, RSC
CC       complex is required both for proper kinetochore function in chromosome
CC       segregation and, via a PKC1-dependent signaling pathway, for
CC       organization of the cellular cytoskeleton. This subunit is essential
CC       for mitotic growth and required for cell cycle progression (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9USM3}.
CC   -!- SIMILARITY: Belongs to the SNF5 family. {ECO:0000305}.
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DR   EMBL; CR382130; CAG80818.1; -; Genomic_DNA.
DR   RefSeq; XP_502630.1; XM_502630.1.
DR   AlphaFoldDB; Q6C9N2; -.
DR   SMR; Q6C9N2; -.
DR   STRING; 4952.CAG80818; -.
DR   EnsemblFungi; CAG80818; CAG80818; YALI0_D09779g.
DR   GeneID; 2910921; -.
DR   KEGG; yli:YALI0D09779g; -.
DR   VEuPathDB; FungiDB:YALI0_D09779g; -.
DR   HOGENOM; CLU_014421_4_0_1; -.
DR   InParanoid; Q6C9N2; -.
DR   OMA; MWNLNES; -.
DR   Proteomes; UP000001300; Chromosome D.
DR   GO; GO:0000228; C:nuclear chromosome; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0016586; C:RSC-type complex; IBA:GO_Central.
DR   GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006338; P:chromatin remodeling; IEA:InterPro.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   InterPro; IPR006939; SNF5.
DR   Pfam; PF04855; SNF5; 2.
PE   3: Inferred from homology;
KW   Cell cycle; Chromatin regulator; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..441
FT                   /note="Chromatin structure-remodeling complex subunit SFH1"
FT                   /id="PRO_0000205961"
FT   REGION          124..183
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          383..407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        124..139
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..166
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   441 AA;  50135 MW;  C984C5BFDA898F14 CRC64;
     MGEKPNRIGR ANISYINHDH IFLPSFQPSY PSRQLHPLIS SQNKVHSSIV HLPKVASPSS
     PETQQHSQAP LFITHIMSGL PQALASGFAA RVREGGTTLY INTTPMLRSA RHNTAVNYAE
     FEEDFDANDF EDDDDDDQSQ RESRDGSEEA EGDEDGTKKE EQDKFAGLKA PLVSNEPKRA
     APPVRPVMYP QEVLEELSQV KEPTLIPIRV AVENIDVFRV QDFFLWDADE KILTPEQFAT
     LTCADLDVPI GYSAQMSAQI KKQLAEYTAA PALPKDVEVH VIVELAVTVD KIVYEDKFEW
     DLSGEYATPQ EFARTVVQDL GLGQEFYPAI TYQLYETLGK LQKAWLERSI PLDVDNRAAF
     GLEAGLRVDQ DNLGESWVPR VEEMTPEEMQ KREMERDRSS RRLKRESARM AEVPYVDLDS
     LYSRKRRRRF DEDSRSGSPM W