ID   HDA3_ASHGO              Reviewed;         637 AA.
AC   Q758V8;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=HDA1 complex subunit 3;
DE   AltName: Full=Histone deacetylase complex 1 subunit 3;
GN   Name=HDA3; OrderedLocusNames=AEL270W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 31.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Required for activity of histone deacetylase complexes that
CC       are responsible for the deacetylation of lysine residues on the N-
CC       terminal part of the core histones (H2A, H2B, H3 and H4). Histone
CC       deacetylation gives a tag for epigenetic repression and plays an
CC       important role in transcriptional regulation, cell cycle progression
CC       and developmental events (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Probable component of some histone deacetylase complex.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the HDA2/3 family. HDA3 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE016818; AAS52414.2; -; Genomic_DNA.
DR   RefSeq; NP_984590.2; NM_209943.2.
DR   AlphaFoldDB; Q758V8; -.
DR   SMR; Q758V8; -.
DR   STRING; 33169.AAS52414; -.
DR   EnsemblFungi; AAS52414; AAS52414; AGOS_AEL270W.
DR   GeneID; 4620770; -.
DR   KEGG; ago:AGOS_AEL270W; -.
DR   eggNOG; ENOG502QT9V; Eukaryota.
DR   HOGENOM; CLU_026579_0_0_1; -.
DR   InParanoid; Q758V8; -.
DR   OMA; NTSGDYW; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0070823; C:HDA1 complex; IEA:EnsemblFungi.
DR   GO; GO:0003682; F:chromatin binding; IEA:EnsemblFungi.
DR   GO; GO:0003677; F:DNA binding; IEA:EnsemblFungi.
DR   GO; GO:0004407; F:histone deacetylase activity; IEA:EnsemblFungi.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0007059; P:chromosome segregation; IEA:EnsemblFungi.
DR   GO; GO:0031047; P:gene silencing by RNA; IEA:EnsemblFungi.
DR   GO; GO:0016575; P:histone deacetylation; IEA:EnsemblFungi.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR   Gene3D; 3.40.50.12360; -; 1.
DR   InterPro; IPR038609; HDA1_su2/3_sf.
DR   InterPro; IPR021006; Hda2/3.
DR   InterPro; IPR026216; HDA3.
DR   Pfam; PF11496; HDA2-3; 1.
DR   PRINTS; PR02093; HDA1SUBUNIT3.
PE   3: Inferred from homology;
KW   Chromatin regulator; Coiled coil; Nucleus; Reference proteome; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..637
FT                   /note="HDA1 complex subunit 3"
FT                   /id="PRO_0000083931"
FT   REGION          618..637
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          443..608
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   637 AA;  72645 MW;  EA1AFED950480F38 CRC64;
     MDLLKILDTA PEPAIVDART MGVSGDTSGD YWLPAPMCLY QKELTDQIVS LHYSDILKYF
     ETSDYKEDIV LQSMKTMCLN SQLVATHPYL LIDHFMPKSL LTKDIPGHLS ETSGKFCVLR
     DLMNLVQEYA METLLVCRPG RTMDLLEALL LGNKVNIRRH DGQSIKTKQK KTRYACTCHL
     VPSEAAKAIA LERDTRLGLV ICVDPTVDTR APHIQSILAQ QQRKYGRTVP TIRVAVINSI
     EHCELFFGKT LDRNTRDYLV NVSAAMVVLR DVVGTLPPDL RPIYSQNLRY LIDWLDTPER
     PWPLPDVYPV KVYTAMDVER SLLTEVKYSQ NNDSLEDAFT NGKKRNHRSH GQGNGGNAPI
     SYYQIKRLKN DYIGNPLKQD MEQLTGISNN KCKDGLLDYH LSSGTLTHKL LQAIGSVYEN
     LQLQDVELSH FAAVEQNQTA IFESHKEALS TIKKQLEDAI SKKQRNNTLV DEYLKNSQNE
     RDQLEVLEAD ISDLLGQLDG RHQGFKQLWD DLNQTENTLA LYRTNANAKR SEASYMEEEL
     IRAEKSVAES ENEQTQLLRD VEHLEALIQD CREKDKQQQQ VIKNKSKDME DDITQKKEAV
     LALQNQLGTI MEYLKQLQTP RVRSPSNGHR SKHRGYV