ID G2WM72_YEASK Unreviewed; 706 AA.
AC G2WM72;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Histone deacetylase {ECO:0000256|PIRNR:PIRNR037919};
DE EC=3.5.1.98 {ECO:0000256|PIRNR:PIRNR037919};
GN Name=K7_HDA1 {ECO:0000313|EMBL:GAA26064.1};
GN ORFNames=SYK7_057891 {ECO:0000313|EMBL:GAA26064.1};
OS Saccharomyces cerevisiae (strain Kyokai no. 7 / NBRC 101557) (Baker's
OS yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=721032 {ECO:0000313|EMBL:GAA26064.1, ECO:0000313|Proteomes:UP000001608};
RN [1] {ECO:0000313|EMBL:GAA26064.1, ECO:0000313|Proteomes:UP000001608}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kyokai no. 7 / NBRC 101557 {ECO:0000313|Proteomes:UP000001608};
RX PubMed=21900213; DOI=10.1093/dnares/dsr029;
RA Akao T., Yashiro I., Hosoyama A., Kitagaki H., Horikawa H., Watanabe D.,
RA Akada R., Ando Y., Harashima S., Inoue T., Inoue Y., Kajiwara S.,
RA Kitamoto K., Kitamoto N., Kobayashi O., Kuhara S., Masubuchi T.,
RA Mizoguchi H., Nakao Y., Nakazato A., Namise M., Oba T., Ogata T., Ohta A.,
RA Sato M., Shibasaki S., Takatsume Y., Tanimoto S., Tsuboi H., Nishimura A.,
RA Yoda K., Ishikawa T., Iwashita K., Fujita N., Shimoi H.;
RT "Whole-genome sequencing of sake yeast Saccharomyces cerevisiae Kyokai no.
RT 7.";
RL DNA Res. 18:423-434(2011).
CC -!- FUNCTION: Responsible for the deacetylation of lysine residues on the
CC N-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. {ECO:0000256|PIRNR:PIRNR037919}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-
CC [histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-
CC COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:61930; EC=3.5.1.98;
CC Evidence={ECO:0000256|PIRNR:PIRNR037919};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR037919}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC subfamily. {ECO:0000256|PIRNR:PIRNR037919}.
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DR EMBL; DG000050; GAA26064.1; -; Genomic_DNA.
DR AlphaFoldDB; G2WM72; -.
DR SMR; G2WM72; -.
DR ESTHER; yeast-hda1; Arb2_domain.
DR HOGENOM; CLU_007727_4_0_1; -.
DR Proteomes; UP000001608; Chromosome XIV.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0031078; F:histone H3K14 deacetylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:UniProt.
DR CDD; cd11600; HDAC_Clr3; 1.
DR Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR InterPro; IPR019154; Arb2-like_domain.
DR InterPro; IPR000286; His_deacetylse.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR017321; Hist_deAcase_II_yeast.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR10625:SF4; HISTONE DEACETYLASE 6, ISOFORM G; 1.
DR PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR Pfam; PF09757; Arb2; 1.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PIRSF; PIRSF037919; HDAC_II_yeast; 1.
DR PRINTS; PR01270; HDASUPER.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|PIRNR:PIRNR037919};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR037919};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR037919};
KW Repressor {ECO:0000256|PIRNR:PIRNR037919};
KW Transcription {ECO:0000256|PIRNR:PIRNR037919};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR037919}.
FT DOMAIN 83..393
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT DOMAIN 456..702
FT /note="Arb2-like"
FT /evidence="ECO:0000259|Pfam:PF09757"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 706 AA; 80070 MW; 4E7069E66D03264D CRC64;
MDSVMVKKEV LENPDHDLKR KLEENKEEEN SLSTTSKSKR QVIVPVCMPK IHYSPLKTGL
CYDVRMRYHA KIFTSYFEYI DPHPEDPRRI YRIYKILAEN GLINDPTLSG VDDLGDLMLK
IPVRAATSEE ILEVHTKEHL EFIESTEKMS REELLKETEK GDSVYFNNDS YASARLPCGG
AIEACKAVVE GRVKNSLAVV RPPGHHAEPQ AAGGFCLFSN VAVAAKNILK NYPESVRRIM
ILDWDIHHGN GTQKSFYQDD QVLYVSLHRF EMGKYYPGTI QGQYDQTGEG KGEGFNCNIT
WPVGGVGDAE YMWAFEQVVM PMGREFKPDL VIISSGFDAA DGDTIGQCHV TPSCYGHMTH
MLKSLARGNL CVVLEGGYNL DAIARSALSV AKVLIGEPPD ELPDPLSDPK PEVIEMIDKV
IRLQSKYWNC FRRRHANSGC NFNEPINDSI ISKNFPLQKA IRQQQQHYLS DEFNFVTLPL
VSMDLPDNTV LCTPNISESN TIIIVVHDTS DIWAKRNVIS GTIDLSSSVI IDNSLDFIKW
GLDRKYGIID VNIPLTLFEP DNYSGMITSQ EVLIYLWDNY IKYFPSVAKI AFIGIGDSYS
GIVHLLGHRD TRAVTKTVIN FLGDKQLKPL VPLVDETLSE WYFKNSLIFS NNSHQCWKEN
ESRKPRKKFG RVLRCDTDGL NNIIEERFEE ATDFILDSFE EWSDEE
//
