ID A0A094DH38_9PEZI Unreviewed; 703 AA.
AC A0A094DH38;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Histone deacetylase {ECO:0000256|PIRNR:PIRNR037919};
DE EC=3.5.1.98 {ECO:0000256|PIRNR:PIRNR037919};
GN ORFNames=V496_05973 {ECO:0000313|EMBL:KFY58770.1};
OS Pseudogymnoascus sp. VKM F-4515 (FW-2607).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420909 {ECO:0000313|EMBL:KFY58770.1, ECO:0000313|Proteomes:UP000029302};
RN [1] {ECO:0000313|EMBL:KFY58770.1, ECO:0000313|Proteomes:UP000029302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4515 (FW-2607) {ECO:0000313|Proteomes:UP000029302};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFY58770.1}.
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DR EMBL; JPJY01001081; KFY58770.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094DH38; -.
DR STRING; 1420909.A0A094DH38; -.
DR ESTHER; 9pezi-a0a094fhw9; Arb2_domain.
DR HOGENOM; CLU_007727_4_0_1; -.
DR OrthoDB; 124800at2759; -.
DR Proteomes; UP000029302; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0031078; F:histone H3K14 deacetylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0010468; P:regulation of gene expression; IEA:UniProt.
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; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000029302};
KW Repressor {ECO:0000256|PIRNR:PIRNR037919};
KW Transcription {ECO:0000256|PIRNR:PIRNR037919};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR037919}.
FT DOMAIN 98..423
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT DOMAIN 473..695
FT /note="Arb2-like"
FT /evidence="ECO:0000259|Pfam:PF09757"
SQ SEQUENCE 703 AA; 77547 MW; 537AF54AA794FAFC CRC64;
MVMMDSPNGG DVFMVESVAE NNGDGFMDPR AMHLPENGNG DIDFEEDDAA NMSDISEHSI
DSQALSPTVR KKYLPTGCCY DDRMKLHANA DFSVEPSHPE DPRRIASIMR AFKEAKLVYN
GDGEGLAEIL KNSPTKFMYR IAARGATPEE ICTVHTALHF KWVADLSGMT SDELRSMSKA
LDNGRKSLYV GNYTYEAALI AAGGAIETCK NVVAGTVKNA IAVIRPPGHH AESDEALGFC
MFNNVPVAAR VCQADFPETC RKILILDWDV HHGNGIQNIF YDDPNVLYIS LHVYIDGSFY
PGFPDDPSVP DGGLGNVGAG PGSGRNVNIP WHAQGMGDGE YLGAFQRIVM PIAQEFDPDL
VIVSAGFDAA DGDELGRCFV SPACYAHMTH MLMSLADGKV AVCLEGGYNL KAISRSALAV
AKTLMGEPPG RIKMPPINKE ALKVLHQVKE AQAPFWECMR PGKINLKEEE DTDGVLITSE
FATAKKILLI IHDPPELLAI PDPIDYSVEP HNSWMNDGLM AYIDWAVNNG YAVIDVNMPM
HIDDSDANIE EEGFIERPTE MVHRERMKEL MCFLWDNYLE VHESEHIVLM GVGDSYSAVR
ELLVNRESKH KVPLVVSFVS GSLRPVRSET DANLAHWYKK HSRVYVAADH LCWTDPELER
KVRKSRFGRV VKSGVEGLNK MLRAHLPEVV GLLGSVGEEG EEE
//
