ID A0A094EKB6_9PEZI Unreviewed; 750 AA.
AC A0A094EKB6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Histone deacetylase {ECO:0000256|PIRNR:PIRNR037919};
DE EC=3.5.1.98 {ECO:0000256|PIRNR:PIRNR037919};
GN ORFNames=V499_01820 {ECO:0000313|EMBL:KFY79161.1};
OS Pseudogymnoascus sp. VKM F-103.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420912 {ECO:0000313|EMBL:KFY79161.1, ECO:0000313|Proteomes:UP000029295};
RN [1] {ECO:0000313|EMBL:KFY79161.1, ECO:0000313|Proteomes:UP000029295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-103 {ECO:0000313|EMBL:KFY79161.1,
RC ECO:0000313|Proteomes:UP000029295};
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:KFY79161.1}.
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DR EMBL; JPKB01000255; KFY79161.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094EKB6; -.
DR ESTHER; 9pezi-a0a094ekb6; Arb2_domain.
DR HOGENOM; CLU_007727_4_0_1; -.
DR Proteomes; UP000029295; 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; 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 107..432
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT DOMAIN 485..742
FT /note="Arb2-like"
FT /evidence="ECO:0000259|Pfam:PF09757"
SQ SEQUENCE 750 AA; 82908 MW; F0A492DADF3AC975 CRC64;
MVMMDSAHGN DVVMAESVVE NGGNGFIDPR DMHIIEHGLT ENGDGIGQLN FEEEEEDAAD
MSDISEHSVD SQALTFTGRK KHLPTGCCYD DRMKLHANAD FSVDPPHPED PRRIQSIMRA
FKEAKLVYTG PEENLAGILK NSPTAYMYRI AARGATPAEI CTVHTPLHFK WVSDLSGMSS
DELRAMSKAL DTGRKSLYVG NYTYEAALIA AGGAIETCKN VVAGTVKNAI AVIRPPGHHA
ESDEALGFCM FNNVPVAARV CQADFPDTCR KVLILDWDVH HGNGIQNIFY DDPNVLYISL
HVYKDGTFYP GFPDDPSVPD GGLGNVGAGP GSGRNVNIPW HAQGMGDGEY LGAFQKIVMP
IAQEFNPDLV IVAAGFDAAD GDELGSCFVS PACYAHMTHM LMSLAGGKVA VCLEGGYNLK
AISRSALAVA KTLMGEPPDR IELPPINKEA LKILHRVKEA HAPFWECMQP GKINVKEEED
ADGARFNAVI RAYQYKVLRE KYKMVDMYVT RDKLAKGLEY QVLITSEFPA AKKILLIVHD
PPELLAISDP IDYSVEPHNS RMNDGVMAYI DWAYNNGYAV IDVNMPMHIE DTDANIEEEG
FIERPTEMVH RERMKELMCY LWDNYLELHD SEHVVLMGVG DSYSAVRELL VNRESKHKVP
LVVSFVSGSL RPVRSETDAS LAHWYKKHSR VYVAADHLCW TDPELERKVT KSRFGRVVKS
GVEGLNNMLR AHLPEVVGLL GSVGEEGEEE
//
