ID A0A179G1M3_METCM Unreviewed; 748 AA.
AC A0A179G1M3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Histone deacetylase {ECO:0000256|PIRNR:PIRNR037919};
DE EC=3.5.1.98 {ECO:0000256|PIRNR:PIRNR037919};
GN ORFNames=VFPPC_03476 {ECO:0000313|EMBL:OAQ71129.1};
OS Pochonia chlamydosporia 170.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Pochonia.
OX NCBI_TaxID=1380566 {ECO:0000313|EMBL:OAQ71129.1, ECO:0000313|Proteomes:UP000078397};
RN [1] {ECO:0000313|EMBL:OAQ71129.1, ECO:0000313|Proteomes:UP000078397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=170 {ECO:0000313|EMBL:OAQ71129.1};
RX PubMed=27416025;
RA Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yang Y., Yin W.B., Xie B.;
RT "Biosynthesis of antibiotic leucinostatins in bio-control fungus
RT Purpureocillium lilacinum and their inhibition on phytophthora revealed by
RT genome mining.";
RL PLoS Pathog. 12:E1005685-E1005685(2016).
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:OAQ71129.1}.
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DR EMBL; LSBJ02000002; OAQ71129.1; -; Genomic_DNA.
DR RefSeq; XP_018147666.1; XM_018282972.1.
DR AlphaFoldDB; A0A179G1M3; -.
DR STRING; 1380566.A0A179G1M3; -.
DR ESTHER; metcm-a0a179g1m3; Arb2_domain.
DR GeneID; 28846966; -.
DR KEGG; pchm:VFPPC_03476; -.
DR OrthoDB; 124800at2759; -.
DR Proteomes; UP000078397; Chromosome 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000078397};
KW Repressor {ECO:0000256|PIRNR:PIRNR037919};
KW Transcription {ECO:0000256|PIRNR:PIRNR037919};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR037919}.
FT DOMAIN 90..415
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT DOMAIN 468..725
FT /note="Arb2-like"
FT /evidence="ECO:0000259|Pfam:PF09757"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..50
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 748 AA; 83733 MW; D85F7A1403F34BEC CRC64;
MEEHLAMDVD DHPMRDADMA NGVSHDTGAR PEDDDDTASE EVSYEDGTDL DAQDLALEQL
RRRGLLPTGC CYDDRMKLHM NADFSPNTHH PEDPRRIHEI FKAFKRVGLV YSGPEAELPK
IIKECPTRYM WRIPVRPATR EEICLAHSSE HMTWVEQLDK LSTAELRELT KRYDQGRESL
YVGSMSYPAA LLSAGGAIDT CKNVVAGQVK NAFAVIRPPG HHAEYDAPMG FCFFNNVPVA
VRVCQQDYSD VCRKVLILDW DVHHGNGIQN IFYDDPNVLY ISIHVYQNGN FYPGKPPNPE
TPDGGIENCG TGPGLGKNIN IGWHDQGMGD GEYMAAFQRI VMPIAKEFNP DLVVISAGFD
AADGDELGGC FVTPPCYAHM THMLMSLADG KVAVCLEGGY NLSAISNSAV AVARTLMGEP
PPKMIIPKLN KEAARTLAKV QAYQAPYWEC MRPGVVDVPA VQSLNANRLH DVIRSAQRLL
LQEKHNMLPL YVQRDQLYKS FENQVLVTPN LHNSRRMLVI IHDPPQLLAQ PDAIDSSLEA
HNAWVVDGVT QYIDWAVGQK FGIMDINVPP YITNDDDMDS YIPGYKERAL QEQVQQLMNY
LWDNFLQLYD ADEIFLMGVG NAYLGVKVLL INRDCKSKIS GVVNFVTGNL RPVKSDIDPD
LSSWYKENSR VYVASDHACW SDHDLTKKVQ KRRFGTVVRS PKLGLNKMMQ EHADEAQEWI
LARVSTTSGG DTTEEEDEDE ENGGTKST
//
