ID A0A395S728_FUSSP Unreviewed; 734 AA.
AC A0A395S728;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Histone deacetylase {ECO:0000256|PIRNR:PIRNR037919};
DE EC=3.5.1.98 {ECO:0000256|PIRNR:PIRNR037919};
GN ORFNames=FSPOR_5502 {ECO:0000313|EMBL:RGP68158.1};
OS Fusarium sporotrichioides.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=5514 {ECO:0000313|EMBL:RGP68158.1, ECO:0000313|Proteomes:UP000266152};
RN [1] {ECO:0000313|EMBL:RGP68158.1, ECO:0000313|Proteomes:UP000266152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3299 {ECO:0000313|EMBL:RGP68158.1,
RC ECO:0000313|Proteomes:UP000266152};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
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:RGP68158.1}.
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DR EMBL; PXOF01000075; RGP68158.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395S728; -.
DR STRING; 5514.A0A395S728; -.
DR ESTHER; gibze-i1rkc4; Arb2_domain.
DR Proteomes; UP000266152; 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 Reference proteome {ECO:0000313|Proteomes:UP000266152};
KW Repressor {ECO:0000256|PIRNR:PIRNR037919};
KW Transcription {ECO:0000256|PIRNR:PIRNR037919};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR037919}.
FT DOMAIN 87..412
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT DOMAIN 465..722
FT /note="Arb2-like"
FT /evidence="ECO:0000259|Pfam:PF09757"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..49
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 734 AA; 82370 MW; 287E700D3E4C5574 CRC64;
MEPNATDIVD HPMKDLDAPN GSYQTRNTSI DDDDTASEDP YEADVDPEPQ DITFDQIRRR
GLLPTGCCYD DRMKLHMNAD FSPNTHHPED PRRIHEIFKA FKKVGLVYTG PEAELPRIMR
ECPTRYMWRI PARAATREEI CLAHSAEHFD WVERLDKMST AELRELTKRY DQGRESLYVG
SMSYPAALLS AGGAIETCKN VVIGQVKNAF AVIRPPGHHA EWDGPMGFCF FNNVPVAVRV
CQQDYPDICR KVLILDWDVH HGNGVQNIFY NDPNVLYISL HVYQNGIFYP GKPPNSMTPD
GGIEHCGSEA GLGKNINIGW HDQGMGDGEY MAAFQKIIMP IAKEFDPDLV VISAGFDAAD
GDELGGCFVS PACYAHMTHM LMSLADGKVA VCLEGGYNLK AISVSAVAVA KTLMGEPPPR
LELPKINKEA ARILAKVQSL QAPFWECMRP GIVNVPEVQS LNSSRLHDVI RNAQRQVLQT
KHNMIPLYIQ RENLYKSYEN QVLVTPGLHE AKKILIIIHD PPQLLAQPDV IDSSLDPHNA
WVVDGVTDYI DWAIDQRFGV MDINIPAYVT HDEDSDAHIP SFKEQALTEQ IQTLVCYLWD
NHLQLYDADD IFIMGVGNAY LGVKVLLINR DCKSRISGVV NFANGTLRPI KSDIDTDLSS
WYKENSRVFI AGDHACWADA SLTKKVHKRR FGSVVRSPMF GLNKMMAHHA KEAREWILER
LEGGSDADMT TEEK
//
