ID A0A166R3Z7_9PEZI Unreviewed; 744 AA.
AC A0A166R3Z7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Histone deacetylase {ECO:0000256|PIRNR:PIRNR037919};
DE EC=3.5.1.98 {ECO:0000256|PIRNR:PIRNR037919};
GN ORFNames=CT0861_12234 {ECO:0000313|EMBL:KZL68728.1};
OS Colletotrichum tofieldiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL68728.1, ECO:0000313|Proteomes:UP000076552};
RN [1] {ECO:0000313|EMBL:KZL68728.1, ECO:0000313|Proteomes:UP000076552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0861 {ECO:0000313|EMBL:KZL68728.1,
RC ECO:0000313|Proteomes:UP000076552};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) 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:KZL68728.1}.
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DR EMBL; LFIV01000121; KZL68728.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166R3Z7; -.
DR STRING; 708197.A0A166R3Z7; -.
DR ESTHER; 9pezi-a0a162q6b7; Arb2_domain.
DR OrthoDB; 124800at2759; -.
DR Proteomes; UP000076552; 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:UP000076552};
KW Repressor {ECO:0000256|PIRNR:PIRNR037919};
KW Transcription {ECO:0000256|PIRNR:PIRNR037919};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR037919}.
FT DOMAIN 94..419
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT DOMAIN 472..730
FT /note="Arb2-like"
FT /evidence="ECO:0000259|Pfam:PF09757"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..56
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 744 AA; 83503 MW; 575909C4CBFA22F1 CRC64;
MEGGDQDVVM GGDDRPSNHT TTPNGVTAPE GDPKNENSTS LDDEDEDDFD EYDDDPDQQV
ANQLRRRGLL PTACCYDDRM KLHVNADFGT TPHHPEDPRR IEEIYKAFKR AGLVYTGPES
KVADVMRDTP TKYMWRIGTR EATKEEILTT HTPLHYHWVE GLSKMDYAEL RETSRQYDQG
RASLYVGSLT FTAALLSCGG AIDTCKHVVE GNVKNAFAVI RPPGHHAEYD QPLGFCFFNN
VPVAVKICQQ EYPNDCRKVL ILDWDVHHGN GIQNIFYDDP NVLYISLHVY QNGIFYPGKP
DNQEIPDGGL EHCGTGPGLG KNINIGWHDQ GMGDGEYMAA FQKIIMPIAK EFNPDLVVIS
AGFDAAAGDE LGGCFVTPTC YAHMTHMLMS LADGKVAVCL EGGYNLQAIS TSAVAVARTL
MGEPPPKMEI PMLNKDAARV LAKVQSYQAP YWECMRPGIV PVPDIQDLNA TRLHDHIRLG
QRQNLAQRHQ MIPLFIQRDL LFKSYENQVL VTPDIPSARR ILVIIHDPPE LLAQPDVIDR
HIESHNAWVV DSVSQYIDWA VNEGIAVMDV NVPSKVSRDE DMDPYSPRTA DKDLLNELQE
LANYLWDNYL QLYEEADDIL LIGVGRSYNG VRALLTGRDC KSRVAGVACF VEGMLRPVKS
DVDNELAAWY KGHSQIYVSH DHPCWNSEDT LRRVTKRRFG TVIRSETNGV QKMMQTHAGE
VQKWMLEMLA ARQNGDTTED DKMT
//
