ID A0A2T3AXK4_AMORE Unreviewed; 761 AA.
AC A0A2T3AXK4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Histone deacetylase {ECO:0000256|PIRNR:PIRNR037919};
DE EC=3.5.1.98 {ECO:0000256|PIRNR:PIRNR037919};
GN ORFNames=M430DRAFT_104637 {ECO:0000313|EMBL:PSS14806.1};
OS Amorphotheca resinae ATCC 22711.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Amorphothecaceae; Amorphotheca.
OX NCBI_TaxID=857342 {ECO:0000313|EMBL:PSS14806.1, ECO:0000313|Proteomes:UP000241818};
RN [1] {ECO:0000313|EMBL:PSS14806.1, ECO:0000313|Proteomes:UP000241818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22711 {ECO:0000313|EMBL:PSS14806.1,
RC ECO:0000313|Proteomes:UP000241818};
RX PubMed=29315638; DOI=10.1111/nph.14974;
RA Martino E., Morin E., Grelet G.A., Kuo A., Kohler A., Daghino S.,
RA Barry K.W., Cichocki N., Clum A., Dockter R.B., Hainaut M., Kuo R.C.,
RA LaButti K., Lindahl B.D., Lindquist E.A., Lipzen A., Khouja H.R.,
RA Magnuson J., Murat C., Ohm R.A., Singer S.W., Spatafora J.W., Wang M.,
RA Veneault-Fourrey C., Henrissat B., Grigoriev I.V., Martin F.M., Perotto S.;
RT "Comparative genomics and transcriptomics depict ericoid mycorrhizal fungi
RT as versatile saprotrophs and plant mutualists.";
RL New Phytol. 217:1213-1229(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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KZ679013; PSS14806.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T3AXK4; -.
DR STRING; 857342.A0A2T3AXK4; -.
DR ESTHER; amore-a0a2t3axk4; Arb2_domain.
DR InParanoid; A0A2T3AXK4; -.
DR OrthoDB; 124800at2759; -.
DR Proteomes; UP000241818; 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:UP000241818};
KW Repressor {ECO:0000256|PIRNR:PIRNR037919};
KW Transcription {ECO:0000256|PIRNR:PIRNR037919};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR037919}.
FT DOMAIN 85..410
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT DOMAIN 463..727
FT /note="Arb2-like"
FT /evidence="ECO:0000259|Pfam:PF09757"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..754
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 761 AA; 84184 MW; 8512A1F80493403E CRC64;
MQNNSHSTNE NHENGFVDPR VLNQIHDHDL DLPDSTQEDS LEQSQTSSGS SSPPTARKAF
LPTGCCYDDR MKLHANADWS ANPHHPEDPR RIEAIMKAFK DAGLVYTGPT SELTQQLKIS
PTRWMWRIAA REATPEEICL AHAASHYEWV RGLSLKSAAE LRRMTVDMDA GRKSLYVGTL
TYEAALISAG GAIETCKNVV AGYVKNAIAV IRPPGHHAEP NEAMGFCVFN NVPIAAKVCM
ADYPEVCRKI LILDWDVHHG NGIQNIFYED PNVLYISLHV YSEGSFYPGQ PEDPGIPDGG
MENCGAGLGA GRNVNIAWHD QGMGDGEYMA AFQRIVMPIA QEFDPDFVII SAGFDAAAGD
ELGGCFVTPA CYSHMTHMLM SLANGKVAVC LEGGYNLSAI SRSALAVAKT LMGEPPERIA
IPPLNKEAAQ VLNRVRQYQA PYWECMRPGV VPVKEIEEQG AVRLHDALRT YQRRILTQKY
KMVSLYILRE QISRSFEDQV LATPGLHNAK KILLIIHDSP EVLAAPDPVD NKVSSHNAWM
TDSVLPYIDQ AISAGYGILD INIPAHLSAP TPTASSTPRP LAPTSPQTPS IESQTRELLC
YLWDNYLSYH PSLTLIPIGI GDSYIGIKQL LLSRPCRTAI PCILSFVSGS LRPIRSETDP
GLSSWYKSHS RIYVSPDHAC WSDVDAVKKV KKNRFGGVVR SEVEGTRAML DRYREEALMW
VEGMVKERWR EMGRGEDGEE LGEGDGEDGD ETEEEVEQDR R
//
