ID A0A178AV54_9PLEO Unreviewed; 837 AA.
AC A0A178AV54;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-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=IQ06DRAFT_346388 {ECO:0000313|EMBL:OAL01766.1};
OS Stagonospora sp. SRC1lsM3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX NCBI_TaxID=765868 {ECO:0000313|EMBL:OAL01766.1, ECO:0000313|Proteomes:UP000077206};
RN [1] {ECO:0000313|EMBL:OAL01766.1, ECO:0000313|Proteomes:UP000077206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAL01766.1,
RC ECO:0000313|Proteomes:UP000077206};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) 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}.
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DR EMBL; KV441710; OAL01766.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178AV54; -.
DR STRING; 765868.A0A178AV54; -.
DR ESTHER; 9pleo-a0a178av54; Arb2_domain.
DR InParanoid; A0A178AV54; -.
DR OrthoDB; 124800at2759; -.
DR Proteomes; UP000077206; 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:UP000077206};
KW Repressor {ECO:0000256|PIRNR:PIRNR037919};
KW Transcription {ECO:0000256|PIRNR:PIRNR037919};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR037919}.
FT DOMAIN 152..463
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT DOMAIN 517..775
FT /note="Arb2-like"
FT /evidence="ECO:0000259|Pfam:PF09757"
FT REGION 84..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 780..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 837 AA; 93467 MW; D709641475F12B24 CRC64;
MERGVNARFM GTADAMDTED FPMADEDSIL ASTELNGQAL PVTVDPSKLG LQGSSHFRNE
PLPFHSPSKA STLMQPNARV GIAKATPLSD DEDMDMSPPR PKRRASPEVR IAPRPRTAVL
PYASSRTGLV YDSRMRFHAE LSSMSLNAND IHPEDPRRIH SIFEEIRQAG LVGSSGASQD
DQTEEHCWRI AIRAATKPEI LLIHSRDHYD FVESLQTMSA EELKYHSERL DSIYFNHSTY
ECAKLAAGGA IEACKAVVQG AVRNAIAIIR PPGHHAESDQ PSGFCIFNNV PIATRVCQEA
YPESCRKVLI LDWDVHHGNG IQHAFYNDPN VLYISLHVFL DGNFYPNLPD GNLDYCGEEA
GEGKNVNIPW AETGMGDAEY IYAFQEVVMP IATEFDPDLV IISAGFDAAE GDLLGGCFVT
PACYGHMTHM LMRLAKGKLV VCLEGGYNLR SIARSALAVT RVLMLEPPDR LEPDLPAPRD
SAIHVIEQIK RQHSKYWKCL YPKHLDKSDP GYQDTLRLHE IIREWQSLRL SYEHAMTPLQ
INKAGLSQTF EHNVIATPEV MGRFPHLVIF HDPPSFRDNP DPVTGRRELH NTWLTDVTKR
YIDWAIDNGF QVIDVNIPRI VAVEDPEEGY VKSDTSATRA FQTREMAHYI WENYLETSEA
SQIFLMGIGD AYLGLVDLLS NNGKLSKTAV ECLIGFVAET TIQSIKRATD DTIQHWYHAH
SQIFVKSSHY VWDPSRQRKL RRKLGNLIKS PQDSLDTMLE QHLSDVQTLL LEKKSEYEER
AEVSSRSDVG PLRSPPIIGG GGSGSAGLLK SPKGPPLGYF SVSSPVPKSP RSPMRRV
//
