ID A0A1L9RKW1_ASPWE Unreviewed; 717 AA.
AC A0A1L9RKW1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=histone deacetylase {ECO:0000256|ARBA:ARBA00012111};
DE EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111};
GN ORFNames=ASPWEDRAFT_110946 {ECO:0000313|EMBL:OJJ35478.1};
OS Aspergillus wentii DTO 134E9.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Cremei.
OX NCBI_TaxID=1073089 {ECO:0000313|EMBL:OJJ35478.1, ECO:0000313|Proteomes:UP000184383};
RN [1] {ECO:0000313|Proteomes:UP000184383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DTO 134E9 {ECO:0000313|Proteomes:UP000184383};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC subfamily. {ECO:0000256|ARBA:ARBA00006457}.
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DR EMBL; KV878212; OJJ35478.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9RKW1; -.
DR STRING; 1073089.A0A1L9RKW1; -.
DR VEuPathDB; FungiDB:ASPWEDRAFT_110946; -.
DR OrthoDB; 1327607at2759; -.
DR Proteomes; UP000184383; Unassembled WGS sequence.
DR GO; GO:1902494; C:catalytic complex; IEA:UniProt.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0004407; F:histone deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0010468; P:regulation of gene expression; IEA:UniProt.
DR CDD; cd10004; RPD3-like; 1.
DR Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR InterPro; IPR000286; His_deacetylse.
DR InterPro; IPR003084; His_deacetylse_1.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR10625:SF13; HISTONE DEACETYLASE HDAC1; 1.
DR PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PRINTS; PR01270; HDASUPER.
DR PRINTS; PR01271; HISDACETLASE.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Reference proteome {ECO:0000313|Proteomes:UP000184383}.
FT DOMAIN 40..328
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 414..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..440
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..517
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..608
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..717
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 717 AA; 78737 MW; 06EDA235866B9D0B CRC64;
MTSSFAPLDP ISVNGSADRN KKVAYFYDSD VGNYAYVSGH PMKPHRIRMT HSLVMNYGLY
KSMEIYRAKP ASKYEMTQFH TDEYIDFLSK VTPDNMDSFA KEQSKYNVGD DCPVFDGLFE
FCGISAGGSM EGAARLNRNK CDIAVNWAGG LHHAKKSEAS GFCYVNDIVL GILELLRFKQ
RVLYVDIDVH HGDGVEEAFY TTDRVMTVSF HKYGEYFPGT GELRDIGVGQ GKHYAVNFPL
RDGIDDISYK SIFEPVIKSV MEWYRPEAVV LQCGGDSLSG DRLGCFNLSM RGHANCVNFM
KSFNLPTLIL GGGGYTMRNV ARTWAFETGI LVGDGLGPEL PYNDYYEYFA PDYELDVRPS
NMDNANTKEY LDKIRTQVVE NLKRTAFAPS VQMTDVPRDP LVGGMDDEAD AILDDLDEDE
NKDKRFTQRR FDQYVEKPGE LSDSEDEDEN AANGVRRQPN AIRRRNEANH RNLGVDSGLD
SGIATPRDES SIADEEMDTT ADAKMGEAPE AEAEERLSPS AAEPPSRAEE ASAAEPSEMA
VDGQEQGASA PISRQTSPKV QDEDTTMEDA GAPEPQPEEP EEPAPAPEKK AQSEPQEGES
KPADETPQPD KTATEPSFPS KAKSPSKETS GVGPAETAGA TEGTEPTKTT ETGESQAAET
TEKAPEAPEA PQTTEAARDT QATEAPKDES APVKAEQETS EESNSKQQPE EPAKNEE
//
