ID A0A1V6QCP7_9EURO Unreviewed; 639 AA.
AC A0A1V6QCP7;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=histone deacetylase {ECO:0000256|ARBA:ARBA00012111};
DE EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111};
GN ORFNames=PENANT_c006G07816 {ECO:0000313|EMBL:OQD86990.1};
OS Penicillium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=416450 {ECO:0000313|EMBL:OQD86990.1, ECO:0000313|Proteomes:UP000191672};
RN [1] {ECO:0000313|Proteomes:UP000191672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 31811 {ECO:0000313|Proteomes:UP000191672};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC subfamily. {ECO:0000256|ARBA:ARBA00006457}.
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:OQD86990.1}.
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DR EMBL; MDYN01000006; OQD86990.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6QCP7; -.
DR STRING; 416450.A0A1V6QCP7; -.
DR OrthoDB; 1327607at2759; -.
DR Proteomes; UP000191672; 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:UP000191672}.
FT DOMAIN 35..324
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 390..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 639 AA; 70821 MW; 630569BE3A2B6601 CRC64;
MAAEPISNGL LGSKNKKVAY FYDSDVGNYA YVSGHPMKPH RIRMTHSLVM NYGLYKKMEI
YRAKPASKYE MTQFHTDEYI DFLSKVTPDN MDHFSKEQSR YNVGDDCPVF DGLFEFCGIS
AGGSMEGAAR LNRNKCDVAV NWAGGLHHAK KSEASGFCYV NDIVLGILEL LRFKQRVLYV
DIDVHHGDGV EEAFYTTDRV MTVSFHKYGE YFPGTGELRD IGVGQGKHYA VNFPLRDGIN
DTSYKSIFEP VIKSVMEWYR PEAVVLQCGG DSLSGDRLGC FNLSMRGHAN CVNFIKSFDL
PTLILGGGGY TMRNVARTWA YETGILVGEG LESELPYNDY YEYFAPDYEL DVRPSNMDNA
NTKEYLDKIR NQVVENLKRT AFAPSVQMTD VPRNPILDGM DDEADDVLDD LDEDENKDKR
FTQRRFDQYT EKAGELSDSE DEEENAANGV RRQPGAIRRR NQVNYRNLEP DSGLDSGMAT
PQDASSAADG EMDSTLDAQM ADVPRTEPES TSGPQAEDTP ATDTDRMVLE TEEQGASTTS
QLQSPAPNDE DTMMEDAAPG PIDPEQAPAE GDSKKTEDTA PAQGSAPSPP RVRSPAKEAA
EPTSEKFEAP SAETSAPAAD INANKEEQST STEELKKEV
//
