ID B8LXQ0_TALSN Unreviewed; 763 AA.
AC B8LXQ0;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Histone deacetylase {ECO:0000256|PIRNR:PIRNR037919};
DE EC=3.5.1.98 {ECO:0000256|PIRNR:PIRNR037919};
GN ORFNames=TSTA_079080 {ECO:0000313|EMBL:EED24551.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED24551.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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; EQ962652; EED24551.1; -; Genomic_DNA.
DR RefSeq; XP_002341938.1; XM_002341897.1.
DR AlphaFoldDB; B8LXQ0; -.
DR STRING; 441959.B8LXQ0; -.
DR ESTHER; talsn-b8lxq0; Arb2_domain.
DR GeneID; 8102298; -.
DR VEuPathDB; FungiDB:TSTA_079080; -.
DR eggNOG; KOG1343; Eukaryota.
DR HOGENOM; CLU_007727_4_0_1; -.
DR InParanoid; B8LXQ0; -.
DR OMA; FVSPACY; -.
DR OrthoDB; 124800at2759; -.
DR PhylomeDB; B8LXQ0; -.
DR Proteomes; UP000001745; 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:UP000001745};
KW Repressor {ECO:0000256|PIRNR:PIRNR037919};
KW Transcription {ECO:0000256|PIRNR:PIRNR037919};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR037919}.
FT DOMAIN 129..442
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT DOMAIN 491..747
FT /note="Arb2-like"
FT /evidence="ECO:0000259|Pfam:PF09757"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 763 AA; 85312 MW; 6E0F02FF5CFC7E5B CRC64;
MDRDEDTVMR DSGPPFSTAP ARATTEDSLQ PATLLGMPKL PSSLLSAPAG NPIPSTDIHG
LTKSIEDEGL HMIKSSEESD SIMEENSDWS VDDTSATAPG LPVASLATGL CYDIRMRYHC
EVRPAAEVHP EDPRRIYYIY KEICRAGLIE DLDIVSSPKP LVPMPLKRID VRNATKEEVE
LVHTDEHFQF VSDTQNLPDE TLIMLEESRD SIYFNRLTFA SALLSAGGAI ETCLAVATRK
VKNAIAVIRP PGHHAEHDKT MGFCLFNNVS IAAKVCQRKL GEACRKILIV DWDVHHGNGI
QKAFYDEPNV LYISLHVYAD GKFYPGGKEG NWDAVGEGAG LGKNINIPWP SQGMGDGDYM
FAFQQVIMPI ASEFDPDLVI VASGFDAAAG DELGGCFVTP ACYSHMTHML MTLANGKVSV
CLEGGYNFRS ISKSALAVTK TLMGEPPARL AATMPSNPAV QVVRTVMAAQ SKYWRCMYPK
IPTQEGLYTD RFHDVIRQYQ AKKLYDNYKL TSLWIYRASI SKSFENQVLA SSNYDKAVPL
VVIFHDPPDM MGIHHPITNK LEPHNCWMAD VVKDYIAWAH RRNYAIIDVN IPKHVTADSS
DIGKFEEDDV DRPAQTEELA GYLWDNYIEP NDATHIFFIG VGDAFYGVAN LLINRDSIYQ
RVNSVISFVA ENPVRAVASP TQTWLSRWYK DNSLVFVAHT HGVWHNENRR KPSKRYGRLL
RSPKTGLNEM LLQHKTEVFT WIEQRVNVDA DETDEDETEE AKE
//
