GenomeNet

Database: UniProt
Entry: A0A1I8CDE5_9BILA
LinkDB: A0A1I8CDE5_9BILA
Original site: A0A1I8CDE5_9BILA 
ID   A0A1I8CDE5_9BILA        Unreviewed;       198 AA.
AC   A0A1I8CDE5;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Hist_deacetyl domain-containing protein {ECO:0000313|WBParaSite:RSKR_0000336300.1};
OS   Rhabditophanes sp. KR3021.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Alloionematidae;
OC   Rhabditophanes.
OX   NCBI_TaxID=114890 {ECO:0000313|Proteomes:UP000095286, ECO:0000313|WBParaSite:RSKR_0000336300.1};
RN   [1] {ECO:0000313|WBParaSite:RSKR_0000336300.1}
RP   IDENTIFICATION.
RC   STRAIN=KR3021 {ECO:0000313|WBParaSite:RSKR_0000336300.1};
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
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|ARBA:ARBA00001028};
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   AlphaFoldDB; A0A1I8CDE5; -.
DR   WBParaSite; RSKR_0000336300.1; RSKR_0000336300.1; RSKR_0000336300.
DR   Proteomes; UP000095286; Unplaced.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR   InterPro; IPR023801; His_deacetylse_dom.
DR   InterPro; IPR037138; His_deacetylse_dom_sf.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   PANTHER; PTHR48252:SF77; HIST_DEACETYL DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR48252; HISTONE DEACETYLASE 2-RELATED; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE   4: Predicted;
FT   DOMAIN          2..73
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
FT   REGION          169..198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        169..189
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   198 AA;  22633 MW;  2A3170B2F15FA322 CRC64;
     MERVLSHFRP EAIVLQLGAD SLSNDRLGCF NLTLKGHGKC AEYLKAQNIP IMFVGGGGYT
     VKNVARCWTY ETSIALDTEI SNELPYNDYF EYFGPDFKLH LPQSNIPNAN TREYLNKTQA
     TIFQNLKNLN FAPSVQMHEH KDHVLQFDPN SMEDMIDPNK RLTQFETDAT REHESELYDT
     EKEGNVRGTD ICHNEPGT
//
DBGET integrated database retrieval system