ID A0A0V1NRF3_9BILA Unreviewed; 511 AA.
AC A0A0V1NRF3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=histone deacetylase {ECO:0000256|ARBA:ARBA00012111};
DE EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111};
DE Flags: Fragment;
GN Name=HDAC1 {ECO:0000313|EMBL:KRZ86366.1};
GN ORFNames=T08_15457 {ECO:0000313|EMBL:KRZ86366.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ86366.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ86366.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ86366.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:KRZ86366.1}.
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DR EMBL; JYDM01000120; KRZ86366.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1NRF3; -.
DR STRING; 92180.A0A0V1NRF3; -.
DR Proteomes; UP000054924; Unassembled WGS sequence.
DR GO; GO:0004407; F:histone deacetylase activity; IEA:UniProtKB-EC.
DR CDD; cd09991; HDAC_classI; 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:SF25; HISTONE DEACETYLASE 3; 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:UP000054924};
KW Repressor {ECO:0000256|ARBA:ARBA00022491}.
FT DOMAIN 137..409
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 467..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..486
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRZ86366.1"
SQ SEQUENCE 511 AA; 58165 MW; C203E9D9557ED989 CRC64;
LLQLVLVVFN SSFEVSIYLG CRHFFIESFH GYHQYYVYSV KRRNTVCSQH ARYVRTGKTA
NVEFPKIFAA SIHTCVLTCK LSRSEWTVRC IFFEKHCDYS IYFLHYVFTQ ILRYSHAMLD
CASMKAEILR FQTPEWTNSL VQSYGLTQCM KVMKTEWASE DDLKVFHTNE YIEAIKVATK
TKSKKRGGDA DCPEFFGVLE YCCAVAGSSL SSARVMNART SDIIINWNGG MHHAKSYEAS
GFCFINDIVL AILELLKVYD RVLYVDIDCH HGDGVEEAFY TTNRVMTVSF HKYGDFFPGS
GRLEDIGLDE GEKYAVNVPL NSGIGDANYV ALFRMIITKI VEHFRPSAIV MQCGADSLAH
DRLGCFNLSV SGHGECVKFV RSLQIPLMLL GGGGYSLHNV ARCWTYETSI ALDVPISNDL
PFHEYYNFYS PSFKLHLPSA KNVLDMNGTR YLEYIRKCIC ENIHDKNSES SNPRKDSEDN
KSGNPPEDSE LLEIFEENEW LPGIDGIVHL K
//
