ID A0A0N4WGT6_HAEPC Unreviewed; 725 AA.
AC A0A0N4WGT6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Hist_deacetyl domain-containing protein {ECO:0000313|WBParaSite:HPLM_0001005001-mRNA-1};
GN ORFNames=HPLM_LOCUS10042 {ECO:0000313|EMBL:VDO39050.1};
OS Haemonchus placei (Barber's pole worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Trichostrongylidae; Haemonchus.
OX NCBI_TaxID=6290 {ECO:0000313|Proteomes:UP000038042, ECO:0000313|WBParaSite:HPLM_0001005001-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:HPLM_0001005001-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDO39050.1, ECO:0000313|Proteomes:UP000268014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHpl1 {ECO:0000313|EMBL:VDO39050.1,
RC ECO:0000313|Proteomes:UP000268014};
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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};
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DR EMBL; UZAF01017201; VDO39050.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N4WGT6; -.
DR STRING; 6290.A0A0N4WGT6; -.
DR WBParaSite; HPLM_0001005001-mRNA-1; HPLM_0001005001-mRNA-1; HPLM_0001005001.
DR OMA; QKVIAIH; -.
DR Proteomes; UP000038042; Unplaced.
DR Proteomes; UP000268014; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR InterPro; IPR000286; His_deacetylse.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR10625:SF15; HISTONE DEACETYLASE; 1.
DR PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PRINTS; PR01270; HDASUPER.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000268014}.
FT DOMAIN 343..656
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 124..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 725 AA; 78325 MW; 12E0BE162A7017B9 CRC64;
MCFPIFSFEC FDNHCFRFFS EHRNASTNST STTISQHTKD RLKNMIAQRN REGSQTNLAG
TASLIPLYGP SLQVNVSSPH FEPYRVPASL HSVQAVSCQP SGEYQLRKVN SEPNLKMRIR
AKLLSKGSSP VQNQSSFSFT HPQLKRSDSE TSSNGGTTGG ANLAMDALLS NAAATAFPPH
LIMPSPSLPN LAAPTLAQPP QLPIGNHSNM ASLMAAAQLT PFLSLPSLLK TQLGLGGGLL
EDDITDRSKL APGVAALGAL SQQVPVGGYP SLLKQQLREL VLRRKSLVRE EPEDDDSLVT
QPVLGQMPTT LGLGELSSGK ATGLAYDSSM ARHECVCGES SSHVEHGGRV QSIWARLLER
GLVQRCERTA AKKASLEQLR MVHSPTYVTF FAVSPTACLK MEASQLPLKS FVQLPCGGIG
IDSDTYFNDA TTQTAARVAA GSLIELASQV AENRLRNGFA CIRPPGHHSE RDQAMGFCFF
NNVAITARYL QQKYPRQCSR IAIIDWDVHH GNGTQLCFEE DPSVLYLSLH RHDNGNFFPG
TGAVTEVGRG AGKGYSVNVP FSGGVMRDAD YLAAWRVVVH PILEQFQPNF ILVSAGFDAC
CGHPNALGGY KISAEMFGFM TRQLMGFAGG RVVLALEGGY DLASISDAAE QCVKVLCGDD
DKAGLLNSEA LEGIPCLSAQ ETIQKVIAIH KGYWPNLTAE QGLTTSELHW QTVGRQFQNL
TMGTV
//