ID A0A0V1BII1_TRISP Unreviewed; 920 AA.
AC A0A0V1BII1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Histone deacetylase 10 {ECO:0000313|EMBL:KRY36794.1};
DE Flags: Fragment;
GN Name=Hdac10 {ECO:0000313|EMBL:KRY36794.1};
GN ORFNames=T01_7552 {ECO:0000313|EMBL:KRY36794.1};
OS Trichinella spiralis (Trichina worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6334 {ECO:0000313|EMBL:KRY36794.1, ECO:0000313|Proteomes:UP000054776};
RN [1] {ECO:0000313|EMBL:KRY36794.1, ECO:0000313|Proteomes:UP000054776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS3 {ECO:0000313|EMBL:KRY36794.1};
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 -!- 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:KRY36794.1}.
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DR EMBL; JYDH01000039; KRY36794.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1BII1; -.
DR STRING; 6334.A0A0V1BII1; -.
DR eggNOG; KOG1343; Eukaryota.
DR InParanoid; A0A0V1BII1; -.
DR Proteomes; UP000054776; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd10002; HDAC10_HDAC6-dom1; 1.
DR Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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 InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR PANTHER; PTHR10625:SF4; HISTONE DEACETYLASE 6, ISOFORM G; 1.
DR PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR PRINTS; PR01270; HDASUPER.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00502};
KW Reference proteome {ECO:0000313|Proteomes:UP000054776};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00502};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00502}.
FT DOMAIN 833..920
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRY36794.1"
SQ SEQUENCE 920 AA; 102965 MW; DF108F7CCE4ED6A4 CRC64;
LASVWPVRRA GLFFVLLKRV MDRSASIGQP FYETVAGVDK SSLATLLFNG DSGNDNDCFL
PGYVTDRRML LHRNIWFPNH IETPERLSSI LDLCDQQGLF DRMKKIPSRL ASLDEIELFH
SKDYVQQVAS FESMGAEELQ KASSTYDSVY ACQHSFTAAR LAVGSLLNAT EAVLMKRCVN
AIALVRPPGH HAMLDAANGF CLFNNVGIAA AHALNAFRLD RILIVDWDVH YGQGIQQKFI
NSKQILCVSI HRHEFGSFWP HMPESDWNNV GQDDGLGFNV NVPLNVRGLG DADYLAIFHH
ILLPLAIEFQ PQLILVSAGF DAAVGCPEGE MLLSPRIFAH FTKMLASVAA GRLVISLEGG
YCIPSLSWSV SCVVRALLND PIPKLAGLNV PVNPYVVDAM LSLARRLKPY WKCMGHLLSA
VNATLTRANQ KPLPAHDSVF SAKRTDQTEA TCTTILETGH VSNQDHLTNV ISDIEKLQLH
ANKNGISARG RVDLRVDMVT QPYGDFNFDR LAVFLPEKRW RDAFLIQSTK NNLKKTMHSF
LKLMFIKCII STSDEHNEDF SRCIKEVEDF AQSLLNGVSV CGCLITEHCV TNFWNMEREV
SATLANSTAC NVLFVCLSSA MVRVERRSVG QLKVTSVAIP FIHDATRVDH NILDENIVHP
DCYNVDLLWS VPNPTTADRL FIFLHFLLPY VTAISPELVI LNVDLDHPNA KHLAPSLLSF
IVSNFLTLAN SRLLVSANVP TVSYPDKYIK SSLTALLSAL AGCDMPIDTL LSNKLSNYSI
TMVAELVYQL RTVLPTLQSV LLPVSLIDGL PVDMNLWFGR MHRPRPLKIL HDYFCKHLKL
NSADLISYRT WSTKTPCKIC SNRIGNWVCL ICSEVFCDSN VNSHREQHRE MERNHNFFVN
VTESSVYCYL CNAESGYRSY
//
