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Database: UniProt/TrEMBL
Entry: V4B2Z9_LOTGI
LinkDB: V4B2Z9_LOTGI
Original site: V4B2Z9_LOTGI 
ID   V4B2Z9_LOTGI            Unreviewed;       413 AA.
AC   V4B2Z9;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   22-NOV-2017, entry version 24.
DE   RecName: Full=Histone deacetylase {ECO:0000256|SAAS:SAAS00894283};
DE            EC=3.5.1.98 {ECO:0000256|SAAS:SAAS00894283};
GN   ORFNames=LOTGIDRAFT_237312 {ECO:0000313|EMBL:ESP04563.1};
OS   Lottia gigantea (Giant owl limpet).
OC   Eukaryota; Metazoa; Lophotrochozoa; Mollusca; Gastropoda;
OC   Patellogastropoda; Lottioidea; Lottiidae; Lottia.
OX   NCBI_TaxID=225164 {ECO:0000313|EMBL:ESP04563.1, ECO:0000313|Proteomes:UP000030746};
RN   [1] {ECO:0000313|EMBL:ESP04563.1, ECO:0000313|Proteomes:UP000030746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23254933; DOI=10.1038/nature11696;
RA   Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA   Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA   Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H.,
RA   Aerts A., Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V.,
RA   Lindberg D.R., Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT   "Insights into bilaterian evolution from three spiralian genomes.";
RL   Nature 493:526-531(2013).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
CC       a histone to yield a deacetylated histone.
CC       {ECO:0000256|SAAS:SAAS00894227}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|SAAS:SAAS00894298}.
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DR   EMBL; KB199699; ESP04563.1; -; Genomic_DNA.
DR   RefSeq; XP_009044732.1; XM_009046484.1.
DR   EnsemblMetazoa; LotgiT237312; LotgiP237312; LotgiG237312.
DR   GeneID; 20250420; -.
DR   KEGG; lgi:LOTGIDRAFT_237312; -.
DR   CTD; 20250420; -.
DR   KO; K11418; -.
DR   OMA; RVFTFSM; -.
DR   OrthoDB; EOG091G0EQP; -.
DR   Proteomes; UP000030746; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0032041; F:NAD-dependent histone deacetylase activity (H3-K14 specific); IEA:UniProtKB-EC.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.800.20; -; 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   Pfam; PF00850; Hist_deacetyl; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   SUPFAM; SSF52768; SSF52768; 1.
PE   4: Predicted;
KW   Chromatin regulator {ECO:0000256|SAAS:SAAS00894233};
KW   Complete proteome {ECO:0000313|Proteomes:UP000030746};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00870288};
KW   Nucleus {ECO:0000256|SAAS:SAAS00894277};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030746};
KW   Transcription {ECO:0000256|SAAS:SAAS00894309};
KW   Transcription regulation {ECO:0000256|SAAS:SAAS00894290}.
FT   DOMAIN       79    341       Hist_deacetyl. {ECO:0000259|Pfam:
FT                                PF00850}.
SQ   SEQUENCE   413 AA;  46926 MW;  3586B7CD671E4FC2 CRC64;
     MEDENDNNKL KRKKKHTTQL YKDVLNTQWP IIYTPEYNIS FMGLEKLHPF DSAKWGRVFE
     FLKGSTVFYH IYNYNVEAQM VRDDTIIKPL EATEEDLNFV HSKTYLNSLK WSWNVAGITE
     VPPVALLPNF VVQKKVLRPF RYQTGGTILA GKLALDRGWC INIGGGFHHC SAERGGGFCA
     YADITLSIKF LFEKVEGVSK VMIVDLDAHQ GNGHERDFMN DNRVYIMDVY NRGIYPHDGF
     AKRAIKRKIE LQHFTDDDVY LDLVRRHIEG ALNEFKPDII VYNAGTDILD GDPLGNLSIT
     PQGIIERDQI VFQKARTRGI PIFMVTSGGY LKQTARIIAD SILNLKTLGL ISWDEAEFAP
     LPEEISLPRS QSDGGLFAKM KRACISRSST QDFNQINNDI SPTSPDKPQI ENG
//
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