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HDT1_SOYBN
ID   HDT1_SOYBN              Reviewed;         295 AA.
AC   Q8LJS2;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Histone deacetylase HDT1;
DE   AltName: Full=Histone deacetylase 2a;
DE            Short=HD2a;
DE   AltName: Full=Nucleolar histone deacetylase HD2-p39;
GN   Name=HDT1; Synonyms=HD2A;
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Seed coat;
RA   Tang T.J., Wang C.S.;
RT   "Nucleotide sequence of a cDNA encoding soybean nucleolar histone
RT   deacetylase HD2-p39.";
RL   Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Mediates the deacetylation of lysine residues on the N-
CC       terminal part of the core histones (H2A, H2B, H3 and H4). Histone
CC       deacetylation gives a tag for epigenetic repression and plays an
CC       important role in transcriptional regulation, cell cycle progression
CC       and developmental events (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase HD2 family.
CC       {ECO:0000305}.
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DR   EMBL; AF532618; AAN03465.1; -; mRNA.
DR   RefSeq; NP_001235884.1; NM_001248955.1.
DR   AlphaFoldDB; Q8LJS2; -.
DR   SMR; Q8LJS2; -.
DR   STRING; 3847.GLYMA12G09000.1; -.
DR   PRIDE; Q8LJS2; -.
DR   GeneID; 547649; -.
DR   KEGG; gmx:547649; -.
DR   eggNOG; ENOG502QVH6; Eukaryota.
DR   InParanoid; Q8LJS2; -.
DR   OrthoDB; 1260281at2759; -.
DR   Proteomes; UP000008827; Unplaced.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR   GO; GO:0010162; P:seed dormancy process; IBA:GO_Central.
DR   InterPro; IPR041232; NPL.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF17800; NPL; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE   2: Evidence at transcript level;
KW   Chromatin regulator; Hydrolase; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repressor; Transcription; Transcription regulation;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..295
FT                   /note="Histone deacetylase HDT1"
FT                   /id="PRO_0000195212"
FT   ZN_FING         269..292
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          105..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..135
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        159..197
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        198..213
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        228..242
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        250..271
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   295 AA;  31354 MW;  63B4B45832CAA039 CRC64;
     MEFWGVEVKV GQTVTVDPMD PVDSYIHISQ VALGEAKKDK PNEPVVLYLK VGEQKIVLGT
     LSRDGIPHLS LDLVLDSDSE LSHTSKSASV FFCGYKVLTG NDNASDFSDS SEEDEELALE
     GQDNGKPELK AEGAKVTKPS KSIPKIGAPA KAADPKKDED DDSDDESDDD LAGEDESGSS
     DEMDDDSNSE EESDGDDEET PAKKVDQGKK RPNESAAKTP ISAKKAKTAT PEKTDGKKSV
     HVATPHPSKK GGKTPNSTKG QTPNSAGQLS CASCKKSFTN EAGLQQHKKA KHGGQ
 
 
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