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Database: UniProt/TrEMBL
Entry: I0ZAS6_COCSC
LinkDB: I0ZAS6_COCSC
Original site: I0ZAS6_COCSC 
ID   I0ZAS6_COCSC            Unreviewed;       428 AA.
AC   I0ZAS6;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   22-NOV-2017, entry version 29.
DE   RecName: Full=Histone deacetylase {ECO:0000256|PIRNR:PIRNR037913, ECO:0000256|SAAS:SAAS00894283};
DE            EC=3.5.1.98 {ECO:0000256|PIRNR:PIRNR037913, ECO:0000256|SAAS:SAAS00894283};
GN   ORFNames=COCSUDRAFT_52257 {ECO:0000313|EMBL:EIE27745.1};
OS   Coccomyxa subellipsoidea (strain C-169) (Green microalga).
OC   Eukaryota; Viridiplantae; Chlorophyta; Trebouxiophyceae;
OC   Trebouxiophyceae incertae sedis; Coccomyxaceae; Coccomyxa.
OX   NCBI_TaxID=574566 {ECO:0000313|EMBL:EIE27745.1, ECO:0000313|Proteomes:UP000007264};
RN   [1] {ECO:0000313|EMBL:EIE27745.1, ECO:0000313|Proteomes:UP000007264}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C-169 {ECO:0000313|EMBL:EIE27745.1,
RC   ECO:0000313|Proteomes:UP000007264};
RX   PubMed=22630137; DOI=10.1186/gb-2012-13-5-r39;
RA   Blanc G., Agarkova I., Grimwood J., Kuo A., Brueggeman A., Dunigan D.,
RA   Gurnon J., Ladunga I., Lindquist E., Lucas S., Pangilinan J.,
RA   Proschold T., Salamov A., Schmutz J., Weeks D., Yamada T.,
RA   Claverie J.M., Grigoriev I., Van Etten J., Lomsadze A., Borodovsky M.;
RT   "The genome of the polar eukaryotic microalga coccomyxa subellipsoidea
RT   reveals traits of cold adaptation.";
RL   Genome Biol. 13:R39-R39(2012).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
CC       a histone to yield a deacetylated histone.
CC       {ECO:0000256|PIRNR:PIRNR037913, ECO:0000256|SAAS:SAAS00894227}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR037913,
CC       ECO:0000256|SAAS:SAAS00894298}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD Type 1
CC       subfamily. {ECO:0000256|PIRNR:PIRNR037913}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EIE27745.1}.
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DR   EMBL; AGSI01000001; EIE27745.1; -; Genomic_DNA.
DR   RefSeq; XP_005652289.1; XM_005652232.1.
DR   ProteinModelPortal; I0ZAS6; -.
DR   GeneID; 17045760; -.
DR   KEGG; csl:COCSUDRAFT_52257; -.
DR   KO; K06067; -.
DR   Proteomes; UP000007264; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 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; PTHR10625; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PIRSF; PIRSF037913; His_deacetylse_1; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   PRINTS; PR01271; HISDACETLASE.
DR   SUPFAM; SSF52768; SSF52768; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator {ECO:0000256|PIRNR:PIRNR037913,
KW   ECO:0000256|SAAS:SAAS00894233};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007264};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR037913,
KW   ECO:0000256|SAAS:SAAS00870288};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR037913-3};
KW   Nucleus {ECO:0000256|PIRNR:PIRNR037913,
KW   ECO:0000256|SAAS:SAAS00894277};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007264};
KW   Transcription {ECO:0000256|PIRNR:PIRNR037913,
KW   ECO:0000256|SAAS:SAAS00894309};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR037913,
KW   ECO:0000256|SAAS:SAAS00894290}.
FT   DOMAIN       24    316       Hist_deacetyl. {ECO:0000259|Pfam:
FT                                PF00850}.
FT   ACT_SITE    137    137       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR037913-1}.
FT   METAL       172    172       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR037913-3}.
FT   METAL       174    174       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR037913-3}.
FT   METAL       261    261       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR037913-3}.
FT   BINDING      95     95       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR037913-2}.
FT   BINDING     145    145       Substrate; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR037913-2}.
FT   BINDING     300    300       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR037913-2}.
SQ   SEQUENCE   428 AA;  49279 MW;  24B05D307CD3B738 CRC64;
     MERKKKVAYF YDSEFGEMYY GANHPMKPHR LCMTHHLVLA YDLHKRLEVY RPRMAYPMEL
     MQFHSEDYVN FLARVTPDNQ EEMHQQLVQF NLGEDCPVFD GLYDFCRRYA GASVEGAVKL
     NQELADIAIN WSGGLHHAKK AEASGFCYVN DLVLGILELL KYHARVLYVD IDIHHGDGVE
     EAFYLTDRVL TVSFHKYGNY FFPGTGDLKD IGERHGKFYS INVPMKDGTD DATFHRLFKP
     IMAKVMEVFS PGAVVLQCGA DSLAADRLGC FNLSLEGHAE AVRFMKKFNV PMLVTGGGGY
     TKNNVSRCWT AETAVLVDQN IADDLPPNDY YEYYAPDYRL HVTPHRHMDN NNAKPDIERI
     KREVLENLRE LAHTPSVQMH EAPPDTYVPE YDIEEEENAD VRLGKYACDH LVVRETEYYE
     DDRDHFGD
//
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