(data stored in SCRATCH zone)

SWISSPROT: C1E1L2_MICCC

ID   C1E1L2_MICCC            Unreviewed;       508 AA.
AC   C1E1L2;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   30-AUG-2017, entry version 39.
DE   RecName: Full=Histone deacetylase {ECO:0000256|PIRNR:PIRNR037913, ECO:0000256|SAAS:SAAS00818223};
DE            EC=3.5.1.98 {ECO:0000256|PIRNR:PIRNR037913, ECO:0000256|SAAS:SAAS00818223};
GN   ORFNames=MICPUN_79903 {ECO:0000313|EMBL:ACO61760.1};
OS   Micromonas commoda (strain RCC299 / NOUM17 / CCMP2709) (Picoplanktonic
OS   green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; prasinophytes; Mamiellophyceae;
OC   Mamiellales; Mamiellaceae; Micromonas.
OX   NCBI_TaxID=296587 {ECO:0000313|EMBL:ACO61760.1, ECO:0000313|Proteomes:UP000002009};
RN   [1] {ECO:0000313|EMBL:ACO61760.1, ECO:0000313|Proteomes:UP000002009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC299 / NOUM17 {ECO:0000313|Proteomes:UP000002009};
RX   PubMed=19359590; DOI=10.1126/science.1167222;
RA   Worden A.Z., Lee J.H., Mock T., Rouze P., Simmons M.P., Aerts A.L.,
RA   Allen A.E., Cuvelier M.L., Derelle E., Everett M.V., Foulon E.,
RA   Grimwood J., Gundlach H., Henrissat B., Napoli C., McDonald S.M.,
RA   Parker M.S., Rombauts S., Salamov A., Von Dassow P., Badger J.H.,
RA   Coutinho P.M., Demir E., Dubchak I., Gentemann C., Eikrem W.,
RA   Gready J.E., John U., Lanier W., Lindquist E.A., Lucas S., Mayer K.F.,
RA   Moreau H., Not F., Otillar R., Panaud O., Pangilinan J., Paulsen I.,
RA   Piegu B., Poliakov A., Robbens S., Schmutz J., Toulza E., Wyss T.,
RA   Zelensky A., Zhou K., Armbrust E.V., Bhattacharya D., Goodenough U.W.,
RA   Van de Peer Y., Grigoriev I.V.;
RT   "Green evolution and dynamic adaptations revealed by genomes of the
RT   marine picoeukaryotes Micromonas.";
RL   Science 324:268-272(2009).
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:SAAS00818219}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR037913,
CC       ECO:0000256|SAAS:SAAS00818221}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD Type 1
CC       subfamily. {ECO:0000256|PIRNR:PIRNR037913}.
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DR   EMBL; CP001324; ACO61760.1; -; Genomic_DNA.
DR   RefSeq; XP_002500502.1; XM_002500456.1.
DR   ProteinModelPortal; C1E1L2; -.
DR   GeneID; 8242119; -.
DR   KEGG; mis:MICPUN_79903; -.
DR   HOGENOM; HOG000225180; -.
DR   InParanoid; C1E1L2; -.
DR   KO; K06067; -.
DR   Proteomes; UP000002009; Chromosome 3.
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   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.
PE   3: Inferred from homology;
DR   PRODOM; C1E1L2.
DR   SWISS-2DPAGE; C1E1L2.
KW   Chromatin regulator {ECO:0000256|PIRNR:PIRNR037913,
KW   ECO:0000256|SAAS:SAAS00818226};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002009};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR037913,
KW   ECO:0000256|SAAS:SAAS00490343};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR037913-3};
KW   Nucleus {ECO:0000256|PIRNR:PIRNR037913,
KW   ECO:0000256|SAAS:SAAS00818233};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002009};
KW   Transcription {ECO:0000256|PIRNR:PIRNR037913,
KW   ECO:0000256|SAAS:SAAS00818215};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR037913,
KW   ECO:0000256|SAAS:SAAS00818213}.
FT   DOMAIN       24    313       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       260    260       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     299    299       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR037913-2}.
SQ   SEQUENCE   508 AA;  56288 MW;  C8D89A5872A56872 CRC64;
     MSGKPKISYF YDPDVGNFYY GQGHPMKPHR VRMTHNLLLH YGIYKEMEVF RPALASAEDM
     TKFHSDEYIE FLRLITPDNQ HEHMRQLKRF NCAEDCPVFD GLFNFCQIYT GGSVGGAVRL
     NHKQTDTVVN WAGGLHHAKK NEASGFCYVN DIVLAILELL KVHQRVLYID IDIHHGDGVE
     EAFYTTDRVM TVSFHKFGEY FPGTGHLQDV GQHRGKYYSV NVPLKDGIDD EAYVALFKPV
     MAKVMEMYQP DAVVFQSGAD SLTGDRLGCF NLSIRGHGEC LKYMQTFNVP LLVLGGGGYT
     IRNVARCWTY ETGCLLGHDL DNKLPVNDYS EYFGPTHELQ IQPSNMENQN TPEYLQGILN
     KILENLSKIP PKPSVPFHDV PPDAIDQDAM RVKEDPDAKG GGAEAEAARR SDPRELEPED
     GDVDDKPSRH DASMRDVEDV DGGEKKVKEE KVEGADAVKA ELGDAADVDD PDAAVKAEKG
     GEGATDANDG DAANAGGPGI MASDHGDQ
//

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