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Database: UniProt
Entry: C1MPA2_MICPC
LinkDB: C1MPA2_MICPC
Original site: C1MPA2_MICPC 
ID   C1MPA2_MICPC            Unreviewed;       818 AA.
AC   C1MPA2;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Histone deacetylase {ECO:0000313|EMBL:EEH58430.1};
GN   ORFNames=MICPUCDRAFT_38694 {ECO:0000313|EMBL:EEH58430.1};
OS   Micromonas pusilla (strain CCMP1545) (Picoplanktonic green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC   Mamiellaceae; Micromonas.
OX   NCBI_TaxID=564608 {ECO:0000313|Proteomes:UP000001876};
RN   [1] {ECO:0000313|EMBL:EEH58430.1, ECO:0000313|Proteomes:UP000001876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1545 {ECO:0000313|EMBL:EEH58430.1,
RC   ECO:0000313|Proteomes:UP000001876};
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., Gready J.E.,
RA   John U., Lanier W., Lindquist E.A., Lucas S., Mayer K.F., Moreau H.,
RA   Not F., Otillar R., Panaud O., Pangilinan J., Paulsen I., Piegu B.,
RA   Poliakov A., Robbens S., Schmutz J., Toulza E., Wyss T., Zelensky A.,
RA   Zhou K., Armbrust E.V., Bhattacharya D., Goodenough U.W., Van de Peer Y.,
RA   Grigoriev I.V.;
RT   "Green evolution and dynamic adaptations revealed by genomes of the marine
RT   picoeukaryotes Micromonas.";
RL   Science 324:268-272(2009).
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DR   EMBL; GG663737; EEH58430.1; -; Genomic_DNA.
DR   RefSeq; XP_003056785.1; XM_003056739.1.
DR   AlphaFoldDB; C1MPA2; -.
DR   STRING; 564608.C1MPA2; -.
DR   GeneID; 9682689; -.
DR   KEGG; mpp:MICPUCDRAFT_38694; -.
DR   eggNOG; KOG1343; Eukaryota.
DR   eggNOG; KOG4177; Eukaryota.
DR   OrthoDB; 69755at2759; -.
DR   Proteomes; UP000001876; Unassembled WGS sequence.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   CDD; cd11599; HDAC_classII_2; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR   Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
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   PANTHER; PTHR10625:SF4; HISTONE DEACETYLASE 6, ISOFORM G; 1.
DR   PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   SMART; SM00248; ANK; 4.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 2.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW   ProRule:PRU00023}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001876}.
FT   REPEAT          63..89
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          127..159
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          257..639
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
FT   REGION          35..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          754..818
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          684..713
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        43..59
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        771..818
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   818 AA;  87772 MW;  7E64C84B33FE425D CRC64;
     MFGSDSDDDE ITGQFALHDA AEAGNAELIA KMLGKEKKDG EFNPEEEEDD DDDDVDVNET
     DRDGCTPLHV ALFNSATECV KLLLENGAES WITVEGSPAL HVAYPTTEQL NTGDEDQPDP
     INARDKLGWT PLHHACYGGH ADIVNKLLAR GSKPGKVTKA GLTSLHAAVV GRNVAAVTAV
     MNAEPSILNN ACNDEKTAVE MADARGYPLI AAVLRGEDTS AVETPPPPPP PVIIAPDECF
     MHHSCPPITR DGRDPPPENV NRLQVLLNKK TGILRAAEFS NVDIVSEVRP ATMADVLRVH
     EYPYVRKIQK ICERIPDWNS NPNGALGTID GDTEVCHSSF SAALCAAGAV VEAVDRVVAG
     SAEKVFCAVR PPGHHAGPNG PVPAPGDPIG SGSHGFCLLN NVALGAAYAR CVHRHSLRRV
     AIIDFDVHHG NGTEAVVQNT TPAAPKFNFS TPYCEGAITV PTYRPWLDET DHEEVFFASV
     HGYGRARGFN FYPGSGPTDD TRHVGDYLTT EEAAQWNEEG VVDDPYHVAT AKSDSTAQGP
     TPWVVDVGME GTGKKAERGA AWRRVWRGKT LPAIAAFKPD LVLISAGFDA HAKDDIQGPV
     NLGVKEADYE WLTEELCKIA NTCCQGRVIS VLEGGYRIQG GVVSAFGRSV ASHLRAMFRE
     NREGWSAEQC QKELDIELKQ RRLAKEADEA KRAAAMEAAR QREEAAIAAA QAAMEAAGGD
     GDEAEAAAAA AAAAVLGDEA PTKRRRKAVD YTQLNAELEK ESNPAAAEAE EPAAEAEEPA
     AEAVEEEGEE DVEENGEELE MEDEDGGEEL EEDLEMEE
//
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