ID A0A2V0PE58_9CHLO Unreviewed; 897 AA.
AC A0A2V0PE58;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Histone deacetylase {ECO:0000313|EMBL:GBF98141.1};
GN ORFNames=Rsub_10553 {ECO:0000313|EMBL:GBF98141.1};
OS Raphidocelis subcapitata.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Sphaeropleales; Selenastraceae; Raphidocelis.
OX NCBI_TaxID=307507 {ECO:0000313|EMBL:GBF98141.1, ECO:0000313|Proteomes:UP000247498};
RN [1] {ECO:0000313|EMBL:GBF98141.1, ECO:0000313|Proteomes:UP000247498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-35 {ECO:0000313|EMBL:GBF98141.1,
RC ECO:0000313|Proteomes:UP000247498};
RX PubMed=29795299; DOI=10.1038/s41598-018-26331-6;
RA Suzuki S., Yamaguchi H., Nakajima N., Kawachi M.;
RT "Raphidocelis subcapitata (=Pseudokirchneriella subcapitata) provides an
RT insight into genome evolution and environmental adaptations in the
RT Sphaeropleales.";
RL Sci. Rep. 8:8058-8058(2018).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GBF98141.1}.
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DR EMBL; BDRX01000117; GBF98141.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V0PE58; -.
DR STRING; 307507.A0A2V0PE58; -.
DR InParanoid; A0A2V0PE58; -.
DR Proteomes; UP000247498; Unassembled WGS sequence.
DR GO; GO:0004407; F:histone deacetylase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.800.20; Histone deacetylase domain; 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 PANTHER; PTHR10625:SF16; HISTONE DEACETYLASE 15; 1.
DR PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PRINTS; PR01270; HDASUPER.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000247498}.
FT DOMAIN 448..766
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 71..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 841..897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..213
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..879
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 897 AA; 87828 MW; 879A8E66FE393580 CRC64;
MRAACPPLAG ARPARLRWLG NRGGGGGGGG GVAASGSVAR PRAARLLRPV ARPAPWRAYS
VQPADGVAAA EPLFKGGDGE LPLADPAAGL DARGGKPGPD AAAIAAATAA GAADSSDESD
AGSDATAIAA ALGSSSSSSN DDDGGSSGAP GPPSSVGSEA AGGGADCEAE DGAADEGAAE
GPWWQGEDEG EGAEGEEEGE WEVVEEGEGE GEGEEQAVGA AAPAAGDDGG PGPSSTALAS
ALALERARGI GADGAVLDIA RDAALALRLM GVLDPTGGAR QPGGGGDGPG SSGGGGDGGG
GAGGSWAGAE AAAAGQQGQG QAQGPSPDVV ADVVIGEARA RMRARPPGFC LNCCSPLERM
TGSGDAACGV CGHSAADDAA LLPPRPDGGW GSATAGTRDP ARAEAAEAVW NAAALARASG
LPAWPAARVL LAWHEDSLLH RAMLPPYPER PERLSAILAR LQASGLLEVC EAMPVLEASD
EALLSVHSAA LVGAIDALSP GTAFPEQLDG AGLSAASPPL APESLGNRHT ARAARLAAGA
AAGLAERLAR GEADAGFALV RPAGHLASEG SAEGGALYNN VAVAARAAQR AGAGRVLILD
WDAHAAKGTA SIFEDDASVV VVSMHKAGSW FYPGGCPLSQ VGRGPAAGTT VNIAWTAPAR
AGGRRGGGAE SMALEDVQPG GGDYLAAVSS IVAPIVREWG PDVILVSAGF DSAEGDPVGL
GSVPPPVFAH MTAMLRALGP PVGMVLEGGY VLKQTSACVE LCVRALMGER PPPLSALGTC
TPTTVGWNTI ARTLAVHQHF WSSLGTLSLA NALAGGAGAA PSPGGAADLA ALIAAAQGEA
ASARGGEGAE EGEQEEEWEV EEDGEWEEDD GEGEDEGSLA VAEVEVGPGE WAGETAA
//
