GenomeNet

Database: UniProt
Entry: X0CQE6_FUSOX
LinkDB: X0CQE6_FUSOX
Original site: X0CQE6_FUSOX 
ID   X0CQE6_FUSOX            Unreviewed;       650 AA.
AC   X0CQE6;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=histone deacetylase {ECO:0000256|ARBA:ARBA00012111};
DE            EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111};
GN   ORFNames=FOQG_03436 {ECO:0000313|EMBL:EXK96376.1};
OS   Fusarium oxysporum f. sp. raphani 54005.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=1089458 {ECO:0000313|EMBL:EXK96376.1, ECO:0000313|Proteomes:UP000030663};
RN   [1] {ECO:0000313|EMBL:EXK96376.1, ECO:0000313|Proteomes:UP000030663}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=54005 {ECO:0000313|EMBL:EXK96376.1,
RC   ECO:0000313|Proteomes:UP000030663};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA   Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusarium oxysporum PHW815.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC       subfamily. {ECO:0000256|ARBA:ARBA00006457}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JH658365; EXK96376.1; -; Genomic_DNA.
DR   AlphaFoldDB; X0CQE6; -.
DR   eggNOG; KOG1342; Eukaryota.
DR   HOGENOM; CLU_007727_0_0_1; -.
DR   Proteomes; UP000030663; Unassembled WGS sequence.
DR   GO; GO:1902494; C:catalytic complex; IEA:UniProt.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR   GO; GO:0004407; F:histone deacetylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0010468; P:regulation of gene expression; IEA:UniProt.
DR   CDD; cd10004; RPD3-like; 1.
DR   Gene3D; 3.40.800.20; Histone deacetylase domain; 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:SF13; HISTONE DEACETYLASE HDAC1; 1.
DR   PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   PRINTS; PR01271; HISDACETLASE.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030663}.
FT   DOMAIN          39..327
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
FT   REGION          384..419
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          449..650
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        461..475
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        521..548
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        556..570
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        600..614
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        623..643
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   650 AA;  72147 MW;  19AFEAF6319FFF89 CRC64;
     MGDDIRVELG SVALNGSSPK KVAYFYDSDI GNYAYVTGHP MKPHRIRLAH SLIMQYNLYQ
     KMEIYRAKPA TRGEMTQFHT DDYIDFLQKV TPDNMDSFMR EQGKYNVGDD CPVFDGLFEF
     CGISAGGSME GAARLNRQKC DIAINWAGGL HHAKKCEASG FCYVNDIVLG ILELLRFKKR
     VLYIDIDVHH GDGVEEAFYT TDRVMTVSFH KYGEYFPGTG ELRDTGIGQG KNYAVNFPLR
     DGITDVSYRS IFQPVIENVM KYYQPEAVVL QCGGDSLSGD RLGCFNLSMD GHANCVNYVK
     SFNLPTLVLG GGGYTMRNVA RTWAFETGVL VGKEMDRTLP YNEYYEYYAP DFELNVRSSN
     MENSNSREYL EKITSSVIDN LRQTGPAPSV QLQDVPRKPF GGMTDEEEAE LDDLDEDENK
     DVRMTEHRWD KHVEHDNEFE ASDDDEMAQA HGATRQNGNK RTFTDYRKGE MEIDNADAPP
     AKVTNGASAD EPAEEQAGED AHDVNDDTID DISAPAPAEK EAPPKESEKP DEATKEAEAS
     KVDGDGDVGM EDSAAPEETT IKKEEVEPEA PAEPSAPTEK ASKDEPAAQE ATDSATKEPT
     TEPKTIEETS DKPAAAPEKA QSEQPDDAMD VDTEKDKPEP PIEKSKSPVN
//
DBGET integrated database retrieval system