ID C9ZIZ6_TRYB9 Unreviewed; 685 AA.
AC C9ZIZ6;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Histone deacetylase, putative {ECO:0000313|EMBL:CBH09354.1};
GN ORFNames=TbgDal_II760 {ECO:0000313|EMBL:CBH09354.1};
OS Trypanosoma brucei gambiense (strain MHOM/CI/86/DAL972).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=679716 {ECO:0000313|EMBL:CBH09354.1, ECO:0000313|Proteomes:UP000002316};
RN [1] {ECO:0000313|Proteomes:UP000002316}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/CI/86/DAL972 {ECO:0000313|Proteomes:UP000002316};
RX PubMed=20404998; DOI=10.1371/journal.pntd.0000658;
RA Jackson A.P., Sanders M., Berry A., McQuillan J., Aslett M.A., Quail M.A.,
RA Chukualim B., Capewell P., MacLeod A., Melville S.E., Gibson W.,
RA Barry J.D., Berriman M., Hertz-Fowler C.;
RT "The genome sequence of Trypanosoma brucei gambiense, causative agent of
RT chronic human african trypanosomiasis.";
RL PLoS Negl. Trop. Dis. 4:E658-E658(2010).
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DR EMBL; FN554965; CBH09354.1; -; Genomic_DNA.
DR RefSeq; XP_011771660.1; XM_011773358.1.
DR AlphaFoldDB; C9ZIZ6; -.
DR GeneID; 23858843; -.
DR KEGG; tbg:TbgDal_II760; -.
DR VEuPathDB; TriTrypDB:Tbg.972.2.760; -.
DR OrthoDB; 124800at2759; -.
DR Proteomes; UP000002316; Chromosome 2.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd09992; HDAC_classII; 1.
DR Gene3D; 3.40.800.20; Histone deacetylase domain; 2.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR10625:SF7; DEACETYLASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR Pfam; PF00850; Hist_deacetyl; 3.
DR SUPFAM; SSF52768; Arginase/deacetylase; 2.
PE 4: Predicted;
FT DOMAIN 141..276
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT DOMAIN 306..341
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT DOMAIN 515..637
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 685 AA; 75261 MW; BC2AA175095ACEC1 CRC64;
MGKETREAES VENDDKRVNK KVKKETSSSS VATRKEGGEP HHDEEMSHPN FRRCTDRLET
YIHNWMGQAH GVPSVLPTAL PPIDPLPTIL DMMIPEVNET SITLTTMTPT LDITAIEAEG
TGVAYDEVTL LHASTDPGDY ERPGRLQRTL DHLEVIGLLK CCRRLHHRSA RTRELRLVHS
TEHIDSVDQL EVATLLRKPG ESCNVGEDLY ANENTSRAAR AAAGCAIAAA LSVVRGEVRN
SFALIRPPGH HAGRDRASGF CFFNNVAVAV RAAQRELKKL QEGGNAAPSP RSSGGPCEPA
STAAEPRVLV IDWDVHHCDG TENIFYEDPS VVVVSIHQHG SKRGHILRKN PTVVDNIVEL
DDLAALMDPI EDVKPELCGG DDSVRNKETD QEVAEGLACG TVPNERSPVK EEEPTGGECK
HESPQDDEEK KESSCRRQRK PVDYNKLAEE MANQDDELAR IFGVNAEELA RFPESGSSGS
ESDSSTSSES HERAGKLSGD SEGYSYSDED SSNEPRPFYP STGHMDRVGG DANPEAKGKN
INIPWPTHNM GDLEYLQVVL DVVLPVMREF EPEVVFVSCG FDSAARDLLG SMQVTPSGYY
LLVKALAAVC PKLVVVLEGG YNLSNVARCS EAVMRALLES NGSRSKLPRS RMLWCQAEEL
VQQVRETHGG YWQCLNPNSF DHMCK
//
