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Database: UniProt
Entry: D0A7U5_TRYB9
LinkDB: D0A7U5_TRYB9
Original site: D0A7U5_TRYB9 
ID   D0A7U5_TRYB9            Unreviewed;       593 AA.
AC   D0A7U5;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Glucose-regulated protein 78, putative {ECO:0000313|EMBL:CBH17746.1};
GN   ORFNames=TbgDal_XI8650 {ECO:0000313|EMBL:CBH17746.1};
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:CBH17746.1, 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).
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|RuleBase:RU003322}.
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DR   EMBL; FN554974; CBH17746.1; -; Genomic_DNA.
DR   RefSeq; XP_011780010.1; XM_011781708.1.
DR   AlphaFoldDB; D0A7U5; -.
DR   GeneID; 23867901; -.
DR   KEGG; tbg:TbgDal_XI8650; -.
DR   VEuPathDB; TriTrypDB:Tbg972.11.8650; -.
DR   OrthoDB; 143at2759; -.
DR   Proteomes; UP000002316; Chromosome 11.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 3.30.30.30; -; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR029048; HSP70_C_sf.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR19375:SF144; ENDOPLASMIC RETICULUM CHAPERONE BIP; 1.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR   SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU003322}.
FT   COILED          474..501
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   593 AA;  65221 MW;  70CFB17B72C1B177 CRC64;
     MGNRITPSVV AFTDTERLIG DGAKNQLPQN PHNTIYTIKR LIGRKYTDAA VQADKKLLSY
     EVIADRDGKP KVQVMVGGKK KQFTPEEISA MVLQKMKEIA ETYLGEKVKN AVVTVPAYFN
     DAQRQSTKDA GTIAGLNVVR IINEPTAAAI AYGLNKAGEK NILVFDLGGG TFDVSLLTID
     EGFFEVVATN GDTHLGGEDF DNNMMRHFVD MLKKKKNVDI SKDQKALARL RKACEAAKRQ
     LSSHPEARVE VDSLTEGFDF SEKITRAKFE ELNMDLFKGT LVPVQRVLED AKLKKSDIHE
     IVLVGGSTRV PKVQQLISDF FGGKELNRGI NPDEAVAYGA AVQAAVLTGE SEVGGRVVLV
     DVIPLSLGIE TVGGVMTKLI ERNTQIPTKK SQVFSTHADN QPGVLIQVYE GERQLTKDNR
     LLGKFELSGI PPAARGVPQI EVTFDVDENS ILQVSAMDKS SGKKEEITIT NDKGRLSEEE
     IERMVREAAE FEDEDRKVRE RVDARNSLES VAYSLRNQVN DKDKLGGKLD PNDKAAVETA
     VAEAIRFLDE NPNAEKEEYK TALETLQSVT NPIIQKTYQS AGGGDKPQPM DDL
//
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