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Database: UniProt
Entry: V5BCB8_TRYCR
LinkDB: V5BCB8_TRYCR
Original site: V5BCB8_TRYCR 
ID   V5BCB8_TRYCR            Unreviewed;       651 AA.
AC   V5BCB8;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   22-FEB-2023, entry version 31.
DE   SubName: Full=Glucose-regulated protein 78 {ECO:0000313|EMBL:ESS63712.1};
GN   ORFNames=TCDM_08367 {ECO:0000313|EMBL:ESS63712.1};
OS   Trypanosoma cruzi Dm28c.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX   NCBI_TaxID=1416333 {ECO:0000313|EMBL:ESS63712.1, ECO:0000313|Proteomes:UP000017861};
RN   [1] {ECO:0000313|EMBL:ESS63712.1, ECO:0000313|Proteomes:UP000017861}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Dm28c {ECO:0000313|EMBL:ESS63712.1,
RC   ECO:0000313|Proteomes:UP000017861};
RX   PubMed=24482508;
RA   Grisard E.C., Teixeira S.M., de Almeida L.G., Stoco P.H., Gerber A.L.,
RA   Talavera-Lopez C., Lima O.C., Andersson B., de Vasconcelos A.T.;
RT   "Trypanosoma cruzi Clone Dm28c Draft Genome Sequence.";
RL   Genome Announc. 2:e01114-13(2014).
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|RuleBase:RU003322}.
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:ESS63712.1}.
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DR   EMBL; AYLP01000115; ESS63712.1; -; Genomic_DNA.
DR   AlphaFoldDB; V5BCB8; -.
DR   SMR; V5BCB8; -.
DR   EnsemblProtists; ESS63712; ESS63712; TCDM_08367.
DR   VEuPathDB; TriTrypDB:TCDM_08367; -.
DR   Proteomes; UP000017861; Unassembled WGS sequence.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   CDD; cd10241; HSPA5-like_NBD; 1.
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; IPR042050; BIP_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; PS00297; HSP70_1; 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   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU003322};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017861};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..651
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004731344"
FT   REGION          602..651
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          529..556
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        604..620
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   651 AA;  71346 MW;  3321776476C67957 CRC64;
     MLLQALLVLS AVVVAVAAPD GTGKVEAPCV GIDLGTTYSV VGVWQKGDVH IIPNDMGNRI
     TPSVVAFTET ERLIGDGAKN QLPQNPHNTI YAIKRLIGRK YSDTTVQTDK KLLSYEVVAD
     KDGKPKVQVE VGGKKKQFTP EEVSAMVLQK MKEIAETYLG EKVKNAVVTV PAYFNDAQRQ
     STKDAGTIAG LNVVRIINEP TAAAIAYGLN KAGEKNILVF DLGGGTFDVS LLTIDEGFFE
     VVATNGDTHL GGEDFDNNMM RYFVDMLKKK KNVDVSKDQK ALARLRKACE AAKRQLSSHP
     EARVEVDSLT EGFDFSEKIT RAKFEELNME LFKGTLVPVQ RVLEDAKLKK SDIHEIVLVG
     GSTRVPKVQQ LIRDFFGGKE PNRGINPDEA VAYGAAVQAA VLTGESEVGG RVVLVDVIPL
     SLGIETVGGV MTKLIERNTQ IPTKKSQVFS TYQDNQPGVL IQVYEGERQM TKDNRLLGKF
     ELSGIPPAPR GVPQIEVTFD VDENSILQVS AVDKSSGKKE EITITNDKGR LSEEEIERMV
     REAAEFEDED RKVRERVDAR NSLESVAYSL RNQVNDKEKL GGKLSADDKS AVEAAVKEAM
     QFLDDNPNAD KEEYDEARDK LQSVTNPIIQ KVYQSGGGAD GDERPEPMDD L
//
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