ID A4I5T0_LEIIN Unreviewed; 660 AA.
AC A4I5T0; A0A2K4Z0P2; A0A381MQN6;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE SubName: Full=Putative heat shock 70-related protein 1, mitochondrial {ECO:0000313|EMBL:CAM70152.1};
GN ORFNames=LINJ_30_2540 {ECO:0000313|EMBL:CAM70152.1};
OS Leishmania infantum.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5671 {ECO:0000313|EMBL:CAM70152.1, ECO:0000313|Proteomes:UP000008153};
RN [1] {ECO:0000313|EMBL:CAM70152.1, ECO:0000313|Proteomes:UP000008153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPCM5 {ECO:0000313|EMBL:CAM70152.1,
RC ECO:0000313|Proteomes:UP000008153};
RX PubMed=17572675; DOI=10.1038/ng2053;
RA Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A.,
RA Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A.,
RA Fraser A., Rajandream M.A., Carver T., Norbertczak H., Chillingworth T.,
RA Hance Z., Jagels K., Moule S., Ormond D., Rutter S., Squares R.,
RA Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S.,
RA Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P.,
RA Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R., Barrell B., Cruz A.K.,
RA Mottram J.C., Smith D.F., Berriman M.;
RT "Comparative genomic analysis of three Leishmania species that cause
RT diverse human disease.";
RL Nat. Genet. 39:839-847(2007).
RN [2] {ECO:0000313|EMBL:CAM70152.1, ECO:0000313|Proteomes:UP000008153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPCM5 {ECO:0000313|EMBL:CAM70152.1,
RC ECO:0000313|Proteomes:UP000008153};
RX PubMed=22038252; DOI=10.1101/gr.122945.111;
RA Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA Hertz-Fowler C., Mottram J.C.;
RT "Chromosome and gene copy number variation allow major structural change
RT between species and strains of Leishmania.";
RL Genome Res. 21:2129-2142(2011).
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|RuleBase:RU003322}.
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DR EMBL; FR796462; CAM70152.1; -; Genomic_DNA.
DR RefSeq; XP_001467099.1; XM_001467062.1.
DR AlphaFoldDB; A4I5T0; -.
DR SMR; A4I5T0; -.
DR STRING; 5671.A4I5T0; -.
DR GeneID; 5071145; -.
DR KEGG; lif:LINJ_30_2540; -.
DR VEuPathDB; TriTrypDB:LINF_300030100; -.
DR eggNOG; KOG0102; Eukaryota.
DR InParanoid; A4I5T0; -.
DR OMA; GREQKMT; -.
DR OrthoDB; 167758at2759; -.
DR Proteomes; UP000008153; Chromosome 30.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 3.30.30.30; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR HAMAP; MF_00332; DnaK; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR012725; Chaperone_DnaK.
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 NCBIfam; TIGR02350; prok_dnaK; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
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|RuleBase:RU003322};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003322};
KW Reference proteome {ECO:0000313|Proteomes:UP000008153};
KW Stress response {ECO:0000313|EMBL:CAM70152.1}.
FT REGION 625..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 272..299
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 549..597
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 625..653
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 660 AA; 71658 MW; 486A305798BC2BC5 CRC64;
MFARRVCGSA AASAARLARH ESQKVQGDVI GVDLGTTYSC VATMDGDKAR VLENSEGFRT
TPSVVAFKGS EKLVGLAAKR QAITNPQSTF YAVKRLIGRR FEDEHIQKDI KNVPYKIVRA
GNGDAWVQDG NGKQYSPSQI GAFVLEKMKE TAENFLGHKV SNAVVTCPAY FNDAQRQATK
DAGTIAGLNV IRVVNEPTAA ALAYGMDKTK DSLIAVYDLG GGTFDISVLE IAGGVFEVKA
TNGDTHLGGE DFDLALSDYI LEEFRKTSGI DLSKERMALQ RVREAAEKAK CELSSAMETE
VNLPFITANA DGAQHIQMHI SRSKFEGITQ RLIERSIAPC KQCMKDAGVE LKEINDVVLV
GGMTRMPKVV EEVKKFFQKD PFRGVNPDEA VALGAATLGG VLRGDVKGLV LLDVTPLSLG
IETLGGVFTR MIPKNTTIPT KKSQTFSTAA DNQTQVGIKV FQGEREMAAD NQMMGQFDLV
GIPPAPRGVP QIEVTFDIDA NGICHVTAKD KATGKTQNIT ITANGGLSKE QIEQMIRDSE
QHAEADRVKR ELVEVRNNAE TQLTTAERQL GEWKYVSDAE KENVKTLVAE LRKAMENPNV
AKDDLAAATD KLQKAVMECG RTEYQQAAAA NSGSTSNSGE QQQQQGQGEQ QQQQNSEEKK
//
