ID   Q7ZA47_PARBR            Unreviewed;       680 AA.
AC   Q7ZA47;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   13-SEP-2023, entry version 95.
DE   SubName: Full=70 kDa heat shock protein {ECO:0000313|EMBL:AAP05987.3};
OS   Paracoccidioides brasiliensis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX   NCBI_TaxID=121759 {ECO:0000313|EMBL:AAP05987.3};
RN   [1] {ECO:0000313|EMBL:AAP05987.3}
RP   NUCLEOTIDE SEQUENCE.
RA   Soares R.B.A., Castro N.S., Felipe M.S.S., Pereira M., Soares C.M.A.;
RT   "Mitochondrial heat shock 70 kDa protein of Paracoccidioides
RT   brasiliensis.";
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|RuleBase:RU003322}.
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; AY254044; AAP05987.3; -; mRNA.
DR   AlphaFoldDB; Q7ZA47; -.
DR   VEuPathDB; FungiDB:PABG_02034; -.
DR   VEuPathDB; FungiDB:PADG_00430; -.
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   CDD; cd11733; HSPA9-like_NBD; 1.
DR   Gene3D; 1.20.1270.10; -; 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   2: Evidence at transcript level;
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};
KW   Stress response {ECO:0000313|EMBL:AAP05987.3}.
FT   REGION          648..680
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          578..605
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        658..673
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   680 AA;  73752 MW;  2232B77CD2C731B7 CRC64;
     MLASRFSRAL PRAVPSFARS SSRSSAYKLP ATPFRRWNST EGGEEKVKGQ VIGIDLGTTN
     SAVAVMEGKT PRIIENAEGA RTTPSVVAFT KDGERLVGIA AKRQAVVNPE NTLFATKRLI
     GRKFTDPECQ RDLKEVPYKI VQHANGDAWV EAQGQKYSPS QIGGFVLQKM KETAEAYLGK
     PVKNGVVTVP AYFNDSQRQA TKDAGQIAGL NVLRVVNEPT AAALAYGLER EQDRVVAVYD
     LGGGTFDISI LEIQKGVFEV KSTNGDTHLG GEDFDITLVR NVVQQFKKES GIDLSNDRMA
     IQRIREACEK AKIELSSALQ TEINLPFITA DSSGAKHINS KMTRSQLEAL VDPLISRTIE
     PVRKALKDAN LQAKDIQEVI LVGGMTRMPK VGESVKSIFG RDPAKSVNPD EAVAIGAAIQ
     GAVLAGEVTD VLLLDVTPLS LGIETLGGVF TRLINRNTTI PTKKSQTFST AADFQTAVEI
     KVYQGERELV RDNKLLGNFQ LVGIPPAHRG VPQIEVTFDI DADSIVHVHA KDKSTGKDQS
     ITIASGSGLS DTEIQNMVDD AEKFGAQDKE RKAAIEAANR ADSVLNDTEK ALKEFEDKLD
     KTEADQIKEK IASLREVVAK SQSGEGSITA DELKAKVDEL QNASLTLFDK MHKARSEEGQ
     QQQSQQSNEG QQGGEGEKKP
//