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Database: UniProt
Entry: Q0PUZ1_9AGAR
LinkDB: Q0PUZ1_9AGAR
Original site: Q0PUZ1_9AGAR 
ID   Q0PUZ1_9AGAR            Unreviewed;       182 AA.
AC   Q0PUZ1;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=non-chaperonin molecular chaperone ATPase {ECO:0000256|ARBA:ARBA00012554};
DE            EC=3.6.4.10 {ECO:0000256|ARBA:ARBA00012554};
DE   Flags: Fragment;
GN   Name=BIPA {ECO:0000313|EMBL:ABG73329.1};
OS   Agaricaceae sp. PA222.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae.
OX   NCBI_TaxID=393667 {ECO:0000313|EMBL:ABG73329.1};
RN   [1] {ECO:0000313|EMBL:ABG73329.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PA222 {ECO:0000313|EMBL:ABG73329.1};
RX   PubMed=16815974; DOI=10.1073/pnas.0601441103;
RA   Mikheyev A.S., Mueller U.G., Abbot P.;
RT   "Cryptic sex and many-to-one coevolution in the fungus-growing ant
RT   symbiosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:10702-10706(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.10;
CC         Evidence={ECO:0000256|ARBA:ARBA00001629};
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DR   EMBL; DQ767946; ABG73329.1; -; Genomic_DNA.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   Gene3D; 3.30.420.40; -; 2.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018181; Heat_shock_70_CS.
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; 1.
DR   SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABG73329.1"
FT   NON_TER         182
FT                   /evidence="ECO:0000313|EMBL:ABG73329.1"
SQ   SEQUENCE   182 AA;  19803 MW;  E794E0C0B76602B2 CRC64;
     LSSQQSTRIE IESFEDGNDF SETLTRAKFE ELNRDLFRKT MKPVEQVLKD ANVKKEDIDE
     VVLVGGSTRI PKVQQLLKEF FNGKEPSKGI NPDEAVAYGA AVXGGILSGA EGTADVVLVD
     VXPLTLGIET TGGVFTKLIP RNTVIPTKKS QIFSTAADNQ PTVLIQVFEG ERSLTKDNNL
     LG
//
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