ID I1CF23_RHIO9 Unreviewed; 271 AA.
AC I1CF23;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 34.
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 ORFNames=RO3G_11764 {ECO:0000313|EMBL:EIE87053.1};
OS Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL
OS 43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=246409 {ECO:0000313|EMBL:EIE87053.1, ECO:0000313|Proteomes:UP000009138};
RN [1] {ECO:0000313|EMBL:EIE87053.1, ECO:0000313|Proteomes:UP000009138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880
RC {ECO:0000313|Proteomes:UP000009138};
RX PubMed=19578406; DOI=10.1371/journal.pgen.1000549;
RA Ma L.-J., Ibrahim A.S., Skory C., Grabherr M.G., Burger G., Butler M.,
RA Elias M., Idnurm A., Lang B.F., Sone T., Abe A., Calvo S.E.,
RA Corrochano L.M., Engels R., Fu J., Hansberg W., Kim J.-M., Kodira C.D.,
RA Koehrsen M.J., Liu B., Miranda-Saavedra D., O'Leary S.,
RA Ortiz-Castellanos L., Poulter R., Rodriguez-Romero J., Ruiz-Herrera J.,
RA Shen Y.-Q., Zeng Q., Galagan J., Birren B.W., Cuomo C.A., Wickes B.L.;
RT "Genomic analysis of the basal lineage fungus Rhizopus oryzae reveals a
RT whole-genome duplication.";
RL PLoS Genet. 5:E1000549-E1000549(2009).
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; CH476740; EIE87053.1; -; Genomic_DNA.
DR AlphaFoldDB; I1CF23; -.
DR STRING; 246409.I1CF23; -.
DR VEuPathDB; FungiDB:RO3G_11764; -.
DR eggNOG; KOG0100; Eukaryota.
DR InParanoid; I1CF23; -.
DR OMA; EESCAPT; -.
DR OrthoDB; 143at2759; -.
DR Proteomes; UP000009138; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR Gene3D; 3.30.30.30; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
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 PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000009138};
KW Signal {ECO:0000256|SAM:SignalP};
KW Stress response {ECO:0000313|EMBL:EIE87053.1}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..271
FT /note="non-chaperonin molecular chaperone ATPase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003638075"
FT NON_TER 271
FT /evidence="ECO:0000313|EMBL:EIE87053.1"
SQ SEQUENCE 271 AA; 29562 MW; 6F1252D207D7DB93 CRC64;
MHTKASLLAL FAFIFTLFIA SNVVEAAEDK ESYGTVIGID LGTTYSCVAV QKNGRVEIIA
NDQGHRITPS YVAFTDDERL IGDAAKNQYS ANPRRTVFDA KRLIGRRYED KEVQQDMKHF
PFDVVSRNGA PHIQVPVKGE DRVFTPEEIS GMVLTKMKET AEAYLGKPVT HAVVTVPAYF
NDAQRQATKD AGTIAGLTIL RIINEPTAAA IAYGLDKTGG EKNVLVYDLG GGTFDVSLLS
IEDGIFEVLS TAGDTHLGGE DFDSRVIDHF V
//
