ID I1C225_RHIO9 Unreviewed; 662 AA.
AC I1C225;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Hsp7-like protein {ECO:0000313|EMBL:EIE82505.1};
GN ORFNames=RO3G_07210 {ECO:0000313|EMBL:EIE82505.1};
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:EIE82505.1, ECO:0000313|Proteomes:UP000009138};
RN [1] {ECO:0000313|EMBL:EIE82505.1, 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 -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|RuleBase:RU003322}.
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DR EMBL; CH476736; EIE82505.1; -; Genomic_DNA.
DR AlphaFoldDB; I1C225; -.
DR STRING; 246409.I1C225; -.
DR VEuPathDB; FungiDB:RO3G_07210; -.
DR eggNOG; KOG0102; Eukaryota.
DR InParanoid; I1C225; -.
DR OMA; DINQVPF; -.
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 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; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322};
KW Reference proteome {ECO:0000313|Proteomes:UP000009138}.
FT REGION 643..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 538..599
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 662 AA; 71086 MW; 610CD62E22942919 CRC64;
MYNLSKVAHR RLLPSLTRNT GVLSTFSRSY SSGVNGPVIG IDLGTTNSCV SVMEGKNPRV
IENAEGARTT PSVVAFTKDG ELLVGQAAKR QAVVNSQNTV YATKRLIGRQ FKDPAVQADI
PAVSYKIVAH NNGDAWVEAN GQKYSPSQIG AFVLGKMKET AEGFLSKKVK HAVITVPAYF
NDAQRQATKD AGKIAGLDVM RVINEPTAAA LAYGLDKSGD STIAVYDLGG GTFDISILEI
QNGVFEVKST NGDTALGGED FDSHLVRHVV KEFKDESGID LSGDRMAIQR IREACEKAKI
ELSSTVQTDI NLPYITADAT GPKHINSKLT RAKYEGLVGD LISRTISPCE KAMKDAGISN
KEVNDVILVG GMSRMPKVVD TVKQVFGREP SKSVNPDEAV AIGAAIQGGV LAGSVTDILL
LDVTPLSLGI ETLGGVFTRL INRNTTIPTK KAQVFSTAAD GQTQVSVRVF QGERELCRDN
KLLGDFNLTG IPPAPKGVPQ IQVEFDIDAD GIVNVSAKDK ATNRDQSMTI AASSGLSNDE
IENMIQQAEA NAEADRARRE TIEMANRADS VMSETEKAMD DFKEQLDKAE AEKLKEKITT
LRTEALKAQS GDSSVNPEEL KAKIDDLQSS SLKLFEMVYK NRAAQSENTS TDNSSSNTTG
SQ
//
