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Database: UniProt
Entry: I1C572_RHIO9
LinkDB: I1C572_RHIO9
Original site: I1C572_RHIO9 
ID   I1C572_RHIO9            Unreviewed;       748 AA.
AC   I1C572;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EIE83602.1};
GN   ORFNames=RO3G_08307 {ECO:0000313|EMBL:EIE83602.1};
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:EIE83602.1, ECO:0000313|Proteomes:UP000009138};
RN   [1] {ECO:0000313|EMBL:EIE83602.1, 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 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239}.
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DR   EMBL; CH476737; EIE83602.1; -; Genomic_DNA.
DR   AlphaFoldDB; I1C572; -.
DR   STRING; 246409.I1C572; -.
DR   VEuPathDB; FungiDB:RO3G_08307; -.
DR   eggNOG; KOG0020; Eukaryota.
DR   InParanoid; I1C572; -.
DR   OMA; ARTHFTA; -.
DR   OrthoDB; 547579at2759; -.
DR   Proteomes; UP000009138; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   CDD; cd16927; HATPase_Hsp90-like; 1.
DR   Gene3D; 3.30.230.80; -; 1.
DR   Gene3D; 3.40.50.11260; -; 1.
DR   Gene3D; 1.20.120.790; Heat shock protein 90, C-terminal domain; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   HAMAP; MF_00505; HSP90; 1.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR037196; HSP90_C.
DR   InterPro; IPR001404; Hsp90_fam.
DR   InterPro; IPR020575; Hsp90_N.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   PANTHER; PTHR11528:SF97; ENDOPLASMIN; 1.
DR   PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR   Pfam; PF13589; HATPase_c_3; 1.
DR   Pfam; PF00183; HSP90; 1.
DR   PIRSF; PIRSF002583; Hsp90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF110942; HSP90 C-terminal domain; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009138};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..748
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003638346"
SQ   SEQUENCE   748 AA;  86318 MW;  C1C8502EE95E92AE CRC64;
     MRVNVLFILI ALLLSCFVFA KQEEQEGIIE NDELIQQIQE AGDHEIYTFQ TEVSRMMHLI
     INSLYKTKEI FLRELISNAS DALDKIRFLS LTDPETLKSA SDLHIRIMTD PVHKTLKIVD
     TGIGMTKRQL KENLGTLAKS GTSEFLAKMQ GNDKDALNQI GQFGVGFYSV FLVADKVTVA
     SKSNEEEDQY VWMSEAVNDF TIAKDPRGNT LGRGTEITLY LKPDAENFLD EKNLKDIVHK
     YSQFITFPIQ VWSAHEEEVI EDDLDAEIVE ESLDETEKKE NKKKTVYDWE QVNTQKPIWT
     RESKEVSDKE HIEFYQSLTL DSEEPIGWSH SKGEGEIEFR SLLYIPRYMS EKFYQTMHDI
     KPIKLFVKRV FISDEFELLP KWLAFLRGVV DADDMPLNVS RETLQKHRNL RIITRHLVKK
     ALDMFNQLAQ NDPEKYKIFL AQYSPMLKYG AIEDVSYRKK LTSLLRFASS HNTTAFTSSL
     DDYISRAKAN QKSIYFMTGS TVSEIEQSPY IESLLARGYE ILYFTDPIDE TFVEQIPGYN
     GKQFVNIAKG ELEFDEEDGL DTKALEEKYK PLADWLKDTL FDHIDKVTIS QRLTTSPFAI
     VAPRHGLSGH AQRVLDAQGQ NTRNPQMEMI LESLRSQKKI LEINPNHPII ERLLDNVIED
     SVPEDMTNLI QLMYETTSIR SGFPLKDINQ FTTRVEGLLR KNIGVSIDEQ AKVNVKKAKE
     KTEKEKLEDE ELKKTNIIYE DAIEHDEL
//
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