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Database: UniProt
Entry: I1BGT7_RHIO9
LinkDB: I1BGT7_RHIO9
Original site: I1BGT7_RHIO9 
ID   I1BGT7_RHIO9            Unreviewed;       698 AA.
AC   I1BGT7;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Hsp83-like protein {ECO:0000313|EMBL:EIE75417.1};
GN   ORFNames=RO3G_00121 {ECO:0000313|EMBL:EIE75417.1};
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:EIE75417.1, ECO:0000313|Proteomes:UP000009138};
RN   [1] {ECO:0000313|EMBL:EIE75417.1, 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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239}.
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DR   EMBL; CH476732; EIE75417.1; -; Genomic_DNA.
DR   AlphaFoldDB; I1BGT7; -.
DR   STRING; 246409.I1BGT7; -.
DR   VEuPathDB; FungiDB:RO3G_00121; -.
DR   eggNOG; KOG0019; Eukaryota.
DR   InParanoid; I1BGT7; -.
DR   OMA; TRMKAEQ; -.
DR   OrthoDB; 547579at2759; -.
DR   Proteomes; UP000009138; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR019805; Heat_shock_protein_90_CS.
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:SF34; HEAT SHOCK PROTEIN 83; 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   SMART; SM00387; HATPase_c; 1.
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; PS00298; HSP90; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009138}.
FT   DOMAIN          28..183
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
FT   REGION          216..247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          668..698
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..233
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        670..684
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   698 AA;  80164 MW;  527147028EF3DAB1 CRC64;
     MTTETETFSF QAEISQLMSL IINTFYSNKE IFLRELISNA SDALDKIRYQ SLTDPSVLDS
     EKELYIRVTP DKQNNILSIR DTGIGMTKAD LVNNLGTIAK SGTKSFMEAL SSGADISMIG
     QFGVGFYSAY LVADKVQVIT KHNDDEQYIW ESSAGGSFTI TRDEVNPSLG RGTEMRLFLK
     EDQLEYLEER RIKDIVKKHS EFISYPIQLV VEKEVEKEVS DDEEEPVTES KIEEVTDDDD
     KKDKKKKTIK ETVTENQELN KTKPLWTRTP EDVKPEEYAE FYKALTNDWE DHLAVKHFSV
     EGQLEFRAIL FVPKRAPFDM FETKKKRNNI KLYVRRVFIM DDCEELIPEW LSFIKGVVDS
     EDLPLNISRE MLQQNKILKV IRKNLVKKCL EMFQEIAEDK EQFDKFYEAF SKNIKLGIHE
     DSQNRSKLAD LLRYHSTKSG DEMTSLKDYV TRMSEKQKNI YYITGESRAA VEHSPFLEGF
     KKKNIEVLLM TDPIDEYSTT QLKEYDGKKL VCITKEGAEL LEEDEEEKKK REEEKKEFEN
     LCKTVKEILG DKVERVVLSA ILTDSPCVLT TGQFGWSANM ERIMKAQALR DSTMSSYMAS
     KKTLEINPHH PIIKALKTKA EADSADRTVK DLVTLLYETS LLTSGFSLDN PSSFASRINR
     MVALGLSIDE EDTPIEEADK EETPAEESTE ASKMEEVD
//
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