ID A0A0T6BAV2_9SCAR Unreviewed; 785 AA.
AC A0A0T6BAV2;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Heat shock protein 83 {ECO:0000256|ARBA:ARBA00021845};
GN ORFNames=AMK59_2424 {ECO:0000313|EMBL:KRT84331.1};
OS Oryctes borbonicus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Scarabaeiformia;
OC Scarabaeidae; Dynastinae; Oryctes.
OX NCBI_TaxID=1629725 {ECO:0000313|EMBL:KRT84331.1, ECO:0000313|Proteomes:UP000051574};
RN [1] {ECO:0000313|EMBL:KRT84331.1, ECO:0000313|Proteomes:UP000051574}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OB123 {ECO:0000313|EMBL:KRT84331.1};
RC TISSUE=Whole animal {ECO:0000313|EMBL:KRT84331.1};
RA Meyer J.M., Markov G.V., Baskaran P., Herrmann M., Sommer R.J.,
RA Roedelsperger C.;
RT "Draft genome of the scarab beetle Oryctes borbonicus.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000256|ARBA:ARBA00004319}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRT84331.1}.
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DR EMBL; LJIG01002609; KRT84331.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T6BAV2; -.
DR OrthoDB; 547579at2759; -.
DR Proteomes; UP000051574; Unassembled WGS sequence.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; 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: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 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000051574};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..785
FT /note="Heat shock protein 83"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006668521"
FT DOMAIN 97..255
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 292..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..785
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 785 AA; 89903 MW; 5EB32565D325E4A6 CRC64;
MKQLAFLILG LFVFIGHVKC DVAEGEGIVE PLDIDLGASR EGSRTDDEVV KREEEAIKLD
GLNVAQMKEL RDKAEKFQFQ TEVNRMMKLI INSLYRNKEI FLRELISNAS DALDKIRLLS
LTEPGVLDTN SELNIRIKAD KEANMLHITD TGIGMSKSDL VNNLGTIAKS GTAEFLSKMQ
DGSSVPDMND MIGQFGVGFY SAFLVADKVI VTSKHNNDVQ YIWESDAGSF SVVEDPRGDT
LKRGTTISLQ LKPEAKDFLE QDTIRNLVKK YSQFINFPIY LWASRTEQVE EVVEDEAEEK
EKSKPETTDE DAAVEEEEGE EDKPKTKKVD KTIWDWELLN DSKPIWTRKA SDVEDKEYDE
FYKTLTKDSS EPLAKVHFVA EGEVTFKALL FVPKVQPSES FNRYGTKTDN IKLYVRRVFI
TDEFNDMMPN YLSFIRGIVD SDDLPLNVSR ETLQQHKLIK VIKKKLIRKV LDMLKKIPED
QYEKFWKEYS TNIKLGTIED PSNRTRLAKL LMFYSSNSDS LTSLGDYVKR MKPKQERIFY
IAGATKDEVR KSPFAERLLR KGYEVLYLVE AVDEYTISAI PEFEGKKFQN VAKEGFSLTE
AEGGKKQLEQ YQSQFEPLTK WLADDVLKEH IAKATVSERL SDSPCALVAS MFGWTGNMER
LAISNAHQKA DDPQRSYYLN QKKTMEINPR HPLMRELLKR VNDDTSDPTA REMAMMLFET
ATLRSGYMLK ETHGFAQNIE MMMRKTLGIS LDEQVEEEED IPEDGIPEEE ADQEVEADSE
EHDEL
//