ID E3W5J8_CARSA Unreviewed; 692 AA.
AC E3W5J8;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Heat shock protein 83 {ECO:0000256|ARBA:ARBA00021845};
DE Flags: Fragment;
GN Name=hsp90 {ECO:0000313|EMBL:ADP01837.1};
OS Carposina sasakii (Peach fruit moth) (Carposina niponensis).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Copromorphoidea;
OC Carposinidae; Carposina.
OX NCBI_TaxID=252295 {ECO:0000313|EMBL:ADP01837.1};
RN [1] {ECO:0000313|EMBL:ADP01837.1}
RP NUCLEOTIDE SEQUENCE.
RA Son Y., Kim Y.;
RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
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; HQ392512; ADP01837.1; -; mRNA.
DR AlphaFoldDB; E3W5J8; -.
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 2: Evidence at transcript level;
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 Stress response {ECO:0000313|EMBL:ADP01837.1}.
FT DOMAIN 11..165
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 198..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADP01837.1"
SQ SEQUENCE 692 AA; 79463 MW; E0B0A15115E6301E CRC64;
MSLIINTFYS NKEIFLRELI SNSSDALDKI RYESLTDPSK LDSGKELYIK TVPNKSEGTL
TLIDTGIGMT KADLVNNLGT IAKSGTKAFM EALQAGADIS MIGQFGVGFY SCYLVADRVT
VHSKHNDDEQ YVWESAAGGS FTVRSDTGEP LGRGTKIVLH IKEDLSEYLE ESKIKEIVKK
HSQFIGYPIK LVVEKEREKE LSDDEAEEEK KEEGEDDKPK IEDVGEDEEE DGKEKKKKKK
TIKEKYSEDE ELNKTKPIWT RNADDITQEE YGDFYKSLTN DWEDHLAVKH FSVEGQLEFR
ALLFIPRRAP FDLFENKKRK NNIKLYVRRV FIMDNCEDLI PEYLNFVKGV VDSEDLPLNI
SREMLQQNKI LKVIRRNLVK KCLELFEELA EDKENYKKYY EQFSENLKLG IHEDTQNRSK
IADLLRYNTS ASGDEACSLK EYVSRMKENQ KHIYYITGEN RDQVANPSFV ERVKKRGYEV
VYMTEPIDEY VVQQMKEYDG KSRLCHQGRS GASEDEEEKK KREEDKVKFE GLCKVMKNIL
DNKVEKVVVS NRLVESPCCI VTAQYGWSAN MERIMKAQAL RDTSTMGYMA AKRHLEINPD
HSIVETFRQK ADADKNDKAV KDLVILLYET ALLSSGFALD EPQVHASRIY RMIKLGLGID
EDEPIQVEEA SAGDVPPLEG EADDASRMEE VD
//
