ID A0A182PIH4_9DIPT Unreviewed; 700 AA.
AC A0A182PIH4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Heat shock protein 83 {ECO:0000256|ARBA:ARBA00021845};
OS Anopheles epiroticus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=199890 {ECO:0000313|EnsemblMetazoa:AEPI006736-PA, ECO:0000313|Proteomes:UP000075885};
RN [1] {ECO:0000313|Proteomes:UP000075885}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Epiroticus2 {ECO:0000313|Proteomes:UP000075885};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Howell P., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles epiroticus epiroticus2.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AEPI006736-PA}
RP IDENTIFICATION.
RC STRAIN=Epiroticus2 {ECO:0000313|EnsemblMetazoa:AEPI006736-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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 AlphaFoldDB; A0A182PIH4; -.
DR STRING; 199890.A0A182PIH4; -.
DR EnsemblMetazoa; AEPI006736-RA; AEPI006736-PA; AEPI006736.
DR VEuPathDB; VectorBase:AEPI006736; -.
DR OrthoDB; 547579at2759; -.
DR Proteomes; UP000075885; 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}.
FT DOMAIN 30..184
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 217..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 700 AA; 79643 MW; 2DEB6452CAF96F7E CRC64;
MPEAPEAETF AFQAEIAQLM SLIINTFYSN KEIFLRELIS NSSDALDKIR YESLTEPSKL
ESGKELFIKI IPNKEAGTLT LIDTGIGMTK ADLVNNLGTI AKSGTKAFME ALQAGADISM
IGQFGVGFYS AYLVADKVVV TSKNNDDEQY VWESSAGGSF TVRPDTGEPL GRGTKIVLHI
KEDQLEYLEE SKIKQIVNKH SQFIGYPIKL LVEKEREKED DEPKLEDAAD DDEDKKDKKK
KTVKVKYTED EELNKTKPIW TRNADDISQE EYGEFYKSLT NDWEDHLAVK HFSVEGQLDF
RALLFVPRRM PFDLFENKKK KNNIKLYVRR VFIMDNCEEL IPDYLNFIKG VVDSEDLPLN
ISREMLQQNK ILKVIRKNLV KKCLELFEEL AEDKETYKKF YDQFSKNLKL GVHEDSQNRQ
KLADLLRFNT SASGDEYCSL GDYVGRMKEN QTQIYFITGE SIDQVKNSAF VERVKKRGFE
VIYMTDAIDE YVIQQLKEYK GKQLVCVTKE GLELPEDEAE KKKREEDKAK FENLCKVMKS
VLESKVEKVM VSNRLVDSPC CIVTSQYGWS ANMERIMKAQ ALRDSSAMGY MAGKKHLEIN
PDHAIIETLR QRADADKNDK AVKDLVILLF ETALLSSGFS LDEPGTHASR IYRMIKLGLG
IDEDEPMTTE ESSGAAAPAS GDAPPLVDDS EDLSHMEEVD
//
