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Database: UniProt
Entry: A0A1D2N1P9_ORCCI
LinkDB: A0A1D2N1P9_ORCCI
Original site: A0A1D2N1P9_ORCCI 
ID   A0A1D2N1P9_ORCCI        Unreviewed;       693 AA.
AC   A0A1D2N1P9;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Heat shock protein 83 {ECO:0000256|ARBA:ARBA00021845};
DE   Flags: Fragment;
GN   ORFNames=Ocin01_07479 {ECO:0000313|EMBL:ODM99213.1};
OS   Orchesella cincta (Springtail) (Podura cincta).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC   Entomobryomorpha; Entomobryoidea; Orchesellidae; Orchesellinae; Orchesella.
OX   NCBI_TaxID=48709 {ECO:0000313|EMBL:ODM99213.1, ECO:0000313|Proteomes:UP000094527};
RN   [1] {ECO:0000313|EMBL:ODM99213.1, ECO:0000313|Proteomes:UP000094527}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Mixed pool {ECO:0000313|EMBL:ODM99213.1};
RX   PubMed=27289101; DOI=10.1093/gbe/evw134;
RA   Faddeeva-Vakhrusheva A., Derks M.F., Anvar S.Y., Agamennone V., Suring W.,
RA   Smit S., van Straalen N.M., Roelofs D.;
RT   "Gene Family Evolution Reflects Adaptation to Soil Environmental Stressors
RT   in the Genome of the Collembolan Orchesella cincta.";
RL   Genome Biol. Evol. 8:2106-2117(2016).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
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:ODM99213.1}.
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DR   EMBL; LJIJ01000294; ODM99213.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D2N1P9; -.
DR   STRING; 48709.A0A1D2N1P9; -.
DR   OMA; DHTQQNE; -.
DR   OrthoDB; 5485387at2759; -.
DR   Proteomes; UP000094527; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; 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; IPR037196; HSP90_C.
DR   InterPro; IPR001404; Hsp90_fam.
DR   InterPro; IPR020575; Hsp90_N.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   PANTHER; PTHR11528:SF44; HEAT SHOCK PROTEIN 75 KDA, MITOCHONDRIAL; 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.
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:UP000094527};
KW   Stress response {ECO:0000313|EMBL:ODM99213.1}.
FT   DOMAIN          96..253
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ODM99213.1"
SQ   SEQUENCE   693 AA;  78223 MW;  01D2120B9AD47BEA CRC64;
     CVVVIFSGIT QGSRTLALSC NSPLKAHPSS FNVHTIRNYS SSAKESEQLT EEAESKDGIH
     SIIKNEETVK GDSEKREFQA ETRMLLDIVA KSLYSESEIF VRELVSNASD ALEKFRYLSK
     TGENLIGADR PLEIHLATDK QSRTFTIQDT GVGMTREEMI ENLGTIAKSG TKVFLEKVRE
     SKSADPNSMI GQFGVGFYSS FMVANRVDVY SKSSKENTHG YKWSSDGSGV YEIQEAEGVQ
     NGTKIVLHLK TDHRQFSDEE TVLSIIKKYS NFVGNPIFLN GKQINTVQAL WLMDPKTVTP
     DMHDEFYNFI GGSYDRPRFT LHFSTDVPLS LRCVLYVPDG KPGLFEMSKD AQIGVGLYSR
     KVMIKNKADN IIPNWLRFLK GVVDSEDIPL NLSRELLQDS ALIRKLRTVV VNRVIRFLHD
     RSQKEAESFM KFYNDYGIFV KEGIITEAEQ VIKEDIAKLL RFESSAMAPG ELVSLPEYIS
     RMQAAQKDVY YLAAPSRSLA ERSPYLEALK EKNVEVLYCF QPYDEMVLIQ LRQFDRKSLT
     SVEKEMRQMK ENVDMDALPL GGLAKSEAEG LLTWLQQSLK GRAHSVKFTQ KLENHPCVVT
     VEEMAAARHF IRTQSAQMTP EVRYSLLQPQ FEVSIKHPLI MKLSTLKDSD PDLAKLLAEQ
     LFANAMVTAG LEEDPRTIIS SLTELLTKAL EKV
//
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