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Database: UniProt
Entry: A0A1D2NIY5_ORCCI
LinkDB: A0A1D2NIY5_ORCCI
Original site: A0A1D2NIY5_ORCCI 
ID   A0A1D2NIY5_ORCCI        Unreviewed;       702 AA.
AC   A0A1D2NIY5;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Heat shock 70 kDa protein cognate 5 {ECO:0000313|EMBL:ODN05197.1};
GN   ORFNames=Ocin01_01470 {ECO:0000313|EMBL:ODN05197.1};
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:ODN05197.1, ECO:0000313|Proteomes:UP000094527};
RN   [1] {ECO:0000313|EMBL:ODN05197.1, ECO:0000313|Proteomes:UP000094527}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Mixed pool {ECO:0000313|EMBL:ODN05197.1};
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   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|ARBA:ARBA00007381, ECO:0000256|RuleBase:RU003322}.
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:ODN05197.1}.
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DR   EMBL; LJIJ01000028; ODN05197.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D2NIY5; -.
DR   STRING; 48709.A0A1D2NIY5; -.
DR   OMA; MGTDWKI; -.
DR   OrthoDB; 143at2759; -.
DR   Proteomes; UP000094527; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   CDD; cd11733; HSPA9-like_NBD; 1.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 3.30.30.30; -; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   HAMAP; MF_00332; DnaK; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR012725; Chaperone_DnaK.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR029048; HSP70_C_sf.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   NCBIfam; TIGR02350; prok_dnaK; 1.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR   PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR   PROSITE; PS00297; HSP70_1; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU003322};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094527};
KW   Stress response {ECO:0000313|EMBL:ODN05197.1}.
FT   REGION          667..702
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        671..687
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        688..702
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   702 AA;  75864 MW;  8888FEBB1CC3BED9 CRC64;
     MRPILSGLSR AILDRQTIAT GLSSPSRNAH IWALNNQING KIVNGLRDRQ NGQLVRHKSD
     QVRGAVIGID LGTTNSCVAV MEGKQAKVIE NAEGARTTPS VVAFSKDAER LVGMPAKRQA
     VTNAANTFYA TKRLIGRRFE DAEVKKDMKT VSYKIVKASN GDAWVQGSDG KVYSPSQIGA
     FVLTKMKETA EAYLGTSAKN AVVTVPAYFN DSQRQATKDA GQISGLNVLR VINEPTAAAL
     AYGMDKTEDK IIAVYDLGGG TFDISILEIQ KGVFEVKSTN GDTFLGGEDF DNVLVNFLAE
     EFKRDQGADL RKDPMAMQRL KEAAEKAKVE LSSALQTDIN LPYITMDSSG PKHMNLKLTR
     SKFESLVGDL IKRTVAPCQK ALQDAEVKKT DIGEVILVGG MSRMPKVQST VLDVFGRQPS
     KSVNPDEAVA VGAAIQGGVL AGNVTDVLLL DVTPLSLGIE TLGGVFTKLI NRNTTIPTKK
     SQVFSTAADG QTQVEIKVFQ GEREMALDNK ILGQFSLIGI PPAPRGVPQV EVTFDIDANG
     IVHVSARDKG TGKEQQIVIQ SSGGLSKDEI ENMVKNAEQF ATQDKAKKER VEAVNQAEGV
     VHDIETKVTE YESQLPTEEV TKIRDLITKT REAIAKKDEL SGEELKAATN ELQQASLKVF
     ELAYKKMASE REGSSGSSSS ESSSTSESTE STEEKEKKEG KN
//
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