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
//