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DNAK_EMIHU
ID   DNAK_EMIHU              Reviewed;         623 AA.
AC   Q4G366;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Chaperone protein dnaK;
DE   AltName: Full=HSP70 {ECO:0000255|HAMAP-Rule:MF_00332};
DE   AltName: Full=Heat shock 70 kDa protein {ECO:0000255|HAMAP-Rule:MF_00332};
DE   AltName: Full=Heat shock protein 70 {ECO:0000255|HAMAP-Rule:MF_00332};
GN   Name=dnaK {ECO:0000255|HAMAP-Rule:MF_00332};
OS   Emiliania huxleyi (Coccolithophore) (Pontosphaera huxleyi).
OG   Plastid; Chloroplast.
OC   Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Isochrysidales;
OC   Noelaerhabdaceae; Emiliania.
OX   NCBI_TaxID=2903;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP373 / CSIRO-CS-57 / BT6;
RX   PubMed=16303746; DOI=10.1093/dnares/12.2.151;
RA   Sanchez-Puerta M.V., Bachvaroff T.R., Delwiche C.F.;
RT   "The complete plastid genome sequence of the haptophyte Emiliania huxleyi:
RT   a comparison to other plastid genomes.";
RL   DNA Res. 12:151-156(2005).
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000255|HAMAP-Rule:MF_00332}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00332}.
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DR   EMBL; AY741371; AAX13900.1; -; Genomic_DNA.
DR   RefSeq; YP_277401.1; NC_007288.1.
DR   AlphaFoldDB; Q4G366; -.
DR   SMR; Q4G366; -.
DR   PRIDE; Q4G366; -.
DR   GeneID; 3562486; -.
DR   Proteomes; UP000013827; Unassembled WGS sequence.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 2.60.34.10; -; 1.
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   PANTHER; PTHR19375; PTHR19375; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   SUPFAM; SSF100920; SSF100920; 1.
DR   SUPFAM; SSF100934; SSF100934; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   TIGRFAMs; TIGR02350; prok_dnaK; 1.
DR   PROSITE; PS00297; HSP70_1; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Chloroplast; Nucleotide-binding; Plastid;
KW   Reference proteome.
FT   CHAIN           1..623
FT                   /note="Chaperone protein dnaK"
FT                   /id="PRO_0000275348"
FT   REGION          598..623
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   623 AA;  67235 MW;  F601F9D5B02A8E9F CRC64;
     MGKVVGIDLG TTNSVVAVME GGKPTVITNS EGQRTTPSVV AYTKKGDLLV GQIAKRQAVI
     NPENTFYSVK RFIGRKTSEV TEALRQVPYK VLQTEDIIKL DCPALGKQFA SEEISAQVLR
     KLADDATKYL GETVTQAVIT VPAYFNDSQR QATKDAGKIA GLEVLRIINE PTAASLSYGL
     DKKDNETILV FDLGGGTFDV SILEVGDGVF EVLATSGDTR LGGDDFDEKI VQWLVNEFKN
     DEGIDLTQDN QALQRLTEAA EKAKVELSTL TQSSINLPFI SVTPEGPKHL EKDLTRAKFE
     ELCSDLIDRC KTPIQNALKD AELSPSSIDQ NVLVGGSTRI PAVQELVEQL LGKKPNQSVN
     PDEVVAVGAA VQAGVLGGEV KDILLLDVTP LSLGVETLGG ITTKITPRNT IIPTKKSETF
     STAVDNQPNV EIHVLQGERE LAKDNKSLGT FRLDGIAPAA RGVPQIEVTF DIDANGILSV
     TAKDKATNKQ QSITISGASN LAKDEVERMV EEAEQNAASD KEKSEQIDVK NKADSLCYQT
     KKQLEELSSK LEAADKEKVE EVLTKLELAV QNDDLEGMKT LSEELQKNMM EVGQKVYTPD
     AGAEGGAAPS QDDAIETDFS TEK
 
 
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