ID D8L659_9GAMM Unreviewed; 309 AA.
AC D8L659;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=DnaJ {ECO:0000313|EMBL:ADB84353.1};
DE Flags: Fragment;
GN Name=dnaJ {ECO:0000313|EMBL:ADB84353.1};
OS Aeromonas bivalvium.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=440079 {ECO:0000313|EMBL:ADB84353.1};
RN [1] {ECO:0000313|EMBL:ADB84353.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=868E {ECO:0000313|EMBL:ADB84353.1};
RX PubMed=20466501; DOI=10.1016/j.syapm.2010.03.007;
RA Loren J.G., Farfan M., Minana-Galbis D., Fuste M.C.;
RT "Prediction of whole-genome DNA G+C content within the genus Aeromonas
RT based on housekeeping gene sequences.";
RL Syst. Appl. Microbiol. 33:237-242(2010).
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DR EMBL; FJ936124; ADB84353.1; -; Genomic_DNA.
DR AlphaFoldDB; D8L659; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0031072; F:heat shock protein binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0009408; P:response to heat; IEA:InterPro.
DR CDD; cd06257; DnaJ; 1.
DR CDD; cd10747; DnaJ_C; 1.
DR CDD; cd10719; DnaJ_zf; 1.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 2.10.230.10; Heat shock protein DnaJ, cysteine-rich domain; 1.
DR Gene3D; 2.60.260.20; Urease metallochaperone UreE, N-terminal domain; 2.
DR HAMAP; MF_01152; DnaJ; 1.
DR InterPro; IPR012724; DnaJ.
DR InterPro; IPR002939; DnaJ_C.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR InterPro; IPR001305; HSP_DnaJ_Cys-rich_dom.
DR InterPro; IPR036410; HSP_DnaJ_Cys-rich_dom_sf.
DR InterPro; IPR036869; J_dom_sf.
DR NCBIfam; TIGR02349; DnaJ_bact; 1.
DR PANTHER; PTHR43096:SF48; CHAPERONE PROTEIN DNAJ; 1.
DR PANTHER; PTHR43096; DNAJ HOMOLOG 1, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF01556; DnaJ_C; 1.
DR Pfam; PF00684; DnaJ_CXXCXGXG; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF57938; DnaJ/Hsp40 cysteine-rich domain; 1.
DR SUPFAM; SSF49493; HSP40/DnaJ peptide-binding domain; 2.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51188; ZF_CR; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00546}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Stress response {ECO:0000256|ARBA:ARBA00023016};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00546};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00546}.
FT DOMAIN 1..50
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 114..192
FT /note="CR-type"
FT /evidence="ECO:0000259|PROSITE:PS51188"
FT ZN_FING 114..192
FT /note="CR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADB84353.1"
FT NON_TER 309
FT /evidence="ECO:0000313|EMBL:ADB84353.1"
SQ SEQUENCE 309 AA; 33174 MW; B577E66234D7D225 CRC64;
IKKAYKRLAM KYHPDRNQGD AASEEKFKEV KEAYEVLTDE NLRARYDQYG HAGVDQSQGG
GHGGFGGGAD FGDIFGDVFG DIFGGSRGGG RRGPARGSDL RYTMELTLEE AVRGVSKEIK
VPTLVHCEVC NGSGAHTGSS AQTCPTCHGA GQVQMRQGFF AVQQACPHCH GRGKIIKDPC
RKCHGEGRYQ KTKTLSVKIP AGVDTGDRIR LSGEGEAGEA GAPAGDLYVQ VHVKEHEIFV
RDGNNLYCEV PISFTAAALG GEIEVPTLDG RVKLKVTPET QTGKMFRMRG KGVKSVRSGQ
VGDLMCKVV
//
