ID C1K9X0_9GAMM Unreviewed; 265 AA. AC C1K9X0; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 27-MAR-2024, entry version 53. DE SubName: Full=Chaperone protein {ECO:0000313|EMBL:ACO37582.1}; DE Flags: Fragment; GN Name=dnaJ {ECO:0000313|EMBL:ACO37582.1}; OS Aeromonas taiwanensis. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales; OC Aeromonadaceae; Aeromonas. OX NCBI_TaxID=633417 {ECO:0000313|EMBL:ACO37582.1}; RN [1] {ECO:0000313|EMBL:ACO37582.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A2-50 {ECO:0000313|EMBL:ACO37582.1}; RX PubMed=19819994; DOI=10.1099/ijs.0.014621-0; RA Alperi A., Martinez-Murcia A.J., Ko W.C., Monera A., Saavedra M.J., RA Figueras M.J.; RT "Aeromonas taiwanensis sp. nov. and Aeromonas sanarellii sp. nov., clinical RT species from Taiwan."; RL Int. J. Syst. Evol. Microbiol. 60:2048-2055(2010). CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; FJ807270; ACO37582.1; -; Genomic_DNA. DR AlphaFoldDB; C1K9X0; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. 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 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 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 PANTHER; PTHR43096:SF48; CHAPERONE PROTEIN DNAJ; 1. DR PANTHER; PTHR43096; DNAJ HOMOLOG 1, MITOCHONDRIAL-RELATED; 1. DR Pfam; PF01556; DnaJ_C; 1. DR Pfam; PF00684; DnaJ_CXXCXGXG; 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 4: Predicted; 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..27 FT /note="J" FT /evidence="ECO:0000259|PROSITE:PS50076" FT DOMAIN 90..168 FT /note="CR-type" FT /evidence="ECO:0000259|PROSITE:PS51188" FT ZN_FING 90..168 FT /note="CR-type" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00546" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:ACO37582.1" FT NON_TER 265 FT /evidence="ECO:0000313|EMBL:ACO37582.1" SQ SEQUENCE 265 AA; 28531 MW; 0CCEAAC46C964203 CRC64; EEKFKEVKEA YEVLTDENLR ARYDQYGHAG VDPSQGGGHG GFGGGADFGD IFGDVFGDIF GGRGGGRRGP ARGSDLRYNM ELTLEEAVRG VSKEIKIPTQ VHCEVCNGSG AHTGSQAQTC PTCHGSGQVQ MRQGFFAVQQ PCPHCHGRGK IIKDPCRKCH GEGRYQKTKT LSVKIPAGVD TGDRIRLSGE GEAGEAGAPA GDLYVQVHVR EHEIFVRDGN DLYCEVPISF TTAALGGEIE VPTLDGRVKL KVTPETQTGK LFRLR //