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Database: UniProt
Entry: B8FUE6_DESHD
LinkDB: B8FUE6_DESHD
Original site: B8FUE6_DESHD 
ID   B8FUE6_DESHD            Unreviewed;       307 AA.
AC   B8FUE6;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=Chaperone DnaJ domain protein {ECO:0000313|EMBL:ACL20560.1};
GN   OrderedLocusNames=Dhaf_2533 {ECO:0000313|EMBL:ACL20560.1};
OS   Desulfitobacterium hafniense (strain DSM 10664 / DCB-2).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfitobacterium.
OX   NCBI_TaxID=272564 {ECO:0000313|EMBL:ACL20560.1, ECO:0000313|Proteomes:UP000007726};
RN   [1] {ECO:0000313|EMBL:ACL20560.1, ECO:0000313|Proteomes:UP000007726}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10664 / DCB-2 {ECO:0000313|Proteomes:UP000007726};
RX   PubMed=22316246; DOI=10.1186/1471-2180-12-21;
RA   Kim S.H., Harzman C., Davis J.K., Hutcheson R., Broderick J.B., Marsh T.L.,
RA   Tiedje J.M.;
RT   "Genome sequence of Desulfitobacterium hafniense DCB-2, a Gram-positive
RT   anaerobe capable of dehalogenation and metal reduction.";
RL   BMC Microbiol. 12:21-21(2012).
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DR   EMBL; CP001336; ACL20560.1; -; Genomic_DNA.
DR   RefSeq; WP_011459679.1; NC_011830.1.
DR   AlphaFoldDB; B8FUE6; -.
DR   KEGG; dhd:Dhaf_2533; -.
DR   HOGENOM; CLU_017633_0_0_9; -.
DR   Proteomes; UP000007726; Chromosome.
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; cd06257; DnaJ; 1.
DR   CDD; cd10747; DnaJ_C; 1.
DR   Gene3D; 1.10.287.110; DnaJ 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; IPR036869; J_dom_sf.
DR   PANTHER; PTHR43096:SF69; CURVED DNA-BINDING PROTEIN; 1.
DR   PANTHER; PTHR43096; DNAJ HOMOLOG 1, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF01556; DnaJ_C; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; Chaperone J-domain; 1.
DR   SUPFAM; SSF49493; HSP40/DnaJ peptide-binding domain; 2.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
PE   4: Predicted;
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705}.
FT   DOMAIN          5..70
FT                   /note="J"
FT                   /evidence="ECO:0000259|PROSITE:PS50076"
SQ   SEQUENCE   307 AA;  34611 MW;  EC1FF512DE6B137D CRC64;
     MQYKDYYQIL GVDKKATLEE IKKAYRGLTK KYHPDINPGN KEAEEKYKEI NEAYEVLGDP
     EKREKYDNFG NEFNYHNGYN FDPSQFGFGN GQFEFKTAGA GDYSDFFNLF FGEGGLDGFF
     GQKGPRTRGA RSQFAYPGED IESELHITLE EGFHGAEKQL SLRGRNGQKS LSVKIPKGIN
     EGEKIRLKGQ GEQGINGGEN GDLYLTIRLH PHRNYIQEGI NLTTTVDVLP WDAALGSEVT
     VKTLDSTIKV RIPPGIQTDS KIRIAGKGYI DRKGTRGDLY IKVRIINPTS ISPEMKSLYE
     KLKDLSK
//
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