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Database: UniProt
Entry: A0A0T5ZPE0_9CHLR
LinkDB: A0A0T5ZPE0_9CHLR
Original site: A0A0T5ZPE0_9CHLR 
ID   A0A0T5ZPE0_9CHLR        Unreviewed;       353 AA.
AC   A0A0T5ZPE0;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Chaperone DnaJ domain-containing protein, curved DNA-binding protein {ECO:0000313|EMBL:KRT64602.1};
GN   ORFNames=XU10_C0001G0051 {ECO:0000313|EMBL:KRT64602.1};
OS   Chloroflexi bacterium CSP1-4.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1640513 {ECO:0000313|EMBL:KRT64602.1, ECO:0000313|Proteomes:UP000051896};
RN   [1] {ECO:0000313|EMBL:KRT64602.1, ECO:0000313|Proteomes:UP000051896}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CSP1-4 {ECO:0000313|EMBL:KRT64602.1};
RA   Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA   Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT   "Critical biogeochemical functions in the subsurface are associated with
RT   bacteria from new phyla and little studied lineages.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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:KRT64602.1}.
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DR   EMBL; LDXM01000001; KRT64602.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0T5ZPE0; -.
DR   STRING; 1640513.XU10_C0001G0051; -.
DR   PATRIC; fig|1640513.3.peg.50; -.
DR   Proteomes; UP000051896; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
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; DNAJ HOMOLOG 1, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR43096:SF52; 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-binding {ECO:0000313|EMBL:KRT64602.1}.
FT   DOMAIN          5..70
FT                   /note="J"
FT                   /evidence="ECO:0000259|PROSITE:PS50076"
FT   REGION          334..353
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   353 AA;  38314 MW;  CD37C88D783B3D05 CRC64;
     MEYRDYYATL AVPRNAAPAE IKKAFRRLAR QYHPDVNKGN AAAERRFKEV NEANEVLSDP
     QKRKAYDALG ADWEAYQRAG TAGAPGGDPF AAFGRGQRGV RFEYRGDPED LAGFSDFFRT
     FFAGGVAGAE ASAGAEHGRR RTATVGLGFD DLLGGLGLDA DGVHARVGTQ RTAPTVRRSL
     QAEVKISLEE AYHGTTRRVE VDGKRLEVTI PRGIDSGRRI RLSGKAGRGP GAGDLYLAVK
     VSEHPVFTRQ GADLQRDLPI TLAEALLGAE VPVATLKGRV LLRIPPETQA GRVFRLAGQG
     MPRFRAEGFG DLFAKVRVVL PGGLDEADRA RLRDFTDHVR QPDPRATSGA PQR
//
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