ID A0A323UWQ9_9RHOO Unreviewed; 336 AA.
AC A0A323UWQ9;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=J domain-containing protein {ECO:0000313|EMBL:PZA16080.1};
GN ORFNames=DNK49_13785 {ECO:0000313|EMBL:PZA16080.1};
OS Parazoarcus communis SWub3 = DSM 12120.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Parazoarcus.
OX NCBI_TaxID=1121029 {ECO:0000313|EMBL:PZA16080.1, ECO:0000313|Proteomes:UP000248259};
RN [1] {ECO:0000313|EMBL:PZA16080.1, ECO:0000313|Proteomes:UP000248259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SWub3 {ECO:0000313|EMBL:PZA16080.1,
RC ECO:0000313|Proteomes:UP000248259};
RA Zorraquino Salvo V., Toubiana D., Blumwald E.;
RT "Azoarcus communis strain SWub3 genome.";
RL Submitted (JUN-2018) 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:PZA16080.1}.
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DR EMBL; QKOE01000009; PZA16080.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A323UWQ9; -.
DR OrthoDB; 9779889at2; -.
DR Proteomes; UP000248259; Unassembled WGS sequence.
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; 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 InterPro; IPR002939; DnaJ_C.
DR InterPro; IPR001623; DnaJ_domain.
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: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; SSF57938; DnaJ/Hsp40 cysteine-rich domain; 1.
DR SUPFAM; SSF49493; HSP40/DnaJ peptide-binding domain; 2.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51188; ZF_CR; 1.
PE 4: Predicted;
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00546}; Reference proteome {ECO:0000313|Proteomes:UP000248259};
KW 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 6..62
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 99..173
FT /note="CR-type"
FT /evidence="ECO:0000259|PROSITE:PS51188"
FT ZN_FING 99..173
FT /note="CR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
FT REGION 64..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 336 AA; 36197 MW; 1E3FE95BC8499216 CRC64;
MVNESEAFSL LELEPGATQA SIKRAFRRLA MRWHPDRNPD PAALEHFKRL RAAHDSLLES
FEADTPLPST QDAGHATSAP RAADRRRDLE IDLEQAVLGG EASLVFDIPS PCSDCDGSGW
QTRAHSRLCP DCHGSGRIRT ANGLTPCAVC NGRGYSNRAP CTCCDGSGQI VGHRTLTVRI
PPGIAEGDLL RLEGEGEPAS DAGSLPGDLL LRIRLRPHPL YRVIGRDVVI ERPVSIFTLL
GGGQIRVPGP SEPHTLNIEA GSAAPRTVRI EGAGLPARSG FAAGALCVSL NPVTPAPTSD
KSVIELYRAI QGRLTQDQHM LLPELDTWEH QWLPPL
//
