ID B6DTM5_BODSA Unreviewed; 431 AA.
AC B6DTM5;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE SubName: Full=DnaJ chaperone protein {ECO:0000313|EMBL:ACI16056.1};
OS Bodo saltans (Flagellated protozoan).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Eubodonida; Bodonidae; Bodo.
OX NCBI_TaxID=75058 {ECO:0000313|EMBL:ACI16056.1};
RN [1] {ECO:0000313|EMBL:ACI16056.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Lake Konstanz {ECO:0000313|EMBL:ACI16056.1};
RA Jackson A.P., Quail M.A., Berriman M.;
RT "Insights into the genome sequence of a free-living kinetoplastid: Bodo
RT saltans (Kinetoplastida: Euglenozoa).";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FJ168557; ACI16056.1; -; Genomic_DNA.
DR AlphaFoldDB; B6DTM5; -.
DR VEuPathDB; TriTrypDB:BSAL_51550; -.
DR GO; GO:0030544; F:Hsp70 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: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; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR044713; DNJA1/2-like.
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; PTHR43888:SF10; DNAJ-LIKE-2, ISOFORM A; 1.
DR PANTHER; PTHR43888; DNAJ-LIKE-2, ISOFORM A-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 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00546}; Repeat {ECO:0000256|ARBA:ARBA00022737};
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..71
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 130..212
FT /note="CR-type"
FT /evidence="ECO:0000259|PROSITE:PS51188"
FT ZN_FING 130..212
FT /note="CR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
FT REGION 361..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 431 AA; 46205 MW; BDAD31AFF9E24F76 CRC64;
MVADKALYDE LCISPTATES EIKSAYRKLA LKYHPDKNGG SEEAATKFKT VAEAYEILSD
PQKRKLYDQG GKAAVDPSAG GGGGGGAGGF NAEDIFSSFF GGGRSAKPGQ KKPHDILAEI
ELTLEEVYNG TNKLVRIARM RKCNGCAGTG STDKQRITCS GCGGSGRRVQ MVRIGGMAMQ
QQVGCPACQG VGVLPPRRPC GGCGAAGYCK EVKNFRVDVP RGTEDSDVVR ISGEGDQSSK
ADIDGDILFV FEVLSHSQFR RVGAADLVVE VRVPLVRLLQ NSFAIPIEHL DKRIIKCRLH
DTEQLFSPSF AYTCAREGMP IKGTSNERGK LTVVVKVTMP VSLTIAQTQL LADALHYERP
KQPAPEGAQY LSDWVPPEGH SSFTAGSEEK QSPKAKKSSN GGGSKRQQQQ QQQGGGGQMP
EGVHVQQCQQ Q
//
