ID M4YPZ0_THEXX Unreviewed; 379 AA.
AC M4YPZ0;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Chaperone protein DnaJ {ECO:0000313|EMBL:AGI48452.1};
GN ORFNames=TALC_01478 {ECO:0000313|EMBL:AGI48452.1};
OS Thermoplasmatales archaeon (strain BRNA1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales.
OX NCBI_TaxID=1054217 {ECO:0000313|EMBL:AGI48452.1, ECO:0000313|Proteomes:UP000012076};
RN [1] {ECO:0000313|EMBL:AGI48452.1, ECO:0000313|Proteomes:UP000012076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRNA1 {ECO:0000313|EMBL:AGI48452.1,
RC ECO:0000313|Proteomes:UP000012076};
RA Denman S.E., Evans P., Bragg L., Padmanahba J., McKenzie M., Edwards D.,
RA Krzycki J., McSweeney C., Morrison M.;
RT "Thermoplasmatales-like gut symbionts are pyrrolysine dependent-
RT methanogens.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP002916; AGI48452.1; -; Genomic_DNA.
DR AlphaFoldDB; M4YPZ0; -.
DR STRING; 1054217.TALC_01478; -.
DR KEGG; tar:TALC_01478; -.
DR PATRIC; fig|1054217.5.peg.1406; -.
DR eggNOG; arCOG06880; Archaea.
DR HOGENOM; CLU_017633_0_1_2; -.
DR Proteomes; UP000012076; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0009408; P:response to heat; 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 HAMAP; MF_01152; DnaJ; 1.
DR InterPro; IPR012724; DnaJ.
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 NCBIfam; TIGR02349; DnaJ_bact; 1.
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 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 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00546}; Reference proteome {ECO:0000313|Proteomes:UP000012076};
KW 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 8..74
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 142..223
FT /note="CR-type"
FT /evidence="ECO:0000259|PROSITE:PS51188"
FT ZN_FING 142..223
FT /note="CR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
FT REGION 360..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 379 AA; 40866 MW; B3F66A691723E29F CRC64;
MPEQQRRDYY EVLGVSKGAS ADEIKKAYRQ MAKKYHPDVS TEPKDVAEAK FKEISEAYEV
LSDPDKRSRY DQYGFAGVDG SFGQGGFDWS DFTHGDDISD IFGDLFGGMF GGGRRRQDPN
APQQGDHLRY DTEIDLLDVL KGKDTEINVP HSAICSDCHG TGGKDGKTNV CPTCGGRGQV
QSVRRTPFGN AVSISPCPKC GGTGKTFDTP CPKCRGRGRV NKTTKVSVHI PAGIEDGMRL
RVPGAGDAGT NGGAPGDLFV VVHVRENGSF ERDGTDLWAV AETTYPRLVL GGTVEVKNVE
GKTIEINVPA GTQVGGVIRV PGQGLPSVNR PSDRGNLYVR VAIKVPKKVT DMEKELLMKL
DSEAGKKPSK KSKGIFGKK
//