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Database: UniProt
Entry: A0A0S7DM86_9EURO
LinkDB: A0A0S7DM86_9EURO
Original site: A0A0S7DM86_9EURO 
ID   A0A0S7DM86_9EURO        Unreviewed;       543 AA.
AC   A0A0S7DM86;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   08-NOV-2023, entry version 29.
DE   SubName: Full=DnaJ homolog 1, mitochondrial {ECO:0000313|EMBL:GFF47504.1};
GN   ORFNames=ALT_000675 {ECO:0000313|EMBL:GIM38293.1}, CNMCM8060_005717
GN   {ECO:0000313|EMBL:KAF4177127.1}, IFM58399_08065
GN   {ECO:0000313|EMBL:GFF47504.1};
OS   Aspergillus lentulus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=293939 {ECO:0000313|EMBL:GIM38293.1};
RN   [1] {ECO:0000313|EMBL:GIM38293.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IFM 54703 {ECO:0000313|EMBL:GIM38293.1};
RA   Kusuya Y., Sakai K., Kamei K., Takahashi H., Yaguchi T.;
RT   "Draft Genome sequence of the pathogenic filamentous fungus Aspergillus
RT   lentulus IFM 54703T.";
RL   Genome Announc. 4:e01568-15(2016).
RN   [2] {ECO:0000313|EMBL:KAF4177127.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CNM-CM8060 {ECO:0000313|EMBL:KAF4177127.1};
RA   dos Santos R.A.C., Steenwyk J.L., Rivero-Menendez O., Mead M.E.,
RA   Silva L.P., Bastos R.W., Alastruey-Izquierdo A., Goldman G.H., Rokas A.;
RT   "Genomic and phenotypic heterogeneity of clinical isolates of the human
RT   pathogens Aspergillus fumigatus, Aspergillus lentulus and Aspergillus
RT   fumigatiaffinis.";
RL   bioRxiv 0:0-0(2020).
RN   [3] {ECO:0000313|EMBL:GFF47504.1, ECO:0000313|Proteomes:UP000465261}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 58399 {ECO:0000313|EMBL:GFF47504.1,
RC   ECO:0000313|Proteomes:UP000465261};
RA   Takahashi H., Yaguchi T.;
RT   "Draft genome sequence of Aspergillus lentulus IFM 58399.";
RL   Submitted (JAN-2020) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:KAF4177127.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CNM-CM8060 {ECO:0000313|EMBL:KAF4177127.1};
RA   Santos R.A.C., Steenwyk J.L., Rivero-Menendez O., Mead M.E., Silva L.P.,
RA   Bastos R.W., Alastruey-Izquierdo A., Goldman G.H., Rokas A.;
RL   Submitted (APR-2020) 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:GIM38293.1}.
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DR   EMBL; BLKH01000062; GFF47504.1; -; Genomic_DNA.
DR   EMBL; BCLY01000008; GIM38293.1; -; Genomic_DNA.
DR   EMBL; JAAAPS010000035; KAF4177127.1; -; Genomic_DNA.
DR   STRING; 293939.A0A0S7DM86; -.
DR   VEuPathDB; FungiDB:TMP_alenIFM54703_3984; -.
DR   OrthoDB; 276132at2759; -.
DR   Proteomes; UP000465261; Unassembled WGS sequence.
DR   Proteomes; UP000713487; Unassembled WGS sequence.
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   PANTHER; PTHR43096; DNAJ HOMOLOG 1, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR43096:SF10; 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}; 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          84..148
FT                   /note="J"
FT                   /evidence="ECO:0000259|PROSITE:PS50076"
FT   DOMAIN          237..318
FT                   /note="CR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51188"
FT   ZN_FING         237..318
FT                   /note="CR-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
FT   REGION          478..543
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        480..502
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   543 AA;  57105 MW;  470CD19365BC7DC2 CRC64;
     MNSTAAAMPK AAAIPARLLR TSRQCSNQTP ANKARSATHI RTYYASTIAS SGNRSRDGVY
     ARRFPSIVSA RGFHTTAALT AVPDPYKVLG VDRNASAGDI KKAYYGLAKK YHPDTNKDPN
     AKEKFAEAQS AYELLSDAKK RETYDRFGSA AFDQNGGFDP NAAAGGNPFA GAGGFHGFGG
     GFPGGFAADI NFEDLFGAFT GGARRSGRGR RGPFQEILVG EDIEVQTNIS FMEAAKGTSK
     DVVITPLTAC GTCKGDGLKE GAKRSQCRQC NGSGTRVHFM QGGFQVAATC DACGGAGMIV
     PRGSECGTCR GNGVVRDKKT ITVDIPGGVE DGMRLRVAGE GDAPPTGTQA TPGTRTQRGD
     LYVSIRVAPD HRFSRSGSDI LYTASIPLTT ALLGGEVTIP TLDGEVKVKV ATGTGTGDRI
     TLSGMGMKKL GGRARGYTPT GDLKVEFKVA MPKYLTANQR TILEVLADEM NDKTARRTMN
     IGKDSPSSEA GNASNESQKN EGFLKSAWHK LMNSAKNGDG GNSASNPSKK EPGDAKKSDK
     ESK
//
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