ID A0A1J9QM98_9PEZI Unreviewed; 528 AA.
AC A0A1J9QM98;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Mitochondrial chaperone {ECO:0000313|EMBL:OJD29601.1};
GN ORFNames=BKCO1_7700016 {ECO:0000313|EMBL:OJD29601.1};
OS Diplodia corticola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Diplodia.
OX NCBI_TaxID=236234 {ECO:0000313|EMBL:OJD29601.1, ECO:0000313|Proteomes:UP000183809};
RN [1] {ECO:0000313|EMBL:OJD29601.1, ECO:0000313|Proteomes:UP000183809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 112549 {ECO:0000313|EMBL:OJD29601.1,
RC ECO:0000313|Proteomes:UP000183809};
RA Fernandes I., De Jonge R., Van De Peer Y., Devreese B., Alves A.,
RA Esteves A.C.;
RT "Proteomics and genomics reveal pathogen-plant mechanisms compatible with a
RT hemibiotrophic lifestyle of Diplodia corticola.";
RL Submitted (OCT-2016) 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:OJD29601.1}.
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DR EMBL; MNUE01000077; OJD29601.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J9QM98; -.
DR STRING; 236234.A0A1J9QM98; -.
DR OrthoDB; 276132at2759; -.
DR Proteomes; UP000183809; 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 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: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:UP000183809};
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 70..134
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 229..309
FT /note="CR-type"
FT /evidence="ECO:0000259|PROSITE:PS51188"
FT ZN_FING 229..309
FT /note="CR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
FT REGION 469..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 528 AA; 55542 MW; C94FA79E1A0546B5 CRC64;
MSLAAPRAAV KKALPVRVAT ASAPQRRRFS SAAPSLPAWR RPALQCGRPP RQFGQGRPFH
ATAVHFATKD PYSVLGVDKN ASASEIKKAY YGLAKKYHPD TNKDAGAKDK FADAQSAYEL
LSDAEKKKAY DTYGSAAFDG GASGFGGGGA GPGGPGGNPF GGFGFGGGAG AGGFGADFNF
EDLFGAFAGA GARRGGRSRG SRNPFQEEIF VGDNIEVQTN ISFMDAAKGT TKEIFITPLV
QCNTCKASGL KKGTKKTSCQ VCHGTGQRVV SMGGFHMATA CEACGGAGVS VPSGSECSTC
DGQGAVRERK TVTVDIPGGV EDGMRLRVSG EGDAPLSGGT VSDKPRTQNG DLYVFIRVAA
DPKFQRSGSD VLYTATVPLT TAVLGGEIRI PTLDGDVKVK VPTGTGTGDK ITLGGMGMKK
LNSRKGMKGD LRVEFKVSMP KYLSANQRTI LEMLADEMGD QNAKRVMNLG SMSQDTKDKM
DEVEKNKHRN EGFLKSAWHN LTGQHKEMEK DSKNDKPDDE QKKASGSG
//
