ID A0A165H8E3_EXIGL Unreviewed; 403 AA.
AC A0A165H8E3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 13-SEP-2023, entry version 23.
DE RecName: Full=DnaJ-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=EXIGLDRAFT_769745 {ECO:0000313|EMBL:KZV91598.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV91598.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV91598.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV91598.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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DR EMBL; KV426024; KZV91598.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165H8E3; -.
DR STRING; 1314781.A0A165H8E3; -.
DR InParanoid; A0A165H8E3; -.
DR OrthoDB; 2785358at2759; -.
DR Proteomes; UP000077266; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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 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; 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 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00546}; Reference proteome {ECO:0000313|Proteomes:UP000077266};
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 6..67
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 128..211
FT /note="CR-type"
FT /evidence="ECO:0000259|PROSITE:PS51188"
FT ZN_FING 128..211
FT /note="CR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
FT REGION 351..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..397
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 403 AA; 44341 MW; 6A0E01A30B22F0AC CRC64;
MVKETKYYDL LEATPDASEA DLKKAYRKRA LRLHPDKGGD PELFKEVTHA YEVLSDPQKR
SIYDTRGEAG LSEQGGMGGM DAHDLFSQLF GGGGGGFFGG GPSRPSGPRK GKDLVHRVHV
TLEELYRGKT SRLALTRHVI CAKCSGKGGK EGAVKTCPGC NGRGVRVLMR QMGPMIQQIQ
QACNECDGSG EIIKEKDRCK TCNGKKTVQE RKMLDVHIDK GMKGGSTIVF NGESDQAPDT
IPGDVVIVVE EKPHDRFTRK DTDLYHKLDI DLLSALGGGV FAIPHLDDRV LHVTVRPGEV
IKPGHQKVIH GQGMPSQRHH EPGDLYVTFN VVFPETIDPA VVSHLEAALP PRTPLPAVPK
GHVVDEVDLD ELDARQRRKA ERSRSEDAMD EDEEQPRVQC QNQ
//
