ID A0A0G4MGP7_9PEZI Unreviewed; 547 AA.
AC A0A0G4MGP7;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=J domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BN1708_001042 {ECO:0000313|EMBL:CRK33354.1};
OS Verticillium longisporum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK33354.1, ECO:0000313|Proteomes:UP000044602};
RN [1] {ECO:0000313|EMBL:CRK33354.1, ECO:0000313|Proteomes:UP000044602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VL1 {ECO:0000313|EMBL:CRK33354.1};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CVQH01022527; CRK33354.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4MGP7; -.
DR STRING; 100787.A0A0G4MGP7; -.
DR OrthoDB; 276132at2759; -.
DR Proteomes; UP000044602; 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; 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; 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:UP000044602};
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 79..143
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 238..319
FT /note="CR-type"
FT /evidence="ECO:0000259|PROSITE:PS51188"
FT ZN_FING 238..319
FT /note="CR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
FT REGION 503..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..547
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 547 AA; 56625 MW; F4E483A8BC56E1B6 CRC64;
MNTSSLLTKA AAAPSRLLPV RACRRPKLGE PLCKHAQIHT AAFAASSRPS VRYLSPANSS
AQSSKRAFHA SPTNLATKDP YKALGVGKSA SASEIKKAYY GLAKKYHPDT NKDASAKETF
GEIQSAYEIL SDPAKKQQYD QFGAAGFDPS GGGGPGGFGG GDPFGGGNPF HGFGGQAGGG
FGGGFNFDDI FSAFTGSQGG PFGGGRGRGG RNPFREEVLV GDNIEVHASI SFMEAAKGVA
KTLHITPLST CGTCSGSGLK AGTKRTECKT CHGTGTRVHT MNGGFQMAST CGSCGGTGST
VPRGGECKPC SGNGVVRERK TITVDIPAGI EDGMRLRVDG SGDAPVTGKA ADPNVRAQKG
DLYVFVRVAS DPKFRRAGSD ILYTANLPIT TAMLGGEVTI PTLTGQVNVK VATGTSTGDR
LTLSGMGMKK LSGRGGSGDL KVEFRVSMPK YLSANQRTLI EMLANEMGDK TAKRIMNVSP
TGSTVDPDAS DSHKNEGFLK SMWHTLTNHP AHNKSETDAS GSGSGSGSST DKPAEKKDEP
PKKPDSP
//