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Database: UniProt
Entry: A0A2T4GCV5_FUSCU
LinkDB: A0A2T4GCV5_FUSCU
Original site: A0A2T4GCV5_FUSCU 
ID   A0A2T4GCV5_FUSCU        Unreviewed;       526 AA.
AC   A0A2T4GCV5;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=DnaJ 1, mitochondrial {ECO:0000313|EMBL:PTD01414.1};
GN   ORFNames=FCULG_00009966 {ECO:0000313|EMBL:PTD01414.1}, HYE67_006241
GN   {ECO:0000313|EMBL:QPC64010.1};
OS   Fusarium culmorum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=5516 {ECO:0000313|EMBL:PTD01414.1, ECO:0000313|Proteomes:UP000241587};
RN   [1] {ECO:0000313|EMBL:PTD01414.1, ECO:0000313|Proteomes:UP000241587}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PV {ECO:0000313|EMBL:PTD01414.1,
RC   ECO:0000313|Proteomes:UP000241587};
RA   Schmidt R.;
RT   "Fusarium culmorum secondary metabolites in fungal-bacterial-plant
RT   interactions.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:QPC64010.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Class2-1B {ECO:0000313|EMBL:QPC64010.1};
RA   Yuan Z.;
RT   "The chromosome-scale genome resource for two endophytic Fusarium species:
RT   F. culmorum and F. pseudograminearum.";
RL   Submitted (NOV-2020) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; PVEM01000028; PTD01414.1; -; Genomic_DNA.
DR   EMBL; CP064749; QPC64010.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T4GCV5; -.
DR   OMA; CPECAGD; -.
DR   Proteomes; UP000241587; Unassembled WGS sequence.
DR   Proteomes; UP000663297; Chromosome 3.
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: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:UP000241587};
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          231..312
FT                   /note="CR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51188"
FT   ZN_FING         231..312
FT                   /note="CR-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
FT   REGION          470..526
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        497..514
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   526 AA;  55532 MW;  9FA23797B17C6ABF CRC64;
     MNPSLISKAT RPTRVLAQNA PKIQCLRKGA QLHTAAWHVG SQRQPSFRKG SQSPSAKRLF
     HATNAVQQKD PYQALGVGKT ASAGDIKKAY YGLAKKYHPD TNKDPQAKDK FADIQSAYEI
     LSDPKKREQF DQFGAAGFDP SGGGAPGGGG GFGGGHPFSG FGGFGGQGGF GGFGGQGGFG
     AGVNFEDIFS AFTGQQGFGR RSRQQAYQQE ILVGENIEVQ STISFMEAAK GTTKTISITP
     LSTCGTCKGN GMKSGSSRSA CSACDGSGTR INYMQGGFQM ASTCGTCDGT GTVIPRGSEC
     KPCSGNGVVR ERKTITVDIP AGIEDGMRLR VDGAGDAALT GRSAEPNARS QNGDLYVFVR
     VAKDPKFRRD GSNILYTANI PLTTALLGGH AEIPTLDGTV NVKVATGTNT GDKITLPGMG
     MKRLGSRRGG NGDLRVEYRV SMPKYLSANQ RTIVEVLADE MGDKTAKRVM GVGSSRDPND
     PDTHRDEGFL KSLWHTLTNH PAHQKPNEDG SQNDGSTKKP GDDDKK
//
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