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Database: UniProt
Entry: A0A0C2ZWS9_9AGAM
LinkDB: A0A0C2ZWS9_9AGAM
Original site: A0A0C2ZWS9_9AGAM 
ID   A0A0C2ZWS9_9AGAM        Unreviewed;       371 AA.
AC   A0A0C2ZWS9;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   13-SEP-2023, entry version 31.
DE   RecName: Full=DnaJ-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=SCLCIDRAFT_1219951 {ECO:0000313|EMBL:KIM56917.1};
OS   Scleroderma citrinum Foug A.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Sclerodermatineae; Sclerodermataceae;
OC   Scleroderma.
OX   NCBI_TaxID=1036808 {ECO:0000313|EMBL:KIM56917.1, ECO:0000313|Proteomes:UP000053989};
RN   [1] {ECO:0000313|EMBL:KIM56917.1, ECO:0000313|Proteomes:UP000053989}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Foug A {ECO:0000313|EMBL:KIM56917.1,
RC   ECO:0000313|Proteomes:UP000053989};
RG   DOE Joint Genome Institute;
RA   Kuo A., Kohler A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA   Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA   Hua S.X.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000053989}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Foug A {ECO:0000313|Proteomes:UP000053989};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KN822108; KIM56917.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C2ZWS9; -.
DR   STRING; 1036808.A0A0C2ZWS9; -.
DR   HOGENOM; CLU_017633_0_2_1; -.
DR   InParanoid; A0A0C2ZWS9; -.
DR   OrthoDB; 2785358at2759; -.
DR   Proteomes; UP000053989; 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; DNAJ-LIKE-2, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR43888:SF53; DNAJ-RELATED PROTEIN SCJ1; 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:UP000053989};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
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   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..371
FT                   /note="DnaJ-domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002172160"
FT   DOMAIN          22..86
FT                   /note="J"
FT                   /evidence="ECO:0000259|PROSITE:PS50076"
FT   DOMAIN          140..223
FT                   /note="CR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51188"
FT   ZN_FING         140..223
FT                   /note="CR-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
SQ   SEQUENCE   371 AA;  41071 MW;  3A9557A4A9ECB579 CRC64;
     MLPTSLFAVL FVLFGLVCAA TDLYKALELS RGASEQDIRK AYKRLSRKYH PDKNKDPGAE
     EKFVEIAHAY EVLSDENKRR IYDQFGEDGL RAHEGGHQQY ANPFDVFSSF FGGGFGGQQT
     RRGPNSIFEV EVSLADMYTG ASLDFTIKKN VLCDYCRGSG AASDRDIHTC RACGGTGVKI
     SKQQIFPGMF AQTQSTCNEC GGRGTVIVKK CPHCSGQKVV EYTQPNTLDI QPGMPDGHEV
     VLEGEGDESP DWEAGDVILR VRSKQEQGGW RRKETSLYWR ETIGVDEALL GFKLNLTHLD
     GHIVELHHKG VTQPGYVQVI EGEGMPVFGQ SGHGNLYIEY NVVLPVDLGS DMRKKLGEAF
     YGSAYHGRDE L
//
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