ID A0A0H2RUB9_9AGAM Unreviewed; 428 AA.
AC A0A0H2RUB9;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 28-JUN-2023, entry version 25.
DE SubName: Full=DnaJ-domain-containing protein {ECO:0000313|EMBL:KLO13048.1};
GN ORFNames=SCHPADRAFT_997681 {ECO:0000313|EMBL:KLO13048.1};
OS Schizopora paradoxa.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Hymenochaetales; Schizoporaceae; Schizopora.
OX NCBI_TaxID=27342 {ECO:0000313|EMBL:KLO13048.1, ECO:0000313|Proteomes:UP000053477};
RN [1] {ECO:0000313|EMBL:KLO13048.1, ECO:0000313|Proteomes:UP000053477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KUC8140 {ECO:0000313|EMBL:KLO13048.1,
RC ECO:0000313|Proteomes:UP000053477};
RG DOE Joint Genome Institute;
RA Min B., Park H., Jang Y., Kim J.-J., Kim K.H., Pangilinan J., Lipzen A.,
RA Riley R., Grigoriev I.V., Spatafora J.W., Choi I.-G.;
RT "Complete genome sequence of Schizopora paradoxa KUC8140, a cosmopolitan
RT wood degrader in East Asia.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KQ085966; KLO13048.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H2RUB9; -.
DR STRING; 27342.A0A0H2RUB9; -.
DR InParanoid; A0A0H2RUB9; -.
DR OrthoDB; 2785358at2759; -.
DR Proteomes; UP000053477; 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:SF12; DNAJ PROTEIN HOMOLOG XDJ1; 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:UP000053477};
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 12..77
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 131..216
FT /note="CR-type"
FT /evidence="ECO:0000259|PROSITE:PS51188"
FT ZN_FING 131..216
FT /note="CR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
FT REGION 32..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..428
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 428 AA; 47271 MW; EDBB80E87A542A8A CRC64;
MVHVVNLVVH TELYEILGVS VTASEDEIKK AYRKKAREHH PDKNPNDPEA SQRFQELSGA
YEILSDSAKR EDYNNYGLEG LAGGSGVDPS DLFEMFAHSG FSFAFGGPPP KRKAKDSTIP
YEVTLEDLYN GKQVKMNMEK DVICSTCNGS GAKGNAKPKT CVKCDGNGFI ITTTPLGGSM
FTQGRSTCPD CQGVGEKLRE KDRCKKCKGK KVVSEKKRHE ITIEKGMANG QRIVLHGEGD
QVPGTPPGDV IFVLQLQRHD AFERSGNDLL AKVQITLSEA LLGFSRVLIK HLDGRGLKVN
SPPNKIIKTS DTIVLKGEGM PHLHRPGEKG DLYIIFSVEF PSEDWLQTVD HQALEKLLPP
KKPELDPQPE VVEEAKYEEG DFVDVRARSF PAGAEFMDQN FTSQFGEGDD DAWTDEDDDE
DGPECSQQ
//
