ID A0A507DZI7_9FUNG Unreviewed; 372 AA.
AC A0A507DZI7;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 13-SEP-2023, entry version 14.
DE RecName: Full=J domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PhCBS80983_g03943 {ECO:0000313|EMBL:TPX57239.1};
OS Powellomyces hirtus.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Spizellomycetales;
OC Powellomycetaceae; Powellomyces.
OX NCBI_TaxID=109895 {ECO:0000313|EMBL:TPX57239.1, ECO:0000313|Proteomes:UP000318582};
RN [1] {ECO:0000313|EMBL:TPX57239.1, ECO:0000313|Proteomes:UP000318582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 809.83 {ECO:0000313|EMBL:TPX57239.1,
RC ECO:0000313|Proteomes:UP000318582};
RX PubMed=31209237; DOI=.1038/s41598-019-45128-9;
RA van de Vossenberg B.T.L.H., Warris S., Nguyen H.D.T.,
RA van Gent-Pelzer M.P.E., Joly D.L., van de Geest H.C., Bonants P.J.M.,
RA Smith D.S., Levesque C.A., van der Lee T.A.J.;
RT "Comparative genomics of chytrid fungi reveal insights into the obligate
RT biotrophic and pathogenic lifestyle of Synchytrium endobioticum.";
RL Sci. Rep. 9:8672-8672(2019).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TPX57239.1}.
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DR EMBL; QEAQ01000055; TPX57239.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A507DZI7; -.
DR STRING; 109895.A0A507DZI7; -.
DR Proteomes; UP000318582; 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:UP000318582};
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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..372
FT /note="J domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5021378471"
FT DOMAIN 26..91
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 151..234
FT /note="CR-type"
FT /evidence="ECO:0000259|PROSITE:PS51188"
FT ZN_FING 151..234
FT /note="CR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
SQ SEQUENCE 372 AA; 40899 MW; 3F6CB5B424073F2F CRC64;
MKLRTIPLVA ALLLLLAIPA ILASADYYKV LGVDRSATKK TIKKAYRESS KKYHPDKNPG
DKVAEDKFVE LAQAYEVLSD DEKRRIYDQY GEEGLKGSGQ QFHNPFDIFA QFGGFGGGGF
GGFGHRHHAQ QQKGPEVHMD VAVTLEELFL GTSIEVEINK QIICPTCRGS GAKHADDVTQ
CTACGGSGIR VVRQMLGPGM YTQMQQHCDA CGGRGKIIKS KCKACSGTKV KRGSHQVTIT
VDRGMADAQR ITLDQESDEA PDIIPGDLVF TLQTQPHPVF TRNGDNLYAK QVISLKEALL
GVDRKLKQLD GSLVTVRREG VTQPGFVQEI RGEGMPKHDR PNERGLLYVE YIVVLPEKLT
NAQIDLADKM FA
//