ID A0A0D1DZE7_USTMA Unreviewed; 409 AA.
AC A0A0D1DZE7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Putative type I HSP40 co-chaperone YDJ1 {ECO:0000313|EMBL:KIS69394.1};
GN ORFNames=UMAG_11722 {ECO:0000313|EMBL:KIS69394.1};
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631 {ECO:0000313|EMBL:KIS69394.1, ECO:0000313|Proteomes:UP000000561};
RN [1] {ECO:0000313|EMBL:KIS69394.1, ECO:0000313|Proteomes:UP000000561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kamper J., Kahmann R., Bolker M., Ma L.J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Muller O., Perlin M.H., Wosten H.A.,
RA de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M.,
RA Perez-Martin J., Feldbrugge M., Basse C.W., Steinberg G., Ibeas J.I.,
RA Holloman W., Guzman P., Farman M., Stajich J.E., Sentandreu R.,
RA Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J.,
RA Mendoza-Mendoza A., Greilinger D., Munch K., Rossel N., Scherer M.,
RA Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S.,
RA Ho E.C., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J.,
RA Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H.,
RA Hauser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schluter T.,
RA Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V.,
RA Mannhaupt G., Guldener U., Munsterkotter M., Haase D., Oesterheld M.,
RA Mewes H.W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.,
RA Jaffe D.B., Calvo S., Nusbaum C., Galagan J., Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2] {ECO:0000313|Proteomes:UP000000561}
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CM003145; KIS69394.1; -; Genomic_DNA.
DR RefSeq; XP_011389233.1; XM_011390931.1.
DR AlphaFoldDB; A0A0D1DZE7; -.
DR STRING; 237631.A0A0D1DZE7; -.
DR EnsemblFungi; KIS69394; KIS69394; UMAG_11722.
DR GeneID; 23567574; -.
DR KEGG; uma:UMAG_11722; -.
DR VEuPathDB; FungiDB:UMAG_11722; -.
DR eggNOG; KOG0712; Eukaryota.
DR InParanoid; A0A0D1DZE7; -.
DR OrthoDB; 2785358at2759; -.
DR Proteomes; UP000000561; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0051087; F:protein-folding chaperone binding; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
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:SF10; DNAJ-LIKE-2, ISOFORM A; 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:UP000000561};
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 6..67
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 128..211
FT /note="CR-type"
FT /evidence="ECO:0000259|PROSITE:PS51188"
FT ZN_FING 128..211
FT /note="CR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
FT REGION 359..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 409 AA; 44726 MW; F55DE7EE850C8B13 CRC64;
MVKETKFYDL LEVTPTASEA ELKKAYRKKA LKEHPDKGGD PEKFKAITAA YEILSDPDKR
DLYDRFGEQG LEGGGMGGGM DPQDLFSQLF GGGGGGFFGG SGGRPRGPRK GKDLVHRVKV
SLEELYVGKV TKLALQKHVL CKKCDGRGGK EGAVKTCGGC NGQGIKVVLR QLGPMVQQMQ
QTCPECQGLG EIINPKDRCK ECNGKKINQE RKVLEVRIDK GMEDGQQITF KEEADQAPNT
IPGDVVIVID EKPHPRFKRR KNDLFIDVEV DLLTALGGGK ILIEHLDDHA LSVDIPAGEV
IKPGDVKVLR GQGMPSYRHH ELGDLYVNLS VAFPETIDID NIPLLEKALP PRNALPKTKK
EIDVEDVQMD ELDEREARNV KPNGAGSHPG MDDDDEDGQG ASNIQCAQS
//
