DNJ1_USTMA
ID DNJ1_USTMA Reviewed; 581 AA.
AC A0A0D1E2P6;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2015, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Tetratricopeptide repeat and J domain-containing co-chaperone DNJ1 {ECO:0000303|PubMed:26487566};
DE Flags: Precursor;
GN Name=DNJ1 {ECO:0000303|PubMed:26487566}; ORFNames=UMAG_05173;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA 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]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INTERACTION WITH
RP BIP1, DOMAIN, INDUCTION, AND MUTAGENESIS OF 495-HIS--ASP-497.
RX PubMed=26487566; DOI=10.1111/nph.13703;
RA Lo Presti L., Lopez Diaz C., Turra D., Di Pietro A., Hampel M., Heimel K.,
RA Kahmann R.;
RT "A conserved co-chaperone is required for virulence in fungal plant
RT pathogens.";
RL New Phytol. 209:1135-1148(2016).
CC -!- FUNCTION: Endoplasmic reticulum (ER) protein that functions as a co-
CC chaperone for BIP1 during ER stress (PubMed:26487566). Might be
CC specifically involved in the refolding of N-glycosylated proteins
CC (PubMed:26487566). {ECO:0000269|PubMed:26487566}.
CC -!- SUBUNIT: Interacts with the ER chaperone BIP1.
CC {ECO:0000269|PubMed:26487566}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000269|PubMed:26487566}.
CC -!- INDUCTION: Expression is induced by the unfolded protein response (UPR)
CC and controled by the UPR-specific transcription factor CIP1.
CC {ECO:0000269|PubMed:26487566}.
CC -!- DOMAIN: The TPR repeats mediate interaction with unfolded polypeptides
CC and the J-domain is essential to stimulate the ATPase activity of the
CC chaperone and to increase its substrate affinity during the folding
CC cycle. {ECO:0000305|PubMed:26487566}.
CC -!- DISRUPTION PHENOTYPE: Leads to hypersensitivity to endoplasmic
CC reticulum (ER) stress caused by the N-glycosylation inhibitor
CC tunicamycin, but only to slight reduction of virulence
CC (PubMed:26487566). Severely affects growth and displays an altered
CC morphology, when the calnexin CNE1 is also deleted (PubMed:26487566).
CC {ECO:0000269|PubMed:26487566}.
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DR EMBL; CM003143; KIS70101.1; -; Genomic_DNA.
DR RefSeq; XP_011388225.1; XM_011389923.1.
DR STRING; 5270.UM05173P0; -.
DR EnsemblFungi; KIS70101; KIS70101; UMAG_05173.
DR GeneID; 23565135; -.
DR KEGG; uma:UMAG_05173; -.
DR VEuPathDB; FungiDB:UMAG_05173; -.
DR eggNOG; KOG0624; Eukaryota.
DR OMA; PFAHFQH; -.
DR OrthoDB; 1106865at2759; -.
DR Proteomes; UP000000561; Chromosome 4.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR GO; GO:0034975; P:protein folding in endoplasmic reticulum; IBA:GO_Central.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF00226; DnaJ; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SMART; SM00028; TPR; 5.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS50005; TPR; 2.
PE 1: Evidence at protein level;
KW Chaperone; Endoplasmic reticulum; Glycoprotein; Reference proteome; Repeat;
KW Signal; TPR repeat; Virulence.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..581
FT /note="Tetratricopeptide repeat and J domain-containing co-
FT chaperone DNJ1"
FT /id="PRO_5002229571"
FT REPEAT 48..81
FT /note="TPR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 82..115
FT /note="TPR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 116..149
FT /note="TPR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 221..254
FT /note="TPR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 257..293
FT /note="TPR 5"
FT /evidence="ECO:0000255"
FT REPEAT 378..411
FT /note="TPR 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 412..445
FT /note="TPR 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT DOMAIN 467..528
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 522..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 495..497
FT /note="HPD->QAA: Affect txunicamycin resistance and
FT virulence."
FT /evidence="ECO:0000269|PubMed:26487566"
SQ SEQUENCE 581 AA; 63837 MW; 9263DCAE322125DE CRC64;
MKATLLPSLL ALSLTLCLAL GLSSSGVLVR ADAFASSQPP VVSDPVLASQ HLTQANVALQ
SGRYQDALSA FDLALQADPS SWLTYYRRAT AQLSLGRTSA ALQDFQSLLK LNPKFDKAYL
QQAKVYLKEG DCDKAKQALK TYDSIRAEKG AANSSPAEAN SVRSKLTLVE TSIKSLGQLV
KELDKAQKAD KKGKAKELDS TKVDHCIHLA GEVLKISPSH LETRLVRARC QTMKGRIEDA
MADWTRAVHL TPSPFLLRRL SVLSYFVVSE PGSQSRDAGL QHLKACLHSD PDNKSCAKMH
RKIKALEKSL KKARNFYNSQ SYRAVLSALK GGKVGRATVV DDIKEAIRSA TEVQSGDEEP
LIPSTYKGDP VQESGLLLEL HTMYCKAYTE LNDMDKAMPY CELVLAKDPD NVEATLARAE
LALQREDYDQ AVRDLTKAFD ASGRTDRAIH QKLQTAQKRL KLSQSKDYYK VLGVKRTDSL
ATIKKAYRKM ARENHPDKGG SQEKMAQINE AWGVLGDEEL RKKYDQGDDP NDPMGGQQGG
YGNPFAQGGH PFDMFFQQQA GFGGFPGGGF PGGQQFHFKM G
