ID   EFUJ_HORCR              Reviewed;         614 AA.
AC   A0A2Z4HPY9;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2018, sequence version 1.
DT   23-FEB-2022, entry version 5.
DE   RecName: Full=Probable self-resistance protein efuJ {ECO:0000303|PubMed:30051576};
DE   AltName: Full=Enfumafungin biosynthesis cluster protein J {ECO:0000303|PubMed:30051576};
DE   Flags: Precursor;
GN   Name=efuJ {ECO:0000303|PubMed:30051576};
OS   Hormonema carpetanum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Dothideales; Dothioraceae; Hormonema.
OX   NCBI_TaxID=284138;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=30051576; DOI=10.1111/1462-2920.14333;
RA   Kuhnert E., Li Y., Lan N., Yue Q., Chen L., Cox R.J., An Z., Yokoyama K.,
RA   Bills G.F.;
RT   "Enfumafungin synthase represents a novel lineage of fungal triterpene
RT   cyclases.";
RL   Environ. Microbiol. 20:3325-3342(2018).
CC   -!- FUNCTION: Probable self-resistance protein; part of the gene cluster
CC       that mediates the biosynthesis of enfumafungin, a glycosylated fernene-
CC       type triterpenoid with potent antifungal activity, mediated by its
CC       interaction with beta-1,3-glucan synthase and the fungal cell wall
CC       (PubMed:30051576). Does not encode any steps in enfumafungin
CC       biosynthesis, but because it is related to a fungal cell wall
CC       structural proteins, it might play a role in self-resistance toward
CC       enfumafungin (Probable). {ECO:0000269|PubMed:30051576,
CC       ECO:0000305|PubMed:30051576}.
CC   -!- SIMILARITY: Belongs to the SED1 family. {ECO:0000305}.
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DR   EMBL; MF611892; AWW17220.1; -; Genomic_DNA.
DR   GO; GO:0005199; F:structural constituent of cell wall; IEA:InterPro.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IEA:InterPro.
DR   InterPro; IPR038843; Sed1/Spi1.
DR   PANTHER; PTHR35523; PTHR35523; 3.
PE   3: Inferred from homology;
KW   Glycoprotein; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..614
FT                   /note="Probable self-resistance protein efuJ"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5016313931"
FT   CARBOHYD        24
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        107
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        140
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        213
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        518
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        529
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   614 AA;  62375 MW;  F3AEE012B5F52A8A CRC64;
     MAARLTAVIA LGVAFVSASP AYSNTTSSAY LCNPAHSYPS GVSCDATART LITPAPSSPS
     SAYFCNPAHS YPGGVSCDAT ARTLITPAPS ASSSAYLCNP AHSYPDNVTC DATARTLITP
     APSASSSVYL CNPAHSYPGN VTCDATARTL VTPTLSSSSA YLCNPAHSYP GGVSCDATAR
     TLFTPAPSPV TLTEVVTSFT TFCPSPTTLV AGNKTYTVTK PTTLTITDCP GGCTLTRTAV
     PSPVTLTEIV TSFTTFCPSP TTLTAGGKTY TVTKATTLTI TDCPGGCTLT KAIVPSPVTV
     TEVVKSFTTF CPAPTTLTAG GKTYTITKPT TLTFTECPGG CTLTKTAIPV AYTTTEAVST
     FTTYCPQPTT ITVDKQTITV TAATTLSVPV TQTLTKPVLP VTSAPSASAS SRAYLCNPAH
     SYPGGVSCDA TARTLIYPST KDAVTGAALI TTIVPAVPAQ TGVASGNCAP VYVTITIKEI
     QTVTVGLGSP VYFTSSSQAP SVSVDTPVYI TGSSYFHNTS APAPTTNANA TSSAYLCNPA
     HSYPGGVSCD ATARTLIYPS TSTASFSSIS GIPGGCNPAH PGSCPSSYFD TTIPAQATAS
     ATKATRRGSK MVRA