ID   ECDJ_ASPRU              Reviewed;         668 AA.
AC   K0DZ91;
DT   25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2012, sequence version 1.
DT   25-MAY-2022, entry version 12.
DE   RecName: Full=Echinocandin B biosynthetic cluster protein J {ECO:0000303|PubMed:22998630};
GN   Name=ecdJ {ECO:0000303|PubMed:22998630};
OS   Aspergillus rugulosus (Emericella rugulosa).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=41736;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, AND BIOTECHNOLOGY.
RC   STRAIN=ATCC 58397 / NRRL 11440;
RX   PubMed=22998630; DOI=10.1021/ja307220z;
RA   Cacho R.A., Jiang W., Chooi Y.H., Walsh C.T., Tang Y.;
RT   "Identification and characterization of the echinocandin B biosynthetic
RT   gene cluster from Emericella rugulosa NRRL 11440.";
RL   J. Am. Chem. Soc. 134:16781-16790(2012).
CC   -!- FUNCTION: Part of the gene cluster that mediates the biosynthesis of
CC       echinocandin B, a fungal lipidated cyclic hexapeptide that acts as an
CC       antifungal agent (PubMed:22998630). Linoleoyl-AMP, produced by the
CC       fatty-acyl-AMP ligase ecdI, is transferred to the initiation carrier
CC       domain (T0) of ecdA (PubMed:22998630). The linoleoyl-S-
CC       phosphopantetheinyl-T0 is sequentially extended with L-ornithine, L-
CC       threonine, L-proline, L-homotyrosine, L-threonine, and 4R-methyl-L-
CC       proline to form the linear hexapeptide (PubMed:22998630). Thereafter,
CC       the terminal condensation (C7) performs macrocyclization of the NRPS
CC       product and the cyclic scaffold is released from ecdA
CC       (PubMed:22998630). All six of the amino acid residues are hydroxylated,
CC       including 4R,5R-dihydroxy-L-ornithine, 4R-hydroxyl-L-proline, 3S,4S-
CC       dihydroxy-L-homotyrosine, and 3S-hydroxyl-4S-methyl-L-prolin
CC       (PubMed:22998630). In the pathway, all the hydroxylation reactions are
CC       proposed to occur following completion of the cyclic peptide, so the
CC       unhydroxylated precursor produced by ecdA will undergo six rounds of
CC       hydroxylation (PubMed:22998630). Five hydroxylase genes (ecdG, ecdH,
CC       ecdK, htyE and htyF) are embedded within the echinocandin B (ecd) and
CC       L-homotyrosine (hty) clusters (PubMed:22998630).
CC       {ECO:0000269|PubMed:22998630}.
CC   -!- PATHWAY: Antifungal biosynthesis. {ECO:0000305|PubMed:22998630}.
CC   -!- BIOTECHNOLOGY: Due to their effectiveness as antifungal agents,
CC       echinocandin derivatives can be used for the treatment of human
CC       invasive candidiasis (PubMed:22998630). {ECO:0000269|PubMed:22998630}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JX421684; AFT91381.1; -; Genomic_DNA.
DR   AlphaFoldDB; K0DZ91; -.
PE   1: Evidence at protein level;
FT   CHAIN           1..668
FT                   /note="Echinocandin B biosynthetic cluster protein J"
FT                   /id="PRO_0000443842"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          92..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          224..322
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          330..349
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          483..506
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        237..258
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        284..300
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        307..322
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   668 AA;  73817 MW;  F95738E457BAA39B CRC64;
     MHFAESVQTP PPSRPSDQSL NQHVLDLGSW DQGCRDLMLV NWLCVDFRQR LLNVLYTSCQ
     KNFNEARSLA RERLLDLVQR IASSDNLHGA LYTPPSLDSR SSATPPQNLP PTPDLVQCIR
     GCDEPFPPLS LPTPAQIDTQ ENERLMCTPE DITYHDRDSQ VVAQARRRSP PGTGPAVLPP
     IAFDNHELPP GCSDFLNFDL LSDGEVFSIG THAGVTSDVC DSMPLDHDLS EMELDPPPDA
     TTTTTTTTVS SPNVHSTHHL AIPNPEPGTP TPPSPLAGTS LTRKPPGTPD SPSAASQRRQ
     RQRRAAAHAT YRSTPSPCQS ADTHIGAENE VAEPAPPSPS TRWTHSIPTH LPSPDTVLAT
     FTHHLGRGKQ SIALLLTRLF YAIGSPDALS QLRDAVKLSR EQTPAIIPVS STNDLATTVK
     ALDHLDSMTT LSHILRRYYL VRLLEHRTRF EQDHVTAKQA WRPPKRMLKY DCARVELIKN
     GGNCSSSSCS SSASKKNEEK REPPLKYRSK SQALADLMQM LYPDLKPAVA EGKDCVYSRK
     LTKLRNRLSC ARNWYRFEQA FPGAILALIP CAGRFSVSID QIEKLPSDTV QIFLDYLQEH
     RGVFSRCVSQ TLGTGIFSVL ARTSADAAPT FAFEKVEEEG FGDLLYDTDE LVSLSIEYDR
     YCDLNSNA