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STTC_ASPTE
ID   STTC_ASPTE              Reviewed;         299 AA.
AC   P9WEV4;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   12-AUG-2020, sequence version 1.
DT   25-MAY-2022, entry version 4.
DE   RecName: Full=Ophiobolin family sesterterpenoid biosynthesis cluster acetyltransferase {ECO:0000303|PubMed:28604695};
DE            EC=2.3.1.- {ECO:0000305|PubMed:28604695};
DE   Flags: Precursor;
OS   Aspergillus terreus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=33178;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC   STRAIN=ATCC 20542 / MF4845;
RX   PubMed=28604695; DOI=10.1038/nchembio.2408;
RA   Clevenger K.D., Bok J.W., Ye R., Miley G.P., Verdan M.H., Velk T., Chen C.,
RA   Yang K., Robey M.T., Gao P., Lamprecht M., Thomas P.M., Islam M.N.,
RA   Palmer J.M., Wu C.C., Keller N.P., Kelleher N.L.;
RT   "A scalable platform to identify fungal secondary metabolites and their
RT   gene clusters.";
RL   Nat. Chem. Biol. 13:895-901(2017).
CC   -!- FUNCTION: Acetyltransferase; part of the gene cluster that mediates the
CC       biosynthesis of an ophiobolin family sesterterpenoid.
CC       {ECO:0000269|PubMed:28604695}.
CC   -!- FUNCTION: Sesterterpenoid synthase; part of the gene cluster that
CC       mediates the biosynthesis of an ophiobolin family sesterterpenoid.
CC       {ECO:0000269|PubMed:28604695}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000305|PubMed:28604695}.
CC   -!- SIMILARITY: Belongs to the bfoA family. {ECO:0000305}.
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DR   EMBL; KX449366; AQM58280.1; -; Genomic_DNA.
DR   AlphaFoldDB; P9WEV4; -.
DR   VEuPathDB; FungiDB:ATEG_03569; -.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
PE   3: Inferred from homology;
KW   Acyltransferase; Glycoprotein; Signal; Transferase.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..299
FT                   /note="Ophiobolin family sesterterpenoid biosynthesis
FT                   cluster acetyltransferase"
FT                   /id="PRO_0000450610"
FT   CARBOHYD        28
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        58
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        77
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        126
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        177
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        212
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        282
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   299 AA;  33650 MW;  5FC7C13C5F4EFC3B CRC64;
     MYFFRALLSP VVLWPALVSG KSNSNTANYT VEELWDLEVT FWDNFLYPAN VKQVEAINST
     LFTTEVQGRV DITRVFNGSE LNTEYIFGLF SDPNHLSLVG VPIAYSITQF IAERNIASAT
     TVVTFNATSF GNLLLPVTID TWIMWDANGR IMQYDATFRW FGFLLDTLVE ALATSINGTA
     SQATAALTQL LATTVCDTHD KYCTGENQQY DNSTACYDFL TTAIPLGKDY ELGRDTLLCR
     EVHEHMVQYD PKMHCPHIGP TGGDYCVNDQ TYEQKVLQKY FNVSWIVGVP WTGNIWLGD
 
 
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