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STTD_ASPTE
ID   STTD_ASPTE              Reviewed;         320 AA.
AC   P9WEV5;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   12-AUG-2020, sequence version 1.
DT   03-AUG-2022, entry version 7.
DE   RecName: Full=Uncharacterized ophiobolin family sesterterpenoid biosynthesis cluster protein {ECO:0000303|PubMed:28604695};
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: Part of the gene cluster that mediates the biosynthesis of an
CC       ophiobolin family sesterterpenoid. {ECO:0000269|PubMed:28604695}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000305|PubMed:28604695}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
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DR   EMBL; KX449366; AQM58279.1; -; Genomic_DNA.
DR   AlphaFoldDB; P9WEV5; -.
DR   VEuPathDB; FungiDB:ATEG_03566; -.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR033481; Dni1/Fig1.
DR   Pfam; PF12351; Fig1; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN           1..320
FT                   /note="Uncharacterized ophiobolin family sesterterpenoid
FT                   biosynthesis cluster protein"
FT                   /id="PRO_0000450611"
FT   TRANSMEM        51..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        186..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        216..236
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        272..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..31
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        92
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        122
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        154
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        167
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        247
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   320 AA;  34422 MW;  724D5DB36E2E498A CRC64;
     MDHPSTSSLP RKKVKAGVKK AGKKTGKKTT GKKKTTPSAI GNRKGKGAAC LLVLLAVLSY
     LAALSLGLYI MTGCISTTAQ SNNIYLAELS TNTTYDMSLR VGYFGGCVSV TELTEAPYTG
     RNSSTQTSTH CVSNLRRKNL DDLSEDLWEP LKLNSSTIQS SLQTFFNTTL PQAKHLQENV
     FFCEPPLVHL LLFFVTGIML FVAMTGTSRK RSYRAMLVTA IALSAFSLAL ALVTVLGSLQ
     SMNALLNTSA SGAQRALGDS LYISRGKAML GVQGALVAIV AVFYLTMGVV FVRRTPEGGA
     GYIIQAFQNV RGPLKRMGRR
 
 
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