ID   LUC8_FUSSX              Reviewed;         439 AA.
AC   A0A6J4B484;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   07-OCT-2020, sequence version 1.
DT   03-AUG-2022, entry version 5.
DE   RecName: Full=Secreted aspartic protease LUC8 {ECO:0000303|PubMed:32043422};
DE            EC=3.4.23.- {ECO:0000250|UniProtKB:D4ATH2};
DE   AltName: Full=Lucilactaene biosynthesis cluster protein 8 {ECO:0000303|PubMed:32043422};
DE   Flags: Precursor;
GN   Name=LUC8 {ECO:0000303|PubMed:32043422};
OS   Fusarium sp.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=29916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC   STRAIN=RK97-94;
RX   PubMed=32043422; DOI=10.1080/09168451.2020.1725419;
RA   Kato S., Motoyama T., Futamura Y., Uramoto M., Nogawa T., Hayashi T.,
RA   Hirota H., Tanaka A., Takahashi-Ando N., Kamakura T., Osada H.;
RT   "Biosynthetic gene cluster identification and biological activity of
RT   lucilactaene from Fusarium sp. RK97-94.";
RL   Biosci. Biotechnol. Biochem. 84:1303-1307(2020).
CC   -!- FUNCTION: Secreted aspartic protease; part of the gene cluster that
CC       mediates the biosynthesis of the mycotoxin lucilactaene and the
CC       lucilactaene-related compound NG-391 that act as cell cycle inhibitors
CC       with potent growth inhibitory activity against malarial parasites,
CC       moderate growth inhibitory activity against cancer cells, and no
CC       activity against bacteria and fungi (PubMed:32043422). Within the
CC       cluster, LUC5, LUC6, LUC2 and LUC1 are sufficient for lucilactaene
CC       production (Probable). The roles of the other LUC members are yet
CC       undetermined (Probable). {ECO:0000269|PubMed:32043422,
CC       ECO:0000305|PubMed:32043422}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:D4ATH2}.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01103}.
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DR   EMBL; LC515193; BBQ09584.1; -; Genomic_DNA.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05471; pepsin_like; 1.
DR   Gene3D; 2.40.70.10; -; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR034164; Pepsin-like_dom.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966; PTHR47966; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; SSF50630; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW   Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..439
FT                   /note="Secreted aspartic protease LUC8"
FT                   /id="PRO_5026878452"
FT   DOMAIN          51..435
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        69
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        300
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   CARBOHYD        33
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        54
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        110
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        179
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        289
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        329
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        373
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        355..391
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
SQ   SEQUENCE   439 AA;  47779 MW;  9D4AB37273B8E0BF CRC64;
     MMHAFHHLAV LLIGSLPASA STLPHPDGYR HVNGSCSKSV AVPAVWNGFG YLFNITVGTP
     PQELTMLSDW TWMSLFVRSG RCLNQYDPSL CLGTSGQTWF DERASTSFAN TSLPQLSWPL
     TAFAPNFTVD YGTDDVCIGD LCSAGTVLQV SDFPYPGEGI PKVPFSGIFG MAPVTAGLNE
     TFHPANYQAW KAGRLGSRVG WNSCAALASS DPCLGGEAKL VFGGTDSSLY DDDTLRIYEI
     QNPDWLSDAF YPLTPPRENY WTTPLTGSWI LGTSEEESRN FAVPFSGSNG SNVTPLAVLD
     EGSEGLGAPL SLNAYNWLVD QVRGTLASND TIEEIHAQGS SGFNTAEQNW YTVSCDDIDS
     YPELVYELNG HTNYTVPPQD YVTKLSDSST CYLNINLWKY GRTEDGNAKV ALLGLAFLKR
     LYVVLDFETQ SFGLAPLSM