ID   ELCF_PHANO              Reviewed;         312 AA.
AC   Q0UHZ9;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Fasciclin-like arabinogalactan protein elcF {ECO:0000303|PubMed:28251756};
DE   AltName: Full=Elsinochrome C biosynthesis cluster protein F {ECO:0000303|PubMed:28251756};
DE   Flags: Precursor;
GN   Name=elcF {ECO:0000303|PubMed:28251756}; ORFNames=SNOG_08615;
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA   Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA   Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
RN   [2]
RP   INDUCTION, FUNCTION, AND PATHWAY.
RX   PubMed=28251756; DOI=10.1111/1462-2920.13711;
RA   Chooi Y.H., Zhang G., Hu J., Muria-Gonzalez M.J., Tran P.N., Pettitt A.,
RA   Maier A.G., Barrow R.A., Solomon P.S.;
RT   "Functional genomics-guided discovery of a light-activated phytotoxin in
RT   the wheat pathogen Parastagonospora nodorum via pathway activation.";
RL   Environ. Microbiol. 19:1975-1986(2017).
RN   [3]
RP   FUNCTION, AND PATHWAY.
RX   PubMed=30809363; DOI=10.1039/c8sc02870b;
RA   Hu J., Sarrami F., Li H., Zhang G., Stubbs K.A., Lacey E., Stewart S.G.,
RA   Karton A., Piggott A.M., Chooi Y.H.;
RT   "Heterologous biosynthesis of elsinochrome A sheds light on the formation
RT   of the photosensitive perylenequinone system.";
RL   Chem. Sci. 10:1457-1465(2019).
CC   -!- FUNCTION: Fasciclin-like arabinogalactan protein; part of the gene
CC       cluster that mediates the biosynthesis of elsinochrome C, a
CC       perelyenequinone phytotoxin structurally similar to cercosporin
CC       (PubMed:28251756, PubMed:30809363). The first step of elsinochrome C
CC       biosynthesis is performed by the polyketide synthase elcA which
CC       catalyzes the formation of nor-toralactone (PubMed:28251756,
CC       PubMed:30809363). The starter unit acyltransferase (SAT) domain of elcA
CC       initiates polyketide extension by the selective utilization of acetyl-
CC       CoA, which is elongated to the heptaketide in the beta-ketoacyl
CC       synthase (KS) domain by successive condensations with six malonyl units
CC       introduced by the malonyl acyltransferase (MAT) domain (By similarity).
CC       The product template (PT) domain catalyzes C4-C9 and C2-C11 aldol
CC       cyclizations and dehydrations to a trihydroxynaphthalene, which is
CC       thought to be delivered to the thioesterase (TE) domain for product
CC       release (By similarity). The bifunctional enzyme elcB then methylates
CC       nor-toralactone to toralactone before conducting an unusual oxidative
CC       aromatic ring opening (PubMed:28251756, PubMed:30809363). The next step
CC       in perylenequinone biosynthesis is an O-methylation at the nascent OH-6
CC       of the elcB product performed by the O-methyltransferase elcD
CC       (PubMed:30809363). The oxidative coupling of the two monomeric naphthol
CC       units in perylenequinone biosynthesis is catalyzed by the FAD-dependent
CC       monooxygenase elcE and the multicopper oxidase elcG (PubMed:30809363).
CC       ElcG might catalyze the first intermolecular coupling in a regio- and
CC       stereo-selective manner via a phenol radical coupling mechanism and the
CC       elcE could forge the second C-C bond intramolecularly via a hydride
CC       transfer mechanism (PubMed:30809363). The fasciclin domain-containing
CC       protein elcF might also play a role duting this step (Probable). The
CC       last piece of the puzzle in the biosynthesis of elsinochrome C is the
CC       additional annulation by enolate coupling to afford the
CC       dihydrobenzo(ghi)perylenequinone system, catalyzed by the FAD-dependent
CC       monooxygenase elcH (PubMed:30809363). {ECO:0000250|UniProtKB:Q6DQW3,
CC       ECO:0000269|PubMed:28251756, ECO:0000269|PubMed:30809363,
CC       ECO:0000305|PubMed:30809363}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:28251756, ECO:0000269|PubMed:30809363}.
CC   -!- INDUCTION: Expression is up-regulated during the late stage of
CC       P.nodorum wheat leaf infection and is controlled by the cluster
CC       specific transporter elcR. {ECO:0000269|PubMed:28251756}.
CC   -!- SIMILARITY: Belongs to the fasciclin-like AGP family. {ECO:0000305}.
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DR   EMBL; CH445337; EAT83783.1; -; Genomic_DNA.
DR   RefSeq; XP_001798924.1; XM_001798872.1.
DR   AlphaFoldDB; Q0UHZ9; -.
DR   SMR; Q0UHZ9; -.
DR   STRING; 321614.Q0UHZ9; -.
DR   EnsemblFungi; SNOT_08615; SNOT_08615; SNOG_08615.
DR   GeneID; 5975823; -.
DR   KEGG; pno:SNOG_08615; -.
DR   eggNOG; KOG1437; Eukaryota.
DR   HOGENOM; CLU_031281_2_0_1; -.
DR   InParanoid; Q0UHZ9; -.
DR   OMA; RVECGIQ; -.
DR   OrthoDB; 984651at2759; -.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IBA:GO_Central.
DR   GO; GO:0016236; P:macroautophagy; IBA:GO_Central.
DR   Gene3D; 2.30.180.10; -; 2.
DR   InterPro; IPR036378; FAS1_dom_sf.
DR   InterPro; IPR000782; FAS1_domain.
DR   Pfam; PF02469; Fasciclin; 2.
DR   SMART; SM00554; FAS1; 2.
DR   SUPFAM; SSF82153; SSF82153; 2.
DR   PROSITE; PS50213; FAS1; 2.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Reference proteome; Repeat; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..312
FT                   /note="Fasciclin-like arabinogalactan protein elcF"
FT                   /id="PRO_5004178039"
FT   DOMAIN          17..160
FT                   /note="FAS1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT   DOMAIN          162..289
FT                   /note="FAS1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT   CARBOHYD        48
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        68
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        113
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        157
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        165
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   312 AA;  33643 MW;  3541875D26FAA739 CRC64;
     MKLFTLLLPA LTSAHSLSTL LSTHPTLSTL HSLLKQFSLL DDFNTLANIT VIAPTNQAYL
     DLANWGFNVS QIPAPVARAL FQYHVLDGEW ESESIIGKGK VVHTYLKPPV LTNVTAGAAV
     KLSSVDGTIM TESGLGVAGG VEDVNLRFDG GVLHTLNASM VLPHNITLTA QINGLGRFLE
     LMNRAGVVAE FEGLKDVTVF VPHDDALEKA DVGKMSKEQL ASLLRGHVVP NRVLYGEVFG
     KKGGYKSSNG WEIHVGKTAD GTLTVNGIKV VKEDVILYAG VAHVIDKVLV ADRVEHKGDR
     SYLHLDAQKP LR