ID FUS4_GIBM7 Reviewed; 439 AA.
AC W7MX26;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Secreted aspartic protease FUS4 {ECO:0000303|PubMed:22652150};
DE EC=3.4.23.- {ECO:0000305};
DE AltName: Full=Fusarin biosynthesis protein 4 {ECO:0000303|PubMed:22652150};
DE Flags: Precursor;
GN Name=FUS4 {ECO:0000303|PubMed:22652150}; ORFNames=FVEG_11083;
OS Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot
OS fungus) (Fusarium verticillioides).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=334819;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M3125 / FGSC 7600;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [2]
RP FUNCTION.
RX PubMed=22652150; DOI=10.1016/j.fgb.2012.05.010;
RA Brown D.W., Butchko R.A., Busman M., Proctor R.H.;
RT "Identification of gene clusters associated with fusaric acid, fusarin, and
RT perithecial pigment production in Fusarium verticillioides.";
RL Fungal Genet. Biol. 49:521-532(2012).
CC -!- FUNCTION: Secreted aspartic protease; part of the gene cluster that
CC mediates the biosynthesis of the mycotoxin fusarin C (PubMed:22652150).
CC Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for
CC fusarin production (By similarity). The other FUS cluster members are
CC not essential for fusarin C biosynthesis (By similarity).
CC {ECO:0000250|UniProtKB:S0ELJ9, ECO:0000269|PubMed:22652150}.
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; DS022257; EWG52305.1; -; Genomic_DNA.
DR RefSeq; XP_018758496.1; XM_018900246.1.
DR AlphaFoldDB; W7MX26; -.
DR SMR; W7MX26; -.
DR GlyCosmos; W7MX26; 5 sites, No reported glycans.
DR EnsemblFungi; FVEG_11083T0; FVEG_11083T0; FVEG_11083.
DR GeneID; 30068619; -.
DR KEGG; fvr:FVEG_11083; -.
DR VEuPathDB; FungiDB:FVEG_11083; -.
DR eggNOG; ENOG502SJHI; Eukaryota.
DR HOGENOM; CLU_039077_0_0_1; -.
DR OMA; FVDWTWI; -.
DR OrthoDB; 2342359at2759; -.
DR Proteomes; UP000009096; Chromosome 9.
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; Acid Proteases; 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; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF51; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..439
FT /note="Secreted aspartic protease FUS4"
FT /id="PRO_5004896697"
FT DOMAIN 49..434
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 67
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 296
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 352..390
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
SQ SEQUENCE 439 AA; 48222 MW; 00F0C537E6CFFD02 CRC64;
MLTIATLHVA LQVFGAFSPS HAAAVTLEHR SARDGNSVAV PANWDVYGYL FNVTVGSPPQ
NITMLSDMTW MAPFVRSGRC LGQFNPELCV AQGQSFFNEH NSTTFANTTF AQATWPVTAF
APNFTVDYGR DKFCIGEICN KDTLMQVSDF PYPGSVVPVI PFGGIFGLAP TPEAITATSE
PVNFQAWKNG KMGPLVGWHT CEVLKSAATC QGGDAQLVFG GTDTTMYSAK KLQSYEIQNP
EWLSDAFYPS TPPRSNYWST SLTGMWIRTD KLSKNYAVPF KAVKTAKRTP PLAVVDEGSE
GLGAPLSLNG YKYLVRHIKS AKLASKAIVQ NIQQQGSSGY NTADQDWYTV ACDGLHEYPD
LVYQLDGRKK YTISAGDYVT KLTDMPGSVC YLNINVWKYG RTENGDARVV LLGRAFLKRK
YLVLNFEDRS FGLAPLRTG
//
