FUS4_GIBF5
ID FUS4_GIBF5 Reviewed; 405 AA.
AC S0ELJ9;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Secreted aspartic protease FUS4 {ECO:0000303|PubMed:23932525};
DE EC=3.4.23.- {ECO:0000305};
DE AltName: Full=Fusarin biosynthesis protein 4 {ECO:0000303|PubMed:23932525};
DE Flags: Precursor;
GN Name=FUS4 {ECO:0000303|PubMed:23932525}; ORFNames=FFUJ_10055;
OS Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS and foot rot disease fungus) (Fusarium fujikuroi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=1279085;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831;
RX PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA Wiemann P., Sieber C.M.K., von Bargen K.W., Studt L., Niehaus E.-M.,
RA Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA Proctor R.H., Muensterkoetter M., Freitag M., Humpf H.-U., Gueldener U.,
RA Tudzynski B.;
RT "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT novel metabolites.";
RL PLoS Pathog. 9:E1003475-E1003475(2013).
RN [2]
RP INDUCTION.
RX PubMed=20572938; DOI=10.1111/j.1365-2958.2010.07263.x;
RA Wiemann P., Brown D.W., Kleigrewe K., Bok J.W., Keller N.P., Humpf H.U.,
RA Tudzynski B.;
RT "FfVel1 and FfLae1, components of a velvet-like complex in Fusarium
RT fujikuroi, affect differentiation, secondary metabolism and virulence.";
RL Mol. Microbiol. 77:972-994(2010).
RN [3]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23932525; DOI=10.1016/j.chembiol.2013.07.004;
RA Niehaus E.M., Kleigrewe K., Wiemann P., Studt L., Sieber C.M.,
RA Connolly L.R., Freitag M., Gueldener U., Tudzynski B., Humpf H.U.;
RT "Genetic manipulation of the Fusarium fujikuroi fusarin gene cluster yields
RT insight into the complex regulation and fusarin biosynthetic pathway.";
RL Chem. Biol. 20:1055-1066(2013).
CC -!- FUNCTION: Secreted aspartic protease; part of the gene cluster that
CC mediates the biosynthesis of the mycotoxin fusarin C (PubMed:23932525).
CC Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for
CC fusarin production (PubMed:23932525). The other FUS cluster members are
CC not essential for fusarin C biosynthesis (PubMed:23932525).
CC {ECO:0000269|PubMed:23932525}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:D4ATH2}.
CC -!- INDUCTION: Expressed under high amounts of nitrogen via regulation by
CC GLN1 (PubMed:23932525). Moreover, components of the fungal-specific
CC velvet complex VEL1, VEL2 and LAE1 act also as positive regulators of
CC expression (PubMed:20572938, PubMed:23932525). Finally, expression is
CC induced under acidic conditions in a PACC-independent manner
CC (PubMed:23932525). {ECO:0000269|PubMed:20572938,
CC ECO:0000269|PubMed:23932525}.
CC -!- DISRUPTION PHENOTYPE: Does not alter fusarin C production
CC (PubMed:23932525). {ECO:0000269|PubMed:23932525}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01103}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HF679031; CCT73263.1; -; Genomic_DNA.
DR AlphaFoldDB; S0ELJ9; -.
DR SMR; S0ELJ9; -.
DR EnsemblFungi; CCT73263; CCT73263; FFUJ_10055.
DR VEuPathDB; FungiDB:FFUJ_10055; -.
DR HOGENOM; CLU_039077_0_0_1; -.
DR Proteomes; UP000016800; 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 Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
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 2: Evidence at transcript level;
KW Aspartyl protease; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..405
FT /note="Secreted aspartic protease FUS4"
FT /id="PRO_5004496207"
FT DOMAIN 49..400
FT /note="Peptidase A1"
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 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 318..356
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
SQ SEQUENCE 405 AA; 44408 MW; A3331CDABB42FA55 CRC64;
MLAIATLHVA LQVFGAFSLS HAAAVTLEHR SAGNSNIAAI PAKWDVYGYL FNVTVGSPPQ
NITMLSDMTW MAPFVRSGRC LSQFNPELCV AQGQSFFNEH DSTTFGNTTF AQATWPVTAF
APNFTVDYGR DKFCIGNICN KDILMQVSDF PYPGSVVPVI PFGGIFGLAP TPKTITETSE
PVNFQAWKNG NMGPLVGWHT CEVLKSAASC QGGDAQLVFG GTDTTMYSAK KIQSYEIQNP
EWLSDAFYPS TPPRSNYWTV VDEGSEGLGA PLSLNGYKYL VRHIKSAKLA SKAIVQNIQQ
QGSSGYNTAN QDWYTVSCDG LDEFPNLVYQ LDGRKKYTIS PGDYVTKLTD MPGSVCYLNV
NVWKYGRTEN GDARVVLLGK AFLKRKYLVL NFEERSFGLA PLLTG
