ID S0E829_GIBF5 Unreviewed; 262 AA.
AC S0E829;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Probable alkaline protease (Oryzin) {ECO:0000313|EMBL:CCT70815.1};
GN ORFNames=FFUJ_06651 {ECO:0000313|EMBL:CCT70815.1};
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 {ECO:0000313|EMBL:CCT70815.1, ECO:0000313|Proteomes:UP000016800};
RN [1] {ECO:0000313|Proteomes:UP000016800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831
RC {ECO:0000313|Proteomes:UP000016800};
RX PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA Wiemann P., Sieber C.M., 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., Munsterkotter M., Freitag M., Humpf H.U., Guldener 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).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; HF679028; CCT70815.1; -; Genomic_DNA.
DR AlphaFoldDB; S0E829; -.
DR STRING; 1279085.S0E829; -.
DR EnsemblFungi; CCT70815; CCT70815; FFUJ_06651.
DR VEuPathDB; FungiDB:FFUJ_06651; -.
DR HOGENOM; CLU_1061912_0_0_1; -.
DR OrthoDB; 2608868at2759; -.
DR Proteomes; UP000016800; Chromosome 6.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:CCT70815.1};
KW Protease {ECO:0000313|EMBL:CCT70815.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000016800}.
FT DOMAIN 81..230
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 223..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 262 AA; 28105 MW; 6CDEA644622D1CC2 CRC64;
MQSTDIEKDT LFNHATRYLH ATNDNPPQCH SNAADGSGAY ISHMLDSLAE LFTEQNSSQG
QQITTNWAMA PRLQELLGGT TRGVAEDCTM ILVKVVNKLG VNKIGWLCQA ILRAPDHSIA
KDIVDKIVMN ISLGGEYTTV INTAVKKATN SGITLVVSAG NSGVSAVIYS PASAVTAITV
AANSPDNRRA PFSNYGPCVN IFAPGVGITS TLISVKQESR RYSGTSSATA GLERLQGREE
ASSIRREFER SNKRFSLEQQ SP
//
