ID G2XVL6_BOTF4 Unreviewed; 432 AA.
AC G2XVL6;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 22-FEB-2023, entry version 50.
DE SubName: Full=Similar to aspartic endopeptidase {ECO:0000313|EMBL:CCD44536.1};
GN ORFNames=BofuT4P50000006001 {ECO:0000313|EMBL:CCD44536.1};
OS Botryotinia fuckeliana (strain T4) (Noble rot fungus) (Botrytis cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=999810 {ECO:0000313|EMBL:CCD44536.1, ECO:0000313|Proteomes:UP000008177};
RN [1] {ECO:0000313|Proteomes:UP000008177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T4 {ECO:0000313|Proteomes:UP000008177};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447}.
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DR EMBL; FQ790271; CCD44536.1; -; Genomic_DNA.
DR AlphaFoldDB; G2XVL6; -.
DR SMR; G2XVL6; -.
DR STRING; 999810.G2XVL6; -.
DR MEROPS; A01.080; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_0_2_1; -.
DR InParanoid; G2XVL6; -.
DR Proteomes; UP000008177; Unplaced contigs.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd06097; Aspergillopepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR034163; Aspergillopepsin-like_cat_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966:SF1; ASPARTYL PROTEINASE; 1.
DR PANTHER; PTHR47966; 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 Reference proteome {ECO:0000313|Proteomes:UP000008177}.
FT DOMAIN 92..418
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 110
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 309
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 432 AA; 46142 MW; 84BD19DBC6D72619 CRC64;
MASLQGLSKI RLIPNKNYKR SGTKSYVYLL NKWGFEPTKP GPYFQMNKAT ATSASFHKFG
HKSQTQRVLA KKTATGENGE VPAEDQQNDS EYLCPVQIGT PAQTLMLDFD TGSSDLWVWS
TELPKATTSN ATGHTIFDPK KSSTFKAAKS SKWQISYGDS SSASGTVGTD TVSLGGLAIK
NQAVELATKL SAQFEQGAGD GLLGLAWGSI NTVTPTPVAT PVENMISQED IPSDAELFTV
NLGSWRDADE ADKGASFYTF GYIDQDVVGS QEIYYTPVDN SQGFWMFDST SATVNGKTVA
QTGNQAIADT GTTLALVSDE TCQAIYDAIP GSTYDSEQQG YTFPSNTSAD DLPVVTFAVG
GKQFAVQKED LGFADAGNGM VYGGIQSRGS MTFDILGDTF LKGIYAIFDQ GNTRFGAVQR
TEATQNTAAP PA
//