ID A7ECZ2_SCLS1 Unreviewed; 402 AA.
AC A7ECZ2;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Aspartate protease {ECO:0000313|EMBL:EDO00708.1};
GN ORFNames=SS1G_03181 {ECO:0000313|EMBL:EDO00708.1};
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079 {ECO:0000313|EMBL:EDO00708.1, ECO:0000313|Proteomes:UP000001312};
RN [1] {ECO:0000313|Proteomes:UP000001312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
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, ECO:0000256|RuleBase:RU000454}.
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; CH476624; EDO00708.1; -; Genomic_DNA.
DR RefSeq; XP_001595093.1; XM_001595043.1.
DR AlphaFoldDB; A7ECZ2; -.
DR EnsemblFungi; EDO00708; EDO00708; SS1G_03181.
DR GeneID; 5491294; -.
DR KEGG; ssl:SS1G_03181; -.
DR VEuPathDB; FungiDB:sscle_07g058540; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_0_1_1; -.
DR InParanoid; A7ECZ2; -.
DR OMA; TKATFDW; -.
DR OrthoDB; 2900143at2759; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd06097; Aspergillopepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR034163; Aspergillopepsin-like_cat_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966:SF2; ASPERGILLOPEPSIN-1-RELATED; 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; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:EDO00708.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001312};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..402
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010252153"
FT DOMAIN 92..397
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 108
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 291
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 327..360
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 402 AA; 41650 MW; B8145C6C23A367AB CRC64;
MLSQITAFLA LGAIAHAAPA PVPATAATGA GAHSVPAIHN PNHVRNGTAA LLKAYAKYHI
QPTQPMSDAF MSALRKRQDS SVTATPADAA EYLIPVTVGG QTLNLDLDTG SADLWVFSSL
LSSSSRSGHD IYTSSKSSTY RSLSGYSWDI SYADGSGASG VVGTDTVTIG KTTVTGQAVE
LANQVSSEFV SDASDGLVGM AFSSINTVYP RSQSTFFDNA ISSLNSPLFA AYLPVNADGA
YDFGYTDSSK YTGSLTYTSV SSGNGFWEFP STSYKVGSAV HSSNGYTGIA DTGTTLILMS
DATNSAYYAQ VKGASYSNSY GGYVFPCSAT LPTLSFKIGN TYVTIPSELL NYGVASGNTC
YGALQSAGGG SQNIYGDVFF NAYYVVFDKS GPSLGFAPSV SA
//
