ID A7EJ36_SCLS1 Unreviewed; 433 AA.
AC A7EJ36;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 24-JAN-2024, entry version 76.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=SS1G_05329 {ECO:0000313|EMBL:EDO02852.1};
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:EDO02852.1, 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}.
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DR EMBL; CH476626; EDO02852.1; -; Genomic_DNA.
DR RefSeq; XP_001593901.1; XM_001593851.1.
DR AlphaFoldDB; A7EJ36; -.
DR MEROPS; A01.080; -.
DR EnsemblFungi; EDO02852; EDO02852; SS1G_05329.
DR GeneID; 5490065; -.
DR KEGG; ssl:SS1G_05329; -.
DR VEuPathDB; FungiDB:sscle_08g065930; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_0_2_1; -.
DR InParanoid; A7EJ36; -.
DR OMA; WYGGVQS; -.
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; 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:UP000001312}.
FT DOMAIN 93..419
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 59..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 111
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 310
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 433 AA; 46909 MW; 7D0A43B2295E1801 CRC64;
MATLQGLSRV RLVPNKNYKR SGIKSYVYLL NKWGFEPTLP GPYFQMNKAT EREATYHKFG
HKSHHHKRHL AKKTPTGENG EVPAQDQQND SEYLCPVQIG TPAQTLMLDF DTGSSDLWVW
STELPKSTTS KATGHTIFDP TKSSTFKASK SSKWQISYGD SSSASGTVGT DTVTIGGLAI
KNQAVELATK LSAQFEDGAG DGLLGLAWGS INTVTPEPVA TPVMNMITQE DIPKDAELFT
VNLGSWRDAE DPDKGESFYT FGYIDKDIVG SQEISYTPID NSQGFWMFDS TSATVNGKTI
TQDKNQAIAD TGTTLALVSD ETCQAIYDAI PGSTYDQTQQ GYTFPSSTSA DDLPVVTFAV
GGKQFAVQKE DLGFADAGNG MVYGGIQSRG SMTFDILGDT FLKGIYAIFD QGNVRFGAVQ
RNEPTQNTSA PPS
//
