ID M7U4J4_BOTF1 Unreviewed; 845 AA.
AC M7U4J4;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Putative peptidase a1 protein {ECO:0000313|EMBL:EMR88554.1};
GN ORFNames=BcDW1_2892 {ECO:0000313|EMBL:EMR88554.1};
OS Botryotinia fuckeliana (strain BcDW1) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=1290391 {ECO:0000313|EMBL:EMR88554.1, ECO:0000313|Proteomes:UP000012045};
RN [1] {ECO:0000313|Proteomes:UP000012045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BcDW1 {ECO:0000313|Proteomes:UP000012045};
RX PubMed=23704180; DOI=10.1128/genomea.00252-13;
RA Blanco-Ulate B., Allen G., Powell A.L., Cantu D.;
RT "Draft genome sequence of Botrytis cinerea BcDW1, inoculum for noble rot of
RT grape berries.";
RL Genome Announc. 1:E0025213-E0025213(2013).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447}.
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DR EMBL; KB707785; EMR88554.1; -; Genomic_DNA.
DR AlphaFoldDB; M7U4J4; -.
DR STRING; 1290391.M7U4J4; -.
DR HOGENOM; CLU_009988_0_0_1; -.
DR Proteomes; UP000012045; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR034164; Pepsin-like_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF89; SACCHAROPEPSIN; 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 Membrane {ECO:0000256|SAM:Phobius}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..845
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004086347"
FT TRANSMEM 439..462
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 50..403
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 489..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..845
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 845 AA; 91124 MW; AEC9F5CE7EAC06F6 CRC64;
MSSWRYLAFF LLPILGLLEQ TLASATSATP VPPLTVLPSG NWNGIDGNWS SFWLTVGTPP
QPVLVFISTA SNQPWVVSPD GCSPSDPGTC YSSRGLNFNS NSSATWVPNT INPGGEFALE
VESSLGLTGN GDYGNDTILL GSPGSGSPSL SSQVLATIAT HDFWLGLFGL NPAPTNFSSK
TEPAPSYMSN LKSQGHIPSL SYGYTAGAYY RNGGGANGGG VLGNLTLGGY EESLFVPNNL
TVDFATSGDD LTIDVNAITV KSPGGTSQVV SSPSSSFPAF IDSSVPYLYL PTSICQKFEE
AIGISYDSES ELYLLTDAQH TALVNRNASV VFTLTNSTSK AMVNITLPYA AFDWWAEYPL
VQNSTRYFPL KRATDNSQIT LGRAFLQEAY LIADYERSQF SIHQRNWTTF YPTSNPTTIF
PLNNPAPLSS SKSKISTPVI AAIVLAILTS IALTLCLTIF ILHRVHQRKQ TPGRSNTVST
FASTSRSLSK KESFRSAPSS PLPLPFISSK DKSDKKSKHV SNAPSELSFF DKGTNSVLLT
PSNRSLVSLN IGKAIGSPNL TLNPQYNNSG VSISRNPSQS NAADTVLNKN LNLVPTEPKP
AFHLASLSTR RKERKKKRKE KAQEIYELSG GSDALCWAEM DEMDEELEEM DMDSRASSPA
LSALSFASDA ALITSNPEKP KPWMDNDREI RGSGSIMNMG MNRDSGMERM NRMDKEAEAY
RERSGGHSHP GTGNDTVTTN NSRGRESHFT NTTMGLDTPT DGVGTGGTWE FEKYLDASRL
PWVQRGSGLG VVVEPPSPVA QPVAAMPALR EGAQAPGKKV EIVNDSMKSS GQKRESEKGV
IWGRF
//