ID M7SYK4_EUTLA Unreviewed; 414 AA.
AC M7SYK4;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE SubName: Full=Putative secreted aspartic proteinase protein {ECO:0000313|EMBL:EMR62646.1};
GN ORFNames=UCREL1_10416 {ECO:0000313|EMBL:EMR62646.1};
OS Eutypa lata (strain UCR-EL1) (Grapevine dieback disease fungus) (Eutypa
OS armeniacae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Diatrypaceae; Eutypa.
OX NCBI_TaxID=1287681 {ECO:0000313|EMBL:EMR62646.1, ECO:0000313|Proteomes:UP000012174};
RN [1] {ECO:0000313|Proteomes:UP000012174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-EL1 {ECO:0000313|Proteomes:UP000012174};
RX PubMed=23723393; DOI=10.1128/genomeA.00228-13;
RA Blanco-Ulate B., Rolshausen P.E., Cantu D.;
RT "Draft genome sequence of the grapevine dieback fungus Eutypa lata UCR-
RT EL1.";
RL Genome Announc. 1:E0022813-E0022813(2013).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; KB707407; EMR62646.1; -; Genomic_DNA.
DR RefSeq; XP_007798261.1; XM_007800070.1.
DR AlphaFoldDB; M7SYK4; -.
DR STRING; 1287681.M7SYK4; -.
DR KEGG; ela:UCREL1_10416; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_0_1_1; -.
DR OMA; KLNGYTW; -.
DR OrthoDB; 2900143at2759; -.
DR Proteomes; UP000012174; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000012174};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..414
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004085147"
FT DOMAIN 99..410
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 78..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 117
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 300
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 414 AA; 42948 MW; D8C63176E86BB45A CRC64;
MPSLSQTVLL ATAAFSSLGA GSPIAARENG HSFTVNQVRN VHYVRNGALA AAKAHRKFGK
AVPESVMTAL SLQNATLARR AGSEQGSAKT TPEPDDLEYL TPVSIGTPAQ TLNLDFDTGS
SDLWVFSSQL SKTLQTGHSV YTAASSSTSK KLSGATWDIS YGDGSGASGN VFTDKVTIGG
VEFDAQAVET ASKISEQFTE DTNNDGLVGL AFSSINTVTP TAQKTFFDNV KSSLSAPLFA
ADLKHDAPGS YDFGFTDTSK FTGDITYTSV DSSQGFWEFT ASGFKVGSAA HNTKLDGIAD
TGTTLLMLPD SVVKAYYGTV TGAQNSNSLG GWVFPCSADL PDFAYTVEGT DVVVPGDLIN
YAAASEDDPD TCYGGLQSSA GIGINIFGDV ALKASYVVFN GGATPKLGFA AKAT
//