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Database: UniProt
Entry: M7SYK4_EUTLA
LinkDB: M7SYK4_EUTLA
Original site: M7SYK4_EUTLA 
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
//
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