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Database: UniProt
Entry: M7T0M7_EUTLA
LinkDB: M7T0M7_EUTLA
Original site: M7T0M7_EUTLA 
ID   M7T0M7_EUTLA            Unreviewed;       469 AA.
AC   M7T0M7;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   SubName: Full=Putative aspartic-type endopeptidase protein {ECO:0000313|EMBL:EMR72464.1};
GN   ORFNames=UCREL1_491 {ECO:0000313|EMBL:EMR72464.1};
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:EMR72464.1, 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}.
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DR   EMBL; KB705455; EMR72464.1; -; Genomic_DNA.
DR   RefSeq; XP_007788451.1; XM_007790260.1.
DR   AlphaFoldDB; M7T0M7; -.
DR   KEGG; ela:UCREL1_491; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_582693_0_0_1; -.
DR   OMA; GAYMELP; -.
DR   OrthoDB; 615305at2759; -.
DR   Proteomes; UP000012174; 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   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
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:SF73; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000012174};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        351..374
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..260
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          322..348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   469 AA;  49030 MW;  57CED9C5190A2E54 CRC64;
     MTDFSTLAVP GTTGIWFTDL LNVGDLSEVN LTMGLAYELV NPWGVLGLQF KPPASNESVW
     GVMTQLVYQG AGVTNAYSLS LGDVDASNGS ILFGAIDTER YTGDLLSLDC YYTGGDDYRT
     VVTLASVQAN SSSGLDTLAG GLPVSTGIWV GRPALNVPSE LAFNMWEVAG AEYWSDLGAP
     TVPCSMKESE GSFTFRLASD EGPAVSVPMR SLVAPPSGLG DNCLFLVYNE TNPRNYYLGE
     AFLQNVYAVF DLANMKFAVA TPNPESTATN IVAFAGVSAP IPSTVAVSSQ LTRAVSTTGS
     VTELPTTTGS FSAAAGFQST SATSGITAAD TPTGESTSEQ DESNGTTNTT AIGVGVGVGV
     GGAALVAIGV VFFLMRRRSQ KAAEPTYDSS ATVGSPANGY PAPEPVKYFT ELEPQNGLAE
     LPPDGRPVEM SGTPYQQYQG GGAYMELPAS DMTYYPNQAT HDVNAWNQR
//
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