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
//