ID A0A0G2DYM8_9PEZI Unreviewed; 475 AA.
AC A0A0G2DYM8;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 22-FEB-2023, entry version 33.
DE SubName: Full=Putative peptidase a1 {ECO:0000313|EMBL:KKY15684.1};
GN ORFNames=UCDDS831_g07528 {ECO:0000313|EMBL:KKY15684.1};
OS Diplodia seriata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Diplodia.
OX NCBI_TaxID=420778 {ECO:0000313|EMBL:KKY15684.1, ECO:0000313|Proteomes:UP000034182};
RN [1] {ECO:0000313|EMBL:KKY15684.1, ECO:0000313|Proteomes:UP000034182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS831 {ECO:0000313|EMBL:KKY15684.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY15684.1, ECO:0000313|Proteomes:UP000034182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS831 {ECO:0000313|EMBL:KKY15684.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKY15684.1}.
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DR EMBL; LAQI01000186; KKY15684.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2DYM8; -.
DR Proteomes; UP000034182; 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; 1.
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}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..475
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002543288"
FT DOMAIN 162..467
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 96..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 475 AA; 49809 MW; 130496B6B330AEAA CRC64;
MHTSTALIAA LAAIWFPQAE ANPIEARQNV GFSLQQQPYG KRLVNGPIAL GNLYKKVERD
MPEEVSAAFA VATESQAPDM VNKIKRAVST TSAAAAAATA GKPKPSSSTS SSSIKTTSSS
TTSSSIKTTS TSSSTSSKTS STSTKQSGSA VATPVNEFDT AYMIPIKVGG TTVYVDLDTG
SSDLWVLSSL QPTTQTSGHN VYKPASSNLK QGYSWNVTYL DGSTAGGLVY NDTVGLGNMN
FPGQAVEAAS SASDAFVEAA YDGMLGLAFD PLNTVKPVQQ KTLFNSIKSQ LPSPLFTSFL
KHNAPGSFDF GYIDSSKYTG SITYANVDTS NGWWQFNAGG YSIGSGAAVS TTFAAVVDTG
TTLMVLPGTI VNAYYAKVAG SSYWSDYGAW VYPCSATLPN LNLIVNNVAQ TIPGSLMTYG
PIDYNGNCYG GLQSSDNIGI AILGTIFIKS QFVVYDQSTT PPRVGFAKQK GLSYN
//