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Database: UniProt
Entry: R1GM42_BOTPV
LinkDB: R1GM42_BOTPV
Original site: R1GM42_BOTPV 
ID   R1GM42_BOTPV            Unreviewed;       401 AA.
AC   R1GM42;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   SubName: Full=Putative aspartic endopeptidase pep1 protein {ECO:0000313|EMBL:EOD47034.1};
GN   ORFNames=UCRNP2_6229 {ECO:0000313|EMBL:EOD47034.1};
OS   Botryosphaeria parva (strain UCR-NP2) (Grapevine canker fungus)
OS   (Neofusicoccum parvum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Neofusicoccum.
OX   NCBI_TaxID=1287680 {ECO:0000313|EMBL:EOD47034.1, ECO:0000313|Proteomes:UP000013521};
RN   [1] {ECO:0000313|Proteomes:UP000013521}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCR-NP2 {ECO:0000313|Proteomes:UP000013521};
RX   PubMed=23766404; DOI=10.1128/genomea.00339-13;
RA   Blanco-Ulate B., Rolshausen P., Cantu D.;
RT   "Draft genome sequence of Neofusicoccum parvum isolate UCR-NP2, a fungal
RT   vascular pathogen associated with grapevine cankers.";
RL   Genome Announc. 1:E0033913-E0033913(2013).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; KB916368; EOD47034.1; -; Genomic_DNA.
DR   RefSeq; XP_007585476.1; XM_007585414.1.
DR   AlphaFoldDB; R1GM42; -.
DR   KEGG; npa:UCRNP2_6229; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_013253_0_1_1; -.
DR   OMA; SHCRFCI; -.
DR   OrthoDB; 2900143at2759; -.
DR   Proteomes; UP000013521; 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};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW   Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013521};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..401
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004350925"
FT   DOMAIN          90..396
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        106
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        288
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        324..357
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   401 AA;  41788 MW;  C79BCAC055A76870 CRC64;
     MPSIWSITAL AALTGVTLAS PVDLASLEKR DTFSFNQVLR GTVRKNGPIQ MSKVYQKYKG
     TAPSDVKAAA AAAATGTVAA TPEDEYDSLY LCPVTVGGTE LELDFDTGSA DLWVFSTLMA
     SSEQTGHAVY NPSKSGTKKT GYTWDISYGD GSGASGTVYA DTVVVGGVTA TSQAVEAATS
     VSSAFTQDTD NDGLLGLAFS SINTVEPQSQ TTFFDTVGDS LAKKLFAVTL KKGEAGSYDF
     GYIDDSKYTG DIVYVDVDTS NGFWEFSPSG YAVGSGSVTT ASIDAIADTG TTLLYLPTAV
     VSAYYAKVSG SSYSSSYGGY VFPCSATLPD FTLVIGGEKR TVPGDYVNYA PATGSTCFGG
     IQRDTGIGFS IVGDIFLKSQ YVVFDASSDT PQLGWAQQAT S
//
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