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
//