ID R1G5F1_BOTPV Unreviewed; 441 AA.
AC R1G5F1;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Putative aspartic endopeptidase protein {ECO:0000313|EMBL:EOD46665.1};
GN ORFNames=UCRNP2_6603 {ECO:0000313|EMBL:EOD46665.1};
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:EOD46665.1, 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}.
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DR EMBL; KB916418; EOD46665.1; -; Genomic_DNA.
DR RefSeq; XP_007585865.1; XM_007585803.1.
DR AlphaFoldDB; R1G5F1; -.
DR MEROPS; A01.080; -.
DR KEGG; npa:UCRNP2_6603; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_0_2_1; -.
DR OMA; WYGGVQS; -.
DR OrthoDB; 2900143at2759; -.
DR Proteomes; UP000013521; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd06097; Aspergillopepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR034163; Aspergillopepsin-like_cat_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966:SF1; ASPARTYL PROTEINASE; 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; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000013521}.
FT DOMAIN 94..425
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 112
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 316
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 441 AA; 47089 MW; 73917F63D92D2A99 CRC64;
MATKSFTRIP IITNKHYKPV GLKSYAYCLH KYGIGPTKEG PYFVSNKIHQ QGKFGAQKAL
GGHARVQRHV LQKRVDAETS GEVPAEDIQN DALYLCEVGI GTPAQTLKLD FDTGSADLWV
WSTELPASTQ STGKSSGHAV FDPSKSSTYK EASGSTWQIQ YGDSSSASGS VGTDNVTLGG
LTVENQAVEL AKTLSDQFVQ GAGDGLLGLA WGSINTVKPT AVKTPVENMI DQADIPKDAE
LFTAYLGSTK DTNEADKGES FYTFGYIDQD VLKAAGVSEP YYVDVDNSQG FWQFQSTSAT
VNGKTVDRSG NTAIADTGTT LALVDDKTVE AIYAAIPGAK YDSANQGYIF PSSTTADQLP
VVTFAVGEKQ FTVQKEDLAF ADAGNGMVYG GIQSRGDMTF DILGDTFLKG IYAIFDQGNT
RFGAVQRTEK EQNVSVPSGS S
//
