ID R1ESA5_BOTPV Unreviewed; 409 AA.
AC R1ESA5;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Putative a chain endothiapepsin {ECO:0000313|EMBL:EOD50683.1};
GN ORFNames=UCRNP2_2534 {ECO:0000313|EMBL:EOD50683.1};
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:EOD50683.1, 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; KB915940; EOD50683.1; -; Genomic_DNA.
DR RefSeq; XP_007581841.1; XM_007581779.1.
DR AlphaFoldDB; R1ESA5; -.
DR MEROPS; A01.017; -.
DR KEGG; npa:UCRNP2_2534; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_0_1_1; -.
DR OMA; TKATFDW; -.
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}; 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..409
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004348935"
FT DOMAIN 97..405
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 115
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 299
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 409 AA; 42563 MW; 4C97287827E88E15 CRC64;
MPSLSQVAIA TLLATAGSAS VIPPRIGVPT EGTASLVQVR NTKHVKSGPY ALAKAYRKYG
VPISEDLQAA VNNATGSTFK RATGSATTTP TQYDSEYLTP VSIGTPAQVL NLDFDTGSSD
LWVFSSETPS NEVSGQTQYN PSKSSTASKL SGATWKISYG DGSSSSGDVY KDKVTVGGLT
VTSQAVELAK TVSDEFTEDT DNDGLLGLAF SSLNTVSPTQ QKTFFDNAKS SLTSPLFTAD
LKHNAAGKYN FGYIDSSAYT GSITYASIST AQGWWQWTSS GYAVGSATFK STSINGIADT
GTTLLLLPDS VVSAYYAKVS GSSYSSSQGG YVFPCSATLP SFTFGVGSAR ITIPGTYMNY
APVTSSSCYG GIQSNSDIGF TIFGDIALKA AFVVFNGGTN QIGWASKSV
//
