ID R1GD85_BOTPV Unreviewed; 476 AA.
AC R1GD85;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE SubName: Full=Putative aspartic-type endopeptidase protein {ECO:0000313|EMBL:EOD49505.1};
GN ORFNames=UCRNP2_3746 {ECO:0000313|EMBL:EOD49505.1};
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:EOD49505.1, 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; KB916079; EOD49505.1; -; Genomic_DNA.
DR RefSeq; XP_007583037.1; XM_007582975.1.
DR AlphaFoldDB; R1GD85; -.
DR KEGG; npa:UCRNP2_3746; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_9_3_1; -.
DR OMA; CNVTLGT; -.
DR OrthoDB; 615305at2759; -.
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; cd05474; SAP_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; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR033876; SAP-like.
DR PANTHER; PTHR47966:SF65; ASPARTIC-TYPE ENDOPEPTIDASE; 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|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..476
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004350606"
FT DOMAIN 71..399
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 89
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 290
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 325..363
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 476 AA; 49777 MW; 7289D7B0D1287DF1 CRC64;
MRCTAALTLA ASLISLTDAL QLAKRQNSAP KVVGAEIQRR EVTNPLARDQ ARRRRKRDSL
QESLDNEETL YFANATLGTP AQSLRLHLDT GSSDLWVNTD ASSLCSDSSS DSCSAAGTYN
ANDSSTYEYV NSLFNISYVD GSGASGDYVK DTFNFGGSNL TEMQFGIGYT SSSTEGVLGI
GYTTNEVAVN RAGLEAYSNL PQLLVDKGII QSNAYSLWLN DLDASKGSIL FGGVDTEKYQ
GTLATLPIIK EYGEYREFII ALTGLGANGK NGSYFSSNDS SSNVVPVLLD SGSSLTYLPD
SVVTSIYEDF NAAYDSTQGA AFVDCDLANN DDTLEFTFSS PTISVPMDEL VLLAGYSRGQ
AICILGISPA GDSTSVLGDT FLRSAYVVYD LANNEISLAQ TNYNATDSNI MEISTGTASV
PDATGVANAV SAVVAATGGA RNGGVSVSGN AAAPMKTAMP VGPMAAAAAA GLLFAL
//
