ID A0A0B1P3E1_UNCNE Unreviewed; 506 AA.
AC A0A0B1P3E1;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 08-NOV-2023, entry version 34.
DE SubName: Full=Putative vacuolar aspartyl protease (Proteinase a) {ECO:0000313|EMBL:KHJ31825.1};
GN ORFNames=EV44_g0018 {ECO:0000313|EMBL:KHJ31825.1};
OS Uncinula necator (Grape powdery mildew).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Erysiphe.
OX NCBI_TaxID=52586 {ECO:0000313|EMBL:KHJ31825.1, ECO:0000313|Proteomes:UP000030854};
RN [1] {ECO:0000313|EMBL:KHJ31825.1, ECO:0000313|Proteomes:UP000030854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=c {ECO:0000313|Proteomes:UP000030854};
RX PubMed=25487071;
RA Jones L., Riaz S., Morales-Cruz A., Amrine K.C., McGuire B., Gubler W.D.,
RA Walker M.A., Cantu D.;
RT "Adaptive genomic structural variation in the grape powdery mildew
RT pathogen, Erysiphe necator.";
RL BMC Genomics 15:1081-1081(2014).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KHJ31825.1}.
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DR EMBL; JNVN01002554; KHJ31825.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B1P3E1; -.
DR STRING; 52586.A0A0B1P3E1; -.
DR HOGENOM; CLU_013253_10_0_1; -.
DR OMA; IFHGGTE; -.
DR OrthoDB; 3087283at2759; -.
DR Proteomes; UP000030854; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR034164; Pepsin-like_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF75; ENDOPEPTIDASE (CTSD), PUTATIVE (AFU_ORTHOLOGUE AFUA_4G07040)-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 Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000313|EMBL:KHJ31825.1};
KW Protease {ECO:0000313|EMBL:KHJ31825.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030854};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..506
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002059324"
FT DOMAIN 125..429
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 143
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 322
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 156..161
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 506 AA; 55108 MW; 423D2BAAB221C644 CRC64;
MCCTKFIYFI ATLFATFGTI TTKILESQCS NFENCSGSRK DSFEEVQESL IDLDIGPLIR
LVQRSGIANP LSHPLNAQET HFIRDFKREA KNPTNRHVSK AIVPPIPPSR PFSAGIFQDG
NDYTYFGEVF LGSRSSKVYM LLDTGADSSW VMGSECKDPI CTSRDTFGGQ NSSTFEVSDT
KFSVNYGSGS CSGVLAKDTV NFAGFSFRMP FGVATMVSKE FDSFEIYGIL GLSFSKSKTP
SFVDSVVASK SLERNLFGIS LSQTKDGNNT GVINFGSPDT SRFSGDLKYY PLSGNKNDWK
IYLGAAGFGE EQITMNRTTL FDTGATNIFA PLEITNMIYS NVPGAGSKDN GSNWQVPCDT
TVNLVFRFGS DEYTLPPAMW VGPPTTTDGQ CWSNLSGTDQ TNGEWVLGDF FLKNYYVVFD
IDKRRIGIAN VKIPTPSTVP SPYITDDDSF LSPTEDGGLI SSGSPPSPKA SLISPKTSAS
INLQTSNILL YSLFISFGST VLKAIS
//