ID A0A0W8CIG4_PHYNI Unreviewed; 388 AA.
AC A0A0W8CIG4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Aspartic protease {ECO:0000313|EMBL:KUF83893.1};
GN ORFNames=AM587_10002369 {ECO:0000313|EMBL:KUF83893.1}, AM587_10005319
GN {ECO:0000313|EMBL:KUF77880.1};
OS Phytophthora nicotianae (Buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4790 {ECO:0000313|EMBL:KUF83893.1, ECO:0000313|Proteomes:UP000052943};
RN [1] {ECO:0000313|EMBL:KUF83893.1, ECO:0000313|Proteomes:UP000052943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 0 {ECO:0000313|Proteomes:UP000052943}, and Race 0
RC {ECO:0000313|EMBL:KUF83893.1};
RA Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT "Genomes and virulence difference between two physiological races of
RT Phytophthora nicotianae.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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:KUF83893.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LNFO01005465; KUF77880.1; -; Genomic_DNA.
DR EMBL; LNFO01003049; KUF83893.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W8CIG4; -.
DR STRING; 4790.A0A0W8CIG4; -.
DR EnsemblProtists; KUF77880; KUF77880; AM587_10005319.
DR EnsemblProtists; KUF83893; KUF83893; AM587_10002369.
DR OMA; EGDAAQC; -.
DR Proteomes; UP000052943; 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 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 PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF51; 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; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:KUF83893.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000052943};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..388
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007440262"
FT DOMAIN 81..385
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 99
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 275
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 388 AA; 42278 MW; 471E52659CBED631 CRC64;
MLRCSVLCSL LLALSSAAVL RVPMIKRSDD EFMSSLLHDV HAMQRPVVWS PDASPLNHDE
GQPSVEGSAN VVIRDFQNAQ YYGEISIGTP PQPFAVIFDT GSSNLWVPDK KFGSHNVYDH
DKSSTYKPNG TAFDIMYGSG PVSGFLSQDT LELGGLTVPD QFFAEVNVTK GLGPAYYLGK
FDGLFGLAFD TISVDHLKTP FHRMIQEGLI DEPVFAFYLG DHKDGELTFG GVDKAHYKGD
LEYVDVTSAT YWSVKLDAVE TKGEKLTDVD KAIVDSGTSL IAGPKDQVAK LAALVGAHKF
IMGEYLISCS AAAPDISFVL NGKSYTLTKE EYTLKSGPIC LFAFMGIDIP APAGPLWILG
DVFMRKHYTV FDWGTDSRKP RVGFALAA
//
