ID   W2L9Q5_PHYPR            Unreviewed;       526 AA.
AC   W2L9Q5;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   ORFNames=L917_08462 {ECO:0000313|EMBL:ETL93375.1};
OS   Phytophthora parasitica (Potato buckeye rot agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4792 {ECO:0000313|EMBL:ETL93375.1};
RN   [1] {ECO:0000313|EMBL:ETL93375.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CHvinca01 {ECO:0000313|EMBL:ETL93375.1};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica CHvinca01.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447}.
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DR   EMBL; KI679611; ETL93375.1; -; Genomic_DNA.
DR   AlphaFoldDB; W2L9Q5; -.
DR   EnsemblProtists; ETL93375; ETL93375; L917_08462.
DR   VEuPathDB; FungiDB:PPTG_11138; -.
DR   Proteomes; UP000054423; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
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; PTHR13683; ASPARTYL PROTEASES; 1.
DR   PANTHER; PTHR13683:SF375; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 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   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        464..487
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          95..429
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        111
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        316
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ   SEQUENCE   526 AA;  58072 MW;  B56E33E45A72A628 CRC64;
     MVLGAVVRYA ALVSLTIWGA YAATSSLDTI QLEMSNTMAR SQAIDALHGR YRYHRSIDEE
     LQAVQTLSDE DPPDGEAARN QATVEMGLRS GAGSHTIQVT VGGQQRELII DTGSGKTAFV
     CVGCNNCGNK RKHQPFVFTV NTTYLSCDRS MIAMSNRGEP PCVDCENGRC KYGQTYVEGD
     HWTAYKASDM MQLSSSFEAR VEFGCIYEQS GVFLDQPSDG IMGFSRHPDS IYEQFYRQKV
     TRSRIFSQCL AEGGGLLTIG GVDLARHTEP VRYTPLRNTG YQYWTVTLLS VSIGNANNTM
     QVDKKEFNAD RGCVLDSGTT FLYMPESTKQ PFRLAWSRAV GSFSFVPESD TFYFMTSEQV
     AALPDVCFWF KNDVHICLPS TRYFAQVGNG IYTGTIFFTA GPKATILGAS VLEGHDVIYD
     VDNHRVGIAE AMCDQPLQAQ VELSLDPGGD KFKPGFDYSQ APQWMLACIT LLAVAGLINA
     IWVAAAIEGD STADIDKNTK PPTVRISNDW QDEEFSFFLM EENAPK
//