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Database: UniProt
Entry: W2KM53_PHYPR
LinkDB: W2KM53_PHYPR
Original site: W2KM53_PHYPR 
ID   W2KM53_PHYPR            Unreviewed;       580 AA.
AC   W2KM53;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   ORFNames=L914_14949 {ECO:0000313|EMBL:ETM38844.1}, L915_15099
GN   {ECO:0000313|EMBL:ETK79004.1}, L916_14992
GN   {ECO:0000313|EMBL:ETL32437.1}, L917_14810
GN   {ECO:0000313|EMBL:ETL85694.1};
OS   Phytophthora parasitica (Potato buckeye rot agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4792 {ECO:0000313|EMBL:ETL85694.1};
RN   [1] {ECO:0000313|EMBL:ETL85694.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CHvinca01 {ECO:0000313|EMBL:ETL85694.1};
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.
RN   [2] {ECO:0000313|EMBL:ETK79004.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CJ02B3 {ECO:0000313|EMBL:ETK79004.1};
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 CJ02B3.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ETL32437.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CJ05E6 {ECO:0000313|EMBL:ETL32437.1};
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 CJ05E6.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:ETM38844.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAC_01/95 {ECO:0000313|EMBL:ETM38844.1};
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 IAC_01/95.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; KI688113; ETK79004.1; -; Genomic_DNA.
DR   EMBL; KI674867; ETL32437.1; -; Genomic_DNA.
DR   EMBL; KI681565; ETL85694.1; -; Genomic_DNA.
DR   EMBL; KI694830; ETM38844.1; -; Genomic_DNA.
DR   EnsemblProtists; ETK79004; ETK79004; L915_15099.
DR   EnsemblProtists; ETL32437; ETL32437; L916_14992.
DR   EnsemblProtists; ETL85694; ETL85694; L917_14810.
DR   EnsemblProtists; ETM38844; ETM38844; L914_14949.
DR   VEuPathDB; FungiDB:PPTG_04592; -.
DR   OMA; DFICAPQ; -.
DR   Proteomes; UP000053236; Unassembled WGS sequence.
DR   Proteomes; UP000053864; Unassembled WGS sequence.
DR   Proteomes; UP000054423; Unassembled WGS sequence.
DR   Proteomes; UP000054532; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
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; IPR001969; Aspartic_peptidase_AS.
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:SF81; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 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|RuleBase:RU000454};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|RuleBase:RU000454}; Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..580
FT                   /note="Peptidase A1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014315253"
FT   TRANSMEM        475..497
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          39..429
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          517..580
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        526..543
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        544..561
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        57
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        274
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ   SEQUENCE   580 AA;  63453 MW;  FDD2172F77DE1077 CRC64;
     MGPRRLRLAA VALSFLSPCA ASASGLLRIP LENYDQMQFF GFIGVGSPPQ RFQVIFDTGS
     SDIWLPETSC ADCAGSRRYH AAVSRSHEPL NEPFRLEYGS GNASGRVVRE QISLFGGDAQ
     DELLTLSKVQ IGSTSKTTKR LQRFQADGIV GLGLEELAII TKPSLLKSDP RLGRFSIYIN
     PLPGALPPAQ LIFGGVDDSL PVAHIPEANG THVSWHHFPL VRYPSSRRAH GFWAIRLHRL
     AVGHFDSRSE SSSKQLAGSG EGIVAVSAAV AIVDSGTSLL LLPRRAFDAT IAEIRQHLRV
     QHGRELRADP HVVSGYSCAD CTAEMFPALR FSFVITEASV DTQMKTQTLV LRGTDYARCD
     DLICAPQLDV HALFTSKKTK SKLVIPSASA MTTNVPQEME HEEVVVLGVT FLRAYYVQFD
     SERKTVGFAC VGSALSTAAN VCSGGWTPKL QFHSAHFSDA EASAWRAGWV FWSRVYLGIG
     VLLLVVAFAL LWLILVVPSS DVEKVLDWLY GPSDKNRRRQ QQTESKLTPS RRSSYQALQI
     EKASDNNRGD EASEEPDSEP ESPHASSAAP SRRKSVCFDV
//
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