ID W2MYT0_PHYPR Unreviewed; 225 AA.
AC W2MYT0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Peptidase S1 domain-containing protein {ECO:0000259|PROSITE:PS50240};
DE Flags: Fragment;
GN ORFNames=L914_12769 {ECO:0000313|EMBL:ETM41445.1};
OS Phytophthora parasitica (Potato buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4792 {ECO:0000313|EMBL:ETM41445.1};
RN [1] {ECO:0000313|EMBL:ETM41445.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAC_01/95 {ECO:0000313|EMBL:ETM41445.1};
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|ARBA:ARBA00007664}.
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DR EMBL; KI694090; ETM41445.1; -; Genomic_DNA.
DR AlphaFoldDB; W2MYT0; -.
DR EnsemblProtists; ETM41445; ETM41445; L914_12769.
DR VEuPathDB; FungiDB:PPTG_03295; -.
DR Proteomes; UP000054532; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24276:SF91; AT26814P-RELATED; 1.
DR PANTHER; PTHR24276; POLYSERASE-RELATED; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Protease {ECO:0000256|RuleBase:RU363034};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT DOMAIN 1..196
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ETM41445.1"
SQ SEQUENCE 225 AA; 24110 MW; 3BCC338E6E924D7B CRC64;
LILTAGHCLE WDMFDVYISL GSKYRWGGGS QHSEMIRAIE AYRHPLYRLL RSTKGITHDV
ALLKLERPSK LQPAHLPAVD GSDNKPGVIA SALGWGLVNN ETSSDILQTV DVEIITNKKC
AKLYSYAAEN STVDDSVICA GLGGGKDSCN GDSGGPLLVH DVVVGITSSG PDECGVLPAT
YARVSNALSF IHDIKAGGST KNVTERLTAE TFTLFDTSQS QEESR
//
