ID W2FX92_PHYPR Unreviewed; 573 AA.
AC W2FX92;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=L915_18686 {ECO:0000313|EMBL:ETK74556.1};
OS Phytophthora parasitica (Potato buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4792 {ECO:0000313|EMBL:ETK74556.1};
RN [1] {ECO:0000313|EMBL:ETK74556.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CJ02B3 {ECO:0000313|EMBL:ETK74556.1};
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.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447}.
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DR EMBL; KI689031; ETK74556.1; -; Genomic_DNA.
DR AlphaFoldDB; W2FX92; -.
DR EnsemblProtists; ETK74556; ETK74556; L915_18686.
DR VEuPathDB; FungiDB:PPTG_05365; -.
DR Proteomes; UP000053236; 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 Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
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 456..478
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..353
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 356..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 29
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 237
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 573 AA; 61349 MW; 8E335ED4889305EE CRC64;
MVMVLMLCST HYAEIHLGIP AQRASVIVDT GSHLTALPCS TCNGCGTHTD PLFDVSKSTT
AKYLGCHDFD SCRSCENDRC MISQSYMEGS MWQAVMIDEL VWVGGFSTPS DEMEGILKTF
GFRFPVGCQT KETGLFITQK ENGIMGLGRH RSTVMSYMLN AGRVTQNLFT LCFAGDGGEL
VFGGVDYSHH TSDVGYTPLI NDNSAYYPVH VKDIRMNGVS LGIDAGTINS GRGVIVDSGT
TDTFFDSKGS RTFMKAFRNA AGREYSEKRM DLTADELAAL PTISIILSGM KGDGTDDVQL
DIPASSYLTP SDNAESYYGN FHFSERSGGV LGASTMIGFD VIFDTENKRV GFAESDCGKS
YANTSTPRPI ASNSTEQPTI QTETPVASNA TNQTAPTEAQ ITEQPVSTNA TSTSSSSNSS
VESNTTTTAL ADAANNVDVV TGSSTGATTS RASPKFGAFI AEVILISLVG VALAVMVWTK
WRTRSWSRIP DATETSRAHM ETVVDIDDSR SLSPTTPPGS PLSPRSRAAR KGPSPKFTIG
SPVDEDADEF REEDEDASSF PITGRSQGPH TNL
//
