GenomeNet

Database: UniProt
Entry: W2QV23_PHYPN
LinkDB: W2QV23_PHYPN
Original site: W2QV23_PHYPN 
ID   W2QV23_PHYPN            Unreviewed;       619 AA.
AC   W2QV23;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   ORFNames=PPTG_06109 {ECO:0000313|EMBL:ETN17072.1};
OS   Phytophthora parasitica (strain INRA-310).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=761204 {ECO:0000313|EMBL:ETN17072.1, ECO:0000313|Proteomes:UP000018817};
RN   [1] {ECO:0000313|Proteomes:UP000018817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=INRA-310 {ECO:0000313|Proteomes:UP000018817};
RG   The Broad Institute Genome Sequencing Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA   Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D.,
RA   Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ETN17072.1, ECO:0000313|Proteomes:UP000018817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=INRA-310 {ECO:0000313|EMBL:ETN17072.1,
RC   ECO:0000313|Proteomes:UP000018817};
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 INRA-310.";
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; KI669568; ETN17072.1; -; Genomic_DNA.
DR   EMBL; KI669568; ETN17073.1; -; Genomic_DNA.
DR   RefSeq; XP_008898142.1; XM_008899894.1.
DR   RefSeq; XP_008898144.1; XM_008899896.1.
DR   AlphaFoldDB; W2QV23; -.
DR   EnsemblProtists; ETN17072; ETN17072; PPTG_06109.
DR   EnsemblProtists; ETN17073; ETN17073; PPTG_06109.
DR   GeneID; 20176100; -.
DR   VEuPathDB; FungiDB:PPTG_06109; -.
DR   OrthoDB; 54298at2759; -.
DR   Proteomes; UP000018817; 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; 1.
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; PTHR47965; ASPARTYL PROTEASE-RELATED; 1.
DR   PANTHER; PTHR47965:SF12; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00026; Asp; 1.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018817};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        430..454
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          26..379
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          467..569
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          589..608
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        471..493
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        512..529
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        530..549
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        555..569
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   619 AA;  69379 MW;  51ABC8969C96DA3D CRC64;
     MSDPFLCVER LPADCRHRLV ERRGAWRWML RLGCKGDLFV RCVIDMHQCW WRRCHASVRW
     SQYSVRNRSL VEWERMLFLT VLLLHDRGQF MTDTWSSDEI GDISKTFLVI EEQDTFYRST
     YDGITGLAYE ALAASTGDTV SSLYNVLVDT AKSTDAFGML LCGTMQPMLQ TGGTDFTYHS
     GQLLIGGTEG VDGETYYSGD MLYTPITREA WYVVTVTDIG YNGASLGLSC DSYNEPQAII
     DSGTSNLAFP SDVYNALMDQ IRAATLEAIP DFDTSYFEDS ASCCDEDYCD PTSSSAALLE
     LPSIYFTLGM EATDGSTSKH FTIEIPPEYY WRPEMNGDNS SMACRAIGIS EGTSTVLGDV
     FMDGLYSYHD RVEGKIGLAV ANNCPNNVTS SKKVYTAEDS VDWCSCFSST MKKKSSWTTF
     LPWGSGCFFW LWWMYVVIAS FLVVIACVCV LLWWHMTNKR MKKLQEEACR SNTSGRRTTR
     LATMQSSGSG RGPTLAPGSP PNDYYAAPVP TPQRRSTRSG RSGSRRGSMK SPRSQDRRSK
     RKEKEVPIMA EPKYSTMSSP RSPLSDTSSI ALLSEPNSSI GSMENWKHKA KPYTPGSHHS
     NYKSNYNDRW GASLKESEF
//
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