ID   RLR73_PLAVT             Reviewed;         402 AA.
AC   P0CV23;
DT   18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2019, sequence version 1.
DT   25-MAY-2022, entry version 9.
DE   RecName: Full=Secreted RxLR effector protein 73 {ECO:0000303|PubMed:29706971};
DE   Flags: Precursor;
GN   Name=RXLR73 {ECO:0000303|PubMed:29706971};
OS   Plasmopara viticola (Downy mildew of grapevine) (Botrytis viticola).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Plasmopara.
OX   NCBI_TaxID=143451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], DOMAIN, FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=29706971; DOI=10.3389/fpls.2018.00286;
RA   Liu Y., Lan X., Song S., Yin L., Dry I.B., Qu J., Xiang J., Lu J.;
RT   "In planta functional analysis and subcellular localization of the oomycete
RT   pathogen Plasmopara viticola candidate RXLR effector repertoire.";
RL   Front. Plant Sci. 9:286-286(2018).
CC   -!- FUNCTION: Secreted effector that completely suppresses the host cell
CC       death induced by cell death-inducing proteins.
CC       {ECO:0000269|PubMed:29706971}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29706971}. Host cell
CC       {ECO:0000305|PubMed:29706971}.
CC   -!- DOMAIN: Has the canonical translocation RxLR motif, but lacks the
CC       canonical EER motif, which characterizes most oomycete effectors
CC       identified so far. {ECO:0000305|PubMed:29706971}.
CC   -!- SIMILARITY: Belongs to the RxLR effector family. {ECO:0000305}.
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DR   AlphaFoldDB; P0CV23; -.
DR   SMR; P0CV23; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0043657; C:host cell; IEA:UniProtKB-SubCell.
DR   Gene3D; 2.40.10.10; -; 2.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   SUPFAM; SSF50494; SSF50494; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Secreted; Signal; Virulence.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..402
FT                   /note="Secreted RxLR effector protein 73"
FT                   /id="PRO_0000447932"
FT   MOTIF           104..107
FT                   /note="RxLR"
FT                   /evidence="ECO:0000305|PubMed:29706971"
FT   CARBOHYD        27
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        111
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        134
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        143
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        165
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        286
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   402 AA;  43062 MW;  CB1FAC575BCE7D6F CRC64;
     MRLLHVVVAT VSLTGAITSL IAAQHYNVSS DVIGGIEKED FGVGCNSRTK YPTAADTSKL
     QPRFAYLITN SLADFIAVHF IKFNLPDNDF VQIRAADPSA VDNRVLRYRG NESNGVFFAD
     ALSTKSVIVE LFTNASSSAQ KTNSSKCVGF AVDSYQYLGE GSTLNGSKEE VCGADNSREA
     SCYSGYTNAF RASNAVVRLL IKKSTGSFFC TGWLIGSEGH LITNNHCIST QSHASNTEFE
     FMAQGSSCSI NCEGARACFG SIRASYATLI YADATLDYAL VKLPINLSGQ YGYLRLRSSG
     AVMNERVYVP QHPAGWGKRI AMKSDNGFGT VTSLTMGGCA PNQVAYYLDT QGGSSGSPVL
     SWSDNAVVAL HHCGGCPNTA INSYKLVNDM KWRGILPANA CT