PSR2_PHYSO
ID PSR2_PHYSO Reviewed; 670 AA.
AC E0W4V5;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 25-MAY-2022, entry version 38.
DE RecName: Full=RxLR effector protein PSR2 {ECO:0000303|PubMed:21653195};
DE AltName: Full=Avirulence homolog protein 146 {ECO:0000303|PubMed:21653195};
DE AltName: Full=Suppressor of RNA silencing protein 2 {ECO:0000303|PubMed:23377181};
DE Flags: Precursor;
GN Name=PSR2 {ECO:0000303|PubMed:23377181};
GN Synonyms=Avh146 {ECO:0000303|PubMed:21653195};
OS Phytophthora sojae (Soybean stem and root rot agent) (Phytophthora
OS megasperma f. sp. glycines).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=67593;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, AND DOMAIN.
RC STRAIN=P7064, P7074, and P7076;
RX PubMed=21653195; DOI=10.1105/tpc.111.086082;
RA Wang Q., Han C., Ferreira A.O., Yu X., Ye W., Tripathy S., Kale S.D.,
RA Gu B., Sheng Y., Sui Y., Wang X., Zhang Z., Cheng B., Dong S., Shan W.,
RA Zheng X., Dou D., Tyler B.M., Wang Y.;
RT "Transcriptional programming and functional interactions within the
RT Phytophthora sojae RXLR effector repertoire.";
RL Plant Cell 23:2064-2086(2011).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23377181; DOI=10.1038/ng.2525;
RA Qiao Y., Liu L., Xiong Q., Flores C., Wong J., Shi J., Wang X., Liu X.,
RA Xiang Q., Jiang S., Zhang F., Wang Y., Judelson H.S., Chen X., Ma W.;
RT "Oomycete pathogens encode RNA silencing suppressors.";
RL Nat. Genet. 45:330-333(2013).
RN [3]
RP FUNCTION, AND INDUCTION.
RX PubMed=25387135; DOI=10.1094/mpmi-06-14-0190-r;
RA Xiong Q., Ye W., Choi D., Wong J., Qiao Y., Tao K., Wang Y., Ma W.;
RT "Phytophthora suppressor of RNA silencing 2 is a conserved RxLR effector
RT that promotes infection in soybean and Arabidopsis thaliana.";
RL Mol. Plant Microbe Interact. 27:1379-1389(2014).
RN [4]
RP FUNCTION, DOMAIN, AND INTERACTION WITH HOST DRB4.
RX PubMed=30595554; DOI=10.1016/j.chom.2018.11.007;
RA Hou Y., Zhai Y., Feng L., Karimi H.Z., Rutter B.D., Zeng L., Choi D.S.,
RA Zhang B., Gu W., Chen X., Ye W., Innes R.W., Zhai J., Ma W.;
RT "A Phytophthora Effector Suppresses Trans-Kingdom RNAi to Promote Disease
RT Susceptibility.";
RL Cell Host Microbe 25:153-165(2019).
RN [5] {ECO:0007744|PDB:5GNC}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 59-670, DOMAIN, FUNCTION, AND
RP MUTAGENESIS OF 79-LYS--ASP-126; 127-SER--ASN-217; 218-PRO--ASN-308;
RP 309-PRO--LYS-399; 400-GLU--ASN-492; 493-PRO--ALA-583 AND 584-PRO--GLY-670.
RX PubMed=30926664; DOI=10.1073/pnas.1819481116;
RA He J., Ye W., Choi D.S., Wu B., Zhai Y., Guo B., Duan S., Wang Y., Gan J.,
RA Ma W., Ma J.;
RT "Structural analysis of Phytophthora suppressor of RNA silencing 2 (PSR2)
RT reveals a conserved modular fold contributing to virulence.";
RL Proc. Natl. Acad. Sci. U.S.A. 116:8054-8059(2019).
CC -!- FUNCTION: Secreted effector that possesses RNA silencing suppression
CC activity by inhibiting the biogenesis of small RNAs in the host plant
CC to promote enhanced susceptibility of host to the pathogen during
CC infection (PubMed:23377181, PubMed:25387135, PubMed:30595554).
CC Interferes with secondary siRNA production by associating with host
CC dsRNA-binding protein DRB4 (PubMed:30595554). Inhibits the host
CC salicylic acid pathway during infection (PubMed:25387135).
CC {ECO:0000269|PubMed:23377181, ECO:0000269|PubMed:25387135,
CC ECO:0000269|PubMed:30595554}.
CC -!- SUBUNIT: Interacts with host dsRNA-binding protein DRB4.
CC {ECO:0000269|PubMed:30595554}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:23377181}. Host cell
CC {ECO:0000305|PubMed:23377181}.
CC -!- INDUCTION: Expressed at specific infection stages in a transient manner
CC (PubMed:25387135). Is not expressed until 24 hours post-infection (hpi)
CC but quickly reaches the maximum expression level at approximately 36
CC hpi (PubMed:25387135). The abundance of transcripts exhibits a more
CC than twofold decrease at 48 hpi (PubMed:25387135).
CC {ECO:0000269|PubMed:25387135}.
CC -!- DOMAIN: The RxLR-dEER motif acts to carry the protein into the host
CC cell cytoplasm through binding to cell surface phosphatidylinositol-3-
CC phosphate. {ECO:0000305|PubMed:21653195}.
CC -!- DOMAIN: The C-terminal region (residues 79 to 670) consists of seven
CC imperfect tandem repeats, including one W-Y motif (WY1) and six L-W-Y
CC motifs (LWY2 to LWY7) (Probable). WY1 forms a 3 alpha-helix fold with
CC one hydrophobic core and each L-W-Y motif forms a highly conserved fold
CC consisting of 5 alpha-helices (Probable). The units contribute
CC differently to the virulence since WY1, LWY2 and LWY6 are important for
CC the ability to suppress the biogenesis of small RNA in host and
CC virulence activity of the pathogen, whereas LWY3, LWY4, LWY5 and LWY7
CC are dispensable for PSR2 function (PubMed:30926664). WY1 and LWY2 are
CC sufficient for association with DRB4, suppress gene silencing and
CC promote infection (PubMed:30595554). These units may function as basic
CC building blocks of Phytophthora effectors to enable virulence activity
CC and accelerate the evolution of novel functions (Probable).
CC {ECO:0000269|PubMed:30595554, ECO:0000269|PubMed:30926664,
CC ECO:0000305|PubMed:30926664}.
CC -!- DISRUPTION PHENOTYPE: Exhibits significantly decreased virulence when
CC infecting soybean seedlings. {ECO:0000269|PubMed:23377181}.
CC -!- SIMILARITY: Belongs to the RxLR effector family. {ECO:0000305}.
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DR EMBL; JN253932; AEK80745.1; -; Genomic_DNA.
DR EMBL; JN253933; AEK80746.1; -; Genomic_DNA.
DR EMBL; JN253934; AEK80747.1; -; Genomic_DNA.
DR RefSeq; XP_009538063.1; XM_009539768.1.
DR PDB; 5GNC; X-ray; 2.80 A; A=59-670.
DR PDBsum; 5GNC; -.
DR AlphaFoldDB; E0W4V5; -.
DR SMR; E0W4V5; -.
DR GeneID; 20640800; -.
DR KEGG; psoj:PHYSODRAFT_289089; -.
DR VEuPathDB; FungiDB:PHYSODRAFT_289089; -.
DR HOGENOM; CLU_021192_3_0_1; -.
DR OMA; TLYMKTD; -.
DR OrthoDB; 717762at2759; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0043657; C:host cell; IEA:UniProtKB-SubCell.
PE 1: Evidence at protein level;
KW 3D-structure; Glycoprotein; Repeat; Secreted; Signal; Virulence.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..670
FT /note="RxLR effector protein PSR2"
FT /id="PRO_5011089660"
FT REPEAT 79..126
FT /note="WY1"
FT /evidence="ECO:0000305|PubMed:30926664"
FT REPEAT 127..217
FT /note="LWY2"
FT /evidence="ECO:0000305|PubMed:30926664"
FT REPEAT 218..308
FT /note="LWY3"
FT /evidence="ECO:0000305|PubMed:30926664"
FT REPEAT 309..399
FT /note="LWY4"
FT /evidence="ECO:0000305|PubMed:30926664"
FT REPEAT 400..492
FT /note="LWY5"
FT /evidence="ECO:0000305|PubMed:30926664"
FT REPEAT 493..583
FT /note="LWY6"
FT /evidence="ECO:0000305|PubMed:30926664"
FT REPEAT 584..670
FT /note="LWY7"
FT /evidence="ECO:0000305|PubMed:30926664"
FT REGION 79..670
FT /note="7 X 93 AA tandem repeats"
FT /evidence="ECO:0000305|PubMed:30926664"
FT MOTIF 39..54
FT /note="RxLR-dEER"
FT /evidence="ECO:0000305|PubMed:21653195"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 79..126
FT /note="Missing: In PSR2delta-WY1; reduces the ability to
FT suppress the biogenesis of small RNA in host and virulence
FT activity of the pathogen."
FT /evidence="ECO:0000269|PubMed:30926664"
FT MUTAGEN 127..217
FT /note="Missing: In PSR2delta-LWY2; reduces the ability to
FT suppress the biogenesis of small RNA in host and virulence
FT activity of the pathogen."
FT /evidence="ECO:0000269|PubMed:30926664"
FT MUTAGEN 218..308
FT /note="Missing: In PSR2delta-LWY3; does not Reduce the
FT ability to suppress the biogenesis of small RNA in host and
FT virulence activity of the pathogen."
FT /evidence="ECO:0000269|PubMed:30926664"
FT MUTAGEN 309..399
FT /note="Missing: In PSR2delta-LWY4; does not Reduce the
FT ability to suppress the biogenesis of small RNA in host and
FT virulence activity of the pathogen."
FT /evidence="ECO:0000269|PubMed:30926664"
FT MUTAGEN 400..492
FT /note="Missing: In PSR2delta-LWY5; does not Reduce the
FT ability to suppress the biogenesis of small RNA in host and
FT virulence activity of the pathogen."
FT /evidence="ECO:0000269|PubMed:30926664"
FT MUTAGEN 493..583
FT /note="Missing: In PSR2delta-LWY6; reduces the ability to
FT suppress the biogenesis of small RNA in host and virulence
FT activity of the pathogen."
FT /evidence="ECO:0000269|PubMed:30926664"
FT MUTAGEN 584..670
FT /note="Missing: In PSR2delta-LWY7; does not Reduce the
FT ability to suppress the biogenesis of small RNA in host and
FT virulence activity of the pathogen."
FT /evidence="ECO:0000269|PubMed:30926664"
FT HELIX 77..85
FT /evidence="ECO:0007829|PDB:5GNC"
FT HELIX 90..96
FT /evidence="ECO:0007829|PDB:5GNC"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:5GNC"
FT HELIX 112..122
FT /evidence="ECO:0007829|PDB:5GNC"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:5GNC"
FT HELIX 126..140
FT /evidence="ECO:0007829|PDB:5GNC"
FT HELIX 143..155
FT /evidence="ECO:0007829|PDB:5GNC"
FT HELIX 160..176
FT /evidence="ECO:0007829|PDB:5GNC"
FT HELIX 181..187
FT /evidence="ECO:0007829|PDB:5GNC"
FT TURN 188..192
FT /evidence="ECO:0007829|PDB:5GNC"
FT HELIX 194..199
FT /evidence="ECO:0007829|PDB:5GNC"
FT HELIX 202..216
FT /evidence="ECO:0007829|PDB:5GNC"
FT HELIX 224..232
FT /evidence="ECO:0007829|PDB:5GNC"
FT HELIX 234..246
FT /evidence="ECO:0007829|PDB:5GNC"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:5GNC"
FT HELIX 251..267
FT /evidence="ECO:0007829|PDB:5GNC"
FT HELIX 272..278
FT /evidence="ECO:0007829|PDB:5GNC"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:5GNC"
FT TURN 288..290
FT /evidence="ECO:0007829|PDB:5GNC"
FT HELIX 292..307
FT /evidence="ECO:0007829|PDB:5GNC"
FT HELIX 315..319
FT /evidence="ECO:0007829|PDB:5GNC"
FT TURN 320..322
FT /evidence="ECO:0007829|PDB:5GNC"
FT HELIX 325..337
FT /evidence="ECO:0007829|PDB:5GNC"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:5GNC"
FT HELIX 342..359
FT /evidence="ECO:0007829|PDB:5GNC"
FT HELIX 363..369
FT /evidence="ECO:0007829|PDB:5GNC"
FT HELIX 372..374
FT /evidence="ECO:0007829|PDB:5GNC"
FT HELIX 376..381
FT /evidence="ECO:0007829|PDB:5GNC"
FT HELIX 385..394
FT /evidence="ECO:0007829|PDB:5GNC"
FT TURN 400..402
FT /evidence="ECO:0007829|PDB:5GNC"
FT HELIX 407..414
FT /evidence="ECO:0007829|PDB:5GNC"
FT HELIX 419..430
FT /evidence="ECO:0007829|PDB:5GNC"
FT HELIX 432..434
FT /evidence="ECO:0007829|PDB:5GNC"
FT HELIX 435..451
FT /evidence="ECO:0007829|PDB:5GNC"
FT HELIX 456..462
FT /evidence="ECO:0007829|PDB:5GNC"
FT HELIX 465..467
FT /evidence="ECO:0007829|PDB:5GNC"
FT HELIX 469..474
FT /evidence="ECO:0007829|PDB:5GNC"
FT HELIX 477..489
FT /evidence="ECO:0007829|PDB:5GNC"
FT HELIX 500..506
FT /evidence="ECO:0007829|PDB:5GNC"
FT HELIX 510..521
FT /evidence="ECO:0007829|PDB:5GNC"
FT HELIX 523..542
FT /evidence="ECO:0007829|PDB:5GNC"
FT HELIX 547..553
FT /evidence="ECO:0007829|PDB:5GNC"
FT TURN 554..557
FT /evidence="ECO:0007829|PDB:5GNC"
FT TURN 561..565
FT /evidence="ECO:0007829|PDB:5GNC"
FT HELIX 567..581
FT /evidence="ECO:0007829|PDB:5GNC"
FT HELIX 590..598
FT /evidence="ECO:0007829|PDB:5GNC"
FT HELIX 600..611
FT /evidence="ECO:0007829|PDB:5GNC"
FT TURN 614..616
FT /evidence="ECO:0007829|PDB:5GNC"
FT HELIX 617..633
FT /evidence="ECO:0007829|PDB:5GNC"
FT HELIX 638..645
FT /evidence="ECO:0007829|PDB:5GNC"
FT TURN 646..648
FT /evidence="ECO:0007829|PDB:5GNC"
FT HELIX 651..669
FT /evidence="ECO:0007829|PDB:5GNC"
SQ SEQUENCE 670 AA; 74613 MW; 44212A36D69674C0 CRC64;
MRLQCVVLFA ALTLVAATHA PPNVKTVLSA EQHDIPVKRL LRPGNPAGKE DEERGINFSS
VPGFEKLANL LKPKPGLKKL LKWADAKKPP ETVFTRLRLD KTGTQLFDNT DFPVWAAYTR
SVAQTDSEAS AVMLKTLVSR YSDEVLSGMI AAAKKSSKTE SIATKLETEQ MRTWLAAKKT
PDDMFLVFKL NKAGDDILSS PLLSAWTNYM KLSNKENPKA QTTLIATMTK HYGDSGVSQI
LAAARKSPAT QSTAKRLEAE QVQLWLKKGR TPDDTFTLLS LDRAGDDLLA SPQFNTWMKY
INYYNKENPD EKTTVLAKLM THFDDEELTP ILVVARKVPS TESTAAKLQA EQFKNWLSAD
KSPEEAFTLL QLDKAGDDLL TNPQLTNWLK YTENFNLNKE INEQVTAIQV FRAQYVDDSR
IANMVIAAEK VPNTQAIAKR VEDELFKGWT VVLNKPDDVF INLKLETVGE NVFESPLWSF
YTKFLEKYNT ANPGKEQTMI SGLARGYNDV TLTNMLLKAK EAPSTKTLAT KLEDELVQYW
LADKKLPDKL FGYLELKESV DGILTNPVFN VWLKYLNAFN DKAPVKKALM IDTLKSAFGD
VAVSNMLFAA KKDPGTAKVA ATLQTALLSK WVLEKKTPGQ VSAILKEGAG ADVSAKLLAT
YSAKFKVRWG
