RXLRT_PHYIT
ID RXLRT_PHYIT Reviewed; 271 AA.
AC D0NSB3;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=RxLR effector protein PITG_15679 {ECO:0000303|PubMed:30329083};
DE EC=3.6.1.- {ECO:0000305};
DE Flags: Precursor;
GN ORFNames=PITG_15679;
OS Phytophthora infestans (strain T30-4) (Potato late blight agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=403677;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND INDUCTION.
RC STRAIN=T30-4;
RX PubMed=19741609; DOI=10.1038/nature08358;
RG The Broad Institute Genome Sequencing Platform;
RA Haas B.J., Kamoun S., Zody M.C., Jiang R.H., Handsaker R.E., Cano L.M.,
RA Grabherr M., Kodira C.D., Raffaele S., Torto-Alalibo T., Bozkurt T.O.,
RA Ah-Fong A.M., Alvarado L., Anderson V.L., Armstrong M.R., Avrova A.,
RA Baxter L., Beynon J., Boevink P.C., Bollmann S.R., Bos J.I., Bulone V.,
RA Cai G., Cakir C., Carrington J.C., Chawner M., Conti L., Costanzo S.,
RA Ewan R., Fahlgren N., Fischbach M.A., Fugelstad J., Gilroy E.M., Gnerre S.,
RA Green P.J., Grenville-Briggs L.J., Griffith J., Grunwald N.J., Horn K.,
RA Horner N.R., Hu C.H., Huitema E., Jeong D.H., Jones A.M., Jones J.D.,
RA Jones R.W., Karlsson E.K., Kunjeti S.G., Lamour K., Liu Z., Ma L.,
RA Maclean D., Chibucos M.C., McDonald H., McWalters J., Meijer H.J.,
RA Morgan W., Morris P.F., Munro C.A., O'Neill K., Ospina-Giraldo M.,
RA Pinzon A., Pritchard L., Ramsahoye B., Ren Q., Restrepo S., Roy S.,
RA Sadanandom A., Savidor A., Schornack S., Schwartz D.C., Schumann U.D.,
RA Schwessinger B., Seyer L., Sharpe T., Silvar C., Song J., Studholme D.J.,
RA Sykes S., Thines M., van de Vondervoort P.J., Phuntumart V., Wawra S.,
RA Weide R., Win J., Young C., Zhou S., Fry W., Meyers B.C., van West P.,
RA Ristaino J., Govers F., Birch P.R., Whisson S.C., Judelson H.S.,
RA Nusbaum C.;
RT "Genome sequence and analysis of the Irish potato famine pathogen
RT Phytophthora infestans.";
RL Nature 461:393-398(2009).
RN [2]
RP INDUCTION, AND DOMAIN.
RX PubMed=29312401; DOI=10.3389/fpls.2017.02155;
RA Yin J., Gu B., Huang G., Tian Y., Quan J., Lindqvist-Kreuze H., Shan W.;
RT "Conserved RXLR effector genes of Phytophthora infestans expressed at the
RT early stage of potato infection are suppressive to host defense.";
RL Front. Plant Sci. 8:2155-2155(2017).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=30329083; DOI=10.1093/jxb/ery360;
RA Wang S., McLellan H., Bukharova T., He Q., Murphy F., Shi J., Sun S.,
RA van Weymers P., Ren Y., Thilliez G., Wang H., Chen X., Engelhardt S.,
RA Vleeshouwers V., Gilroy E.M., Whisson S.C., Hein I., Wang X., Tian Z.,
RA Birch P.R.J., Boevink P.C.;
RT "Phytophthora infestans RXLR effectors act in concert at diverse
RT subcellular locations to enhance host colonization.";
RL J. Exp. Bot. 70:343-356(2019).
CC -!- FUNCTION: Effector that enhances P.infestans colonization of Nicotiana
CC benthamiana leaves. {ECO:0000269|PubMed:30329083}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30329083}. Host
CC cytoplasm {ECO:0000269|PubMed:30329083}. Host nucleus
CC {ECO:0000269|PubMed:30329083}.
CC -!- INDUCTION: Expression is induced during host plant infection.
CC {ECO:0000269|PubMed:19741609, ECO:0000269|PubMed:29312401}.
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:29312401}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the RxLR effector
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the Nudix hydrolase
CC family. {ECO:0000305}.
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DR EMBL; DS028157; EEY64458.1; -; Genomic_DNA.
DR RefSeq; XP_002897961.1; XM_002897915.1.
DR AlphaFoldDB; D0NSB3; -.
DR SMR; D0NSB3; -.
DR STRING; 4787.PITG_15679T0; -.
DR EnsemblProtists; PITG_15679T0; PITG_15679T0; PITG_15679.
DR GeneID; 9475430; -.
DR KEGG; pif:PITG_15679; -.
DR VEuPathDB; FungiDB:PITG_15679; -.
DR eggNOG; KOG2839; Eukaryota.
DR HOGENOM; CLU_069948_1_0_1; -.
DR InParanoid; D0NSB3; -.
DR OMA; RAMHMDA; -.
DR OrthoDB; 1324716at2759; -.
DR Proteomes; UP000006643; Partially assembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR Pfam; PF00293; NUDIX; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 2: Evidence at transcript level;
KW Host cytoplasm; Host nucleus; Hydrolase; Metal-binding; Reference proteome;
KW Secreted; Signal; Virulence.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..271
FT /note="RxLR effector protein PITG_15679"
FT /id="PRO_5003013620"
FT DOMAIN 212..271
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 49..69
FT /note="RxLR-dEER"
FT /evidence="ECO:0000305|PubMed:29312401"
FT MOTIF 248..269
FT /note="Nudix box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
SQ SEQUENCE 271 AA; 29615 MW; 64DB8DF1E3D01D51 CRC64;
MKVLQLIALT ALVSSCVAAS AADPSGLAKT KSDVDVLSRV LADHEQTNRS LRRYDLEGLD
SVNSNREERN SITMVDDVVT KASGLVDDVM GKTDDVVGKA GQFGKVPTKL RDVATKNMDK
IKEMTARSAL VKTLTGRYDY AEKLSLSALK QLDDIEKVRA VDIKKGIKGS KETPDGMRRV
IEPFEGMKVA PKKFLESHVG RADQRYGKDG SRLLSANVVM RLNDKGEKQI LLISSSNPKK
GDFLLPKGGW DKGEDVKKAA LREVIEEGGV R
