CRE5_PHYIT
ID CRE5_PHYIT Reviewed; 254 AA.
AC D0N4K2;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=RxLR effector protein CRE5 {ECO:0000303|PubMed:30329083};
DE EC=3.6.1.- {ECO:0000305};
DE AltName: Full=Core RXLR effector 5 {ECO:0000303|PubMed:29312401};
DE Flags: Precursor;
GN Name=CRE5 {ECO:0000303|PubMed:29312401}; ORFNames=PITG_06308;
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.
RX PubMed=28228125; DOI=10.1186/s12864-017-3585-x;
RA Ah-Fong A.M., Kim K.S., Judelson H.S.;
RT "RNA-seq of life stages of the oomycete Phytophthora infestans reveals
RT dynamic changes in metabolic, signal transduction, and pathogenesis genes
RT and a major role for calcium signaling in development.";
RL BMC Genomics 18:198-198(2017).
RN [3]
RP INDUCTION, FUNCTION, 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 [4]
RP SUBCELLULAR LOCATION, AND FUNCTION.
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 is involved in host plant infection.
CC Contributes to virulence during the early infection stage, by
CC inhibiting plant defense responses induced by both PAMP-triggered
CC immunity (PTI) and effector-triggered immunity (ETI).
CC {ECO:0000269|PubMed:29312401, ECO:0000269|PubMed:30329083}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30329083}. Host
CC cytoplasm {ECO:0000269|PubMed:30329083}. Host nucleus, host nucleolus
CC {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:28228125,
CC 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; DS028125; EEY69810.1; -; Genomic_DNA.
DR RefSeq; XP_002998457.1; XM_002998411.1.
DR AlphaFoldDB; D0N4K2; -.
DR SMR; D0N4K2; -.
DR STRING; 4787.PITG_06308T0; -.
DR EnsemblProtists; PITG_06308T0; PITG_06308T0; PITG_06308.
DR GeneID; 9465996; -.
DR KEGG; pif:PITG_06308; -.
DR VEuPathDB; FungiDB:PITG_06308; -.
DR eggNOG; KOG2839; Eukaryota.
DR HOGENOM; CLU_069948_1_0_1; -.
DR InParanoid; D0N4K2; -.
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:0044196; C:host cell nucleolus; 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 Glycoprotein; Host cytoplasm; Host nucleus; Hydrolase; Metal-binding;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..254
FT /note="RxLR effector protein CRE5"
FT /id="PRO_5003012945"
FT DOMAIN 191..254
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 53..63
FT /note="RxLR-dEER"
FT /evidence="ECO:0000305|PubMed:29312401"
FT MOTIF 228..249
FT /note="Nudix box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 254 AA; 28176 MW; F9A64D5F67D9C58C CRC64;
MQTIQLIIFV AFVLSRAAAS ISSFSDPTSI VNINHDANRL SRALAAGQNQ TQRSLRQHEG
EDRGAIDKAD EVVSKMKALM GTAKNVPNNL AALIAKRSKT AGEFVRRPFL VSKLSKRYNI
ADQLSFSTLK QLDKIDNMRI VDIKNGIKGN KKTPNGMRRK IKHFEGMKTA PQKFLESHVG
RDMQRYGKDG SRWLSAGVVT RTTDQGERQI LLISSSNPAR GDFLLPKGGW DRGEKIKKAA
LREVMEEGGV CRAL
