424Y_VERDV
ID 424Y_VERDV Reviewed; 223 AA.
AC G2X4G0;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Effector Vd424Y {ECO:0000303|PubMed:34233072};
DE EC=3.2.1.8 {ECO:0000255|PROSITE-ProRule:PRU01097};
DE AltName: Full=Endo-1,4-beta-xylanase {ECO:0000255|PROSITE-ProRule:PRU01097};
DE Flags: Precursor;
GN ORFNames=VDAG_05042 {ECO:0000312|EMBL:EGY23604.1};
OS Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137)
OS (Verticillium wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=498257 {ECO:0000312|Proteomes:UP000001611};
RN [1] {ECO:0000312|Proteomes:UP000001611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VdLs.17 / ATCC MYA-4575 / FGSC 10137
RC {ECO:0000312|Proteomes:UP000001611};
RX PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT "Comparative genomics yields insights into niche adaptation of plant
RT vascular wilt pathogens.";
RL PLoS Pathog. 7:E1002137-E1002137(2011).
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF 1-MET--SER-20 AND 174-ARG--ASN-184.
RC STRAIN=Vd991 {ECO:0000303|PubMed:34233072};
RX PubMed=34233072; DOI=10.1111/mpp.13100;
RA Liu L., Wang Z., Li J., Wang Y., Yuan J., Zhan J., Wang P., Lin Y., Li F.,
RA Ge X.;
RT "Verticillium dahliae secreted protein Vd424Y is required for full
RT virulence, targets the nucleus of plant cells, and induces cell death.";
RL Mol. Plant Pathol. 34:mpp.13100-mpp.13100(2021).
CC -!- FUNCTION: Secreted effector that localizes to the host nucleus to
CC contribute to the virulence process (PubMed:34233072). Induces host
CC innate immunity responses; triggers BAK1-and SOBIR1-dependent cell
CC death, salicylic acid signaling and jasmonic acid signaling
CC (PubMed:34233072). {ECO:0000269|PubMed:34233072}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC EC=3.2.1.8; Evidence={ECO:0000255|PROSITE-ProRule:PRU01097};
CC -!- PATHWAY: Glycan degradation; xylan degradation. {ECO:0000255|PROSITE-
CC ProRule:PRU01097}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:34233072}. Host
CC nucleus {ECO:0000269|PubMed:34233072}.
CC -!- DEVELOPMENTAL STAGE: Induced in the early stages of infection of cotton
CC plant. {ECO:0000269|PubMed:34233072}.
CC -!- DISRUPTION PHENOTYPE: Decreases virulence during cotton plant
CC infection. {ECO:0000269|PubMed:34233072}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC {ECO:0000305}.
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DR EMBL; DS572703; EGY23604.1; -; Genomic_DNA.
DR RefSeq; XP_009653073.1; XM_009654778.1.
DR STRING; 498257.G2X4G0; -.
DR EnsemblFungi; EGY23604; EGY23604; VDAG_05042.
DR GeneID; 20706505; -.
DR KEGG; vda:VDAG_05042; -.
DR eggNOG; ENOG502RXA7; Eukaryota.
DR HOGENOM; CLU_052631_0_0_1; -.
DR InParanoid; G2X4G0; -.
DR OMA; DYWQNWT; -.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000001611; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR GO; GO:0140404; P:effector-mediated modulation of host innate immune response by symbiont; IMP:UniProtKB.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.60.120.180; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR013319; GH11/12.
DR InterPro; IPR018208; GH11_AS_1.
DR InterPro; IPR033123; GH11_dom.
DR InterPro; IPR001137; Glyco_hydro_11.
DR Pfam; PF00457; Glyco_hydro_11; 1.
DR PRINTS; PR00911; GLHYDRLASE11.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS00776; GH11_1; 1.
DR PROSITE; PS51761; GH11_3; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Glycosidase; Host nucleus; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal;
KW Virulence; Xylan degradation.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..223
FT /note="Effector Vd424Y"
FT /evidence="ECO:0000255"
FT /id="PRO_5003439435"
FT DOMAIN 34..223
FT /note="GH11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT REGION 174..184
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:34233072"
FT ACT_SITE 119
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT ACT_SITE 210
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT MUTAGEN 1..20
FT /note="Missing: Abolishes secretion. Impairs activation of
FT host N.benthamiana immune response."
FT /evidence="ECO:0000269|PubMed:34233072"
FT MUTAGEN 174..184
FT /note="RRTKRTSGSVN->AAAAAAAAAAA: Abolishes localization to
FT host nucleus. Impairs activation of host N.benthamiana
FT immune response."
FT /evidence="ECO:0000269|PubMed:34233072"
SQ SEQUENCE 223 AA; 23968 MW; DC5258DDC13BC4D0 CRC64;
MVSFTSLLAA FSVVSGVLTS PIAVVPEVNT ALAKRTPSST GTSGGFYYSF WTDTPNSVTY
TNGDAGKFSV SWKNNNGNHV GGKGWRTGSA RTIKYSGSYK PNGNSYLAIY GWTRSPLIEY
YIVESFGTYN PSTGATSKGQ FTVDGSVYDL YTSTRTNAPS IEGTRTFTQF WSVRRTKRTS
GSVNTGAHFA AWKKAGMNLG SHDYQILAVE GYKSSGSATM TVS
