TAO1_ARATH
ID TAO1_ARATH Reviewed; 1187 AA.
AC Q9FI14;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Disease resistance protein TAO1 {ECO:0000305};
DE EC=3.2.2.6 {ECO:0000255|PROSITE-ProRule:PRU00204};
DE AltName: Full=Protein TARGET OF AVRB OPERATION 1 {ECO:0000303|PubMed:18424557};
GN Name=TAO1 {ECO:0000303|PubMed:18424557};
GN OrderedLocusNames=At5g44510 {ECO:0000312|Araport:AT5G44510};
GN ORFNames=MFC16.19 {ECO:0000312|EMBL:BAB09158.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP FUNCTION.
RC STRAIN=cv. Mt-0;
RX PubMed=18424557; DOI=10.1073/pnas.0802157105;
RA Eitas T.K., Nimchuk Z.L., Dangl J.L.;
RT "Arabidopsis TAO1 is a TIR-NB-LRR protein that contributes to disease
RT resistance induced by the Pseudomonas syringae effector AvrB.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:6475-6480(2008).
CC -!- FUNCTION: TIR-NB-LRR receptor-like protein that contributes to disease
CC resistance induced by the Pseudomonas syringae type III effector AvrB.
CC Acts additively with RPM1 to generate a full disease resistance
CC response to P.syringae expressing this type III effector.
CC {ECO:0000269|PubMed:18424557}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide;
CC Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00204};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00204};
CC -!- DOMAIN: The TIR domain mediates NAD(+) hydrolase (NADase) activity.
CC Self-association of TIR domains is required for NADase activity.
CC {ECO:0000255|PROSITE-ProRule:PRU00204}.
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DR EMBL; AB017065; BAB09158.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95118.1; -; Genomic_DNA.
DR RefSeq; NP_199264.1; NM_123818.2.
DR AlphaFoldDB; Q9FI14; -.
DR SMR; Q9FI14; -.
DR STRING; 3702.AT5G44510.1; -.
DR iPTMnet; Q9FI14; -.
DR PaxDb; Q9FI14; -.
DR PRIDE; Q9FI14; -.
DR ProteomicsDB; 234124; -.
DR EnsemblPlants; AT5G44510.1; AT5G44510.1; AT5G44510.
DR GeneID; 834478; -.
DR Gramene; AT5G44510.1; AT5G44510.1; AT5G44510.
DR KEGG; ath:AT5G44510; -.
DR Araport; AT5G44510; -.
DR TAIR; locus:2163426; AT5G44510.
DR eggNOG; ENOG502QWPX; Eukaryota.
DR HOGENOM; CLU_001561_0_1_1; -.
DR InParanoid; Q9FI14; -.
DR OrthoDB; 187323at2759; -.
DR PhylomeDB; Q9FI14; -.
DR PRO; PR:Q9FI14; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FI14; baseline and differential.
DR Genevisible; Q9FI14; AT.
DR GO; GO:0043531; F:ADP binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0050135; F:NAD(P)+ nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0061809; F:NAD+ nucleotidase, cyclic ADP-ribose generating; IEA:UniProtKB-EC.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.8.430; -; 1.
DR Gene3D; 3.40.50.10140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR042197; Apaf_helical.
DR InterPro; IPR045344; C-JID.
DR InterPro; IPR044974; Disease_R_plants.
DR InterPro; IPR011713; Leu-rich_rpt_3.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR002182; NB-ARC.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000157; TIR_dom.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11017; PTHR11017; 6.
DR Pfam; PF20160; C-JID; 1.
DR Pfam; PF07725; LRR_3; 1.
DR Pfam; PF00931; NB-ARC; 1.
DR Pfam; PF01582; TIR; 1.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF52200; SSF52200; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50104; TIR; 1.
PE 3: Inferred from homology;
KW ATP-binding; Hydrolase; Leucine-rich repeat; NAD; Nucleotide-binding;
KW Plant defense; Reference proteome; Repeat.
FT CHAIN 1..1187
FT /note="Disease resistance protein TAO1"
FT /id="PRO_0000433377"
FT DOMAIN 38..202
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT DOMAIN 217..478
FT /note="NB-ARC"
FT /evidence="ECO:0000255"
FT REPEAT 498..522
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 611..633
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 635..658
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 660..679
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 680..703
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 704..727
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 728..750
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 752..775
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 799..823
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 824..849
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 870..894
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 895..918
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 920..942
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 953..974
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT ACT_SITE 113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
SQ SEQUENCE 1187 AA; 134222 MW; DBDE51E680BB8429 CRC64;
MDSSCFLVYR IFRFRKRNKN ISSSLSSSSP PSSLSQNWLH PVFLSFRGED VRKGLLSHIQ
KEFQRNGITP FIDNEMKRGG SIGPELLQAI RGSKIAIILL SRNYGSSKWC LDELVEIMKC
REELGQTVMT VFYDVDPSDV RKQKGDFGKV FKKTCVGRPE EMVQRWKQAL TSAANILGED
SRNWENEADM IIKISKDVSD VLSFTPSKDF DEFVGIEAHT TEITSLLQLD LEEVRMIGIW
GPAGIGKTTI SRVLYNKLFH QFQLGAIIDN IKVRYPRPCH DEYSAKLQLQ KELLSQMINQ
KDMVVPHLGV AQERLKDKKV LLVLDDVDGL VQLDAMAKDV QWFGLGSRII VVTQDLKLLK
AHGIKYIYKV DFPTSDEALE IFCMYAFGEK SPKVGFEQIA RTVTTLAGKL PLGLRVMGSY
LRRMSKQEWA KSIPRLRTSL DDDIESVLKF SYNSLAEQEK DLFLHITCFF RRERIETLEV
FLAKKSVDMR QGLQILADKS LLSLNLGNIE MHNLLVQLGL DIVRKQSIHK PGKRQFLVDT
EDICEVLTDD TGTRTLIGID LELSGVIEGV INISERAFER MCNLQFLRFH HPYGDRCHDI
LYLPQGLSHI SRKLRLLHWE RYPLTCLPPK FNPEFLVKIN MRDSMLEKLW DGNEPIRNLK
WMDLSFCVNL KELPDFSTAT NLQELRLINC LSLVELPSSI GNATNLLELD LIDCSSLVKL
PSSIGNLTNL KKLFLNRCSS LVKLPSSFGN VTSLKELNLS GCSSLLEIPS SIGNIVNLKK
VYADGCSSLV QLPSSIGNNT NLKELHLLNC SSLMECPSSM LNLTRLEDLN LSGCLSLVKL
PSIGNVINLQ SLYLSDCSSL MELPFTIENA TNLDTLYLDG CSNLLELPSS IWNITNLQSL
YLNGCSSLKE LPSLVENAIN LQSLSLMKCS SLVELPSSIW RISNLSYLDV SNCSSLLELN
LVSHPVVPDS LILDAGDCES LVQRLDCFFQ NPKIVLNFAN CFKLNQEARD LIIQTSACRN
AILPGEKVPA YFTYRATGDS LTVKLNQKYL LQSLRFKACL LLVEGQNKWP NWGMNLVTSR
EPDGHIVLYT PSSHLQGPLL MENLYTFEFE LVVTSSEFVL EFRADRYKCA LGRFDKFGVH
VVWCHLDQYE SKSPSCKPFW RDFPIVISNG QNILDAILKT PMPSINQ
