RPS4B_ARATH
ID RPS4B_ARATH Reviewed; 1165 AA.
AC Q9FHF0;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Disease resistance protein RPS4B {ECO:0000303|PubMed:25744164};
DE EC=3.2.2.6 {ECO:0000255|PROSITE-ProRule:PRU00204};
GN Name=RPS4B {ECO:0000303|PubMed:25744164};
GN OrderedLocusNames=At5g45060 {ECO:0000312|Araport:AT5G45060};
GN ORFNames=K17O22.2 {ECO:0000312|EMBL:BAB09489.1};
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
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, INTERACTION WITH RRS1B, SUBUNIT, AND DOMAIN.
RX PubMed=25744164; DOI=10.1038/ncomms7338;
RA Saucet S.B., Ma Y., Sarris P.F., Furzer O.J., Sohn K.H., Jones J.D.;
RT "Two linked pairs of Arabidopsis TNL resistance genes independently confer
RT recognition of bacterial effector AvrRps4.";
RL Nat. Commun. 6:6338-6338(2015).
CC -!- FUNCTION: Disease resistance (R) protein that specifically recognizes
CC the AvrRps4 type III effector avirulence protein from P.syringae.
CC Heterodimerization with RRS1B is required to form a functional complex
CC to recognize AvrRps4 and to mediate the hypersensitive response.
CC {ECO:0000269|PubMed:25744164}.
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 -!- SUBUNIT: Interacts with RRS1B. RPS4B-RRS1B heterodimer interacts with
CC the bacterial effectors AvrRps4 and PopP2.
CC {ECO:0000269|PubMed:25744164}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- DOMAIN: The TIR domain is a signaling domain involved in cell death
CC induction. It is involved in heterodimerization of RPS4B with RRS1B,
CC but other domains also contribute to the interaction.
CC {ECO:0000269|PubMed:25744164}.
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}.
CC -!- SIMILARITY: Belongs to the disease resistance TIR-NB-LRR family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIB-LRRS; Note=Functional and comparative genomics
CC of disease resistance gene homologs;
CC URL="http://niblrrs.ucdavis.edu";
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DR EMBL; AB019224; BAB09489.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95196.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69267.1; -; Genomic_DNA.
DR RefSeq; NP_001330960.1; NM_001344584.1.
DR RefSeq; NP_199319.1; NM_123874.3.
DR AlphaFoldDB; Q9FHF0; -.
DR SMR; Q9FHF0; -.
DR STRING; 3702.AT5G45060.1; -.
DR iPTMnet; Q9FHF0; -.
DR PaxDb; Q9FHF0; -.
DR PRIDE; Q9FHF0; -.
DR ProteomicsDB; 228251; -.
DR EnsemblPlants; AT5G45060.1; AT5G45060.1; AT5G45060.
DR EnsemblPlants; AT5G45060.2; AT5G45060.2; AT5G45060.
DR GeneID; 834537; -.
DR Gramene; AT5G45060.1; AT5G45060.1; AT5G45060.
DR Gramene; AT5G45060.2; AT5G45060.2; AT5G45060.
DR KEGG; ath:AT5G45060; -.
DR Araport; AT5G45060; -.
DR TAIR; locus:2153207; AT5G45060.
DR eggNOG; ENOG502SI7S; Eukaryota.
DR HOGENOM; CLU_001561_0_3_1; -.
DR InParanoid; Q9FHF0; -.
DR OMA; PEHGIME; -.
DR OrthoDB; 106111at2759; -.
DR PhylomeDB; Q9FHF0; -.
DR PRO; PR:Q9FHF0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FHF0; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0002758; P:innate immune response-activating signal transduction; IDA:UniProtKB.
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; -; 2.
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 PANTHER; PTHR11017; PTHR11017; 1.
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; SSF52200; SSF52200; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50104; TIR; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Hydrolase; Leucine-rich repeat; NAD; Nucleotide-binding;
KW Nucleus; Plant defense; Reference proteome; Repeat.
FT CHAIN 1..1165
FT /note="Disease resistance protein RPS4B"
FT /id="PRO_0000444576"
FT DOMAIN 12..174
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT DOMAIN 211..474
FT /note="NB-ARC"
FT /evidence="ECO:0000255"
FT REPEAT 592..613
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 614..635
FT /note="LRR 2; degenerate"
FT /evidence="ECO:0000305"
FT REPEAT 636..659
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 684..703
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 704..725
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 726..748
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 772..794
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 795..818
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 819..836
FT /note="LRR 9; degenerate"
FT /evidence="ECO:0000305"
FT REPEAT 837..863
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT ACT_SITE 86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
SQ SEQUENCE 1165 AA; 132401 MW; F7763287C2E4D90F CRC64;
MAASSSSTGL PPQHQVFINF RGEDLRLGFV SHLVEALEND NIKVFIDNYA DKGEPLETLL
TKIHDSKIAL AIFSGKYTES TWCLRELAMI KDCVEKGKLV AIPIFYKVDP STVRGVRGQF
GDAFRDLEER DVIKKKEWKQ ALKWIPGLIG ITVHDKSPES EILNEIVKEV KKVLKKVSLE
GSQKVVSVDP SQSIDTLSSV GGEKDKTFGI KQRLKELEEK LDLVKYKGTR VIGVVGMPGI
GKTTLVKELY KTWQGKFSRY ALIDQIRGKS NNFRLECLPT LLLEKLLPEL NNPQLDSIEE
PYKTHKGLLR ERKVLVVLDD VSRREQIYAL LGKYDLHSKH EWIKDGSRII IATNDISSLK
GLVHDTYVVR QLNHRDGLQL FRYHAFHYDQ ATPPKVDFMK LSDEFVHYAR GHPLALKILG
RELYEKNMKH WETKLIILAQ SPTTYIGEVV QVSYDELSLA QKDAFLDIAC FRSQDVDYVE
SLLVSSDPGS AEAIKALKNK FLIDTCDGRV EMHDLLYRFS RELDLKASTQ GGSKQRRLWV
RQDIINVQQK TMGAANVRGI FLDLSEVKVE TSLDREHFKN MRNLRYLKLY NSHCPHECLT
NNKINMPDGL ELPLKEVRCL HWLKFPLEEL PNDFDPINLV DLKLPYSEIE RLWDGVKDTP
VLKWVDLNHS SKLCSLSGLS KAQNLQRLNL EGCTSLESLR DVNLTSLKTL TLSNCSNFKE
FPLIPENLKA LYLDGTSISQ LPDNVGNLKR LVLLNMKDCK VLETIPTCVS ELKTLQKLVL
SGCSKLKEFP EINKSSLKIL LLDGTSIKTM PQLPSVQYLC LSRNDHLIYL PAGINQVSQL
TRLDLKYCTK LTYVPELPPT LQYLDAHGCS SLKNVAKPLA RIMSTVQNHY TFNFTNCGNL
EQAAKEEITS YAQRKCQLLS DARKHYNEGS EALFSTCFPG CEVPSWFGHE AVGSLLQRKL
LPHWHDKRLS GIALCAVVSF PDSQDQLSCF SVTCTFKIKA EDKSWVPFTC PVGIWTREGN
KKDRIESDHV FIAYISSPHS IRCLEEKNSD KCNFSEASLE FTVTSDTSGI GVFKVLKCGL
SLVYENDKNK NSSLEAKYDV PVEVSFQEPE HGIMEEERYI NKRRSDDRRP KKKRKTKRDD
IMIISTVTQT CVPSVNARIE DKVTG
