ID R13L1_ARATH Reviewed; 1054 AA.
AC Q9LRR4;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 152.
DE RecName: Full=Putative disease resistance RPP13-like protein 1;
GN Name=RPPL1; OrderedLocusNames=At3g14470; ORFNames=MOA2.9;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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).
CC -!- FUNCTION: Potential disease resistance protein.
CC -!- DOMAIN: The LRR repeats probably act as specificity determinant of
CC pathogen recognition. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the disease resistance NB-LRR family. RPP13
CC subfamily. {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; AB028617; BAB01339.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75530.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64509.1; -; Genomic_DNA.
DR RefSeq; NP_001319549.1; NM_001338120.1.
DR RefSeq; NP_188065.1; NM_112307.3.
DR AlphaFoldDB; Q9LRR4; -.
DR SMR; Q9LRR4; -.
DR BioGRID; 6004; 1.
DR IntAct; Q9LRR4; 1.
DR STRING; 3702.Q9LRR4; -.
DR PaxDb; 3702-AT3G14470-1; -.
DR ProteomicsDB; 236479; -.
DR EnsemblPlants; AT3G14470.1; AT3G14470.1; AT3G14470.
DR EnsemblPlants; AT3G14470.2; AT3G14470.2; AT3G14470.
DR GeneID; 820670; -.
DR Gramene; AT3G14470.1; AT3G14470.1; AT3G14470.
DR Gramene; AT3G14470.2; AT3G14470.2; AT3G14470.
DR KEGG; ath:AT3G14470; -.
DR Araport; AT3G14470; -.
DR TAIR; AT3G14470; -.
DR eggNOG; KOG4658; Eukaryota.
DR HOGENOM; CLU_000837_8_8_1; -.
DR InParanoid; Q9LRR4; -.
DR OMA; NPHRTQN; -.
DR OrthoDB; 524180at2759; -.
DR PhylomeDB; Q9LRR4; -.
DR PRO; PR:Q9LRR4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LRR4; baseline and differential.
DR Genevisible; Q9LRR4; AT.
DR GO; GO:0043531; F:ADP binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0051707; P:response to other organism; IEA:UniProt.
DR Gene3D; 1.20.5.4130; -; 1.
DR Gene3D; 1.10.8.430; Helical domain of apoptotic protease-activating factors; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR042197; Apaf_helical.
DR InterPro; IPR044974; Disease_R_plants.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR002182; NB-ARC.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR041118; Rx_N.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR23155; DISEASE RESISTANCE PROTEIN RP; 1.
DR PANTHER; PTHR23155:SF1237; DISEASE RESISTANCE RPP13-LIKE PROTEIN 1-RELATED; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF00931; NB-ARC; 1.
DR Pfam; PF18052; Rx_N; 1.
DR PRINTS; PR00364; DISEASERSIST.
DR SMART; SM00369; LRR_TYP; 2.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; Leucine-rich repeat; Nucleotide-binding;
KW Plant defense; Reference proteome; Repeat.
FT CHAIN 1..1054
FT /note="Putative disease resistance RPP13-like protein 1"
FT /id="PRO_0000212726"
FT DOMAIN 152..462
FT /note="NB-ARC"
FT REPEAT 579..600
FT /note="LRR 1"
FT REPEAT 603..624
FT /note="LRR 2"
FT REPEAT 626..648
FT /note="LRR 3"
FT REPEAT 650..672
FT /note="LRR 4"
FT REPEAT 676..697
FT /note="LRR 5"
FT REGION 9..20
FT /note="Leucine-zipper 1"
FT REGION 39..53
FT /note="Leucine-zipper 2"
FT REGION 1018..1054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 117..147
FT /evidence="ECO:0000255"
FT COMPBIAS 1018..1040
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 203..210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1054 AA; 121418 MW; 10C878EE0B9F4738 CRC64;
MTGIGEMFLA AFLQALFQTL VSEPFRSFFK RRELNENLLE RLSTALLTIT AVLIDAEEKQ
ITNPVVEKWV NELRDVVYHA EDALDDIATE ALRLNIGAES SSSNRLRQLR GRMSLGDFLD
GNSEHLETRL EKVTIRLERL ASQRNILGLK ELTAMIPKQR LPTTSLVDES EVFGRDDDKD
EIMRFLIPEN GKDNGITVVA IVGIGGVGKT TLSQLLYNDQ HVRSYFGTKV WAHVSEEFDV
FKITKKVYES VTSRPCEFTD LDVLQVKLKE RLTGTGLPFL LVLDDLWNEN FADWDLLRQP
FIHAAQGSQI LVTTRSQRVA SIMCAVHVHN LQPLSDGDCW SLFMKTVFGN QEPCLNREIG
DLAERIVHKC RGLPLAVKTL GGVLRFEGKV IEWERVLSSR IWDLPADKSN LLPVLRVSYY
YLPAHLKRCF AYCSIFPKGH AFEKDKVVLL WMAEGFLQQT RSSKNLEELG NEYFSELESR
SLLQKTKTRY IMHDFINELA QFASGEFSSK FEDGCKLQVS ERTRYLSYLR DNYAEPMEFE
ALREVKFLRT FLPLSLTNSS RSCCLDQMVS EKLLPTLTRL RVLSLSHYKI ARLPPDFFKN
ISHARFLDLS RTELEKLPKS LCYMYNLQTL LLSYCSSLKE LPTDISNLIN LRYLDLIGTK
LRQMPRRFGR LKSLQTLTTF FVSASDGSRI SELGGLHDLH GKLKIVELQR VVDVADAAEA
NLNSKKHLRE IDFVWRTGSS SSENNTNPHR TQNEAEVFEK LRPHRHIEKL AIERYKGRRF
PDWLSDPSFS RIVCIRLREC QYCTSLPSLG QLPCLKELHI SGMVGLQSIG RKFYFSDQQL
RDQDQQPFRS LETLRFDNLP DWQEWLDVRV TRGDLFPSLK KLFILRCPEL TGTLPTFLPS
LISLHIYKCG LLDFQPDHHE YSYRNLQTLS IKSSCDTLVK FPLNHFANLD KLEVDQCTSL
YSLELSNEHL RGPNALRNLR INDCQNLQLL PKLNALPQNL QVTITNCRYL RQPMEQQPQY
HHPQFHLPRS NVSGSPKSHG SHRSYDSRSS SRYD
//
