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PBS1_ARATH
ID   PBS1_ARATH              Reviewed;         456 AA.
AC   Q9FE20;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 155.
DE   RecName: Full=Serine/threonine-protein kinase PBS1 {ECO:0000303|PubMed:11359614};
DE            EC=2.7.11.1 {ECO:0000269|PubMed:11359614};
DE   AltName: Full=AvrPphB susceptible protein 1 {ECO:0000303|PubMed:11359614};
GN   Name=PBS1 {ECO:0000303|PubMed:11359614};
GN   OrderedLocusNames=At5g13160 {ECO:0000312|Araport:AT5G13160};
GN   ORFNames=T19L5.120 {ECO:0000312|EMBL:CAC05444.1};
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 [MRNA], FUNCTION, ENZYME ACTIVITY, AUTOPHOSPHORYLATION,
RP   MUTANT PBS1-2, AND MUTAGENESIS OF GLY-252.
RX   PubMed=11359614; DOI=10.1046/j.1365-313x.2001.01014.x;
RA   Swiderski M.R., Innes R.W.;
RT   "The Arabidopsis PBS1 resistance gene encodes a member of a novel protein
RT   kinase subfamily.";
RL   Plant J. 26:101-112(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(2000).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   PARTIAL PROTEIN SEQUENCE, FUNCTION, CLEAVAGE, INTERACTION WITH AVRPPHB, AND
RP   MUTAGENESIS OF LYS-115; GLY-241; ASP-242 AND LYS-243.
RX   PubMed=12947197; DOI=10.1126/science.1085671;
RA   Shao F., Golstein C., Ade J., Stoutemyer M., Dixon J.E., Innes R.W.;
RT   "Cleavage of Arabidopsis PBS1 by a bacterial type III effector.";
RL   Science 301:1230-1233(2003).
RN   [6]
RP   FUNCTION, INTERACTION WITH RPS5, AND MUTAGENESIS OF LYS-115 AND GLY-252.
RX   PubMed=17277084; DOI=10.1073/pnas.0608779104;
RA   Ade J., DeYoung B.J., Golstein C., Innes R.W.;
RT   "Indirect activation of a plant nucleotide binding site-leucine-rich repeat
RT   protein by a bacterial protease.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2531-2536(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
RN   [8]
RP   INTERACTION WITH FLS2, DISRUPTION PHENOTYPE, FUNCTION, AND INDUCTION BY
RP   FLAGELLIN.
RX   PubMed=20413097; DOI=10.1016/j.chom.2010.03.007;
RA   Zhang J., Li W., Xiang T., Liu Z., Laluk K., Ding X., Zou Y., Gao M.,
RA   Zhang X., Chen S., Mengiste T., Zhang Y., Zhou J.M.;
RT   "Receptor-like cytoplasmic kinases integrate signaling from multiple plant
RT   immune receptors and are targeted by a Pseudomonas syringae effector.";
RL   Cell Host Microbe 7:290-301(2010).
RN   [9]
RP   FUNCTION, INTERACTION WITH RPS5, AND MUTAGENESIS OF LYS-115 AND GLY-252.
RX   PubMed=22372664; DOI=10.1111/j.1462-5822.2012.01779.x;
RA   DeYoung B.J., Qi D., Kim S.H., Burke T.P., Innes R.W.;
RT   "Activation of a plant nucleotide binding-leucine rich repeat disease
RT   resistance protein by a modified self protein.";
RL   Cell. Microbiol. 14:1071-1084(2012).
RN   [10]
RP   SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-2; CYS-3; PHE-4 AND CYS-6, AND
RP   MYRISTOYLATION AT GLY-2.
RX   PubMed=22046960; DOI=10.1094/mpmi-11-10-0272;
RA   Takemoto D., Rafiqi M., Hurley U., Lawrence G.J., Bernoux M., Hardham A.R.,
RA   Ellis J.G., Dodds P.N., Jones D.A.;
RT   "N-terminal motifs in some plant disease resistance proteins function in
RT   membrane attachment and contribute to disease resistance.";
RL   Mol. Plant Microbe Interact. 25:379-392(2012).
RN   [11]
RP   SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-2; CYS-3; CYS-6; GLY-98; GLY-103;
RP   SER-244 AND GLY-286, PALMITOYLATION AT CYS-3 AND CYS-6, AND MOTIF.
RX   PubMed=24225654; DOI=10.1104/pp.113.227686;
RA   Qi D., Dubiella U., Kim S.H., Sloss D.I., Dowen R.H., Dixon J.E.,
RA   Innes R.W.;
RT   "Recognition of the protein kinase AVRPPHB SUSCEPTIBLE1 by the disease
RT   resistance protein RESISTANCE TO PSEUDOMONAS SYRINGAE5 is dependent on s-
RT   acylation and an exposed loop in AVRPPHB SUSCEPTIBLE1.";
RL   Plant Physiol. 164:340-351(2014).
CC   -!- FUNCTION: Protein kinase required for plant defense mechanism mediated
CC       by the disease resistance (R) protein RPS5. In case of infection by
CC       Pseudomonas syringae, AvrPphB triggers RPS5-mediated defense mechanism
CC       via the cleavage of PBS1. Both kinase activity and cleavage by avrPphB
CC       are independently required to trigger the RPS5-mediated resistance.
CC       Contributes to PAMP-triggered immunity (PTI) signaling and defense
CC       responses downstream of FLS2. {ECO:0000269|PubMed:11359614,
CC       ECO:0000269|PubMed:12947197, ECO:0000269|PubMed:17277084,
CC       ECO:0000269|PubMed:20413097, ECO:0000269|PubMed:22372664}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000269|PubMed:11359614};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000269|PubMed:11359614};
CC   -!- SUBUNIT: In infected plant cells, it interacts with the P.syringae
CC       virulence protein avrPphB. In uninfected plants, autophosphorylated
CC       form interacts with RPS5. Interacts with FLS2.
CC       {ECO:0000269|PubMed:12947197, ECO:0000269|PubMed:17277084,
CC       ECO:0000269|PubMed:20413097}.
CC   -!- INTERACTION:
CC       Q9FE20; O64973: RPS5; NbExp=2; IntAct=EBI-2357898, EBI-15620767;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor
CC       {ECO:0000269|PubMed:22046960, ECO:0000269|PubMed:24225654}.
CC   -!- INDUCTION: Induced by flagellin (flg22). {ECO:0000269|PubMed:20413097}.
CC   -!- PTM: Cleaved by avrPphB in infected plant cells. Its cleavage serves as
CC       a signal that triggers the RPS5-mediated defense system.
CC       {ECO:0000269|PubMed:12947197, ECO:0000269|PubMed:17277084}.
CC   -!- PTM: Autophosphorylates (Probable). Autophosphorylation may be required
CC       to trigger the RPS5-mediated plant defense system. {ECO:0000305}.
CC   -!- PTM: Palmitoylation at Cys-3 and Cys-6 are required for plasma membrane
CC       location that is essential for the RPS5-mediated plant defense
CC       response. {ECO:0000269|PubMed:24225654}.
CC   -!- DISRUPTION PHENOTYPE: Reduction in H(2)O(2) accumulation and callose
CC       deposits. {ECO:0000269|PubMed:20413097}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; AF314176; AAG38109.1; -; mRNA.
DR   EMBL; AL391711; CAC05444.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED91858.1; -; Genomic_DNA.
DR   EMBL; AF372927; AAK50067.1; -; mRNA.
DR   EMBL; AY078037; AAL77738.1; -; mRNA.
DR   RefSeq; NP_196820.1; NM_121319.5.
DR   AlphaFoldDB; Q9FE20; -.
DR   SMR; Q9FE20; -.
DR   BioGRID; 16433; 2.
DR   DIP; DIP-53310N; -.
DR   IntAct; Q9FE20; 3.
DR   STRING; 3702.AT5G13160.1; -.
DR   iPTMnet; Q9FE20; -.
DR   SwissPalm; Q9FE20; -.
DR   PaxDb; Q9FE20; -.
DR   PRIDE; Q9FE20; -.
DR   ProteomicsDB; 236798; -.
DR   EnsemblPlants; AT5G13160.1; AT5G13160.1; AT5G13160.
DR   GeneID; 831155; -.
DR   Gramene; AT5G13160.1; AT5G13160.1; AT5G13160.
DR   KEGG; ath:AT5G13160; -.
DR   Araport; AT5G13160; -.
DR   TAIR; locus:2179857; AT5G13160.
DR   eggNOG; KOG1187; Eukaryota.
DR   HOGENOM; CLU_000288_21_0_1; -.
DR   InParanoid; Q9FE20; -.
DR   OMA; RIFRNED; -.
DR   OrthoDB; 684563at2759; -.
DR   PhylomeDB; Q9FE20; -.
DR   PRO; PR:Q9FE20; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FE20; baseline and differential.
DR   Genevisible; Q9FE20; AT.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:TAIR.
DR   GO; GO:0006952; P:defense response; TAS:TAIR.
DR   GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
DR   GO; GO:0002221; P:pattern recognition receptor signaling pathway; IMP:UniProtKB.
DR   GO; GO:0046777; P:protein autophosphorylation; IDA:TAIR.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Direct protein sequencing; Kinase; Lipoprotein;
KW   Membrane; Myristate; Nucleotide-binding; Palmitate; Phosphoprotein;
KW   Plant defense; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000305|PubMed:22046960"
FT   CHAIN           2..456
FT                   /note="Serine/threonine-protein kinase PBS1"
FT                   /id="PRO_0000086482"
FT   DOMAIN          86..363
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          368..456
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           292..296
FT                   /note="Recognition motif required for RPS5-mediated plant
FT                   resistance to P.syringae"
FT                   /evidence="ECO:0000269|PubMed:24225654"
FT   COMPBIAS        22..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        370..388
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        401..447
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        213
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         92..100
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         115
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   SITE            243..244
FT                   /note="Cleavage; by avrPphB"
FT   MOD_RES         21
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19376835"
FT   MOD_RES         160
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   MOD_RES         217
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   MOD_RES         247
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   MOD_RES         248
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   MOD_RES         253
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   MOD_RES         261
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000303|PubMed:22046960"
FT   LIPID           3
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000269|PubMed:24225654"
FT   LIPID           6
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000269|PubMed:24225654"
FT   MUTAGEN         2
FT                   /note="G->A: Slightly affects plasma membrane location.
FT                   Abolishes plasma membrane location; when associated with A-
FT                   3 and A-6."
FT                   /evidence="ECO:0000269|PubMed:22046960,
FT                   ECO:0000269|PubMed:24225654"
FT   MUTAGEN         3
FT                   /note="C->A: Affects plasma membrane location. Abolishes
FT                   plasma membrane location; when associated with A-2 and A-
FT                   6."
FT                   /evidence="ECO:0000269|PubMed:22046960,
FT                   ECO:0000269|PubMed:24225654"
FT   MUTAGEN         4
FT                   /note="F->A: Affects plasma membrane location."
FT                   /evidence="ECO:0000269|PubMed:22046960"
FT   MUTAGEN         6
FT                   /note="C->A: Affects plasma membrane location. Abolishes
FT                   plasma membrane location; when associated with A-2 and A-
FT                   3."
FT                   /evidence="ECO:0000269|PubMed:22046960,
FT                   ECO:0000269|PubMed:24225654"
FT   MUTAGEN         98
FT                   /note="G->E: In pbs1-5; strongly impairs RPS5-mediated
FT                   plant resistance to P.syringae."
FT                   /evidence="ECO:0000269|PubMed:24225654"
FT   MUTAGEN         103
FT                   /note="G->R: In pbs1-3; strongly impairs cleavage by
FT                   avrPphB and RPS5-mediated plant resistance to P.syringae."
FT                   /evidence="ECO:0000269|PubMed:24225654"
FT   MUTAGEN         115
FT                   /note="K->N: Abolishes kinase activity and RPS5-mediated
FT                   plant resistance to P.syringae."
FT                   /evidence="ECO:0000269|PubMed:12947197,
FT                   ECO:0000269|PubMed:17277084, ECO:0000269|PubMed:22372664"
FT   MUTAGEN         241
FT                   /note="G->A: Abolishes cleavage by avrPphB and RPS5-
FT                   mediated plant resistance to P.syringae."
FT                   /evidence="ECO:0000269|PubMed:12947197"
FT   MUTAGEN         242
FT                   /note="D->A: Strongly impairs cleavage by avrPphB and RPS5-
FT                   mediated plant resistance to P.syringae."
FT                   /evidence="ECO:0000269|PubMed:12947197"
FT   MUTAGEN         243
FT                   /note="K->A: Affects cleavage by avrPphB and RPS5-mediated
FT                   plant resistance to P.syringae."
FT                   /evidence="ECO:0000269|PubMed:12947197"
FT   MUTAGEN         244
FT                   /note="S->F: In pbs1-6; strongly impairs RPS5-mediated
FT                   plant resistance to P.syringae."
FT                   /evidence="ECO:0000269|PubMed:24225654"
FT   MUTAGEN         252
FT                   /note="G->R: In pbs1-2; strongly impairs RPS5-mediated
FT                   plant resistance to P.syringae."
FT                   /evidence="ECO:0000269|PubMed:11359614,
FT                   ECO:0000269|PubMed:17277084, ECO:0000269|PubMed:22372664"
FT   MUTAGEN         286
FT                   /note="G->D: In pbs1-4; strongly impairs cleavage by
FT                   avrPphB and RPS5-mediated plant resistance to P.syringae."
FT                   /evidence="ECO:0000269|PubMed:24225654"
SQ   SEQUENCE   456 AA;  50384 MW;  C167E4E3F47ACBC3 CRC64;
     MGCFSCFDSS DDEKLNPVDE SNHGQKKQSQ PTVSNNISGL PSGGEKLSSK TNGGSKRELL
     LPRDGLGQIA AHTFAFRELA AATMNFHPDT FLGEGGFGRV YKGRLDSTGQ VVAVKQLDRN
     GLQGNREFLV EVLMLSLLHH PNLVNLIGYC ADGDQRLLVY EFMPLGSLED HLHDLPPDKE
     ALDWNMRMKI AAGAAKGLEF LHDKANPPVI YRDFKSSNIL LDEGFHPKLS DFGLAKLGPT
     GDKSHVSTRV MGTYGYCAPE YAMTGQLTVK SDVYSFGVVF LELITGRKAI DSEMPHGEQN
     LVAWARPLFN DRRKFIKLAD PRLKGRFPTR ALYQALAVAS MCIQEQAATR PLIADVVTAL
     SYLANQAYDP SKDDSRRNRD ERGARLITRN DDGGGSGSKF DLEGSEKEDS PRETARILNR
     DINRERAVAE AKMWGESLRE KRRQSEQGTS ESNSTG
 
 
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