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C0LGT6 (EFR_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
LRR receptor-like serine/threonine-protein kinase EFR

EC=2.7.11.1
Alternative name(s):
Elongation factor Tu receptor
Short name=EF-Tu receptor
Gene names
Name:EFR
Ordered Locus Names:At5g20480
ORF Names:F7C8.70
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length1031 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Constitutes the pattern-recognition receptor (PPR) that determines the specific perception of elongation factor Tu (EF-Tu), a potent elicitor of the defense response to pathogen-associated molecular patterns (PAMPs). Reduces transformation by Rhizobium radiobacter probably by inducing plant defense during the interaction. Binding to the effector AvrPto1 from P.syringae blocks the downstream plant immune response while interaction with hopD2 decreases the phosphorylation level of EFR upon elf18 treatment. Specific endoplasmic reticulum quality control components (ERD2B, CRT3, UGGT and STT3A) are required for the biogenesis of EFR. Ref.6 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subunit structure

Binds to Pseudomonas syringae AvrPto1 and (via the kinase and cytoplasmic domains) to hopD2. Interacts with SERK3/BAK1, SERK4/BKK1, SERK1 and SERK2 in a specific ligand-induced manner. Ref.7 Ref.13 Ref.14

Subcellular location

Cell membrane; Single-pass type I membrane protein. Endomembrane system; Single-pass type I membrane protein Ref.9 Ref.11 Ref.14.

Domain

The last two LRR (561-597) are necessary for elf18 binding and functionality. Ref.11

Post-translational modification

Autophosphorylated after elicitation with elfl18. Autophosphorylation is inhibited by the binding with avrPto1. Phosphorylation at T-836 is required for immune signaling. Ref.7 Ref.14

Polyubiquitinated at the kinase domain mediated by P.syringae AvrPtoB.

Disruption phenotype

Enhanced susceptibility to R.radiobacter. Ref.6

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.

Contains 21 LRR (leucine-rich) repeats.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processPlant defense
   Cellular componentCell membrane
Membrane
   DomainLeucine-rich repeat
Repeat
Signal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Serine/threonine-protein kinase
Transferase
   PTMGlycoprotein
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdefense response signaling pathway, resistance gene-independent

Inferred from mutant phenotype Ref.6. Source: TAIR

detection of bacterium

Inferred from direct assay Ref.6. Source: TAIR

immune response-regulating signaling pathway

Inferred from mutant phenotype Ref.9. Source: TAIR

plant-type hypersensitive response

Inferred from mutant phenotype Ref.9. Source: TAIR

regulation of anion channel activity

Inferred from mutant phenotype PubMed 20113440. Source: TAIR

   Cellular_componentendomembrane system

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.7. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

transmembrane receptor protein kinase activity

Traceable author statement Ref.9. Source: TAIR

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RBG7Q032504EBI-8801168,EBI-1393626

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 10311007LRR receptor-like serine/threonine-protein kinase EFR
PRO_0000387508

Regions

Topological domain25 – 653629Extracellular Potential
Transmembrane654 – 67421Helical; Potential
Topological domain675 – 1031357Cytoplasmic Potential
Repeat98 – 12023LRR 1
Repeat122 – 14423LRR 2
Repeat146 – 16823LRR 3
Repeat170 – 19324LRR 4
Repeat194 – 21623LRR 5
Repeat218 – 24023LRR 6
Repeat242 – 26423LRR 7
Repeat267 – 28923LRR 8
Repeat291 – 31222LRR 9
Repeat315 – 33521LRR 10
Repeat345 – 36824LRR 11
Repeat370 – 39223LRR 12
Repeat394 – 41623LRR 13
Repeat418 – 44023LRR 14
Repeat442 – 46423LRR 15
Repeat466 – 48722LRR 16
Repeat490 – 51223LRR 17
Repeat514 – 53623LRR 18
Repeat538 – 56023LRR 19
Repeat561 – 58424LRR 20
Repeat585 – 59713LRR 21
Domain712 – 1001290Protein kinase
Nucleotide binding718 – 7269ATP By similarity

Sites

Active site8491Proton acceptor By similarity
Binding site7411ATP By similarity

Amino acid modifications

Modified residue7091Phosphothreonine By similarity
Modified residue7911Phosphotyrosine By similarity
Modified residue8361Phosphotyrosine Ref.14
Modified residue8971Phosphotyrosine Ref.14
Glycosylation281N-linked (GlcNAc...) Potential
Glycosylation551N-linked (GlcNAc...) Potential
Glycosylation951N-linked (GlcNAc...) Potential
Glycosylation1271N-linked (GlcNAc...) Potential
Glycosylation1431N-linked (GlcNAc...) Potential
Glycosylation1801N-linked (GlcNAc...) Potential
Glycosylation1911N-linked (GlcNAc...) Potential
Glycosylation2391N-linked (GlcNAc...) Potential
Glycosylation2881N-linked (GlcNAc...) Potential
Glycosylation3231N-linked (GlcNAc...) Potential
Glycosylation3291N-linked (GlcNAc...) Potential
Glycosylation3421N-linked (GlcNAc...) Potential
Glycosylation3661N-linked (GlcNAc...) Potential
Glycosylation4391N-linked (GlcNAc...) Potential
Glycosylation4781N-linked (GlcNAc...) Potential
Glycosylation5711N-linked (GlcNAc...) Potential
Glycosylation5901N-linked (GlcNAc...) Potential
Glycosylation6081N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis76 – 772IS → AA: No effect on elf18 sensitivity.
Mutagenesis81 – 822GG → AA: No effect on elf18 sensitivity.
Mutagenesis103 – 1064NLAD → ALAA: Insensitive to elf18.
Mutagenesis274 – 2752GT → AA: No effect on elf18 sensitivity.
Mutagenesis293 – 2942ER → AA: No effect on elf18 sensitivity.
Mutagenesis298 – 2992SS → AA: No effect on elf18 sensitivity.
Mutagenesis317 – 3182WW → AA: Decreased elf18 sensitivity.
Mutagenesis347 – 3482EY → AA: Decreased elf18 sensitivity.
Mutagenesis373 – 3753SLF → ALA: No effect on elf18 sensitivity.
Mutagenesis397 – 3993ELS → ALA: Decreased elf18 sensitivity.
Mutagenesis447 – 4493HLN → ALA: Insensitive to elf18.
Mutagenesis469 – 4735DLWMD → ALWMA: Insensitive to elf18.
Mutagenesis564 – 5685NVDFS → AVDFA: Decreased elf18 sensitivity. Ref.12
Mutagenesis588 – 5903NLN → ALA: Insensitive to elf18. Ref.12
Mutagenesis7021Y → F: No effect on elf18-triggered immunity. Ref.14
Mutagenesis7911Y → F: No effect on elf18-triggered immunity. Ref.14
Mutagenesis8361Y → F: Loss of elf18-triggered immunity, but no effect on the kinase activity. Ref.14
Mutagenesis8491D → N: Loss of kinase activity. Ref.14
Mutagenesis8751Y → F: No effect on elf18-triggered immunity. Ref.14
Mutagenesis8771Y → F: No effect on elf18-triggered immunity. Ref.14
Mutagenesis8971Y → F: No effect on elf18-triggered immunity. Ref.14
Mutagenesis9021Y → F: No effect on elf18-triggered immunity. Ref.14
Mutagenesis9151Y → F: No effect on elf18-triggered immunity. Ref.14
Mutagenesis9391Y → F: No effect on elf18-triggered immunity. Ref.14
Mutagenesis9441Y → F: No effect on elf18-triggered immunity. Ref.14
Mutagenesis9791Y → F: No effect on elf18-triggered immunity. Ref.14
Sequence conflict8931G → L in BAE98400. Ref.5
Sequence conflict9291K → E in AAL77697. Ref.3
Sequence conflict9291K → E in AAO64755. Ref.3

Sequences

Sequence LengthMass (Da)Tools
C0LGT6 [UniParc].

Last modified May 5, 2009. Version 1.
Checksum: E0E0AE671DA9124D

FASTA1,031113,353
        10         20         30         40         50         60 
MKLSFSLVFN ALTLLLQVCI FAQARFSNET DMQALLEFKS QVSENNKREV LASWNHSSPF 

        70         80         90        100        110        120 
CNWIGVTCGR RRERVISLNL GGFKLTGVIS PSIGNLSFLR LLNLADNSFG STIPQKVGRL 

       130        140        150        160        170        180 
FRLQYLNMSY NLLEGRIPSS LSNCSRLSTV DLSSNHLGHG VPSELGSLSK LAILDLSKNN 

       190        200        210        220        230        240 
LTGNFPASLG NLTSLQKLDF AYNQMRGEIP DEVARLTQMV FFQIALNSFS GGFPPALYNI 

       250        260        270        280        290        300 
SSLESLSLAD NSFSGNLRAD FGYLLPNLRR LLLGTNQFTG AIPKTLANIS SLERFDISSN 

       310        320        330        340        350        360 
YLSGSIPLSF GKLRNLWWLG IRNNSLGNNS SSGLEFIGAV ANCTQLEYLD VGYNRLGGEL 

       370        380        390        400        410        420 
PASIANLSTT LTSLFLGQNL ISGTIPHDIG NLVSLQELSL ETNMLSGELP VSFGKLLNLQ 

       430        440        450        460        470        480 
VVDLYSNAIS GEIPSYFGNM TRLQKLHLNS NSFHGRIPQS LGRCRYLLDL WMDTNRLNGT 

       490        500        510        520        530        540 
IPQEILQIPS LAYIDLSNNF LTGHFPEEVG KLELLVGLGA SYNKLSGKMP QAIGGCLSME 

       550        560        570        580        590        600 
FLFMQGNSFD GAIPDISRLV SLKNVDFSNN NLSGRIPRYL ASLPSLRNLN LSMNKFEGRV 

       610        620        630        640        650        660 
PTTGVFRNAT AVSVFGNTNI CGGVREMQLK PCIVQASPRK RKPLSVRKKV VSGICIGIAS 

       670        680        690        700        710        720 
LLLIIIVASL CWFMKRKKKN NASDGNPSDS TTLGMFHEKV SYEELHSATS RFSSTNLIGS 

       730        740        750        760        770        780 
GNFGNVFKGL LGPENKLVAV KVLNLLKHGA TKSFMAECET FKGIRHRNLV KLITVCSSLD 

       790        800        810        820        830        840 
SEGNDFRALV YEFMPKGSLD MWLQLEDLER VNDHSRSLTP AEKLNIAIDV ASALEYLHVH 

       850        860        870        880        890        900 
CHDPVAHCDI KPSNILLDDD LTAHVSDFGL AQLLYKYDRE SFLNQFSSAG VRGTIGYAAP 

       910        920        930        940        950        960 
EYGMGGQPSI QGDVYSFGIL LLEMFSGKKP TDESFAGDYN LHSYTKSILS GCTSSGGSNA 

       970        980        990       1000       1010       1020 
IDEGLRLVLQ VGIKCSEEYP RDRMRTDEAV RELISIRSKF FSSKTTITES PRDAPQSSPQ 

      1030 
EWMLNTDMHT M 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. expand/collapse author list , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-like protein kinase genes in Arabidopsis thaliana."
Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.
BMC Genomics 11:19-19(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 893-1031.
Strain: cv. Columbia.
[6]"Perception of the bacterial PAMP EF-Tu by the receptor EFR restricts Agrobacterium-mediated transformation."
Zipfel C., Kunze G., Chinchilla D., Caniard A., Jones J.D.G., Boller T., Felix G.
Cell 125:749-760(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[7]"Pseudomonas syringae effector AvrPto blocks innate immunity by targeting receptor kinases."
Xiang T., Zong N., Zou Y., Wu Y., Zhang J., Xing W., Li Y., Tang X., Zhu L., Chai J., Zhou J.-M.
Curr. Biol. 18:74-80(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PSEUDOMONAS SYRINGAE AVRPTO1, AUTOPHOSPHORYLATION.
[8]"Plant pattern-recognition receptor FLS2 is directed for degradation by the bacterial ubiquitin ligase AvrPtoB."
Goehre V., Spallek T., Haeweker H., Mersmann S., Mentzel T., Boller T., de Torres M., Mansfield J.W., Robatzek S.
Curr. Biol. 18:1824-1832(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION BY AVRPTOB.
[9]"Receptor quality control in the endoplasmic reticulum for plant innate immunity."
Saijo Y., Tintor N., Lu X., Rauf P., Pajerowska-Mukhtar K., Haeweker H., Dong X., Robatzek S., Schulze-Lefert P.
EMBO J. 28:3439-3449(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[10]"Specific ER quality control components required for biogenesis of the plant innate immune receptor EFR."
Li J., Zhao-Hui C., Batoux M., Nekrasov V., Roux M., Chinchilla D., Zipfel C., Jones J.D.
Proc. Natl. Acad. Sci. U.S.A. 106:15973-15978(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Arabidopsis thaliana pattern recognition receptors for bacterial elongation factor Tu and flagellin can be combined to form functional chimeric receptors."
Albert M., Jehle A.K., Mueller K., Eisele C., Lipschis M., Felix G.
J. Biol. Chem. 285:19035-19042(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DOMAIN, SUBCELLULAR LOCATION.
[12]"LRR conservation mapping to predict functional sites within protein leucine-rich repeat domains."
Helft L., Reddy V., Chen X., Koller T., Federici L., Fernandez-Recio J., Gupta R., Bent A.
PLoS ONE 6:E21614-E21614(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING, MUTAGENESIS OF 76-ILE-SER-77; 81-GLY-GLY-82; 103-ASN--ASP-106; 274-GLY-THR-275; 293-GLU-ARG-294; 298-SER-SER-299; 317-TRP-TRP-318; 347-GLU-TYR-348; 373-SER--PHE-375; 397-GLU--SER-399; 447-HIS--ASN-449; 469-ASP--ASP-473; 564-ASN--SER-568 AND 588-ASN--ASN-590.
[13]"The Arabidopsis leucine-rich repeat receptor-like kinases BAK1/SERK3 and BKK1/SERK4 are required for innate immunity to hemibiotrophic and biotrophic pathogens."
Roux M., Schwessinger B., Albrecht C., Chinchilla D., Jones A., Holton N., Malinovsky F.G., Tor M., de Vries S., Zipfel C.
Plant Cell 23:2440-2455(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SERK3/BAK1; SERK4/BKK1; SERK1 AND SERK2.
Strain: cv. Columbia.
[14]"A bacterial tyrosine phosphatase inhibits plant pattern recognition receptor activation."
Macho A.P., Schwessinger B., Ntoukakis V., Brutus A., Segonzac C., Roy S., Kadota Y., Oh M.H., Sklenar J., Derbyshire P., Lozano-Duran R., Malinovsky F.G., Monaghan J., Menke F.L., Huber S.C., He S.Y., Zipfel C.
Science 343:1509-1512(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT TYR-836 AND TYR-897, MUTAGENESIS OF TYR-702; TYR-791; TYR-836; ASP-849; TYR-875; TYR-877; TYR-897; TYR-902; TYR-915; TYR-939; TYR-944 AND TYR-979, SUBCELLULAR LOCATION, INTERACTION WITH HOPD2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF296833 Genomic DNA. No translation available.
CP002688 Genomic DNA. Translation: AED92850.1.
AY075690 mRNA. Translation: AAL77697.1.
BT005820 mRNA. Translation: AAO64755.1.
FJ708780 mRNA. Translation: ACN59371.1.
AK226237 mRNA. Translation: BAE98400.1.
RefSeqNP_197548.1. NM_122055.4.
UniGeneAt.31176.

3D structure databases

ProteinModelPortalC0LGT6.
SMRC0LGT6. Positions 27-622, 698-993.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid17446. 1 interaction.
IntActC0LGT6. 1 interaction.
STRING3702.AT5G20480.1-P.

Proteomic databases

PaxDbC0LGT6.
PRIDEC0LGT6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G20480.1; AT5G20480.1; AT5G20480.
GeneID832170.
KEGGath:AT5G20480.

Organism-specific databases

GeneFarm2543. 56.
TAIRAT5G20480.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000116551.
InParanoidQ8S9I3.
KOK13428.
OMASGRIPRY.
PhylomeDBC0LGT6.

Enzyme and pathway databases

BioCycARA:AT5G20480-MONOMER.

Family and domain databases

Gene3D2.60.120.200. 1 hit.
InterProIPR013320. ConA-like_subgrp.
IPR011009. Kinase-like_dom.
IPR001611. Leu-rich_rpt.
IPR013210. LRR-contain_N2.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00560. LRR_1. 2 hits.
PF13855. LRR_8. 2 hits.
PF08263. LRRNT_2. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROC0LGT6.

Entry information

Entry nameEFR_ARATH
AccessionPrimary (citable) accession number: C0LGT6
Secondary accession number(s): Q0WWU8, Q8S9I3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: May 5, 2009
Last modified: July 9, 2014
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names