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Protein

Arginine--tRNA ligase, chloroplastic/mitochondrial

Gene

EMB1027

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis.By similarity

Catalytic activityi

ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg).Curated

GO - Molecular functioni

GO - Biological processi

  • arginyl-tRNA aminoacylation Source: GO_Central
  • embryo development ending in seed dormancy Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT4G26300-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Arginine--tRNA ligase, chloroplastic/mitochondrialCurated (EC:6.1.1.19Curated)
Alternative name(s):
Arginyl-tRNA synthetaseCurated
Short name:
ArgRSCurated
Protein EMBRYO DEFECTIVE 10271 Publication
Gene namesi
Name:EMB10271 Publication
Ordered Locus Names:At4g26300Imported
ORF Names:T25K17.110Imported
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G26300.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • chloroplast stroma Source: TAIR
  • mitochondrion Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Mitochondrion, Plastid

Pathology & Biotechi

Disruption phenotypei

Embryo defective. Developmental arrest of the embryo at the globular stage.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5353Chloroplast and mitochondrionCombined sourcesAdd
BLAST
Chaini54 – 642589Arginine--tRNA ligase, chloroplastic/mitochondrialCuratedPRO_0000433552Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei54 – 541N-acetylalanineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiO23247.
PRIDEiO23247.

Expressioni

Gene expression databases

GenevisibleiO23247. AT.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT4G26300.1.

Structurei

3D structure databases

ProteinModelPortaliO23247.
SMRiO23247. Positions 62-642.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi190 – 20112"HIGH" regionCuratedAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG4426. Eukaryota.
COG0018. LUCA.
HOGENOMiHOG000247212.
InParanoidiO23247.
KOiK01887.
OMAiKAWELIC.
PhylomeDBiO23247.

Family and domain databases

Gene3Di1.10.730.10. 1 hit.
3.30.1360.70. 1 hit.
3.40.50.620. 1 hit.
HAMAPiMF_00123. Arg_tRNA_synth.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR001278. Arg-tRNA-ligase.
IPR005148. Arg-tRNA-synth_N.
IPR008909. DALR_anticod-bd.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
[Graphical view]
PANTHERiPTHR11956. PTHR11956. 1 hit.
PfamiPF03485. Arg_tRNA_synt_N. 1 hit.
PF05746. DALR_1. 1 hit.
PF00750. tRNA-synt_1d. 1 hit.
[Graphical view]
PRINTSiPR01038. TRNASYNTHARG.
SMARTiSM01016. Arg_tRNA_synt_N. 1 hit.
SM00836. DALR_1. 1 hit.
[Graphical view]
SUPFAMiSSF47323. SSF47323. 1 hit.
SSF55190. SSF55190. 1 hit.
TIGRFAMsiTIGR00456. argS. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O23247-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFIFPKDENR RETLTTKLRF SADHLTFTTV TEKLRATAWR FAFSSRAKSV
60 70 80 90 100
VAMAANEEFT GNLKRQLAKL FDVSLKLTVP DEPSVEPLVA ASALGKFGDY
110 120 130 140 150
QCNNAMGLWS IIKGKGTQFK GPPAVGQALV KSLPTSEMVE SCSVAGPGFI
160 170 180 190 200
NVVLSAKWMA KSIENMLIDG VDTWAPTLSV KRAVVDFSSP NIAKEMHVGH
210 220 230 240 250
LRSTIIGDTL ARMLEYSHVE VLRRNHVGDW GTQFGMLIEY LFEKFPDTDS
260 270 280 290 300
VTETAIGDLQ VFYKASKHKF DLDEAFKEKA QQAVVRLQGG DPVYRKAWAK
310 320 330 340 350
ICDISRTEFA KVYQRLRVEL EEKGESFYNP HIAKVIEELN SKGLVEESEG
360 370 380 390 400
ARVIFLEGFD IPLMVVKSDG GFNYASTDLT ALWYRLNEEK AEWIIYVTDV
410 420 430 440 450
GQQQHFNMFF KAARKAGWLP DNDKTYPRVN HVGFGLVLGE DGKRFRTRAT
460 470 480 490 500
DVVRLVDLLD EAKTRSKLAL IERGKDKEWT PEELDQTAEA VGYGAVKYAD
510 520 530 540 550
LKNNRLTNYT FSFDQMLNDK GNTAVYLLYA HARICSIIRK SGKDIDELKK
560 570 580 590 600
TGKLALDHAD ERALGLHLLR FAETVEEACT NLLPSVLCEY LYNLSEHFTR
610 620 630 640
FYSNCQVNGS PEETSRLLLC EATAIVMRKC FHLLGITPVY KI
Length:642
Mass (Da):72,387
Last modified:January 1, 1998 - v1
Checksum:i0CE2674AE2BBEEFC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z98760 Genomic DNA. Translation: CAB11468.1.
AL049171 Genomic DNA. Translation: CAB38959.1.
AL161565 Genomic DNA. Translation: CAB79485.1.
CP002687 Genomic DNA. Translation: AEE85182.1.
PIRiT06014.
RefSeqiNP_194360.1. NM_118763.3.
UniGeneiAt.42946.
At.75603.

Genome annotation databases

EnsemblPlantsiAT4G26300.1; AT4G26300.1; AT4G26300.
GeneIDi828736.
GrameneiAT4G26300.1; AT4G26300.1; AT4G26300.
KEGGiath:AT4G26300.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z98760 Genomic DNA. Translation: CAB11468.1.
AL049171 Genomic DNA. Translation: CAB38959.1.
AL161565 Genomic DNA. Translation: CAB79485.1.
CP002687 Genomic DNA. Translation: AEE85182.1.
PIRiT06014.
RefSeqiNP_194360.1. NM_118763.3.
UniGeneiAt.42946.
At.75603.

3D structure databases

ProteinModelPortaliO23247.
SMRiO23247. Positions 62-642.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT4G26300.1.

Proteomic databases

PaxDbiO23247.
PRIDEiO23247.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G26300.1; AT4G26300.1; AT4G26300.
GeneIDi828736.
GrameneiAT4G26300.1; AT4G26300.1; AT4G26300.
KEGGiath:AT4G26300.

Organism-specific databases

TAIRiAT4G26300.

Phylogenomic databases

eggNOGiKOG4426. Eukaryota.
COG0018. LUCA.
HOGENOMiHOG000247212.
InParanoidiO23247.
KOiK01887.
OMAiKAWELIC.
PhylomeDBiO23247.

Enzyme and pathway databases

BioCyciARA:AT4G26300-MONOMER.

Miscellaneous databases

PROiO23247.

Gene expression databases

GenevisibleiO23247. AT.

Family and domain databases

Gene3Di1.10.730.10. 1 hit.
3.30.1360.70. 1 hit.
3.40.50.620. 1 hit.
HAMAPiMF_00123. Arg_tRNA_synth.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR001278. Arg-tRNA-ligase.
IPR005148. Arg-tRNA-synth_N.
IPR008909. DALR_anticod-bd.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
[Graphical view]
PANTHERiPTHR11956. PTHR11956. 1 hit.
PfamiPF03485. Arg_tRNA_synt_N. 1 hit.
PF05746. DALR_1. 1 hit.
PF00750. tRNA-synt_1d. 1 hit.
[Graphical view]
PRINTSiPR01038. TRNASYNTHARG.
SMARTiSM01016. Arg_tRNA_synt_N. 1 hit.
SM00836. DALR_1. 1 hit.
[Graphical view]
SUPFAMiSSF47323. SSF47323. 1 hit.
SSF55190. SSF55190. 1 hit.
TIGRFAMsiTIGR00456. argS. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Duplicated arginyl-tRNA synthetase genes in Arabidopsis thaliana."
    Small I.D., Lancelin D.
    Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Requirement of aminoacyl-tRNA synthetases for gametogenesis and embryo development in Arabidopsis."
    Berg M., Rogers R., Muralla R., Meinke D.
    Plant J. 44:866-878(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  5. "Dual targeting is the rule for organellar aminoacyl-tRNA synthetases in Arabidopsis thaliana."
    Duchene A.-M., Giritch A., Hoffmann B., Cognat V., Lancelin D., Peeters N.M., Zaepfel M., Marechal-Drouard L., Small I.D.
    Proc. Natl. Acad. Sci. U.S.A. 102:16484-16489(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  6. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-54, CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER MET-53, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSYRM_ARATH
AccessioniPrimary (citable) accession number: O23247
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 22, 2015
Last sequence update: January 1, 1998
Last modified: February 17, 2016
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.