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Protein

Methionine--tRNA ligase, cytoplasmic

Gene

At4g13780

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met).Curated

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei351 – 3511ATPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding, tRNA-binding

Enzyme and pathway databases

BioCyciARA:AT4G13780-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine--tRNA ligase, cytoplasmicCurated (EC:6.1.1.10Curated)
Alternative name(s):
Methionyl-tRNA synthetaseCurated
Short name:
MetRSCurated
Gene namesi
Ordered Locus Names:At4g13780
ORF Names:F18A5.170
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G13780.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 797797Methionine--tRNA ligase, cytoplasmicPRO_0000139266Add
BLAST

Proteomic databases

PaxDbiQ9SVN5.
PRIDEiQ9SVN5.

PTM databases

iPTMnetiQ9SVN5.

Expressioni

Gene expression databases

GenevisibleiQ9SVN5. AT.

Interactioni

Protein-protein interaction databases

BioGridi12309. 2 interactions.
STRINGi3702.AT4G13780.1.

Structurei

3D structure databases

ProteinModelPortaliQ9SVN5.
SMRiQ9SVN5. Positions 20-593, 634-797.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini635 – 738104tRNA-bindingPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi26 – 3611"HIGH" regionCuratedAdd
BLAST
Motifi348 – 3525"KMSKS" regionCurated

Sequence similaritiesi

Contains 1 tRNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410JTYU. Eukaryota.
KOG1247. Eukaryota.
KOG2241. Eukaryota.
COG0073. LUCA.
COG0143. LUCA.
HOGENOMiHOG000200402.
InParanoidiQ9SVN5.
KOiK01874.
OMAiAVHSEVY.
PhylomeDBiQ9SVN5.

Family and domain databases

Gene3Di1.10.730.10. 1 hit.
2.20.28.20. 1 hit.
2.40.50.140. 1 hit.
3.40.50.620. 2 hits.
HAMAPiMF_00098. Met_tRNA_synth_type1.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR023458. Met-tRNA_ligase_1.
IPR014758. Met-tRNA_synth.
IPR015413. Methionyl/Leucyl_tRNA_Synth.
IPR029038. MetRS_Zn.
IPR012340. NA-bd_OB-fold.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002547. tRNA-bd_dom.
IPR009080. tRNAsynth_Ia_anticodon-bd.
[Graphical view]
PfamiPF09334. tRNA-synt_1g. 1 hit.
PF01588. tRNA_bind. 1 hit.
[Graphical view]
PRINTSiPR01041. TRNASYNTHMET.
SUPFAMiSSF47323. SSF47323. 1 hit.
SSF50249. SSF50249. 1 hit.
SSF57770. SSF57770. 1 hit.
TIGRFAMsiTIGR00398. metG. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
PS50886. TRBD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9SVN5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEDDGKSSPK LPIPGKRNIL ITSALPYVNN VPHLGNIIGC VLSADVYARY
60 70 80 90 100
CRLRGYNAIY ICGTDEYGTA TETKALEENC TPKEICDKYH AIHKEVYDWF
110 120 130 140 150
GISFDKFGRT STPEQTEVCQ AIFNKLWDNK WLSENTMQQL YCDTCKKFLA
160 170 180 190 200
DRLVEGSCPF EGCNYDSARG DQCEKCGKLL NPTELKDPKC KVCQNTPRIR
210 220 230 240 250
DTDHLFIELP LLKDRLEAYI KKTSVTGSWS QNAIQTTNAW LRDGLRQRCI
260 270 280 290 300
TRDLKWGVPV PHEKYKDKVF YVWFDAPIGY VSITSCYTSE WEKWWKNPEN
310 320 330 340 350
VELYQFMGKD NVPFHTVMFP STQLGTEENW TLMKTISVTE YLNYEDGKFS
360 370 380 390 400
KSKGVGVFGN DVKDTNIPVE VWRYYLLTNR PEVSDTSFSW TDLQAKLNGE
410 420 430 440 450
LLSNLGNFVN RVLSFIAKPD NAGYGSVIPD AHDAESHSLT KSLAEKVEKF
460 470 480 490 500
VAEYVEAMEK VKLKQGLKTA MLISSEGNYY LQASQFWKLY KEDKPLCAVV
510 520 530 540 550
IRTAAGLVHL LAQLLEPFMP SFSCEVFKQL NLPPQFSLSD ERGEVLLASR
560 570 580 590 600
PWDILPPSHR IGTPQPLFKE LENDEVARYR EKFAGSQSDR RARDEAANLA
610 620 630 640 650
DQLNKTKLSD AKKQKASSKG GGKPKPQPAA DREITMARLD IRVGKIVKAE
660 670 680 690 700
KHPKADALYV EEIDVGGGEI RTVVSGLVKY IPLEEMQNRM VCVLCNLKPA
710 720 730 740 750
KMRDIVSQAM VLAASSSDGS KVELVEPPKT ANIGERVTFP GFEGEPDDVL
760 770 780 790
NPKKKVWETL LVDLNTKENL VACYKDVPFT TSAGVCKVSS ISNGTIR
Length:797
Mass (Da):89,854
Last modified:May 1, 2000 - v1
Checksum:iB0F523C2E0C1017F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL035528 Genomic DNA. Translation: CAB36842.1.
AL161537 Genomic DNA. Translation: CAB78420.1.
CP002687 Genomic DNA. Translation: AEE83324.1.
AY064009 mRNA. Translation: AAL36365.1.
AY091454 mRNA. Translation: AAM14393.1.
PIRiT05247.
RefSeqiNP_193114.1. NM_117452.4.
UniGeneiAt.27407.

Genome annotation databases

EnsemblPlantsiAT4G13780.1; AT4G13780.1; AT4G13780.
GeneIDi827012.
GrameneiAT4G13780.1; AT4G13780.1; AT4G13780.
KEGGiath:AT4G13780.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL035528 Genomic DNA. Translation: CAB36842.1.
AL161537 Genomic DNA. Translation: CAB78420.1.
CP002687 Genomic DNA. Translation: AEE83324.1.
AY064009 mRNA. Translation: AAL36365.1.
AY091454 mRNA. Translation: AAM14393.1.
PIRiT05247.
RefSeqiNP_193114.1. NM_117452.4.
UniGeneiAt.27407.

3D structure databases

ProteinModelPortaliQ9SVN5.
SMRiQ9SVN5. Positions 20-593, 634-797.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi12309. 2 interactions.
STRINGi3702.AT4G13780.1.

PTM databases

iPTMnetiQ9SVN5.

Proteomic databases

PaxDbiQ9SVN5.
PRIDEiQ9SVN5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G13780.1; AT4G13780.1; AT4G13780.
GeneIDi827012.
GrameneiAT4G13780.1; AT4G13780.1; AT4G13780.
KEGGiath:AT4G13780.

Organism-specific databases

TAIRiAT4G13780.

Phylogenomic databases

eggNOGiENOG410JTYU. Eukaryota.
KOG1247. Eukaryota.
KOG2241. Eukaryota.
COG0073. LUCA.
COG0143. LUCA.
HOGENOMiHOG000200402.
InParanoidiQ9SVN5.
KOiK01874.
OMAiAVHSEVY.
PhylomeDBiQ9SVN5.

Enzyme and pathway databases

BioCyciARA:AT4G13780-MONOMER.

Miscellaneous databases

PROiQ9SVN5.

Gene expression databases

GenevisibleiQ9SVN5. AT.

Family and domain databases

Gene3Di1.10.730.10. 1 hit.
2.20.28.20. 1 hit.
2.40.50.140. 1 hit.
3.40.50.620. 2 hits.
HAMAPiMF_00098. Met_tRNA_synth_type1.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR023458. Met-tRNA_ligase_1.
IPR014758. Met-tRNA_synth.
IPR015413. Methionyl/Leucyl_tRNA_Synth.
IPR029038. MetRS_Zn.
IPR012340. NA-bd_OB-fold.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002547. tRNA-bd_dom.
IPR009080. tRNAsynth_Ia_anticodon-bd.
[Graphical view]
PfamiPF09334. tRNA-synt_1g. 1 hit.
PF01588. tRNA_bind. 1 hit.
[Graphical view]
PRINTSiPR01041. TRNASYNTHMET.
SUPFAMiSSF47323. SSF47323. 1 hit.
SSF50249. SSF50249. 1 hit.
SSF57770. SSF57770. 1 hit.
TIGRFAMsiTIGR00398. metG. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
PS50886. TRBD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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.
  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.
    , 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. "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: SUBCELLULAR LOCATION.
  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.

Entry informationi

Entry nameiSYMC_ARATH
AccessioniPrimary (citable) accession number: Q9SVN5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: May 1, 2000
Last modified: July 6, 2016
This is version 120 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.