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Protein

Aspartate--tRNA ligase 2, cytoplasmic

Gene

IBI1

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

Functioni

Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA (By similarity). Involved in the perception of beta-aminobutyric acid (BABA) and required for BABA priming effect in disease resistance (PubMed:24776930).By similarity1 Publication

Catalytic activityi

ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp).Curated

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei286 – 2861AspartateBy similarity
Binding sitei330 – 3301AspartateBy similarity
Metal bindingi481 – 4811Magnesium 2By similarity
Metal bindingi481 – 4811Magnesium 3By similarity
Binding sitei481 – 4811ATPBy similarity
Metal bindingi484 – 4841Magnesium 2By similarity
Binding sitei484 – 4841AspartateBy similarity
Binding sitei488 – 4881AspartateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi110 – 19586OBSequence analysisAdd
BLAST
Nucleotide bindingi330 – 3323ATPBy similarity
Nucleotide bindingi338 – 3403ATPBy similarity
Nucleotide bindingi529 – 5324ATPBy similarity

GO - Molecular functioni

  • aspartate-tRNA ligase activity Source: TAIR
  • ATP binding Source: UniProtKB-KW
  • DNA binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • aspartyl-tRNA aminoacylation Source: InterPro
  • defense response to fungus Source: TAIR
  • response to cadmium ion Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, DNA-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT4G31180-MONOMER.
ARA:GQT-63-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartate--tRNA ligase 2, cytoplasmicCurated (EC:6.1.1.12Curated)
Alternative name(s):
Aspartyl-tRNA synthetaseCurated
Short name:
AspRSCurated
Protein IMPAIRED IN BABA-INDUCED DISEASE IMMUNITY 11 Publication
Gene namesi
Name:IBI11 Publication
Ordered Locus Names:At4g31180Imported
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G31180.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: TAIR
  • endoplasmic reticulum Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 558557Aspartate--tRNA ligase 2, cytoplasmicPRO_0000433560Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ9M084.

Expressioni

Gene expression databases

GenevisibleiQ9M084. AT.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT4G31180.1.

Structurei

3D structure databases

ProteinModelPortaliQ9M084.
SMRiQ9M084. Positions 65-558.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni308 – 3114AspartateBy similarity

Sequence similaritiesi

Contains 1 OB DNA-binding domain.Sequence analysis

Phylogenomic databases

eggNOGiKOG0556. Eukaryota.
COG0017. LUCA.
HOGENOMiHOG000226032.
KOiK01876.
OMAiMEIRKHY.
PhylomeDBiQ9M084.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
InterProiIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II.
IPR004523. Asp-tRNA_synthase_arc.
IPR002312. Asp/Asn-tRNA-synth_IIb.
IPR012340. NA-bd_OB-fold.
IPR004365. NA-bd_OB_tRNA.
[Graphical view]
PANTHERiPTHR22594. PTHR22594. 2 hits.
PTHR22594:SF33. PTHR22594:SF33. 2 hits.
PfamiPF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti-codon. 1 hit.
[Graphical view]
PRINTSiPR01042. TRNASYNTHASP.
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00458. aspS_nondisc. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9M084-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSESEIPPL SSSTAAAEES GEKTSKKAAK KEAAKLEKLR RRQEQEEATR
60 70 80 90 100
RTASISLEEN DEFSNNYGDV TLTELQSSAD PKAGKWIEAV EGKEWTDVSD
110 120 130 140 150
LVEEMLESEV LIRGRVHTNR PTSNKLGFVV LRESGSTVQC VVSQSEKTKV
160 170 180 190 200
GANMVKYLKQ LSRESFVDVI GVVTLPKEPL TGTTQQVEIQ VRKVYCINKS
210 220 230 240 250
LAKLPLSVED AARSEADIEA SLQTPSPAAR VNQDTRLNYR VLDLRTPANQ
260 270 280 290 300
AIFQLQYEVE YAFREKLRFK NFVGIHTPKL MAGSSEGGSA VFRLEYKGQP
310 320 330 340 350
ACLAQSPQLH KQMAICGDLR RVFEVGPVFR AEDSFTHRHL CEFVGLDVEM
360 370 380 390 400
EIRKHYSEIM DLVDELFVFI FTSLNERCKK ELQAVGKQYP FEPLKFLPKT
410 420 430 440 450
LRLTFEEGVQ MLKEAGVEVD PLGDLNTESE RKLGQLVLEK YNTEFYILHR
460 470 480 490 500
YPKAVRPFYT MTCADNPLYS NSFDVFIRGE EIISGAQRVH IPEVLEQRAG
510 520 530 540 550
ECGIDVKTIS TYIDSFRYGA PLHGGFGVGL ERVVMLFCAL NNIRKTSLFP

RDPQRLSP
Length:558
Mass (Da):62,918
Last modified:October 1, 2000 - v1
Checksum:i598518C65AD9A4B3
GO

Sequence cautioni

The sequence AAL61938.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL161578 Genomic DNA. Translation: CAB79836.1.
CP002687 Genomic DNA. Translation: AEE85872.1.
CP002687 Genomic DNA. Translation: AEE85873.1.
AK317607 mRNA. Translation: BAH20270.1.
AY072331 mRNA. Translation: AAL61938.1. Sequence problems.
BT002567 mRNA. Translation: AAO00927.1.
PIRiT10672.
RefSeqiNP_194847.3. NM_119268.4.
NP_849558.1. NM_179227.2.
UniGeneiAt.4593.

Genome annotation databases

EnsemblPlantsiAT4G31180.1; AT4G31180.1; AT4G31180.
AT4G31180.2; AT4G31180.2; AT4G31180.
GeneIDi829246.
GrameneiAT4G31180.1; AT4G31180.1; AT4G31180.
AT4G31180.2; AT4G31180.2; AT4G31180.
KEGGiath:AT4G31180.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL161578 Genomic DNA. Translation: CAB79836.1.
CP002687 Genomic DNA. Translation: AEE85872.1.
CP002687 Genomic DNA. Translation: AEE85873.1.
AK317607 mRNA. Translation: BAH20270.1.
AY072331 mRNA. Translation: AAL61938.1. Sequence problems.
BT002567 mRNA. Translation: AAO00927.1.
PIRiT10672.
RefSeqiNP_194847.3. NM_119268.4.
NP_849558.1. NM_179227.2.
UniGeneiAt.4593.

3D structure databases

ProteinModelPortaliQ9M084.
SMRiQ9M084. Positions 65-558.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT4G31180.1.

Proteomic databases

PaxDbiQ9M084.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G31180.1; AT4G31180.1; AT4G31180.
AT4G31180.2; AT4G31180.2; AT4G31180.
GeneIDi829246.
GrameneiAT4G31180.1; AT4G31180.1; AT4G31180.
AT4G31180.2; AT4G31180.2; AT4G31180.
KEGGiath:AT4G31180.

Organism-specific databases

TAIRiAT4G31180.

Phylogenomic databases

eggNOGiKOG0556. Eukaryota.
COG0017. LUCA.
HOGENOMiHOG000226032.
KOiK01876.
OMAiMEIRKHY.
PhylomeDBiQ9M084.

Enzyme and pathway databases

BioCyciARA:AT4G31180-MONOMER.
ARA:GQT-63-MONOMER.

Miscellaneous databases

PROiQ9M084.

Gene expression databases

GenevisibleiQ9M084. AT.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
InterProiIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II.
IPR004523. Asp-tRNA_synthase_arc.
IPR002312. Asp/Asn-tRNA-synth_IIb.
IPR012340. NA-bd_OB-fold.
IPR004365. NA-bd_OB_tRNA.
[Graphical view]
PANTHERiPTHR22594. PTHR22594. 2 hits.
PTHR22594:SF33. PTHR22594:SF33. 2 hits.
PfamiPF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti-codon. 1 hit.
[Graphical view]
PRINTSiPR01042. TRNASYNTHASP.
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00458. aspS_nondisc. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 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. "Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs."
    Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K.
    DNA Res. 16:155-164(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "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] OF 107-558 AND 154-558.
    Strain: cv. Columbia.
  5. "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.
  6. "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.
  7. "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 SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: FUNCTION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiSYDC2_ARATH
AccessioniPrimary (citable) accession number: Q9M084
Secondary accession number(s): Q8VYA0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 22, 2015
Last sequence update: October 1, 2000
Last modified: February 17, 2016
This is version 122 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.