Reviewed, UniProtKB/Swiss-Prot O48593 (SYNO_ARATH)

Names and origin

Protein names

Recommended name:
    Asparaginyl-tRNA synthetase, chloroplastic/mitochondrial
    EC=6.1.1.22
Alternative name(s):
    Asparagine--tRNA ligase
      Short name=AsnRS

Gene names

Name:	SYNO
Synonyms:	NS1
Ordered Locus Names:	At4g17300
ORF Names:	dl4685w

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	567 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + L-asparaginyl-tRNA(Asn).
Subcellular location	Plastid › chloroplast. Mitochondrion. Ref.4
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family.
Sequence caution	The sequence CAB10511.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAB78733.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Chloroplast Mitochondrion Plastid
Domain	Transit peptide
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	asparaginyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro aspartyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro ovule development Inferred from mutant phenotype. Source: TAIR
Cellular component	chloroplast Inferred from direct assay. Source: TAIR mitochondrion Inferred from direct assay. Source: TAIR
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW asparagine-tRNA ligase activity Inferred from electronic annotation. Source: EC aspartate-tRNA ligase activity Inferred from electronic annotation. Source: InterPro nucleic acid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Chloroplast and mitochondrion Potential
	Chain	? – 567		Asparaginyl-tRNA synthetase, chloroplastic/mitochondrial		PRO_0000035800
Experimental info
	Sequence conflict	279	1	N → Y in CAA10904. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	O48593-1 [UniParc]. Last modified November 9, 2004. Version 3. Checksum: D5CAE4EBB7780264	FASTA	567	63,698
	10 20 30 40 50 60 MAATFLPATS LRLTQNSTLR FLSFFTISNP SYSLFRPLRR RVLPPFDAFP ANSRRRCFCT 70 80 90 100 110 120 AVSESLGSGD GNKVESYEKR FGSKVGEFRK KLRIAEVKGG ADEGLSRVGQ SLNIMGWVRT 130 140 150 160 170 180 LRSQSSVTFI EINDGSCLSN LQCVMTSDAE GYDQVESGSI LTGASVSVQG TIVASQGTKQ 190 200 210 220 230 240 KVELKVEKII VVGECDSSYP IQKKRVSREF LRTKAHLRPR TNTFGAVARV RNTLAYATHK 250 260 270 280 290 300 FFQESGFVWV ASPIITASDC EGAGEQFCVT TLIPSSHENT DTSIDAIPKT KGGLIDWSQD 310 320 330 340 350 360 FFGKPAFLTV SGQLNGETYA TALSDVYTFG PTFRAENSNT SRHLAEFWMI EPELAFADLD 370 380 390 400 410 420 DDMACATAYL QYVVKYVLDN CKEDMEFFDT WIEKGIIRRL SDVAEKEFLQ LGYTDAIEIL 430 440 450 460 470 480 LKANKKFDFP VKWGLDLQSE HERYITEEAF GGRPVIIRDY PKEIKAFYMR ENDDGKTVAA 490 500 510 520 530 540 MDMLVPRIGE LIGGSQREER LEVLEARLDE LKLNKESYWW YLDLRRYGSV PHAGFGLGFE 550 560 RLVQFVTGID NIRDVIPFPR TPASAEF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis thaliana." Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C., Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E. , Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A., Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N. Nature 391:485-488(1998) [PubMed: 9461215] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[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: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Structure and expression of an asparaginyl-tRNA synthetase gene located on chromosome IV of Arabidopsis thaliana and adjacent to a novel large gene of 15 exons." Aubourg S., Cheron A., Kreis M., Lecharny A. Biochim. Biophys. Acta 1398:225-231(1998) [PubMed: 9655910] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-566. Strain: cv. Columbia.
[4]	"Duplication and quadruplication of Arabidopsis thaliana cysteinyl- and asparaginyl-tRNA synthetase genes of organellar origin." Peeters N.M., Chapron A., Giritch A., Grandjean O., Lancelin D., Lhomme T., Vivrel A., Small I. J. Mol. Evol. 50:413-423(2000) [PubMed: 10824085] [Abstract] Cited for: SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z97343 Genomic DNA. Translation: CAB10511.1. Sequence problems. AL161546 Genomic DNA. Translation: CAB78733.1. Sequence problems. AJ222644 mRNA. Translation: CAA10904.1.
IPI	IPI00530771.
RefSeq	NP_193462.1.
UniGene	At.123 At.26556
3D structure databases
HSSP	HSSP built from PDB template 1B8A based on UniProtKB Q52428.
ModBase	Search...
Protein-protein interaction databases
STRING	O48593.
Proteomic databases
PRIDE	O48593.
Genome annotation databases
GeneID	827443.
GenomeReviews	Gene locus AT4G17300 in contig CT486007_GR.
KEGG	ath:AT4G17300.
Organism-specific databases
GeneFarm	2406. 269.
TAIR	At4g17300.
Phylogenomic databases
OMA	VGELCGG.
Enzyme and pathway databases
BRENDA	6.1.1.22. 302.
Gene expression databases
ArrayExpress	O48593.
Genevestigator	O48593.
GermOnline	AT4G17300. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR004364. aa-tRNA-synt_II. IPR018150. aa-tRNA-synt_II-like. IPR006195. aa-tRNA-synth_II_cons-reg. IPR004522. Asn-tRNA-synth_IIb. IPR002312. Asp-tRNA-synth_IIb. IPR004365. NA_bd_OB_tRNA-helicase. [Graphical view]
PANTHER	PTHR22594. aa-tRNA-synt_II. 1 hit.
Pfam	PF00152. tRNA-synt_2. 1 hit. PF01336. tRNA_anti. 1 hit. [Graphical view]
PRINTS	PR01042. TRNASYNTHASP.
TIGRFAMs	TIGR00457. asnS. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYNO_ARATH

Accession

Primary (citable) accession number: O48593
Secondary accession number(s): O23573

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 31, 2002
Last sequence update:	November 9, 2004
Last modified:	November 3, 2009
This is version 76 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)