Arginine--tRNA ligase, cytoplasmic - Rattus norvegicus (Rat)

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P40329 (SYRC_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 70. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Arginine--tRNA ligase, cytoplasmic
EC=6.1.1.19

Alternative name(s):
Arginyl-tRNA synthetase
Short name=ArgRS

Gene names

Name:

Rars

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	660 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis. Modulates the secretion of AIMP1 and may be involved in generation of the inflammatory cytokine EMAP2 from AIMP1 By similarity.
Catalytic activity	ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg).
Subunit structure	Interacts (via N-terminus) with AIMP1 (via N-terminus); this stimulates its catalytic activity. Interacts with EPRS (via N-terminus). Interacts with LARS2. Monomer; also part of a multisubunit complex that groups tRNA ligases for Arg, Asp, Glu, Gln, Ile, Leu, Lys, Met and Pro By similarity.
Subcellular location	Cytoplasm.
Domain	The N-terminus (AA 1-72) has two regions predicted to be alpha-helical that might be involved in the multisynthetase complex assembly By similarity.
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	arginyl-tRNA aminoacylation Inferred from direct assay PubMed 7082655. Source: RGD
Cellular_component	aminoacyl-tRNA synthetase multienzyme complex Inferred from direct assay PubMed 7082655. Source: RGD mitochondrion Inferred from electronic annotation. Source: Compara nucleus Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from direct assay PubMed 7082655. Source: RGD arginine binding Inferred from direct assay PubMed 7082655. Source: RGD arginine-tRNA ligase activity Inferred from direct assay PubMed 7082655. Source: RGD tRNA binding Inferred from direct assay PubMed 7082655. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 660

660

Arginine--tRNA ligase, cytoplasmic

PRO_0000151660

Regions

Region

1 – 72

Could be involved in the assembly of the multisynthetase complex By similarity

Motif

201 – 212

"HIGH" region By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P40329 [UniParc].

Last modified July 13, 2010. Version 2.
Checksum: 3C2D718AECDC4655
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FASTA

660

75,810

        10         20         30         40         50         60 
MDGLVAQCSA RLLQQEKEIK SLTAEIDRLK NCSYLEASPS LEQLREENLK LKYRLNILRR 

        70         80         90        100        110        120 
SLQAERKRPT KNMININSRL QELFGCAIKA AYPDLENPPL VVTPSQQPKF GDYQCNSAMG 

       130        140        150        160        170        180 
ISQMLKAKEQ KVSPREIAEN ITKHLPNNEY IDRVEIAGPG FINVHLRKDF VSEQLTNLLV 

       190        200        210        220        230        240 
NGVQLPVLGE NEKVIVDFSS PNIAKEMHVG HLRSTIIGES MSRLFEFAGY NVLRLNHVGD 

       250        260        270        280        290        300 
WGTQFGMLIA HLQDKFPDYL TVSPPIGDLQ AFYKESKKRF DTEEEFKKRA YECVVLLQSK 

       310        320        330        340        350        360 
NPDIMKAWNL ICDVSREEFN KIYDALDITL IERGESFYQD RMKDIVKEFE DKGFVQVDDG 

       370        380        390        400        410        420 
RKIVFVPGCS VPLTIVKSDG GYTYDTSDLA AIKQRLFEEK ANKIIYVVDN GQATHFQTVF 

       430        440        450        460        470        480 
AAAQMIGWYD PKVTRVAHVG FGVVLGEDKK KFKTRSGETV RLMDLLEEGL RRSMDKLKEK 

       490        500        510        520        530        540 
ERDKVLTEEE LKAAQTSVAY GCIKYADLSH NRLNDYVFSF DKMLDDRGNT AAYLLYAFTR 

       550        560        570        580        590        600 
IRSIARLANI DEEMLQRAAR ETKIILDHEK EWKLGRCILR FPEILQKILD DLFLHTLCDY 

       610        620        630        640        650        660 
IYELATTFTE FYDSCYCVEK DRQTGKVLKV NMWRMLLCEA VAAVMAKGFD ILGIKPVQRM

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Brown Norway/NHsdMcwi. Tissue: Liver.
[2]	"Existence of two forms of rat liver arginyl-tRNA synthetase suggests channeling of aminoacyl-tRNA for protein synthesis." Sivaram P., Deutscher M.P. Proc. Natl. Acad. Sci. U.S.A. 87:3665-3669(1990) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 73-92.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC161929 mRNA. Translation: AAI61929.1.
IPI	IPI00188665.
PIR	A35857.
RefSeq	NP_001099247.2. NM_001105777.2.
UniGene	Rn.18711.
3D structure databases
ProteinModelPortal	P40329.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000010252.
Proteomic databases
PRIDE	P40329.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000010252; ENSRNOP00000010252; ENSRNOG00000007739.
GeneID	287191.
KEGG	rno:287191.
UCSC	RGD:1309215. rat.
Organism-specific databases
CTD	5917.
RGD	1309215. Rars.
Phylogenomic databases
GeneTree	ENSGT00530000063407.
HOGENOM	HOG000247212.
HOVERGEN	HBG029238.
KO	K01887.
OrthoDB	EOG4D52X9.
Gene expression databases
Genevestigator	P40329.
Family and domain databases
Gene3D	3.30.1360.70. 1 hit. 3.40.50.620. 1 hit.
InterPro	IPR001412. aa-tRNA-synth_I_CS. IPR001278. Arg-tRNA-ligase_Ia. IPR015945. Arg-tRNA-synth_Ia_core. IPR005148. Arg-tRNA-synth_N. IPR008909. DALR_anticod-bd. IPR014729. Rossmann-like_a/b/a_fold. IPR009080. tRNAsynth_1a_anticodon-bd. [Graphical view]
PANTHER	PTHR11956. PTHR11956. 1 hit.
Pfam	PF03485. Arg_tRNA_synt_N. 1 hit. PF05746. DALR_1. 1 hit. PF00750. tRNA-synt_1d. 1 hit. [Graphical view]
PRINTS	PR01038. TRNASYNTHARG.
SMART	SM01016. Arg_tRNA_synt_N. 1 hit. SM00836. DALR_1. 1 hit. [Graphical view]
SUPFAM	SSF55190. Arg-tRNA-synth_Ic_N. 1 hit. SSF47323. tRNAsyn_1a_bind. 1 hit.
TIGRFAMs	TIGR00456. argS. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	625686.

Entry information

Entry name

SYRC_RAT

Accession

Primary (citable) accession number: P40329
Secondary accession number(s): B1WBX8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	July 13, 2010
Last modified:	April 3, 2013
This is version 70 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents