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A7YW98 (SYRC_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Arginine--tRNA ligase, cytoplasmic

EC=6.1.1.19
Alternative name(s):
Arginyl-tRNA synthetase
Short name=ArgRS
Gene names
Name:RARS
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length660 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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. HAMAP-Rule MF_00123

Catalytic activity

ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg). HAMAP-Rule MF_00123

Subunit structure

Interacts (via N-terminus) with AIMP1 (via N-terminus); this stimulates its catalytic activity. Interacts (via N-terminus) with LARS2 (via C-terminus). 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 By similarity HAMAP-Rule MF_00123.

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. HAMAP-Rule MF_00123

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processarginyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

arginine-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 660660Arginine--tRNA ligase, cytoplasmic HAMAP-Rule MF_00123
PRO_0000395433

Regions

Region1 – 7272Could be involved in the assembly of the multisynthetase complex By similarity
Motif201 – 21212"HIGH" region By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity

Sequences

Sequence LengthMass (Da)Tools
A7YW98 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: EA5DCB46414C81C1

FASTA66075,561
        10         20         30         40         50         60 
MDALVAHCSA RLLQQEKEIK FLTAEVDRLK NYSCSEASAD LEKLREENLK LKYRLNILRK 

        70         80         90        100        110        120 
SLQAERNKPT KTMININSCL EEVFGCAIKA AYPVLENPPL IVTPSQQPKF GDYQCNSAMG 

       130        140        150        160        170        180 
ICQMLKTKEQ KVNPREIAEN IVKHLPDNEY IEKVEIAGPG FINIHLRKGF VSQQLTNLLV 

       190        200        210        220        230        240 
NGVKIPSIGE NKKVIVDFSS PNIAKEMHVG HLRSTIIGES MCRLFEFAGY NVLRLNHVGD 

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

       310        320        330        340        350        360 
NPDIIKAWKL ICDVSRQEFN KIYEALDISL IERGESFYQD RMHDIVKEFE DRGFVQVDDG 

       370        380        390        400        410        420 
RKIVFVPGCS VPLTIVKSDG GYTYDTSDLA AIKQRLFEEK ADMIIYVVDN GQSLHFQTVF 

       430        440        450        460        470        480 
GAAQMIGWYD PAVTRVSHAG FGVVLGEDKK KFKTRSGETV RLIDLLEEGL KRSMDKLKEK 

       490        500        510        520        530        540 
ERDKVLTTEE LKAAQTSVAY GCIKYADLSH NRLNDYIFSF DKMLDDRGNT AAYLLYAFTR 

       550        560        570        580        590        600 
IRSIARLANI DEEMLRKAAH ETEIILDHEK EWKLGRCILR FPEVLQKILD DLLLHTLCDY 

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

« Hide

References

[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Thymus.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC134468 mRNA. Translation: AAI34469.1.
RefSeqNP_001098808.1. NM_001105338.2.
UniGeneBt.22038.

3D structure databases

ProteinModelPortalA7YW98.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000019475.

Proteomic databases

PRIDEA7YW98.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000019475; ENSBTAP00000019475; ENSBTAG00000014626.
GeneID506305.
KEGGbta:506305.

Organism-specific databases

CTD5917.

Phylogenomic databases

eggNOGCOG0018.
GeneTreeENSGT00530000063407.
HOGENOMHOG000247212.
HOVERGENHBG029238.
InParanoidA7YW98.
KOK01887.
OMAKCFDILG.
OrthoDBEOG764725.
TreeFamTF106111.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.30.1360.70. 1 hit.
3.40.50.620. 1 hit.
HAMAPMF_00123. Arg_tRNA_synth.
InterProIPR001412. 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]
PANTHERPTHR11956. PTHR11956. 1 hit.
PfamPF03485. Arg_tRNA_synt_N. 1 hit.
PF05746. DALR_1. 1 hit.
PF00750. tRNA-synt_1d. 1 hit.
[Graphical view]
PRINTSPR01038. TRNASYNTHARG.
SMARTSM01016. Arg_tRNA_synt_N. 1 hit.
SM00836. DALR_1. 1 hit.
[Graphical view]
SUPFAMSSF47323. SSF47323. 1 hit.
SSF55190. SSF55190. 1 hit.
TIGRFAMsTIGR00456. argS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20867548.

Entry information

Entry nameSYRC_BOVIN
AccessionPrimary (citable) accession number: A7YW98
Entry history
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: October 23, 2007
Last modified: May 14, 2014
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries