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P37880 (SYRC_CRIGR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 94. 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·Alt products·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
Synonyms:RRS1
OrganismCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Taxonomic identifier10029 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

Protein attributes

Sequence length661 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 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 HAMAP-Rule MF_00123.

Domain

The N-terminus (AA 1-73) has two regions predicted to be alpha-helical that might be involved in the multisynthetase complex assembly. HAMAP-Rule MF_00123

Sequence similarities

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

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   Coding sequence diversityAlternative initiation
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   PTMAcetylation
Gene Ontology (GO)
   Biological_processarginyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

arginine-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform Complexed (identifier: P37880-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Monomeric (identifier: P37880-2)

Also known as: Free;

The sequence of this isoform differs from the canonical sequence as follows:
     1-73: Missing.
Note: The alternative initiation site Met-74 is uncertain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 661661Arginine--tRNA ligase, cytoplasmic HAMAP-Rule MF_00123
PRO_0000035795

Regions

Region1 – 7373Could be involved in the assembly of the multisynthetase complex HAMAP-Rule MF_00123
Motif202 – 21312"HIGH" region HAMAP-Rule MF_00123

Amino acid modifications

Modified residue11N-acetylmethionine By similarity

Natural variations

Alternative sequence1 – 7373Missing in isoform Monomeric.
VSP_018904

Sequences

Sequence LengthMass (Da)Tools
Isoform Complexed [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: 12EB1C85655EB8F4

FASTA66175,602
        10         20         30         40         50         60 
MDGLVAQCSA RLLQQEKEIK SLTAEIDRLK NCGHLEDSPS LDQLREENLK LKYRLNILQR 

        70         80         90        100        110        120 
SLQAEKRRRP TKNMININSR LQDVFGCAIK AAYPDLDNPP LVVTPSQQPK FGDYQCNSAM 

       130        140        150        160        170        180 
GISQMLKAKE QKVNPRGIAE NITKHLPNNE YIDRVEIAGP GFINVHLRKD FVSEQLTNLL 

       190        200        210        220        230        240 
VNGIQLPALG ENKKVIVDFS SPNIAKEMHV GHLRSTIIGE SMSRLFEFAG YDVLRLNHVG 

       250        260        270        280        290        300 
DWGTQFGMLI AHLQDQFPDY LTVSPPIGDL QAFYKESKKR FDTEEEFKKR AYQCVVSLQS 

       310        320        330        340        350        360 
KDPDFIKAWN LICDVSRAEF NKIYDALDIT LIERGESFYQ DRMKDIVKEF EDKGYVQVDD 

       370        380        390        400        410        420 
GRKIVFVPGC SIPLTIVKSD GGFTYDTSDL AAIKQRLFEE KANKIIYVVD NGQAVHFQTI 

       430        440        450        460        470        480 
FAAAQMIGWY DPKVTQVTHV GFGVVLGEDK KKFKTRSGET VRLVDLLGEG LKRSMDKLKE 

       490        500        510        520        530        540 
KERDKVLTEE ELTAAQTSIA YGCIKYADLS HNRLNDYIFS FDKMLDDRGN TAAYLLYAFT 

       550        560        570        580        590        600 
RIRSIARLAN VDEEMLQKAA RETKIVLDHE KEWKLGRCIL RFPEILQKML DDLFLHTLCD 

       610        620        630        640        650        660 
YIYELATTFT EFYDSCYCVE KDRQTGKVLK VNMWRMLLCE AVAAVMAKGF DILGIKPVQR 


M 

« Hide

Isoform Monomeric (Free) [UniParc].

Checksum: 623A7303E0156F90
Show »

FASTA58867,088

References

[1]"Cloning and analysis of a cDNA encoding mammalian arginyl-tRNA synthetase, a component of the multisynthetase complex with a hydrophobic N-terminal extension."
Lazard M., Mirande M.
Gene 132:237-245(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Ovary.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X63415 mRNA. Translation: CAA45012.1.

3D structure databases

ProteinModelPortalP37880.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP37880.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG029238.

Enzyme and pathway databases

SABIO-RKP37880.

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...

Entry information

Entry nameSYRC_CRIGR
AccessionPrimary (citable) accession number: P37880
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: April 16, 2014
This is version 94 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