Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q5RA20 (SYRC_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 60. 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
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

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 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 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_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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 660660Arginine--tRNA ligase, cytoplasmic HAMAP-Rule MF_00123
PRO_0000250728

Regions

Region1 – 7272Could be involved in the assembly of the multisynthetase complex HAMAP-Rule MF_00123
Motif201 – 21212"HIGH" region HAMAP-Rule MF_00123

Amino acid modifications

Modified residue11N-acetylmethionine By similarity

Experimental info

Sequence conflict1641I → V in CAI29693. Ref.1
Sequence conflict2711V → A in CAI29693. Ref.1
Sequence conflict4021Missing in CAI29693. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q5RA20 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: C114CA5ED797D8E8

FASTA66075,344
        10         20         30         40         50         60 
MDVLVTECSA RLLQQEEEIK SLTAEIDRLK NCGCLGASAN LEQLQEENLK LKYRLNILQK 

        70         80         90        100        110        120 
SLQAERNKPT KNMINVISRL QEVFGHAIKA AYPDLENPPL LVTPSQQAKF GDYQCNSAMG 

       130        140        150        160        170        180 
ISQMLKTKEQ KVNPREIAEN ITKHLPDNEC IEKVEIAGPG FINIHLRKDF VSEQLTSLLV 

       190        200        210        220        230        240 
NGVQLPALGE NKKVIVDFSS PNIAKEMHVG HLRSTIIGES ISRLFEFAGY DVLRLNHIGD 

       250        260        270        280        290        300 
WGTQFGMLIA HLQDKFPDYL TVSPPIGDLQ VFYKESKKRF DTEEEFKKRA YQCVVLLQGK 

       310        320        330        340        350        360 
NPDITKAWKL ICDVSRQELN KIYDALDVSL IERGESFYQD MMNDIVKEFE DRGFVQVDDG 

       370        380        390        400        410        420 
RKIVFVPGCS IPLTILKSDG GYTYDTSDLA AIKQRLFEEK ADMIIYVVDN GQSVHFQTIF 

       430        440        450        460        470        480 
AAAQMIGWYD PKVTRVFHAG FGVVLGEDKK KFKTRSGETV RLMDLLGEGL KRSMDKLKEK 

       490        500        510        520        530        540 
ERDKVLTAEE LNAAQTSIAY GCVKYADLSH NRLNDYIFSF DKMLDDKGNT AAYLLYAFTR 

       550        560        570        580        590        600 
IRSIARLANI DEEMLQKAAR ETKILLDHEK EWKLGRCILR FPEILQKILD DLFLHTLCDY 

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

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain cortex.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR859203 mRNA. Translation: CAH91390.1.
CR926065 mRNA. Translation: CAI29693.1.
RefSeqNP_001127107.1. NM_001133635.1.

3D structure databases

ProteinModelPortalQ5RA20.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ5RA20.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100174147.
KEGGpon:100174147.

Organism-specific databases

CTD5917.

Phylogenomic databases

HOVERGENHBG029238.
InParanoidQ5RA20.
KOK01887.

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_PONAB
AccessionPrimary (citable) accession number: Q5RA20
Secondary accession number(s): Q5NVH0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: December 21, 2004
Last modified: April 16, 2014
This is version 60 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