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Reviewed, UniProtKB/Swiss-Prot Q5RA20 (SYRC_PONAB)

Last modified February 9, 2010. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Arginyl-tRNA synthetase, cytoplasmic
    EC=6.1.1.19
Alternative name(s):
    Arginine--tRNA ligase
      Short name=ArgRS
Gene names
Name: RARS
OrganismPongo abelii (Sumatran orangutan)
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length660 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Catalytic activity

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

Subunit structure

Interacts (via N-terminus) with AIMP1 (via N-terminus); stimulates its catalytic activity. 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.

Domain

The N-terminal (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 processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   PTMAcetylation
Phosphoprotein
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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 660660Arginyl-tRNA synthetase, cytoplasmic
PRO_0000250728

Regions

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

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue381Phosphoserine By similarity
Modified residue601N6-acetyllysine By similarity
Modified residue2051N6-acetyllysine 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
Q5RA20-1 [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.
UniGenePab.18398

3D structure databases

SMRQ5RA20. Positions 72-660.
ModBaseSearch...

Genome annotation databases

GeneID100174147.

Organism-specific databases

CTD100174147.

Phylogenomic databases

HOVERGENQ5RA20.
InParanoidQ5RA20.

Enzyme and pathway databases

BRENDA6.1.1.19. 269192.

Family and domain databases

InterProIPR001412. aa-tRNA-synth_I_CS.
IPR001278. Arg-tRNA-synth_Ic.
IPR015945. Arg-tRNA-synth_Ic_core.
IPR005148. Arg-tRNA-synth_Ic_N.
IPR008909. DALR_anticod_bd.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
[Graphical view]
Gene3DG3DSA:3.30.1360.70. Arg-tRNA-synth_Ic_N. 1 hit.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHERPTHR11956. Arg_tRNA-synt_1c. 1 hit.
PfamPF03485. Arg_tRNA_synt_N. 1 hit.
PF05746. DALR_1. 1 hit.
PF00750. tRNA-synt_1d. 1 hit.
[Graphical view]
PRINTSPR01038. TRNASYNTHARG.
SMARTSM00836. DALR_1. 1 hit.
[Graphical view]
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: February 9, 2010
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents