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Q5REH3 (SYRM_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 56. 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:
Probable arginine--tRNA ligase, mitochondrial

EC=6.1.1.19
Alternative name(s):
Arginyl-tRNA synthetase
Short name=ArgRS
Gene names
Name:RARS2
Synonyms:RARSL
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length578 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

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

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

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

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentMitochondrion
   DomainTransit peptide
   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_componentmitochondrial matrix

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

Transit peptide1 – 1616Mitochondrion Potential
Chain17 – 578562Probable arginine--tRNA ligase, mitochondrial
PRO_0000250733

Regions

Motif133 – 14412"HIGH" region

Amino acid modifications

Modified residue5681N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5REH3 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 17F28D28E8805284

FASTA57865,533
        10         20         30         40         50         60 
MACGFRRAIA CQLSRVLNLP PENLITSISA VPISQKEEVA DFQLSVDSLL EKDNDHSRPD 

        70         80         90        100        110        120 
IQVQAKRLAE KLRCDTVVSE ISTGQRTVNF KINRELLTKT VLQQVIEDGS KYGLKSELFS 

       130        140        150        160        170        180 
GLPQKKIVVE FSSPNVAKKF HVGHLRSTII GNFIANLKEA LGHQVIRINY LGDWGMQFGL 

       190        200        210        220        230        240 
LGTGFQLFGY EEKLQSNPLQ HLFEVYVQVN KEAADDKSVA KAAQEFFQRL ELGDVQALSL 

       250        260        270        280        290        300 
WQKFRDLSIE EYIRVYKRLG VYFDEYSGES FYREKSQEVL KLLESKGLLL RTIKGTAVVD 

       310        320        330        340        350        360 
LSGNGDPSSI CTVMRSDGTS LYATRDLAAA IDRMDKYNFD TMIYVTDKGQ KKHFQQVFQM 

       370        380        390        400        410        420 
LKIMGYDWAE RCQHVPFGVV QGMKTRRGDV TFLEDVLNEI QLRMLQNMAS IKTTKELKNP 

       430        440        450        460        470        480 
QETAERVGLA ALIIQDFKGL LLSDYKFSWD RVFQSRGDTG VFLQYTHARL HSLEETFGCG 

       490        500        510        520        530        540 
YLNDFNTACL QEPQSVSILQ HLLRFDEVLY KSSQDFQPRH IVSYLLTLSH LAAVAHKTLQ 

       550        560        570 
IKDSPPEVAG ARLHLFKAVR SVLANGMKLL GITPVCRM 

« Hide

References

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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR857556 mRNA. Translation: CAH89834.1.
RefSeqNP_001128754.1. NM_001135282.1.
UniGenePab.6387.

3D structure databases

ProteinModelPortalQ5REH3.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100189650.
KEGGpon:100189650.

Phylogenomic databases

HOVERGENHBG057355.
InParanoidQ5REH3.
KOK01887.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.30.1360.70. 1 hit.
3.40.50.620. 1 hit.
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.
PfamPF05746. DALR_1. 1 hit.
PF00750. tRNA-synt_1d. 1 hit.
[Graphical view]
PRINTSPR01038. TRNASYNTHARG.
SMARTSM00836. 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 nameSYRM_PONAB
AccessionPrimary (citable) accession number: Q5REH3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: December 21, 2004
Last modified: April 16, 2014
This is version 56 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