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Q0P5H7 (SYRM_BOVIN) 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:
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
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

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_0000284070

Regions

Motif133 – 14412"HIGH" region

Amino acid modifications

Modified residue5681N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0P5H7 [UniParc].

Last modified September 19, 2006. Version 1.
Checksum: 1CFCBDCA6492CB42

FASTA57865,631
        10         20         30         40         50         60 
MACGFRRSIA SQLSRVLDLP PENLIKSISA VPISRKEEVA DFQLSVDSLL ENNNDHSRPD 

        70         80         90        100        110        120 
IQIQAMRLAE KLKCDTVVSE ISTGQGTVNF KINRELLTKT VLQQVIEDGS KYGLKSELFS 

       130        140        150        160        170        180 
GLPKKRIVVE FSSPNVAKKF HVGHLRSTII GNFIANLKEA LGHQVTRINY LGDWGMQFGL 

       190        200        210        220        230        240 
LGTGFQLFGY EEKLQSSPLQ HLFEVYVQVN KEAADDKNVA KSAHEFFQRL ELGDMQALAL 

       250        260        270        280        290        300 
WQKFRDLSID EYMRIYQRLG VHFDEYSGES FYREKSQEVL KLLDSKGLLQ KTLKGTAVVD 

       310        320        330        340        350        360 
LSGNGDPSSV CTVMRSDGTS LYATRDLAAA IDRMEKYNFD KMIYVTDKGQ KKHFQQVFQI 

       370        380        390        400        410        420 
LQIMGYDWAE RCQHVPFGVV QGMKTRRGDV TFLEDVLNEI RLRMLQNMAS IKTTKELENP 

       430        440        450        460        470        480 
EETAEQVGLA ALIIQDFRGF LLSDYQFSWD RVFQSRGDTG VFLQYTHARL HSLEETFGCG 

       490        500        510        520        530        540 
YLNDFNTACL QEPQSVSILQ HLLRFDEVLY RSSQDLQPRH IVSYLLTLSH LAAVAHRTLH 

       550        560        570 
VRNSPPEVAG ARLHLFRAVR SVLANGMKLL GITPVCRM 

« Hide

References

[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Fetal cerebellum.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC120020 mRNA. Translation: AAI20021.1.
RefSeqNP_001069346.1. NM_001075878.1.
UniGeneBt.16559.

3D structure databases

ProteinModelPortalQ0P5H7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000052997.

Proteomic databases

PRIDEQ0P5H7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000022568; ENSBTAP00000022568; ENSBTAG00000016967.
GeneID525894.
KEGGbta:525894.

Organism-specific databases

CTD57038.

Phylogenomic databases

eggNOGCOG0018.
GeneTreeENSGT00530000063407.
HOGENOMHOG000247211.
HOVERGENHBG057355.
KOK01887.
OMAARLHLFK.
OrthoDBEOG7DNNTT.
TreeFamTF300888.

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...

Other

NextBio20874255.

Entry information

Entry nameSYRM_BOVIN
AccessionPrimary (citable) accession number: Q0P5H7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: September 19, 2006
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