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B8DWR0 (SYR_BIFA0) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 32. 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

EC=6.1.1.19
Alternative name(s):
Arginyl-tRNA synthetase
Short name=ArgRS
Gene names
Name:argS
Ordered Locus Names:BLA_0618
OrganismBifidobacterium animalis subsp. lactis (strain AD011) [Complete proteome] [HAMAP]
Taxonomic identifier442563 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeBifidobacterialesBifidobacteriaceaeBifidobacterium

Protein attributes

Sequence length598 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg). HAMAP-Rule MF_00123

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00123

Subcellular location

Cytoplasm 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
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processarginyl-tRNA aminoacylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

arginine-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 598598Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000198874

Regions

Motif135 – 14511"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
B8DWR0 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: 7D962679DCF11F41

FASTA59865,586
        10         20         30         40         50         60 
MSPEALQELI FTIANNLVSE GKAGTLTAEE LPDSAKFAVM RPKDRAHGDW ASNAAMQLAK 

        70         80         90        100        110        120 
KAGMKPRDLA QLFADALNGT DGIAAVEVAG PGFINITLDS ASAAAVVDQV LDEGNRFGKN 

       130        140        150        160        170        180 
NHLSGKTLNL EFVSANPTGP IHIGGTRWAA VGDSMARILQ ANGATVVREY YFNDHGEQIN 

       190        200        210        220        230        240 
RFAKSLVAAA HDEPTPVDGY KGAYIDEIAR RVIVEANAEG IDILNLPRVD GGTDEKGEPL 

       250        260        270        280        290        300 
GEGDSEQREE FRKRAVPMMF DEIRQSMKEF RVHFDVWFHE NSLYEDGEVE KAIADLRNAG 

       310        320        330        340        350        360 
DIYEKDGATW FESTEHGDDK DRVIIKSDGT YAYFAADIAY YRNKRHRKTD PADVAIYMLG 

       370        380        390        400        410        420 
ADHHGYIGRM MAMCAAFGDK PGENMQILIG QMVNVMKDGK PVRMSKRAGN IVTIDDLIDA 

       430        440        450        460        470        480 
IGVDASRYSL ARTDYNSPVD IDLNLLASHS NDNPVYYVQY AHARSCNVDR NAEAAQINAA 

       490        500        510        520        530        540 
DADLSLLDTE ADGEVIAALA QWPALLTLAG DLRAPHRIAH YLEDLAAAYH KWYNVERVVP 

       550        560        570        580        590 
MPLTEAEERA DEQTRERTRI AKNPEPARAA ARLKLNDAVQ TVIAEGLDLL GVTAPDKM 

« Hide

References

[1]"Genome sequence of the probiotic bacterium Bifidobacterium animalis subsp. lactis AD011."
Kim J.F., Jeong H., Yu D.S., Choi S.-H., Hur C.-G., Park M.-S., Yoon S.H., Kim D.-W., Ji G.E., Park H.-S., Oh T.K.
J. Bacteriol. 191:678-679(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AD011.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001213 Genomic DNA. Translation: ACL28911.1.
RefSeqYP_002469487.1. NC_011835.1.

3D structure databases

ProteinModelPortalB8DWR0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING442563.BLA_0618.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL28911; ACL28911; BLA_0618.
GeneID7264025.
KEGGbla:BLA_0618.
PATRIC21104121. VBIBifAni98964_0649.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247214.
KOK01887.
OMANPNGPLH.
OrthoDBEOG6JB13C.
ProtClustDBPRK01611.

Enzyme and pathway databases

BioCycBANI442563:GHG0-613-MONOMER.

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 nameSYR_BIFA0
AccessionPrimary (citable) accession number: B8DWR0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: April 16, 2014
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries