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A5VL03 (SYR_LACRD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 51. 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:Lreu_1270
OrganismLactobacillus reuteri (strain DSM 20016) [Complete proteome] [HAMAP]
Taxonomic identifier557436 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length562 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 – 562562Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000057811

Regions

Motif121 – 13111"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
A5VL03 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: 2CC1383DE68EEF03

FASTA56263,879
        10         20         30         40         50         60 
MSDKQQVAAA LAQALPEMDV KEIEAKIERP KDSSNGDYAF PTFFLAKTLH KAPQMIASEL 

        70         80         90        100        110        120 
VEKVDQNGFE KVVVAGPYIN FFLDKAQVGA KILQTILADP EHYGEIDLGH QSNVTIDYSS 

       130        140        150        160        170        180 
PNIAKPMGMG HLRSTMIGEA VARILEKVNY NLIRIDYLGD WGTQFGKLMA AYEMWGDEAE 

       190        200        210        220        230        240 
VKKDPINTLL KYYVRINNEA DEHPEYTEAG RNWFAKLEHG DEEAWRLWHW FREVSLERFQ 

       250        260        270        280        290        300 
RVYKMLDVNF DSFNGEAFSA QKMEEPIQLL RDKDLLKPSR GAEIVDLDEY NLPPLLIIKS 

       310        320        330        340        350        360 
NGTTTYITRD LATALFRKRM YGHAKSLYVV GAEQETYFKQ LRAALKEMGF NWWDQIEHIS 

       370        380        390        400        410        420 
FGLMNLNGKK MSTRKGNVVS LEDVLNDSID LARKQIAEKN PDLENADEVA KEVGVGAVIF 

       430        440        450        460        470        480 
HDLKNYRRNA VNFKLEDVVK FEGETGPYVQ YARARAESIL RKGGIRDFSD VDLTKAGAEA 

       490        500        510        520        530        540 
WELISFLGQY SEAIKRAALN YDPSVIAKYA LELAKKFNQY YAHTRILDKD EAQPARLALT 

       550        560 
QAVSDVLKSA LDLLDIKAPD EM 

« Hide

References

[1]"The evolution of host specialization in the vertebrate gut symbiont Lactobacillus reuteri."
Frese S.A., Benson A.K., Tannock G.W., Loach D.M., Kim J., Zhang M., Oh P.L., Heng N.C., Patil P.B., Juge N., Mackenzie D.A., Pearson B.M., Lapidus A., Dalin E., Tice H., Goltsman E., Land M., Hauser L. expand/collapse author list , Ivanova N., Kyrpides N.C., Walter J.
PLoS Genet. 7:E1001314-E1001314(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 20016.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000705 Genomic DNA. Translation: ABQ83527.1.
RefSeqYP_001271864.1. NC_009513.1.

3D structure databases

ProteinModelPortalA5VL03.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING557436.Lreu_1270.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ83527; ABQ83527; Lreu_1270.
GeneID5189067.
KEGGlre:Lreu_1270.
PATRIC22255744. VBILacReu87937_1284.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247211.
KOK01887.
OMAYVKFHDE.
OrthoDBEOG6JB13C.

Enzyme and pathway databases

BioCycLREU557436:GC7Y-1331-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.
InterProIPR001278. 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.
ProtoNetSearch...

Entry information

Entry nameSYR_LACRD
AccessionPrimary (citable) accession number: A5VL03
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: July 10, 2007
Last modified: May 14, 2014
This is version 51 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