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Q74KR5 (SYR_LACJO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 67. 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:LJ_0686
OrganismLactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533) [Complete proteome] [HAMAP]
Taxonomic identifier257314 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length558 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 – 558558Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_0000242035

Regions

Motif119 – 12911"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q74KR5 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: E780DC71AA356BE4

FASTA55863,028
        10         20         30         40         50         60 
MDFKQKVVDL VSEQVDLPKE KISMLIERPK NPKMGDYAFP AFALAKIEHK NPALIAKDIA 

        70         80         90        100        110        120 
EKISDDNFTS IQAVGPYVNF AIDHAKLVNA TLNDVLTEKE HFGDQKLGEG NVPIDMSSPN 

       130        140        150        160        170        180 
IAKPMSMGHL RSTVIGNSIA KTLEKVGYTP IKINYLGDYG TQFGKLITAY RLWGNEGDVK 

       190        200        210        220        230        240 
KDPITNLFHY YVKFHEEAEK DPKLEDEGRA AFKKLENGDE EEIKLWKWFR EVSLQEFNRI 

       250        260        270        280        290        300 
YKELGVTFDS YNGEAFFNDK MQPVVDELRE KGLLEESRGA QVVNLGEDEN PALILKSDGS 

       310        320        330        340        350        360 
SLYMTRDLAA ALYRKKEYDF VMSLYVAGGE QTGHFKQLKQ VLKKMGYDWS DNIHHIPFGL 

       370        380        390        400        410        420 
ITQGGKKLST RKGNVVFLDQ VLKDAVSLAE QQIEEKNPNL SNKKQVAHDV GVGAVVFHDL 

       430        440        450        460        470        480 
KNDRMDNFDF DLEEVVRFEG DTGPYVQYTN ARAQSILRKA NKEISMDNLS LNDDWSFAVA 

       490        500        510        520        530        540 
KALADFPAIV EKASEKFEPS IIAKYALDLS KKFNKYYANV RILDEDNQLN ARLALVQATS 

       550 
IVLTEALRLL GVNAPKEM 

« Hide

References

[1]"The genome sequence of the probiotic intestinal bacterium Lactobacillus johnsonii NCC 533."
Pridmore R.D., Berger B., Desiere F., Vilanova D., Barretto C., Pittet A.-C., Zwahlen M.-C., Rouvet M., Altermann E., Barrangou R., Mollet B., Mercenier A., Klaenhammer T., Arigoni F., Schell M.A.
Proc. Natl. Acad. Sci. U.S.A. 101:2512-2517(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CNCM I-1225 / La1 / NCC 533.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017198 Genomic DNA. Translation: AAS08504.1.
RefSeqNP_964538.1. NC_005362.1.

3D structure databases

ProteinModelPortalQ74KR5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING257314.LJ0686.

Proteomic databases

PRIDEQ74KR5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAS08504; AAS08504; LJ_0686.
GeneID2742414.
KEGGljo:LJ0686.
PATRIC22237714. VBILacJoh1832_0539.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
KOK01887.
OMANPNGPLH.
OrthoDBEOG6JB13C.
ProtClustDBPRK01611.

Enzyme and pathway databases

BioCycLJOH257314:GJN3-543-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_LACJO
AccessionPrimary (citable) accession number: Q74KR5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 67 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