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B2GDD7 (SYR_LACF3) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 40. 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:LAF_1333
OrganismLactobacillus fermentum (strain NBRC 3956 / LMG 18251) [Complete proteome] [HAMAP]
Taxonomic identifier334390 [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_1000095375

Regions

Motif121 – 13111"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
B2GDD7 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: 61264C0712B34613

FASTA56263,150
        10         20         30         40         50         60 
MNERQQVASA LQKVLPNLSV EDLEAKLERP KDAKNGDYAF PTFFLAKELH RAPQVIASEL 

        70         80         90        100        110        120 
AEQIDQSGFE RVVVAGPYIN FFLDKASVGG EILAAVLADP ANYGSTDLGH QGHVTIDLSS 

       130        140        150        160        170        180 
PNIAKPMGMG HLRSTVIGNA IANILAKVNY VPVRINHLGD WGTQFGKLMA AYEMWGDEAE 

       190        200        210        220        230        240 
VQKDPINTLQ KYYVKINTEA DEHPEYDDLG REWFAKLEQG DPEAQRLWKW FREVSLQRFM 

       250        260        270        280        290        300 
KIYNLLDIDF DSFNGEAFYN DKMDEVVTLL EDKQLLKESR GAEIIDLEKY DLNPAMIRKS 

       310        320        330        340        350        360 
DGSTLYLTRD LAAALFRKRM YHHAQSLYVV GAEQSNHFAQ LKAVLSEMGF TWSDQIHHIP 

       370        380        390        400        410        420 
FGLMSLNGKK MSTRKGNIIQ LEDVLNDSIK LARQQIEEKN PTLANADQVA EEVGVGAVIF 

       430        440        450        460        470        480 
HDLKNERTNS VDFKLEEVVK FEGETGPYVQ YAHARAESIL RKAGRPSFEG ATLTVDGQEA 

       490        500        510        520        530        540 
WEVAKKIGQY QETIVRAANE YDPSLIGKYA LSLAKSFNQY YAHTRILEED DQKLSRLALV 

       550        560 
QAVSDVLKSA LALLGVKAPD EM 

« Hide

References

[1]"Comparative genome analysis of Lactobacillus reuteri and Lactobacillus fermentum reveal a genomic island for reuterin and cobalamin production."
Morita H., Toh H., Fukuda S., Horikawa H., Oshima K., Suzuki T., Murakami M., Hisamatsu S., Kato Y., Takizawa T., Fukuoka H., Yoshimura T., Itoh K., O'Sullivan D.J., McKay L.L., Ohno H., Kikuchi J., Masaoka T., Hattori M.
DNA Res. 15:151-161(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NBRC 3956 / LMG 18251.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008937 Genomic DNA. Translation: BAG27669.1.
RefSeqYP_001844149.1. NC_010610.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING334390.LAF_1333.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAG27669; BAG27669; LAF_1333.
GeneID6232658.
KEGGlfe:LAF_1333.
PATRIC22226950. VBILacFer15497_1458.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247211.
KOK01887.
OMANPNGPLH.
OrthoDBEOG6JB13C.

Enzyme and pathway databases

BioCycLFER334390:GJ2S-1381-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_LACF3
AccessionPrimary (citable) accession number: B2GDD7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: June 10, 2008
Last modified: April 16, 2014
This is version 40 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