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Q64MX8 (SYR_BACFR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 66. 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:BF4421
OrganismBacteroides fragilis (strain YCH46) [Complete proteome] [HAMAP]
Taxonomic identifier295405 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

Protein attributes

Sequence length597 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 – 597597Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_0000241986

Regions

Motif125 – 13511"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q64MX8 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 726304A8005A4503

FASTA59766,759
        10         20         30         40         50         60 
MKIEDKLVTS VISGLKALYG QDVPAAQVQL QKTKKEFEGH LTLVVFPFLK MSKKGPEQTA 

        70         80         90        100        110        120 
QEIGEYLKAN EPAVAAFNVI KGFLNLTVAS ATWIELLNEI HADAQYGIVS ADENAPLVMI 

       130        140        150        160        170        180 
EYSSPNTNKP LHLGHVRNNL LGNALANIVM ANGNKVVKTN IVNDRGIHIC KSMLAWQKYG 

       190        200        210        220        230        240 
KGETPESSGK KGDHLVGDYY VAFDKHYKAE VAELMEKGMS KEEAEAASPL MNEAREMLVK 

       250        260        270        280        290        300 
WEAGDPEVRA LWQMMNNWVY TGFDETYRKM GVGFDKIYYE SNTYLEGKEK VMEGLEKGFF 

       310        320        330        340        350        360 
FKKEDGSVWA DLTAEGLDHK LLLRGDGTSV YMTQDIGTAK LRFADYPIDK MIYVVGNEQN 

       370        380        390        400        410        420 
YHFQVLSILL DKLGFEWGKS LVHFSYGMVE LPEGKMKSRE GTVVDADDLM AEMIATAKET 

       430        440        450        460        470        480 
SQELGKLDGL TQEEADDIAR IVGLGALKYF ILKVDARKNM TFNPKESIDF NGNTGPFIQY 

       490        500        510        520        530        540 
TYARIRSVLR KAAEAGIVIP EVLPANIELS EKEEGLIQMV ADFAAVVRQA GEDYSPSGIA 

       550        560        570        580        590 
NYVYDLVKEY NQFYHDFSIL REENEDVKLF RIALSANIAK VVRLGMGLLG IEVPDRM 

« Hide

References

[1]"Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions regulating cell surface adaptation."
Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N., Kuhara S., Hattori M., Hayashi T., Ohnishi Y.
Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: YCH46.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006841 Genomic DNA. Translation: BAD51159.1.
RefSeqYP_101693.1. NC_006347.1.

3D structure databases

ProteinModelPortalQ64MX8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING295405.BF4421.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD51159; BAD51159; BF4421.
GeneID3085498.
KEGGbfr:BF4421.
PATRIC21054427. VBIBacFra17906_4263.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247211.
KOK01887.
OMAPDIAYHI.
OrthoDBEOG6JB13C.

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_BACFR
AccessionPrimary (citable) accession number: Q64MX8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: October 25, 2004
Last modified: May 14, 2014
This is version 66 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