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B5EEF0 (SYR_GEOBB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 34. 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:Gbem_2283
OrganismGeobacter bemidjiensis (strain Bem / ATCC BAA-1014 / DSM 16622) [Complete proteome] [HAMAP]
Taxonomic identifier404380 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesGeobacteraceaeGeobacter

Protein attributes

Sequence length554 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 – 554554Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000095367

Regions

Motif129 – 13911"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
B5EEF0 [UniParc].

Last modified October 14, 2008. Version 1.
Checksum: 3D44CDE9A882E3C5

FASTA55461,652
        10         20         30         40         50         60 
MKEQLRACIL KGIEGCFADG TLTSGEVPAI NVEKPAHAEH GDFATNVAMQ MAKQQRKAPR 

        70         80         90        100        110        120 
AVAEILVAKL AGASDLIESL EIAGPGFINF FIKDSAWRRT LTEIDRAGDA WGKSGIGRGK 

       130        140        150        160        170        180 
KVQVEFVSAN PTGPLHIGHG RGAATGDAVA SLLSAAGFDV QREYYINDAG NQMNTLGLSG 

       190        200        210        220        230        240 
LLRYKELLGE KIDFPETCYQ GDYMKDIARD AVTKYGDRFL KVSQEDGVAF FSKMGGDLIL 

       250        260        270        280        290        300 
AGIDQDLQDF GIRFDHWFSE QSLFDEGKVK SAIEEMQAKG LIYEQEGALW FRTTDYGDDK 

       310        320        330        340        350        360 
DRVVVRSNGV TTYFASDIAY HRDKFARGFD WVIDVWGADH HGYVPRLKSV VQGLGRDASD 

       370        380        390        400        410        420 
LGIILVQLVS LLRDGVPVAM STRSGEFVTL KEVVDEVGRD AARFFFLMRR SDSQLDFDLE 

       430        440        450        460        470        480 
LAKRQSNDNP VYYVQYAHAR IKSIFDTARE RGVEPRFDSV KLELLQTPED LSLVKKLSVY 

       490        500        510        520        530        540 
PEILEGGAVN FEPHRITYYL QELAGEFHSF YNKSRVITPE EPELTQARLF LLHCVAITLK 

       550 
NALTVLGISA PERM 

« Hide

References

[1]"Complete sequence of Geobacter bemidjiensis BEM."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Lykidis A., Lovley D., Richardson P.
Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bem / ATCC BAA-1014 / DSM 16622.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001124 Genomic DNA. Translation: ACH39295.1.
RefSeqYP_002139091.1. NC_011146.1.

3D structure databases

ProteinModelPortalB5EEF0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING404380.Gbem_2283.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACH39295; ACH39295; Gbem_2283.
GeneID6782279.
KEGGgbm:Gbem_2283.
PATRIC21988238. VBIGeoBem56306_2239.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycGBEM404380:GHFR-2335-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_GEOBB
AccessionPrimary (citable) accession number: B5EEF0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: October 14, 2008
Last modified: April 16, 2014
This is version 34 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