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B9MBD2 (SYR_ACIET) 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:Dtpsy_0332
OrganismAcidovorax ebreus (strain TPSY) (Diaphorobacter sp. (strain TPSY)) [Complete proteome] [HAMAP]
Taxonomic identifier535289 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeAcidovorax

Protein attributes

Sequence length567 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 – 567567Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000198899

Regions

Motif128 – 13811"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
B9MBD2 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: ABF21C040138C1DF

FASTA56762,703
        10         20         30         40         50         60 
MLSVKQELLA ALADELEKVS PGAGSRAAFE SPKVAAHGDL ACTAAMQLAK PLKQNPRALG 

        70         80         90        100        110        120 
EQLQAALEAT PAFQKWVQAI EIAGPGFLNI RLKPAAKQQV VREVLAQGAQ YGYQPARGEK 

       130        140        150        160        170        180 
VLVEFVSANP TGPLHVGHGR QAAIGDAISH LYATQGWSVH REFYYNDAGV QIDTLTKSTQ 

       190        200        210        220        230        240 
LRAKGFKPGD DCWPTDSENP LAKNFYNGDY IQDIADAFLA KATVQADDRA FTANGDVEDY 

       250        260        270        280        290        300 
ENIRQFAVAY LRNEQDKDLQ AFNLQFDQYY LESSLYANGH VDATVQRLVA NGKTYEQDGA 

       310        320        330        340        350        360 
LWLKSTDYGD DKDRVMRKQD GTYTYFVPDV AYHIQKFQRG FTKVVNIQGT DHHGTIARVR 

       370        380        390        400        410        420 
AGLQAADVGI PQGYPDYVLH TMVRVVRNGE EVKISKRAGS YVTLRDLIEW TSKDAVRFFL 

       430        440        450        460        470        480 
LSRKPDTEYT FDVDLAVAQN NDNPVYYVQY AHARICSVLR GWREDYDVAA LRDVDLSPLE 

       490        500        510        520        530        540 
GPQAQALMLL LAKYPEMLTA AAAGNAPHDV TFYLRDLAAA YHSYYDAERI LVDDEAVKQA 

       550        560 
RLALVAATAQ VLHNGLAVLG VSAPARM 

« Hide

References

[1]"Complete sequence of Diaphorobacter sp. TPSY."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Coates J.D.
Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TPSY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001392 Genomic DNA. Translation: ACM31816.1.
RefSeqYP_002551816.1. NC_011992.1.

3D structure databases

ProteinModelPortalB9MBD2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING535289.Dtpsy_0332.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACM31816; ACM31816; Dtpsy_0332.
GeneID7385340.
KEGGdia:Dtpsy_0332.
PATRIC21777660. VBIDiaSp55748_0346.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycAEBR535289:GHOO-333-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_ACIET
AccessionPrimary (citable) accession number: B9MBD2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
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