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Q67TI9 (SYR_SYMTH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 69. 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:STH19
OrganismSymbiobacterium thermophilum (strain T / IAM 14863) [Complete proteome] [HAMAP]
Taxonomic identifier292459 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiales Family XVIII. Incertae SedisSymbiobacterium

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_0000242103

Regions

Motif134 – 14411"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q67TI9 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: BA0FA42459141ED8

FASTA55863,061
        10         20         30         40         50         60 
MRIVEQIKSE IRQALADAVS RAVAAGALVG PAPEVFLETP KAREHGDFAT NLAMVMARQE 

        70         80         90        100        110        120 
KKAPRVIAQA IVDHLQTEGT WIESAEIAGP GFINLRLRQG WVHQVLPAIQ AEGADYGKSD 

       130        140        150        160        170        180 
HGGKQRILLE YVSANPTGPM VLVQARAGAF GSSLARLLNW AGYECHTEFY VNDAGNQVKI 

       190        200        210        220        230        240 
LARTVDLRAQ ELRGATVEIP EGYYPGEDVI DCARALLEQY PDFLEKPEEE RLAFLERWAP 

       250        260        270        280        290        300 
EYFRSGHERV LRSYGVEFDR WFSERSLREA GAPARLVEWL KERGEAYEKD GAVWMRTTAY 

       310        320        330        340        350        360 
GDDKDRVLVK SDGEYTYFAA DACYHKDKYD RGYATLIDIL GQDHHGYLGR MKAMVECLGH 

       370        380        390        400        410        420 
PRDSLEILFT QMVRLFKDGQ EFRMSKRRGN YVTLEDLLEQ VSVDAARYFF LMRSLDTHMD 

       430        440        450        460        470        480 
FDLDLANLKS SDNPVFYVQY AHARICSILR QAREQGLEVP AASEVDTALL ADESEVELMR 

       490        500        510        520        530        540 
KLAEFPEEII GAADAREVHR IPRYLNELAT LFHQFYSRCR VVSDDVPLSR ARLLLVDCTR 

       550 
TVLANALGIL GVSAPERM 

« Hide

References

[1]"Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium that depends on microbial commensalism."
Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K., Ikeda H., Hattori M., Beppu T.
Nucleic Acids Res. 32:4937-4944(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: T / IAM 14863.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006840 Genomic DNA. Translation: BAD39004.1.
RefSeqYP_073848.1. NC_006177.1.

3D structure databases

ProteinModelPortalQ67TI9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING292459.STH19.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD39004; BAD39004; STH19.
GeneID2980355.
KEGGsth:STH19.
PATRIC23778098. VBISymThe116959_0021.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247214.
KOK01887.
OMAMEHMGFG.
OrthoDBEOG6JB13C.

Enzyme and pathway databases

BioCycSTHE292459:GJMM-35-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_SYMTH
AccessionPrimary (citable) accession number: Q67TI9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: October 11, 2004
Last modified: May 14, 2014
This is version 69 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