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B1L826 (SYR_THESQ) 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:TRQ2_1723
OrganismThermotoga sp. (strain RQ2) [Complete proteome] [HAMAP]
Taxonomic identifier126740 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

Protein attributes

Sequence length546 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 – 546546Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000095416

Regions

Motif122 – 13211"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
B1L826 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: 7FD330E302C899D2

FASTA54662,500
        10         20         30         40         50         60 
MLVNAIRQKV SEVISKAYGS EIEFEVEIPP RKEFGDLSTN VAMKLAKTLK KNPREIAKEI 

        70         80         90        100        110        120 
VKSLDEDPSF DRIEIMGPGF INFFLSNELL RGVVKTVLEK KDEYGRENVG NGMKVQFEYG 

       130        140        150        160        170        180 
SANPTGPFTV GHGRQIIIGD VLSEVYKELG YDVTREMYIN DAGKQIRLLA QSLWARYNQL 

       190        200        210        220        230        240 
LGVEKEIPEG GYRGEYLVDI ARDLVNEIGD RYKDLWNEEV EEFFKQTALN RMLSSMKDTL 

       250        260        270        280        290        300 
EKIGSSFDVY FSEKSLIEDG TVEEVLKLLK NKDVVYEKDG AVWLKVSAFI DEEDKVLVRS 

       310        320        330        340        350        360 
DGTYTYFMTD IAYHYKKYKR GFRKVYDIWG SDHHGHIPRM KAAMKALDIP DDFFNVILHQ 

       370        380        390        400        410        420 
FVTLKRGGEI VRMSTRAGEF VTLDELLDEV GRDATRYFFA MVDPNTHMVF DIDLAKAKSM 

       430        440        450        460        470        480 
DNPVYYVQYA HARIHNLFSN AEKKGVKFEE GKHLELLGNE EERVLMRNLG MFNTALKEVA 

       490        500        510        520        530        540 
QMFAPNRLTN YLQSLAESFH AFYTKHVIVD PENPELSNAR LNLALATGIV LRKGLKLIGV 


SAPERM 

« Hide

References

[1]"Complete sequence of Thermotoga sp. RQ2."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Bruce D.B., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RQ2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000969 Genomic DNA. Translation: ACB10056.1.
RefSeqYP_001739739.1. NC_010483.1.

3D structure databases

ProteinModelPortalB1L826.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING126740.TRQ2_1723.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB10056; ACB10056; TRQ2_1723.
GeneID6093174.
KEGGtrq:TRQ2_1723.
PATRIC23950106. VBITheSp108950_1758.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycTSP126740:GH49-1775-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_THESQ
AccessionPrimary (citable) accession number: B1L826
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 29, 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