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Q47TB0 (SYR_THEFY) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 62. 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:Tfu_0269
OrganismThermobifida fusca (strain YX) [Complete proteome] [HAMAP]
Taxonomic identifier269800 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptosporangineaeNocardiopsaceaeThermobifida

Protein attributes

Sequence length576 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 – 576576Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_0000242110

Regions

Motif122 – 13211"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q47TB0 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 8523BC37722CB1E1

FASTA57663,414
        10         20         30         40         50         60 
MADPQTVLAR RVQSALGAAF GPEYRDTDPV IRPSQFADFQ ANVALALAKR LRRSPRDVAT 

        70         80         90        100        110        120 
AITEHLDISD VCSKVEISGP GFINLTLRDD WIAHQVHDLL TDERLGTPVQ ESQNIPIDYS 

       130        140        150        160        170        180 
APNVAKEMHV GHLRTTVVGD ALARILEFLG HHVIRQNHIG DWGTPFGMLI EHLLEVGEDS 

       190        200        210        220        230        240 
AEAAQLKSDP NAFYQAARAK FDSDEDFADR ARRRVVALQS GDAETLRLWR DLIELSKIYF 

       250        260        270        280        290        300 
NRIYRKLDVT LTDAHLAGES TYNDMLGPVC DELAEKGLAV VSDGALCVFL EGFTGREGKP 

       310        320        330        340        350        360 
VPLIIRKSDG GYGYATTDLA TIKYRVEQLK ADRIIYVVGA PQSLHLRMVY ETARQAGWLG 

       370        380        390        400        410        420 
NAEPIHVQIG NVLGSDGKIL RTRSGAPVRL MALLDEAVER ASAVVAQTRP DLDEETRAAI 

       430        440        450        460        470        480 
ARDVGIGAVK YADLSIAHDT EYVFDFDRML ALNGNTGPYL QYAVARIRSI FRKGGIDPAQ 

       490        500        510        520        530        540 
VTGPIQVTEP AERALALKLL DFGATVVQVG DTLEPHRLCT YLFDLAQTFT AFYEACPVLK 

       550        560        570 
ADRDEVRNSR LALTAVTLHT LVKGLDLLGV RAPEQM 

« Hide

References

[1]"Genome sequence and analysis of the soil cellulolytic actinomycete Thermobifida fusca YX."
Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M., DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A., Richardson P., Wilson D.B., Kyrpides N.
J. Bacteriol. 189:2477-2486(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: YX.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000088 Genomic DNA. Translation: AAZ54307.1.
RefSeqYP_288330.1. NC_007333.1.

3D structure databases

ProteinModelPortalQ47TB0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING269800.Tfu_0269.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ54307; AAZ54307; Tfu_0269.
GeneID3579925.
KEGGtfu:Tfu_0269.
PATRIC23900934. VBITheFus33945_0276.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247212.
KOK01887.
OMADGTAVYM.
OrthoDBEOG6JB13C.
ProtClustDBPRK01611.

Enzyme and pathway databases

BioCycTFUS269800:GI42-276-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_THEFY
AccessionPrimary (citable) accession number: Q47TB0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: September 13, 2005
Last modified: April 16, 2014
This is version 62 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