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Q0AU94 (SYR_SYNWW) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 53. 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:Swol_2421
OrganismSyntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen) [Complete proteome] [HAMAP]
Taxonomic identifier335541 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesSyntrophomonadaceaeSyntrophomonas

Protein attributes

Sequence length559 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 – 559559Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000018139

Regions

Motif134 – 14411"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q0AU94 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: BDB8DA6E5A61D822

FASTA55963,845
        10         20         30         40         50         60 
MNPIQKVLAS LHSMVIEALE KAKSRDLIKF DQIPEFLIEV PREKEHGDFA CNVALLMARQ 

        70         80         90        100        110        120 
ARQAPRAIAE VLVELMEASG RPVEKIEIAG AGFINFFLDR SWLYEIPLMV YKSKDKYGFN 

       130        140        150        160        170        180 
GEKAKKVQVE FVSANPTGNL HMGNARGGAI GDTLANILER AGYEVEREFY INDAGNQIEI 

       190        200        210        220        230        240 
FTDSMEARYL QLTGHDVQFP ENGYAGRDLI DTVRNIIARY GEGLYDLPRE ERRQIIVDFA 

       250        260        270        280        290        300 
LEEKIDYIQK TLASFGINYD VWFSEKSLHE NGKIMAVFND LRDKGYIYES EGAWWFKSTA 

       310        320        330        340        350        360 
FGDEKDEVVL RANGMPTYFM ADIAYHQNKF ERGFDWVINV WGADHHGHVA RMKGAIEALG 

       370        380        390        400        410        420 
YDPARLDILL MQLVRLYRGG NIVRMSKRTG TTVSLDELIE DVGKDAARFF FVMRSPDSHL 

       430        440        450        460        470        480 
DFDLELARQK SQENPVYYVQ YAHARICSIF RQARAEGITM AEINEIDISC LKEEEELAIL 

       490        500        510        520        530        540 
RKIADFPEEI SIAARTLAPH RIARYVLDLA ALFHSFYNHH RVLNDNRALQ DARLLLMEIT 

       550 
RITIHNALDV LGVAAPEQM 

« Hide

References

[1]"The genome of Syntrophomonas wolfei: new insights into syntrophic metabolism and biohydrogen production."
Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L., McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.
Environ. Microbiol. 12:2289-2301(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 2245B / Goettingen.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000448 Genomic DNA. Translation: ABI69710.1.
RefSeqYP_755081.1. NC_008346.1.

3D structure databases

ProteinModelPortalQ0AU94.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING335541.Swol_2421.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI69710; ABI69710; Swol_2421.
GeneID4281825.
KEGGswo:Swol_2421.
PATRIC23860002. VBISynWol51738_2629.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247214.
KOK01887.
OMADGTAVYM.
OrthoDBEOG6JB13C.
ProtClustDBPRK01611.

Enzyme and pathway databases

BioCycSWOL335541:GHL1-2484-MONOMER.

Family and domain databases

Gene3D3.30.1360.70. 1 hit.
3.40.50.620. 1 hit.
HAMAPMF_00123. Arg_tRNA_synth.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR001278. Arg-tRNA-ligase_Ia.
IPR015945. Arg-tRNA-synth_Ia_core.
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_SYNWW
AccessionPrimary (citable) accession number: Q0AU94
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 17, 2006
Last modified: February 19, 2014
This is version 53 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