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Q5GT78 (SYR_WOLTR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:Wbm0205
OrganismWolbachia sp. subsp. Brugia malayi (strain TRS) [Complete proteome] [HAMAP]
Taxonomic identifier292805 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Wolbachieae › Wolbachia ›

Protein attributes

Sequence length565 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.

Subcellular location

Cytoplasm By similarity.

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: HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: HAMAP

arginine-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 565565Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_0000242121

Regions

Motif126 – 13611"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q5GT78 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: CD7307E0A40995E5

FASTA56564,200
        10         20         30         40         50         60 
MNIFKRISSL ILSKLDKLKQ GVSSVTNFIV EPPSNRAHGD IYTNIAMVLA KHEKKKPVEI 

        70         80         90        100        110        120 
AEVLAKEFAL FDEIARVEIA GPGFINMHLK IEVWHGILEQ INELKTEFGT LNIGNNQAIN 

       130        140        150        160        170        180 
VEFVSANPTG PLHIGHARGA VFGDVLTNLL KKVGYRVTKE YYINDAGAQI DTLVRSVYLR 

       190        200        210        220        230        240 
YKEALGEKIS IEKGLYPGEY LKPIGEELAK KYGRELLEKQ DNRVIREYTL SSILELIKEG 

       250        260        270        280        290        300 
MNLLGVSHDV FTSEYELQKS GKIEKSIKLL SDKGLVYEGY LEKPKSKESE NWTSRKEMLF 

       310        320        330        340        350        360 
RSTEFGDDVD RALKKEDGSW TYFASDIAYH FDKISRGFNN MIVALGSDHG GYIKRLKAVI 

       370        380        390        400        410        420 
SALSDNQAKI EVKLHNVVNF FENGKPVKMS KRSGNFLTVR DVVEEVGRDI TRFIMLTRKN 

       430        440        450        460        470        480 
DMVLDFDFTK VKEQSKDNPI FYVQYAHVRA HSLMRNAPKE LPKANPSLLK TNGELFLIKT 

       490        500        510        520        530        540 
LAKWPDVVET AARLCEPHRI TFYLLEVAEA FHILWGYGKS DLNMRFILED NPNLTAARMF 

       550        560 
LVQALVHVIA SGLSMFNIEP LEEMK

« Hide

References

[1]"The Wolbachia genome of Brugia malayi: endosymbiont evolution within a human pathogenic nematode."
Foster J., Ganatra M., Kamal I., Ware J., Makarova K., Ivanova N., Bhattacharyya A., Kapatral V., Kumar S., Posfai J., Vincze T., Ingram J., Moran L., Lapidus A., Omelchenko M., Kyrpides N., Ghedin E., Wang S. expand/collapse author list , Goltsman E., Joukov V., Ostrovskaya O., Tsukerman K., Mazur M., Comb D., Koonin E., Slatko B.
PLoS Biol. 3:599-614(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TRS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE017321 Genomic DNA. Translation: AAW70796.1.
RefSeqYP_198038.1. NC_006833.1.

3D structure databases

ProteinModelPortalQ5GT78.
ModBaseSearch...

Protein-protein interaction databases

STRING292805.Wbm0205.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW70796; AAW70796; Wbm0205.
GeneID3266960.
KEGGwbm:Wbm0205.
PATRIC24031919. VBIWolEnd7741_0341.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247214.
KOK01887.
OMAHTSANPN.
ProtClustDBPRK01611.

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]
SUPFAMSSF55190. Arg-tRNA-synth_Ic_N. 1 hit.
SSF47323. tRNAsyn_1a_bind. 1 hit.
TIGRFAMsTIGR00456. argS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYR_WOLTR
AccessionPrimary (citable) accession number: Q5GT78
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: March 1, 2005
Last modified: May 1, 2013
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

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