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Q1LTI8 (SYR_BAUCH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 56. 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:BCI_0276
OrganismBaumannia cicadellinicola subsp. Homalodisca coagulata [Complete proteome] [HAMAP]
Taxonomic identifier374463 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaCandidatus Baumannia

Protein attributes

Sequence length578 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 – 578578Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000017990

Regions

Motif123 – 13311"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q1LTI8 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: 40F42DA61DD484DD

FASTA57865,685
        10         20         30         40         50         60 
MNIHAIISDQ IHKAMLAAGV PPYYRVQVRP SVKKKFGDYQ INGLMATAKQ LGVPSYFLAK 

        70         80         90        100        110        120 
KVVSFLQLNG IARQIDIAGP GFINIYLDSQ WLATKIATAI ASPRLGISLI ELPQTIVVDY 

       130        140        150        160        170        180 
SSPNIAKEMH VGHIRSTIIG DASARILDFI GHKVIRINHI GDWGTHFGML IAYLQQVEKN 

       190        200        210        220        230        240 
IDPEIPLSFL DQLYRQAKDK YDTDPSFAQE ARNCVVKLQC GDSFCLKIWQ KLVKITINEN 

       250        260        270        280        290        300 
QKIYNRLNIS LSHENIMGES KYNNMLPNII ADLKAKGLAV ESAGATVIFL NEFQDKQGNP 

       310        320        330        340        350        360 
LGVIIQKKDG AYLYTTTDIA CIKYRYEQLK ADRIIYYVDS RQHQHLKQIW TIVRKAGYIP 

       370        380        390        400        410        420 
QTMQLDHHMF GMIFDKEGKP FKTRVGVNIK LNDLLDEALK RARCLILSKN MDVDPVELEH 

       430        440        450        460        470        480 
LAQVISISAI KYAELSKNRT TDYIFNWDDM LSFEGNTAPY ILYAYTRIAS ILKRSNYNKQ 

       490        500        510        520        530        540 
QILTGSILLE KEHEHLLAVR LLQYHETITT VAHDGRPHIL CGYLYNLAVR FSSFYEHCSI 

       550        560        570 
INANSDIQRK SRLQLALLTS KTLQHGLSLL GIETVDKM 

« Hide

References

[1]"Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters."
Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.
PLoS Biol. 4:1079-1092(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000238 Genomic DNA. Translation: ABF13938.1.
RefSeqYP_588726.1. NC_007984.1.

3D structure databases

ProteinModelPortalQ1LTI8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING374463.BCI_0276.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABF13938; ABF13938; BCI_0276.
GeneID4056684.
KEGGbci:BCI_0276.
PATRIC21074055. VBIBauCic75062_0263.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247212.
KOK01887.
OMANPNGPLH.
OrthoDBEOG6JB13C.

Enzyme and pathway databases

BioCycBCIC374463:GI6Q-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_BAUCH
AccessionPrimary (citable) accession number: Q1LTI8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 30, 2006
Last modified: April 16, 2014
This is version 56 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