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C1AMT6 (SYR_MYCBT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 35. 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:JTY_1327
OrganismMycobacterium bovis (strain BCG / Tokyo 172 / ATCC 35737 / TMC 1019) [Complete proteome] [HAMAP]
Taxonomic identifier561275 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length550 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 – 550550Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000198924

Regions

Motif130 – 14011"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
C1AMT6 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: 4F11239A6238124D

FASTA55059,709
        10         20         30         40         50         60 
MTPADLAELL KATAAAVLAE RGLDASALPQ MVTVERPRIP EHGDYASNLA MQLAKKVGTN 

        70         80         90        100        110        120 
PRELAGWLAE ALTKVDGIAS AEVAGPGFIN MRLETAAQAK VVTSVIDAGH SYGHSLLLAG 

       130        140        150        160        170        180 
RKVNLEFVSA NPTGPIHIGG TRWAAVGDAL GRLLTTQGAD VVREYYFNDH GAQIDRFANS 

       190        200        210        220        230        240 
LIAAAKGEPT PQDGYAGSYI TNIAEQVLQK APDALSLPDA ELRETFRAIG VDLMFDHIKQ 

       250        260        270        280        290        300 
SLHEFGTDFD VYTHEDSMHT GGRVENAIAR LRETGNIYEK DGATWLRTSA FGDDKDRVVI 

       310        320        330        340        350        360 
KSDGKPAYIA GDLAYYLDKR QRGFDLCIYM LGADHHGYIA RLKAAAAAFG DDPATVEVLI 

       370        380        390        400        410        420 
GQMVNLVRDG QPVRMSKRAG TVLTLDDLVE AIGVDAARYS LIRSSVDTAI DIDLALWSSA 

       430        440        450        460        470        480 
SNENPVYYVQ YAHARLSALA RNAAELALIP DTNHLELLNH DKEGTLLRTL GEFPRVLETA 

       490        500        510        520        530        540 
ASLREPHRVC RYLEDLAGDY HRFYDSCRVL PQGDEQPTDL HTARLALCQA TRQVIANGLA 

       550 
IIGVTAPERM 

« Hide

References

[1]"Whole genome sequence analysis of Mycobacterium bovis bacillus Calmette-Guerin (BCG) Tokyo 172: a comparative study of BCG vaccine substrains."
Seki M., Honda I., Fujita I., Yano I., Yamamoto S., Koyama A.
Vaccine 27:1710-1716(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BCG / Tokyo 172 / ATCC 35737 / TMC 1019.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP010918 Genomic DNA. Translation: BAH25615.1.
RefSeqYP_002644383.1. NC_012207.1.

3D structure databases

ProteinModelPortalC1AMT6.
SMRC1AMT6. Positions 5-550.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING561275.JTY_1327.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAH25615; BAH25615; JTY_1327.
GeneID7563994.
KEGGmbt:JTY_1327.
PATRIC18022133. VBIMycBov85238_1450.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247214.
KOK01887.
OMAQQEVFRS.
OrthoDBEOG6JB13C.

Enzyme and pathway databases

BioCycMBOV561275:GHDN-1344-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_MYCBT
AccessionPrimary (citable) accession number: C1AMT6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 26, 2009
Last modified: May 14, 2014
This is version 35 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