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A1TD77 (SYR_MYCVP) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 50. 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:Mvan_4350
OrganismMycobacterium vanbaalenii (strain DSM 7251 / PYR-1) [Complete proteome] [HAMAP]
Taxonomic identifier350058 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

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_1000018074

Regions

Motif130 – 14011"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
A1TD77 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: E42FACF436A5881B

FASTA55058,867
        10         20         30         40         50         60 
MTPADLAELL KATAAAVLAE HGLDSAALPA IVTVERPRNP EHGDYATNLA LQLGKKVGAN 

        70         80         90        100        110        120 
PRELAGWLAA ALVAKDGIAA ADVAGPGFVN LRIEASAQNV IVGDVIAAGA TYGASGELDG 

       130        140        150        160        170        180 
RRVNLEFVSA NPTGPIHIGG TRWAAVGDAL GRLLSTQGAE VVREYYFNDH GAQIDRFTNS 

       190        200        210        220        230        240 
LIAAAKGEPA PEDGYAGTYI ADIAAQVLAK EPGALELPDA EMRETFRAVG VNLMFDHIKE 

       250        260        270        280        290        300 
SLHEFGTDFD VYTHEDSMHT SGRVDQAIAK LRETGSIYEK DGAVWLRTTD FGDDKDRVVI 

       310        320        330        340        350        360 
KSDGQPAYIA GDLAYFLDKR KRGFDLCIYM LGADHHGYIA RLKAAAAALG DDPDTVEVLI 

       370        380        390        400        410        420 
GQMVNLVRDG QPVRMSKRAG TVITLDDLVD AIGVDAARYA LIRSSVDTPI DIDLALWSSA 

       430        440        450        460        470        480 
SNENPVYYVQ YAHARLSALA RNAAELGVAA DTAHLDLLTH DKEGTLIRNI GEFPRVLKTA 

       490        500        510        520        530        540 
ASLREPHRVS RYLEDLAGDY HRFYDSCRVL PQGDETPGDL HAARLALCAA TRQVIANGLG 

       550 
ILGVSAPERM 

« Hide

References

[1]"Complete sequence of Mycobacterium vanbaalenii PYR-1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.J., Miller C., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 7251 / PYR-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000511 Genomic DNA. Translation: ABM15127.1.
RefSeqYP_955133.1. NC_008726.1.

3D structure databases

ProteinModelPortalA1TD77.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING350058.Mvan_4350.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM15127; ABM15127; Mvan_4350.
GeneID4647345.
KEGGmva:Mvan_4350.
PATRIC18187035. VBIMycVan31953_4422.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247214.
KOK01887.
OMANPNGPLH.
OrthoDBEOG6JB13C.
ProtClustDBPRK01611.

Enzyme and pathway databases

BioCycMVAN350058:GIWR-4389-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_MYCVP
AccessionPrimary (citable) accession number: A1TD77
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: April 16, 2014
This is version 50 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