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Q9X5M0 (SYR_MYCS2) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 92. 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:MSMEG_4959, MSMEI_4832
OrganismMycobacterium smegmatis (strain ATCC 700084 / mc(2)155) [Reference proteome] [HAMAP]
Taxonomic identifier246196 [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
Reference 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_0000151579

Regions

Motif130 – 14011"HIGH" region HAMAP-Rule MF_00123

Experimental info

Sequence conflict1491A → T in AAD32590. Ref.1
Sequence conflict2321D → N in AAD32590. Ref.1
Sequence conflict255 – 2573EDS → GDW in AAD32590. Ref.1
Sequence conflict3311L → V in AAD32590. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9X5M0 [UniParc].

Last modified July 10, 2007. Version 2.
Checksum: 4DAB7844FFFCFCEC

FASTA55059,429
        10         20         30         40         50         60 
MTPADLAELL KATAAAVLTE HDLDVAALPA TVTVERPRNP EHGDYATNLA LQLGKKVGVN 

        70         80         90        100        110        120 
PRELAGWLAT ALTAADGIAV AEVAGPGFVN LRIEASAQGV IITNVLAAEG SYGSSDQYAG 

       130        140        150        160        170        180 
RNVNLEFVSA NPTGPIHIGG TRWAAVGDAL GRLLATQGAA VTREYYFNDH GAQIDRFVNS 

       190        200        210        220        230        240 
LIASAKGEPT PEDGYAGDYI VDIAQQVIAK APDVLGLPED QQRETFRAIG VDLMFTHIKQ 

       250        260        270        280        290        300 
SLHDFGTDFD VYTHEDSMHT SGRVDQAITQ LREAGSIYEK DGAVWLRTTD FGDDKDRVVI 

       310        320        330        340        350        360 
KSDGNAAYIA GDLAYYLDKR KRGFDLCIYM LGADHHGYIA RLKAAAAALG DDPDTVEVLI 

       370        380        390        400        410        420 
GQMVNLVRDG QPVRMSKRAG TVITLDDLVE AIGVDAARYA LIRSSVDTPI DIDLELWSSA 

       430        440        450        460        470        480 
SNENPVYYVQ YAHARLCALA RNAADLGVSV NTDHLDLLTH EKEGALIRNL GEFPRVLKTA 

       490        500        510        520        530        540 
ASLREPHRVC RYLEDLAGDY HRFYDSCRVL PQGDEEPGDL HSARLALCRA TRQVIANGLA 

       550 
ILGVSAPERM 

« Hide

References

« Hide 'large scale' references
[1]"A comparison of the construction of unmarked deletion mutations in Mycobacterium smegmatis, M. bovis bacille Calmette-Guerin (BCG) and M. tuberculosis H37Rv by allelic exchange."
Pavelka M.S. Jr., Jacobs W.R. Jr.
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700084 / mc(2)155.
[3]"Interrupted coding sequences in Mycobacterium smegmatis: authentic mutations or sequencing errors?"
Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C., Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.
Genome Biol. 8:R20.1-R20.9(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700084 / mc(2)155.
[4]"Ortho-proteogenomics: multiple proteomes investigation through orthology and a new MS-based protocol."
Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.
Genome Res. 19:128-135(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700084 / mc(2)155.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF126720 Genomic DNA. Translation: AAD32590.1.
CP000480 Genomic DNA. Translation: ABK70921.1.
CP001663 Genomic DNA. Translation: AFP41277.1.
RefSeqYP_006569572.1. NC_018289.1.
YP_889211.1. NC_008596.1.

3D structure databases

ProteinModelPortalQ9X5M0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING246196.MSMEG_4959.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK70921; ABK70921; MSMEG_4959.
AFP41277; AFP41277; MSMEI_4832.
GeneID4534266.
KEGGmsg:MSMEI_4832.
msm:MSMEG_4959.
PATRIC18082217. VBIMycSme59918_4838.

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247214.
KOK01887.
OMAIRNTIND.
OrthoDBEOG6JB13C.

Enzyme and pathway databases

BioCycMSME246196:GJ4Y-4958-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_MYCS2
AccessionPrimary (citable) accession number: Q9X5M0
Secondary accession number(s): A0R223, I7G6F4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 10, 2007
Last modified: July 9, 2014
This is version 92 of the entry and version 2 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