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B2IMZ8 (SYR_STRPS) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 40. 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:SPCG_2045
OrganismStreptococcus pneumoniae (strain CGSP14) [Complete proteome] [HAMAP]
Taxonomic identifier516950 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length563 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 – 563563Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000095413

Regions

Motif121 – 13111"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
B2IMZ8 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: 3ECEED708A50F365

FASTA56363,488
        10         20         30         40         50         60 
MNTKELIASE LSSIIDSLDQ EAILKLLETP KNSEMGDIAF PAFSLAKVER KAPQMIAAEL 

        70         80         90        100        110        120 
AEKMNSQAFE KVVATGPYVN FFLDKSAISA QVLQAVTTEK EHYADQNIGK QENVVIDMSS 

       130        140        150        160        170        180 
PNIAKPFSIG HLRSTVIGDS LSHIFQKIGY QTVKVNHLGD WGKQFGMLIV AYKKWGDEEA 

       190        200        210        220        230        240 
VKAHPIDELL KLYVRINAEA ENDPSLDEEA REWFRKLENG DEEALALWQW FRDESLVEFN 

       250        260        270        280        290        300 
RLYNELKVEF DSYNGEAFYN DKMDAVVDIL SEKGLLLESE GAQVVNLEKY GIEHPALIKK 

       310        320        330        340        350        360 
SDGATLYITR DLAAALYRKN EYQFAKSIYV VGQEQSAHFK QLKAVLQEMG YDWSDDITHV 

       370        380        390        400        410        420 
PFGLVTKEGK KLSTRKGNVI LLEPTIAEAV SRAKVQIEAK NPELENKDQV AHAVGVGAIK 

       430        440        450        460        470        480 
FYDLKTDRTN GYDFDLEAMV SFEGETGPYV QYAYARIQSI LRKADFKPET SGNYSLNDTE 

       490        500        510        520        530        540 
SWEIIKLIQD FPRIINRAAD NFEPSIIAKF AISLAQSFNK YYAHTRILDE SPERDSRLAL 

       550        560 
SYATAVVLKE ALRLLGVEAP EKM 

« Hide

References

[1]"Genome evolution driven by host adaptations results in a more virulent and antimicrobial-resistant Streptococcus pneumoniae serotype 14."
Ding F., Tang P., Hsu M.-H., Cui P., Hu S., Yu J., Chiu C.-H.
BMC Genomics 10:158-158(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CGSP14.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001033 Genomic DNA. Translation: ACB91297.1.
RefSeqYP_001836762.1. NC_010582.1.

3D structure databases

ProteinModelPortalB2IMZ8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING516950.SPCG_2045.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB91297; ACB91297; SPCG_2045.
GeneID6217861.
KEGGspw:SPCG_2045.
PATRIC19680579. VBIStrPne123335_2193.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247211.
KOK01887.
OMANPNGPLH.
OrthoDBEOG6JB13C.
ProtClustDBPRK01611.

Enzyme and pathway databases

BioCycSPNE516950:GI38-2112-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.
InterProIPR001278. 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.
ProtoNetSearch...

Entry information

Entry nameSYR_STRPS
AccessionPrimary (citable) accession number: B2IMZ8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: June 10, 2008
Last modified: April 16, 2014
This is version 40 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