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Q5WB34 (SYR_BACSK) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 65. 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:ABC3895
OrganismBacillus clausii (strain KSM-K16) [Complete proteome] [HAMAP]
Taxonomic identifier66692 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length556 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 – 556556Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_0000241982

Regions

Motif132 – 14211"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q5WB34 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 16141FBCD803792D

FASTA55662,498
        10         20         30         40         50         60 
MNHMERKKEQ LRVEVRRAVL QAELATESEV PSVLLEAPKD KAHGDFATNI AMQLARIAKK 

        70         80         90        100        110        120 
APRAIAEELV ANFDRKQAGI EKIEIAGPGF INFFLDNGYL RELIPQVLTE KDDYGSSDVG 

       130        140        150        160        170        180 
QGEKVLIEFV SANPTGDLHL GHARGAAVGD TIANIMDKAG YKVSREYYIN DAGNQIENLA 

       190        200        210        220        230        240 
ASLNARYLQV LGEDQPMPED GYHGQDIIDI AKQLVDEAGD QYRQLDEKER LAFMRDYGLK 

       250        260        270        280        290        300 
KELEKIKQDL NAYRVEFDKW FSETSLYESG QVERGLQVLK DKNETYEKDG ATWLRSTAYG 

       310        320        330        340        350        360 
DDKDRVLVKQ DGTYTYLTPD ISYHLDKFDR GHDRLIDVLG ADHHGYIPRM RAAIQALGYD 

       370        380        390        400        410        420 
PARFNVQIIQ MVSLFQGGEK VKMSKRTGKA VTLRELMEEV GVDATRYFFA MRSPDTHLDF 

       430        440        450        460        470        480 
DMDLAVSKSN ENPVYYIQYA HARVCSILRQ GEELGIPYSA NTDLSPIASE KEYELLKAIG 

       490        500        510        520        530        540 
EFPGAVAEAA TKQIPQRIAN YAYDLAQALH SFYNVTRVID TENKDLSAAR LALMKATQMT 

       550 
IKNALALLGV EAPEKM 

« Hide

References

[1]"The complete genome sequence of the alkaliphilic Bacillus clausii KSM-K16."
Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y., Kawai S., Ito S., Horikoshi K.
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KSM-K16.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006627 Genomic DNA. Translation: BAD66426.1.
RefSeqYP_177387.1. NC_006582.1.

3D structure databases

ProteinModelPortalQ5WB34.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING66692.ABC3895.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD66426; BAD66426; ABC3895.
GeneID3201720.
KEGGbcl:ABC3895.
PATRIC18927592. VBIBacCla58185_4144.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247214.
KOK01887.
OMAMEHMGFG.
OrthoDBEOG6JB13C.

Enzyme and pathway databases

BioCycBCLA66692:GHMP-3975-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_BACSK
AccessionPrimary (citable) accession number: Q5WB34
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: November 23, 2004
Last modified: May 14, 2014
This is version 65 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