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Q6MLI2 (SYR_BDEBA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 67. 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:Bd2027
OrganismBdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIB 9529 / HD100) [Complete proteome] [HAMAP]
Taxonomic identifier264462 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaBdellovibrionalesBdellovibrionaceaeBdellovibrio

Protein attributes

Sequence length580 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 – 580580Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_0000241990

Regions

Motif127 – 13711"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q6MLI2 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: F4A9AA2260E1B08D

FASTA58065,364
        10         20         30         40         50         60 
MIKHDSIRLL ATNLLKDAIG RAYPDFSASE DDIYKALVNP PKSDLGDLAF GCFILAKALK 

        70         80         90        100        110        120 
TAPPQVATAV AAQMKGATAV AAGPYINIRF DEQTHGEQVL ATILDGSYFK KPLMEKSPKT 

       130        140        150        160        170        180 
MIEYSQPNTH KELHVGHMRN LCLGDAIVRM LRYSGREIVS STFPGDMGTH VAKCLWYMKK 

       190        200        210        220        230        240 
HNQEPVPETE KGEWLGRMYS KANLLLEDQN GTPQEDINRQ ELTAILHQLE GKTGPYYDLW 

       250        260        270        280        290        300 
LETREWSIEL MKKVYAWADV TFDEWYFESE MDSPSAAWVK QLYAEGKLEM SQGAIGKDLE 

       310        320        330        340        350        360 
SEKLGFCMLL KSDGTGLYAT KDLLLAKHKF EDVKIEKSVY VVDMRQALHF KQVFRVLEIL 

       370        380        390        400        410        420 
GFEQAKNCFH LQYNYVELPD GAMSSRKGNI VPLRELVHRM EDHVKTTYLS RYKGEWSEED 

       430        440        450        460        470        480 
VEKIAGQVAK GAIFYGMLRM DTNKKIVFDM NEWLKLDGES GPFVQYSYAR ISSLGRKFPR 

       490        500        510        520        530        540 
TAGAKIDWSR LNHASERQLM QSLGGFNTAV AAAAENFKPS AICTYLYDLA KSFNVFYHEC 

       550        560        570        580 
PIGTEADVAT REARLALSEA VGLTLKNGLA VLGMPAPEKM 

« Hide

References

[1]"A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a genomic perspective."
Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C., Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E., Schuster S.C.
Science 303:689-692(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15356 / DSM 50701 / NCIB 9529 / HD100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX842651 Genomic DNA. Translation: CAE79875.1.
RefSeqNP_968882.1. NC_005363.1.

3D structure databases

ProteinModelPortalQ6MLI2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264462.Bd2027.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE79875; CAE79875; Bd2027.
GeneID2734744.
KEGGbba:Bd2027.
PATRIC21078558. VBIBdeBac73187_1846.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
KOK01887.
OMAYVKFHDE.
OrthoDBEOG6JB13C.

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_BDEBA
AccessionPrimary (citable) accession number: Q6MLI2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: July 5, 2004
Last modified: May 14, 2014
This is version 67 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