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Q03GE2 (SYR_PEDPA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 52. 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:PEPE_0669
OrganismPediococcus pentosaceus (strain ATCC 25745 / 183-1w) [Complete proteome] [HAMAP]
Taxonomic identifier278197 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaePediococcus

Protein attributes

Sequence length562 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 – 562562Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000018084

Regions

Motif122 – 13211"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q03GE2 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: 356510C014CBE991

FASTA56263,511
        10         20         30         40         50         60 
MDYKKKVAAA LAPALNEYLT DTEIYEKIEI PKESKMGDYA FPTFTLAKVL RKAPQMIASE 

        70         80         90        100        110        120 
LVEKIDQDQF EKVEVAGPYI NFFLDKTAFG AEVLGTVLSQ KAEYGQNDDG NQGNVPIDMS 

       130        140        150        160        170        180 
SPNIAKPISM GHLRSTVIGN SLSLIMSKNG YNPIKINHLG DWGTQFGKLI TAYKLWGSEE 

       190        200        210        220        230        240 
EVKADPINKL LEYYVRFHKE DQEKPELDDI ARDWFKKLED GDEEAMNLWQ WFREESLKSF 

       250        260        270        280        290        300 
KQIYDKLGIT FDSYKGEAFY NDKMDEIVQI LEDKGLLKES QGAQVVDLEK YNLNPALIKK 

       310        320        330        340        350        360 
TDGATLYITR DLAAALYRYR TYDFNQSLYV VGAEQTNHFK QLKAVLKEMG FDWSDDVHHI 

       370        380        390        400        410        420 
PFGLITLNGK KLSTRSGRVV LLDEVLNDAV SLAKKQINDK NPDLANADTV AKEVGVGAVI 

       430        440        450        460        470        480 
FHDLKNERTN SFDFNLEDVV RFEGETGPYV QYSRARAESI LRKAGDVEEF AQLNITDPKA 

       490        500        510        520        530        540 
WDTLKALQDF PNIVKRAAAQ YEPSVIAKYA LGLAKAFNKY YANSKILADD EEKTARLALV 

       550        560 
KSVSIVLEES LRLLGVKAPD EM 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000422 Genomic DNA. Translation: ABJ67730.1.
RefSeqYP_804172.1. NC_008525.1.

3D structure databases

ProteinModelPortalQ03GE2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING278197.PEPE_0669.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ67730; ABJ67730; PEPE_0669.
GeneID4418134.
KEGGppe:PEPE_0669.
PATRIC22874694. VBIPedPen34213_0632.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247211.
KOK01887.
OMAYVKFHDE.
OrthoDBEOG6JB13C.

Enzyme and pathway databases

BioCycPPEN278197:GI4Y-669-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_PEDPA
AccessionPrimary (citable) accession number: Q03GE2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 14, 2006
Last modified: May 14, 2014
This is version 52 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