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Q88X53 (SYR_LACPL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 69. 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:lp_1391
OrganismLactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1) [Reference proteome] [HAMAP]
Taxonomic identifier220668 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

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
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 – 562562Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_0000151568

Regions

Motif121 – 13111"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q88X53 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: D3B1F7AF5B6682C2

FASTA56262,910
        10         20         30         40         50         60 
MDYKQLVAAA LAPALPDLTQ EAILDKIEQP KTSKQGDLAF PTFTLAKTLH KAPQMIASDI 

        70         80         90        100        110        120 
VEKVDSSDFE KVVAMGPYVN FFFKKDAFAA DILNQVLSNG GHFGDAKLGE AGQVPIDMSS 

       130        140        150        160        170        180 
PNIAKPISMG HLRSTVIGNS LANILSKLDY QPVKINHLGD WGTQFGKLIT AYKMWGSEAE 

       190        200        210        220        230        240 
VKADPINNLL KYYVRFHKED VDHPEMDDEA REWFKKLENG DEEATHLWSW FRSESLKAFK 

       250        260        270        280        290        300 
KIYQRLDIDF DSFKGEAFYN DKMQEVVDIL EDKHLLQESQ GAEVVDLSKY DLNPALIKKS 

       310        320        330        340        350        360 
DGATLYITRD LAAAIYRKRT YDFVQSLYVV GNEQTNHFKQ LKAVLTEMGF DWADQIHHIP 

       370        380        390        400        410        420 
FGLITSGGKK LSTRSGRVIL LDKVLDDAVA LAHEQIEAKN PDLPNKDEVA DAVGIGAVVF 

       430        440        450        460        470        480 
HDLKNERMNS FDFNLEEVVR FEGETGPYVQ YAHARAESIL RKAGSPEIAA TEQTLSDPAA 

       490        500        510        520        530        540 
WDTLKLLSEF PATVVRASTE YEPSVIAKYA IHLAKAYNKY YANTKILVED DELNARLALV 

       550        560 
KSVSIVLKEA LRLLGVKAPD EM 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL935263 Genomic DNA. Translation: CCC78734.1.
RefSeqYP_004889248.1. NC_004567.2.

3D structure databases

ProteinModelPortalQ88X53.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING220668.lp_1391.

Proteomic databases

PRIDEQ88X53.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCCC78734; CCC78734; lp_1391.
GeneID1062530.
KEGGlpl:lp_1391.
PATRIC22249045. VBILacPla27411_1165.

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247211.
KOK01887.
OMANPNGPLH.
ProtClustDBPRK01611.

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_LACPL
AccessionPrimary (citable) accession number: Q88X53
Secondary accession number(s): F9UNE5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: June 1, 2003
Last modified: April 16, 2014
This is version 69 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