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Q88CU1 (SYR_PSEPK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 72. 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:PP_5089
OrganismPseudomonas putida (strain KT2440) [Complete proteome] [HAMAP]
Taxonomic identifier160488 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length578 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 – 578578Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_0000151593

Regions

Motif127 – 13711"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q88CU1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 3EB8E057F3D392E0

FASTA57863,669
        10         20         30         40         50         60 
MKDTIRQLIQ QALTQLVTDG VLPEGLSPAI QVENARDKTH GDFASNIAMM LAKPAGMKPR 

        70         80         90        100        110        120 
DLAEKLINAL PASADISKVE IAGPGFLNFF QNTDALANRL DAALADAHLG ARKAGPAQKV 

       130        140        150        160        170        180 
VIDMSAPNLA KEMHVGHLRS TIIGDSVARV LEFLGDNVIR QNHVGDWGTQ FGMLMAYLQE 

       190        200        210        220        230        240 
NPITSDELSD LENFYRAAKK RFDESEEFAT RARGLVVKLQ AGDPECLALW TRFKDISLSH 

       250        260        270        280        290        300 
CQKTYELLNV KLTMADVMGE SAYNDDLANV VADLKAKGLL VEDQGAQCVF LEEFKNSDGD 

       310        320        330        340        350        360 
PLPVIVQKAD GGYLYATTDL AAVRYRSNVL KADRALYFVD QRQALHFNQV FEVARRAGFV 

       370        380        390        400        410        420 
GHPMQMEHMG FGTMNGADGR PFKTRDGGTV KLIDLLTEAK ERAYALVKEK NPSLADDELR 

       430        440        450        460        470        480 
HIGEVVGIGA VKYADLSKHR TSDYSFNFEL MLNFEGNTAP YLLYAYTRVA GVFRKLGKGF 

       490        500        510        520        530        540 
DEVDGKIVLQ AAHEQDLAAR LAQFGEILNN VAEKGTPHVL CSYLYDLAGL FSSFYENCPI 

       550        560        570 
LAAETPSQQQ SRLRLAALTG RTLKQGLELL GLETLERM 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE015451 Genomic DNA. Translation: AAN70654.1.
RefSeqNP_747190.1. NC_002947.3.

3D structure databases

ProteinModelPortalQ88CU1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING160488.PP_5089.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN70654; AAN70654; PP_5089.
GeneID1041719.
KEGGppu:PP_5089.
PATRIC19949006. VBIPsePut30601_5432.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247212.
KOK01887.
OMANPNGPLH.
OrthoDBEOG6JB13C.
ProtClustDBPRK01611.

Enzyme and pathway databases

BioCycPPUT160488:GIXO-5185-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_PSEPK
AccessionPrimary (citable) accession number: Q88CU1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: June 1, 2003
Last modified: April 16, 2014
This is version 72 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