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A5CXW2 (SYR_VESOH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 47. 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:COSY_0085
OrganismVesicomyosocius okutanii subsp. Calyptogena okutanii (strain HA) [Complete proteome] [HAMAP]
Taxonomic identifier412965 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriasulfur-oxidizing symbionts

Protein attributes

Sequence length572 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 – 572572Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000018143

Regions

Motif127 – 13711"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
A5CXW2 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 4900D5213CB3B058

FASTA57265,124
        10         20         30         40         50         60 
MKQLLQQLLV QSLEVLMDNN ILESMPENIR VDHSKDKAQG DFASNIAMLL SEQAQCSSKV 

        70         80         90        100        110        120 
LAQKIKANFP DSVDVEKIEI VGPGFINFFM SQSSNALVVE DIIKQGGNYG LSNIGMGQRV 

       130        140        150        160        170        180 
LLEFVSANPT GPLHVGHGRG VAYGAAVAHL LRAVGFEVDC EYYVNDAGRQ MDILAISVYL 

       190        200        210        220        230        240 
RYVETEQFPD NCYKGDYIFD IAKKISGVKK LDIFTNTCKD TSEWKVQKNS IDKERYIDDL 

       250        260        270        280        290        300 
IANCKLQLGS DYRKVFDFAI NSILSDIKID LADFGVEYHQ WFSEQSLVDS GLSEEIVKKL 

       310        320        330        340        350        360 
QDLGYIYEKE GALWFRTTDF GDDLDRVVVR DNGIHTYFSY DIAYHLGKFE RGYDRIINIW 

       370        380        390        400        410        420 
GADHHGYIAR VKASIKALNY NPDKLEILLV QFVNLFRDGK KVSMSTRSGS FITLKELREE 

       430        440        450        460        470        480 
VGNDVVRFFY ILRKSTQHMD FNLDLAKSKS NENPVFYIQY AYVRICSVLK QGMPFMADID 

       490        500        510        520        530        540 
LLVLNNELET LLIKELNRYK DILQSSALNY EPHVLACYLR KLAGYFHSYY NNCEFLVDDD 

       550        560        570 
KLRNSRLLLI TAVQQILANG LNLLGISTPN SM 

« Hide

References

[1]"Reduced genome of the thioautotrophic intracellular symbiont in a deep-sea clam, Calyptogena okutanii."
Kuwahara H., Yoshida T., Takaki Y., Shimamura S., Nishi S., Harada M., Matsuyama K., Takishita K., Kawato M., Uematsu K., Fujiwara Y., Sato T., Kato C., Kitagawa M., Kato I., Maruyama T.
Curr. Biol. 17:881-886(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HA.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009247 Genomic DNA. Translation: BAF61221.1.
RefSeqYP_001218945.1. NC_009465.1.

3D structure databases

ProteinModelPortalA5CXW2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING412965.COSY_0085.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAF61221; BAF61221; COSY_0085.
GeneID5172418.
KEGGvok:COSY_0085.
PATRIC32019981. VBICanVes128383_0084.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247214.
KOK01887.
OMANPNGPLH.
OrthoDBEOG6JB13C.
ProtClustDBPRK01611.

Enzyme and pathway databases

BioCycCVES412965:GHZZ-86-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_VESOH
AccessionPrimary (citable) accession number: A5CXW2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 12, 2007
Last modified: April 16, 2014
This is version 47 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