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Q7U3V8 (SYR_SYNPX) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 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:SYNW2319
OrganismSynechococcus sp. (strain WH8102) [Complete proteome] [HAMAP]
Taxonomic identifier84588 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length597 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 – 597597Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_0000151626

Regions

Motif137 – 14711"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q7U3V8 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: EC115129CA50D277

FASTA59765,486
        10         20         30         40         50         60 
MPDVPALMLS LSNTLDAQLR AAMQRAFPVA DAVLDPQLAP ASKPEFGDFQ ANGALPLAKP 

        70         80         90        100        110        120 
LKQAPRQIAT AIVEQLQADS GFTDLCLEPQ IAGPGFINLT IRPERLAAEV SARLGDERLG 

       130        140        150        160        170        180 
VPAVEQAAPV VVDFSSPNIA KEMHVGHLRS TIIGDSLARV LEFRGHTVLR LNHVGDWGTQ 

       190        200        210        220        230        240 
FGMLITHLKQ VAPDALETAD AVDLGDLVAF YREAKKRFDD DEAFQSTSRE EVVKLQGGDP 

       250        260        270        280        290        300 
VSLKAWGLLC DQSRREFQKI YDRLDIRLNE RGESFYNPFL PAVIDGLKAA ELLVTDDGAQ 

       310        320        330        340        350        360 
CVFLEGVQGK DGKPLPVIVQ KSDGGFNYAT TDLAAIRYRF GAAPDGDGAR RVVYVTDAGQ 

       370        380        390        400        410        420 
ANHFAGVFQV AERAGWIPDG ARLEHVPFGL VQGEDGKKLK TRAGDTVRLR DLLDEAVERA 

       430        440        450        460        470        480 
ETDLRSRLKE EERSESEEFI QNVAGTVGLA AVKYADLSQN RITNYQFSFD RMLALQGNTA 

       490        500        510        520        530        540 
PYLLYAVVRI AGIARKGGDL EVSTGQLQFS EPQEWALVRE LLKFDSVIAE VEEELLPNRL 

       550        560        570        580        590 
CSYLFELSQV FNRFYDQVPV LKADPEALAS RLALCRLTAD TLRLGLGLLG IATLDRM 

« Hide

References

[1]"The genome of a motile marine Synechococcus."
Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P., Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T., Dufresne A., Partensky F., Webb E.A., Waterbury J.
Nature 424:1037-1042(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: WH8102.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX569695 Genomic DNA. Translation: CAE08834.1.
RefSeqNP_898408.1. NC_005070.1.

3D structure databases

ProteinModelPortalQ7U3V8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING84588.SYNW2319.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE08834; CAE08834; SYNW2319.
GeneID1730769.
KEGGsyw:SYNW2319.
PATRIC23836392. VBISynSp27240_2466.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247212.
KOK01887.
OMADGTAVYM.
OrthoDBEOG6JB13C.
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.
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_SYNPX
AccessionPrimary (citable) accession number: Q7U3V8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2003
Last modified: April 16, 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