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C4K487 (SYR_HAMD5) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 30. 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:HDEF_0639
OrganismHamiltonella defensa subsp. Acyrthosiphon pisum (strain 5AT) [Complete proteome] [HAMAP]
Taxonomic identifier572265 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeaphid secondary symbiontsCandidatus Hamiltonella

Protein attributes

Sequence length576 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 – 576576Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000203098

Regions

Motif122 – 13211"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
C4K487 [UniParc].

Last modified July 7, 2009. Version 1.
Checksum: 4C6852EFECDFFBFB

FASTA57665,553
        10         20         30         40         50         60 
MNIQLFLSDR IRHALIMAGA PDDSDAQLHP STKAQFGDYQ ANGVMSAAKK QRIPPRELAE 

        70         80         90        100        110        120 
RVLEHLDLSD IAKKVEIAGP GFINIFLNEQ WISQKIESVF IGPKLGLTPV TPQRIVIDYS 

       130        140        150        160        170        180 
APNVAKEMHV GHLRSTIIGD AMARTLSFLG HHVIRANHIG DWGTQFGMLI AYLEKIQHDH 

       190        200        210        220        230        240 
ALEMVLSDLE HFYREAKKHY DEDEIFAQRA RDYVVKLQSG DPYCREMWRK LVDITMTQNH 

       250        260        270        280        290        300 
LSYERLKVTL TPEDMMGESL YNDMLPNIVE DLIAKGVAVK DQGSVLVFLE EYQNKIGEPM 

       310        320        330        340        350        360 
GVVIQKKDGG YLYATTDIAC VKYRCETLKA DRILYYIDSR QNQHLAQVWT ITRLAGYVPE 

       370        380        390        400        410        420 
SVSLEHHMFG MMLGKDGKPF KTRTGGTVKL SDLLDEAVER AGQLIRGKNP DLNETDLNNL 

       430        440        450        460        470        480 
IQAVAIGAVK YADLSKNRTT DYIFDWDRML SFEGNTAPYI QYAYSRVTSL FKKSGLDEKK 

       490        500        510        520        530        540 
IMSPVIIQEE KERSLAILLL QFEEMISTVA RDGTPHLMCS YLYDLATRFS IFYEHCPILN 

       550        560        570 
AKNEQIRQSR LKLAWLTAKT LKLGLKNLGI ETVERM 

« Hide

References

[1]"Hamiltonella defensa, genome evolution of protective bacterial endosymbiont from pathogenic ancestors."
Degnan P.H., Yu Y., Sisneros N., Wing R.A., Moran N.A.
Proc. Natl. Acad. Sci. U.S.A. 106:9063-9068(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 5AT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001277 Genomic DNA. Translation: ACQ67380.1.
RefSeqYP_002923528.1. NC_012751.1.

3D structure databases

ProteinModelPortalC4K487.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING572265.HDEF_0639.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACQ67380; ACQ67380; HDEF_0639.
GeneID7950242.
KEGGhde:HDEF_0639.
PATRIC31972731. VBICanHam112931_0652.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
KOK01887.
OMANPNGPLH.
OrthoDBEOG6JB13C.

Enzyme and pathway databases

BioCycHDEF572265:GJAB-644-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_HAMD5
AccessionPrimary (citable) accession number: C4K487
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 7, 2009
Last modified: April 16, 2014
This is version 30 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