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A8FQM2 (SYR_SHESH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 44. 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:Ssed_0533
OrganismShewanella sediminis (strain HAW-EB3) [Complete proteome] [HAMAP]
Taxonomic identifier425104 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length581 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 – 581581Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000076232

Regions

Motif126 – 13611"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
A8FQM2 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: 0EA349F8DCC74CDC

FASTA58165,066
        10         20         30         40         50         60 
MKSHIQSLLI QALDALKQQG VIPTDFEARV QVDRTKDKTH GDFATNLAMM LTKVARKNPR 

        70         80         90        100        110        120 
ELAQLIIDSL PQDSQVAKVE IAGPGFINFF IDENALASQL MAALNDDHLG IQLPEPQTVV 

       130        140        150        160        170        180 
VDYSSPNLAK EMHVGHLRST IIGDSVVRAL EFQGHNVIRQ NHVGDWGTQF GMLLAYMEEL 

       190        200        210        220        230        240 
RAENGEQAQM ELSDLETFYR AAKVRFDESE DFAIRARKLV VSLQSGDEYC NKLWREFNDI 

       250        260        270        280        290        300 
SLSHCHDVYE RLGVSLTRKD VRGESTYNDD LEQVVKDLDA KGLLSESNGA KVVFQDEFKT 

       310        320        330        340        350        360 
KDGDPLPVII QKADGGYLYA TSDLAAMRYR SNVLKADRAL YFVDLRQGLH FQQVFKLART 

       370        380        390        400        410        420 
AEFINPDMSL EHMGFGTMNG DDGRPFKTRS GGVVKLVDLL TEADTRALEL VRSKNPDMDQ 

       430        440        450        460        470        480 
AELEKIAKVV GISSVKYADL SKNRASDYIF SFEQMLSFEG NTAPYLLYAY TRVAGIFKRA 

       490        500        510        520        530        540 
TDIDLSDAKM QLDHDKEKDL GNKLAQFGEV LSRMVTKGQP HALCGYLFEL AGAFSSFYEA 

       550        560        570        580 
CPVLAAESEE QKKSRLLLSQ LTAKTLKQGL DLLGIETLER M 

« Hide

References

[1]"Complete sequence of Shewanella sediminis HAW-EB3."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Zhao J.-S., Richardson P.
Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HAW-EB3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000821 Genomic DNA. Translation: ABV35145.1.
RefSeqYP_001472273.1. NC_009831.1.

3D structure databases

ProteinModelPortalA8FQM2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING425104.Ssed_0533.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV35145; ABV35145; Ssed_0533.
GeneID5613785.
KEGGsse:Ssed_0533.
PATRIC23558298. VBISheSed62411_0564.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSSED425104:GH7Q-555-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_SHESH
AccessionPrimary (citable) accession number: A8FQM2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: November 13, 2007
Last modified: April 16, 2014
This is version 44 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