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B4RU34 (SYR_ALTMD) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 40. 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:MADE_1006385
OrganismAlteromonas macleodii (strain DSM 17117 / Deep ecotype) [Complete proteome] [HAMAP]
Taxonomic identifier314275 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesAlteromonadaceaeAlteromonas

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_1000095331

Regions

Motif121 – 13111"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
B4RU34 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: ED517638A3E21E08

FASTA57664,273
        10         20         30         40         50         60 
MNIHALLVNR FTEALQEMGV ENAPVPVSRS ARPEFGEYQF NGAMALAKQL KQKPRDIAEK 

        70         80         90        100        110        120 
IVETVKLDDI ASKLEVAGPG FINVHLNDAW LANQCELSLT DPRLGIAKSP EQNIVVDYSS 

       130        140        150        160        170        180 
PNLAKEMHVG HLRTTIIGDA VVKVLEFLGH NVIRQNHMGD WGTQFGMLLA HLSDKLQEEV 

       190        200        210        220        230        240 
AETALSDLED FYREAKVRFD EEEGFADRAR EYVVKLQGGD AQCLALWEKF IDVSITHSEE 

       250        260        270        280        290        300 
VYDKLNVSLT RKDIMGESAY NDDLANVISD LKTKGLAVED QGAQVVFIPE LADKEGNPAV 

       310        320        330        340        350        360 
YIVQKSGGGY LYATTDLAAM RYRSGKLNAD RTLILTDARQ ALHFKQTEIV GRKAGFMKEE 

       370        380        390        400        410        420 
QTYEHCPFGM MLGSDGKPFK TRTGGTVKLV ELLDEAVERA GKLIAERDND LSEEELKEVA 

       430        440        450        460        470        480 
RKVGIGAVKY ADLSKNRTTD YMFNWDSMLS FEGNTAPYLQ YAYTRVKSLF RKAGVDMATM 

       490        500        510        520        530        540 
PVDIKLVEKQ EHALAVLLMQ FEEVIGMVSR EATPHVLCTY LYDVASAFMT FYEACPMLKE 

       550        560        570 
GIEPQVRDSR LALSALVAKT LEKGLTLLGI ETLEKM 

« Hide

References

[1]"Comparative genomics of two ecotypes of the marine planktonic copiotroph Alteromonas macleodii suggests alternative lifestyles associated with different kinds of particulate organic matter."
Ivars-Martinez E., Martin-Cuadrado A.-B., D'Auria G., Mira A., Ferriera S., Johnson J., Friedman R., Rodriguez-Valera F.
ISME J. 2:1194-1212(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17117 / Deep ecotype.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001103 Genomic DNA. Translation: AEA97419.1.
RefSeqYP_004426417.1. NC_011138.3.

3D structure databases

ProteinModelPortalB4RU34.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING314275.MADE_02786.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEA97419; AEA97419; MADE_1006385.
GeneID10556619.
KEGGamc:MADE_1006385.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
KOK01887.
OMANPNGPLH.
ProtClustDBPRK01611.

Enzyme and pathway databases

BioCycAMAC314275:GHA7-1294-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_ALTMD
AccessionPrimary (citable) accession number: B4RU34
Secondary accession number(s): F2G4W5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 23, 2008
Last modified: April 16, 2014
This is version 40 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