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A0L5I2 (SYR_MAGSM) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 51. 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:Mmc1_0704
OrganismMagnetococcus sp. (strain MC-1) [Complete proteome] [HAMAP]
Taxonomic identifier156889 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaMagnetococcalesMagnetococcaceaeMagnetococcus

Protein attributes

Sequence length575 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 – 575575Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000095379

Regions

Motif130 – 14011"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
A0L5I2 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: EDB8C99DE49200EB

FASTA57563,647
        10         20         30         40         50         60 
MRQSIEELME HAQNTLLAEG VIPADAKLGG IKVERPKDKS HGDFSINTAM VLAKQARMKP 

        70         80         90        100        110        120 
RDLAQRLVDA LPSGQGVVSR CEIAGPGFIN FFVTPERLRG VVADVLQRGG SYGQGNVGAG 

       130        140        150        160        170        180 
QKVLVEFVSA NPTGPMHVGH GRGAVTGDVL ARILECAGYA VQREYYLNDA GVQVQVLGRS 

       190        200        210        220        230        240 
VMLRYRQLFG DAVEVAEGCY PGDYVVDIAR ALKEKDQDKW LEVARAEPDE YPREMLEFAM 

       250        260        270        280        290        300 
QQVLTWIKAD LARLNIRFDH WFSEFSLHSE GRIEHALEVL SQKGCLYEGV LEPPKGKKSE 

       310        320        330        340        350        360 
AWASRPQLLF KATDFGDEVD RALRKSDGSY TYFAADVAYH LNKAERGFER LVNIWGADHG 

       370        380        390        400        410        420 
GYVRRVQAAL GALTGKQNLL DVVLIQMVNL TRGGEPVKMS KRAGTFVTLE EVVEATSSDA 

       430        440        450        460        470        480 
VRFWFLSRGS GAQLDFDLDL AVAKNNDNPV YYVQYAHARI CSIWDKAQHE GVALQAQGWS 

       490        500        510        520        530        540 
GVDLSPLGEG AEWDLIRKLD LFPDVVEGAA VHQEPHRIPY YLLDLAAAFH TFYNSHRIMD 

       550        560        570 
VDAGTRDARL VLILAVKQVI ANGLELLGVQ QPRSM 

« Hide

References

[1]"Complete sequence of Magnetococcus sp. MC-1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Goodwin L.A., Brettin T., Bruce D., Han C., Tapia R., Gilna P. expand/collapse author list , Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MC-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000471 Genomic DNA. Translation: ABK43225.1.
RefSeqYP_864631.1. NC_008576.1.

3D structure databases

ProteinModelPortalA0L5I2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING156889.Mmc1_0704.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK43225; ABK43225; Mmc1_0704.
GeneID4481277.
KEGGmgm:Mmc1_0704.
PATRIC22427924. VBIMagSp23654_0729.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247214.
KOK01887.
OMARFIMLTR.
OrthoDBEOG6JB13C.

Enzyme and pathway databases

BioCycMSP156889:GH36-709-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_MAGSM
AccessionPrimary (citable) accession number: A0L5I2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: December 12, 2006
Last modified: April 16, 2014
This is version 51 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