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Reviewed, UniProtKB/Swiss-Prot O51540 (SYR_BORBU)

Last modified November 3, 2009. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Arginyl-tRNA synthetase
    EC=6.1.1.19
Alternative name(s):
    Arginine--tRNA ligase
      Short name=ArgRS
Gene names
Name: argS
Ordered Locus Names: BB_0594
OrganismBorrelia burgdorferi (Lyme disease spirochete) [Complete proteome] [HAMAP]
Taxonomic identifier139 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeBorreliaBorrelia burgdorferi group

Protein attributes

Sequence length591 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg). HAMAP MF_00123

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm. HAMAP 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: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

arginine-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 591591Arginyl-tRNA synthetase HAMAP MF_00123
PRO_0000151534

Regions

Motif133 – 14311"HIGH" region HAMAP MF_00123

Sequences

Sequence LengthMass (Da)Tools
O51540-1 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 83B10D702CB0DEBF

FASTA59167,637
        10         20         30         40         50         60 
MLKRKKMNKS VKKKIKDEIN VIVTNLALSN NIKLDNININ IQKPPKSDLG DISILMFEIG 

        70         80         90        100        110        120 
KTLKLPIEII SEEIIKNLKT KYEIKAVGPY LNIKISRKEY INNTIQMVNT QKDTYGTSKY 

       130        140        150        160        170        180 
LDNKKIILEF SSPNTNKPLH VGHLRNDVIG ESLSRILKAV GAKITKINLI NDRGVHICKS 

       190        200        210        220        230        240 
MLAYKKFGNG ITPEKAFKKG DHLIGDFYVK YNKYSQENEN AEKEIQDLLL LWEQKDVSTI 

       250        260        270        280        290        300 
ELWKKLNKWA IEGIKETYEI TNTSFDKIYL ESEIFKIGKN VVLEGLEKGF CYKREDGAIC 

       310        320        330        340        350        360 
IDLPSDSDEK ADTKVKQKVL IRSNGTSIYL TQDLGNIAVR TKEFNFEEMI YVVGSEQIQH 

       370        380        390        400        410        420 
FKSLFFVAEK LGLSKNKKLI HLSHGMVNLV DGKMKSREGN VIDADNLISN LIELIIPEMT 

       430        440        450        460        470        480 
QKIENKESAK KNALNIALGA IHYYLLKSAI HKDIVFNKKE SLSFTGNSGP YIQYVGARIN 

       490        500        510        520        530        540 
SILEKYKALS IPVMEKIDFE LLKHEKEWEI IKIISELEEN IINAAKDLNP SILTSYSYSL 

       550        560        570        580        590 
AKHFSTYYQE VKVIDTNNIN LTAARIEFLK AILQTIKNCM YLLNIPYMLK M 

« Hide

Cross-references

Sequence databases

AE000783 Genomic DNA. Translation: AAC66956.1.
PIRA70174.
RefSeqNP_212728.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID1195441.
GenomeReviewsGene locus BB_0594 in contig AE000783_GR.
KEGGbbu:BB0594.
NMPDRfig|224326.1.peg.978.
TIGRBB_0594.

Phylogenomic databases

HOGENOMO51540.
OMAGKLITAY.

Enzyme and pathway databases

BioCycBBUR224326:BB_0594-MON.
BRENDA6.1.1.19. 142596.

Family and domain databases

HAMAPMF_00123.
[Tree]
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR001278. Arg-tRNA-synth_Ic.
IPR015945. Arg-tRNA-synth_Ic_core.
IPR005148. Arg-tRNA-synth_Ic_N.
IPR008909. DALR_anticod_bd.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA:3.30.1360.70. Arg-tRNA-synth_Ic_N. 1 hit.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHERPTHR11956. Arg_tRNA-synt_1c. 1 hit.
PfamPF03485. Arg_tRNA_synt_N. 1 hit.
PF05746. DALR_1. 1 hit.
PF00750. tRNA-synt_1d. 1 hit.
[Graphical view]
PRINTSPR01038. TRNASYNTHARG.
TIGRFAMsTIGR00456. argS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYR_BORBU
AccessionPrimary (citable) accession number: O51540
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 1, 1998
Last modified: November 3, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents