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Reviewed, UniProtKB/Swiss-Prot Q8A3X5 (SYR_BACTN)

Last modified November 3, 2009. Version 47. 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: BT_2829
OrganismBacteroides thetaiotaomicron [Complete proteome] [HAMAP]
Taxonomic identifier818 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

Protein attributes

Sequence length597 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 – 597597Arginyl-tRNA synthetase HAMAP MF_00123
PRO_0000151531

Regions

Motif125 – 13511"HIGH" region HAMAP MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q8A3X5-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 14983726E8F617B0

FASTA59766,954
        10         20         30         40         50         60 
MKIEDKLVAS VINGLKALYG QEVPEKMVQL QKTKKEFEGH LTLVVFPFLK MSRKGPEQTA 

        70         80         90        100        110        120 
QEIGEYLKAN EPAVAAFNVI KGFLNLTIAS ATWIELLNEI QSDEEYGLVK ATETSPLVMI 

       130        140        150        160        170        180 
EYSSPNTNKP LHLGHVRNNL LGNALANIVA ANGNRVVKTN IVNDRGIHIC KSMLAWKKYG 

       190        200        210        220        230        240 
NGETPESTGK KGDHLVGDYY VSFDKHYKAE LAELMEKGMT KEEAEAASPL MQEAREMLVK 

       250        260        270        280        290        300 
WEAGDPEVRA LWEMMNNWVY AGFDETYRKM GVGFDKIYYE SNTYLEGKEK VMEGLEKGFF 

       310        320        330        340        350        360 
FKKEDGSVWV DLTAEGLDHK LLLRGDGTSV YMTQDIGTAK LRFADYPIDK MIYVVGNEQN 

       370        380        390        400        410        420 
YHFQVLSILL DKLGFEWGKG LVHFSYGMVE LPEGKMKSRE GTVVDADDLM EEMVSTAKET 

       430        440        450        460        470        480 
SQELGKLDGL TQEEADDIAR IVGLGALKYF ILKVDARKNM TFNPKESIDF NGNTGPFIQY 

       490        500        510        520        530        540 
TYARIQSVLR KAAESGIVIP EQIPAGIELS EKEEGLIQLV ADFAAVVKQA GEDYSPSIIA 

       550        560        570        580        590 
NYTYDLVKEY NQFYHDFSIL REENEAVKVF RIALSANVAK VVRLGMGLLG IEVPSRM 

« Hide

References

[1]"A genomic view of the human-Bacteroides thetaiotaomicron symbiosis."
Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I.
Science 299:2074-2076(2003) [PubMed: 12663928] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.

Cross-references

Sequence databases

AE015928 Genomic DNA. Translation: AAO77935.1.
RefSeqNP_811741.1.

3D structure databases

HSSPHSSP built from PDB template 1IQ0 based on UniProtKB Q93RP5.
ModBaseSearch...

Genome annotation databases

GeneID1076299.
GenomeReviewsGene locus BT_2829 in contig AE015928_GR.
KEGGbth:BT_2829.
NMPDRfig|226186.1.peg.2828.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8A3X5.
OMAYNDDLQP.

Enzyme and pathway databases

BioCycBTHE226186:BT_2829-MON.
BRENDA6.1.1.19. 21018.

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:3.40.50.620. 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_BACTN
AccessionPrimary (citable) accession number: Q8A3X5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 14, 2003
Last sequence update: June 1, 2003
Last modified: November 3, 2009
This is version 47 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