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Reviewed, UniProtKB/Swiss-Prot Q057S1 (SYR_BUCCC)

Last modified June 16, 2009. Version 18. 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: BCc_152
OrganismBuchnera aphidicola subsp. Cinara cedri [Complete proteome] [HAMAP]
Taxonomic identifier372461 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length571 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 – 571571Arginyl-tRNA synthetase HAMAP MF_00123
PRO_1000017996

Regions

Motif122 – 13211"HIGH" region HAMAP MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q057S1-1 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: C6AFCC0856C9BEB5

FASTA57167,427
        10         20         30         40         50         60 
MNIQKFLKKK IKKICIKLGL PENFNPIIQK NIKKKNIDYQ INGIIKLKKK KSNYHYKLAK 

        70         80         90        100        110        120 
KISYYMNKSK IYKKISISKP GFINITLDSN WICTNINNMF IAKNFNISFK KPKKIIIDYS 

       130        140        150        160        170        180 
SPNIAKEMHV GHLRSTILGD TTARILKFLG HNVIKQNHIG DWGIQFGMLI TQLKLESKIS 

       190        200        210        220        230        240 
FKNIEKIYKK SYLNYKKNPI FFKKTKKNVV KLQKKDKKCI YIWKKIVKKS IKKNNKVYKK 

       250        260        270        280        290        300 
LNVSLKKKDI RGESFYNFML PGIISDLKKK KIAVNYQGCV IVYLKNFKNR LGKKMGVVIQ 

       310        320        330        340        350        360 
KKDGAFLYTT TDIACLKYRC KTLKADRIIY YIDNRQKQHL LQIWNIAKKA KYFTKKILLE 

       370        380        390        400        410        420 
HHSFGMILHK NKKPFKTRNG DTIKLIKLLN KGVTKAKEKI KKKNRKIKKK ELKKIAHNIG 

       430        440        450        460        470        480 
IGAIKYFDLS KKRKLDYIFD WDKMLSLEGN TAPYIQYAYI RIKSIIKKNT TIFQNDKYKI 

       490        500        510        520        530        540 
NIFTSFERQL IFSIFQFEEI IHILEKKGTP HLMCNYLYDL SGKFSKFYEN CSILNAKEKH 

       550        560        570 
IKISRIKLSI LTSKIIKKCL YFLGIKTVSK M 

« Hide

References

[1]"A small microbial genome: the end of a long symbiotic relationship?"
Perez-Brocal V., Gil R., Ramos S., Lamelas A., Postigo M., Michelena J.M., Silva F.J., Moya A., Latorre A.
Science 314:312-313(2006) [PubMed: 17038625] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000263 Genomic DNA. Translation: ABJ90628.1.
RefSeqYP_802721.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4440620.
GenomeReviewsGene locus BCc_152 in contig CP000263_GR.
KEGGbcc:BCc_152.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAQ057S1. YNDDLQP.

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_BUCCC
AccessionPrimary (citable) accession number: Q057S1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 14, 2006
Last modified: June 16, 2009
This is version 18 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