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Q6A5X8 (SYR_PROAC) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 64. 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:PPA2128
OrganismPropionibacterium acnes (strain KPA171202 / DSM 16379) [Complete proteome] [HAMAP]
Taxonomic identifier267747 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesPropionibacterineaePropionibacteriaceaePropionibacterium

Protein attributes

Sequence length556 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 – 556556Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_0000242067

Regions

Motif117 – 12711"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q6A5X8 [UniParc].

Last modified September 13, 2004. Version 1.
Checksum: 700CFFC132291245

FASTA55661,178
        10         20         30         40         50         60 
MSSLPSRLAA RIESAIGVDP QLRPATKPQF GHFQSNVALR LAKEEKRPPR DVAADIVAKL 

        70         80         90        100        110        120 
DIEDLCETPE IAGPGFINLR LRADVLARVA SDFVTDPNAG IAQAEKPERV VIDYSAPNVA 

       130        140        150        160        170        180 
KQMHVGHLRS TIIGDCFNRV LSAQGHTVIP QNHIGDWGTQ FGMLIEYIVE KRMDVEDFDL 

       190        200        210        220        230        240 
SGVEQLYQDS KKTFDADPQF ADRARRRVVK LQGGDAETLR IWRTLIDISL EGFNATYSRL 

       250        260        270        280        290        300 
SVLLTDEDVA GESSYNDDLP RVVDELVADG LAVEDNGALC VFVEGQDAPM IVRKRDGGFG 

       310        320        330        340        350        360 
YDATDLAAIR RRVGKLKADR IIYVTDVRQS HHFEVLFQVA RMAGFLPDDV EAEHVGYGMV 

       370        380        390        400        410        420 
LGPDGRPFKT REGGTVSLSD LLDEAETHAA PNIALAAIKY ADLSNGLQKD YVFDAERMVQ 

       430        440        450        460        470        480 
TTGDTGPYLQ YAHARVSQIL RKAAAEANPN VDPEADLDAM DWGRISVLDE PAEQQLALLL 

       490        500        510        520        530        540 
SRFGEIVEVV ATDLTPHKLC TYLYELAGAY SVFYEQCPVL RSTGEVRGSR LALCAATRRV 

       550 
LGRGLDLLGI DAPDRM 

« Hide

References

[1]"The complete genome sequence of Propionibacterium acnes, a commensal of human skin."
Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A., Strittmatter A., Hujer S., Duerre P., Gottschalk G.
Science 305:671-673(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KPA171202 / DSM 16379.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017283 Genomic DNA. Translation: AAT83835.1.
RefSeqYP_056793.1. NC_006085.1.

3D structure databases

ProteinModelPortalQ6A5X8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING267747.PPA2128.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAT83835; AAT83835; PPA2128.
GeneID2932484.
KEGGpac:PPA2128.
PATRIC23039083. VBIProAcn64440_2182.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247212.
KOK01887.
OMADGTAVYM.
OrthoDBEOG6JB13C.
ProtClustDBCLSK2764372.

Enzyme and pathway databases

BioCycPACN267747:GHO9-2134-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_PROAC
AccessionPrimary (citable) accession number: Q6A5X8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: September 13, 2004
Last modified: April 16, 2014
This is version 64 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