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Q8XJU2 (SYR_CLOPE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 79. 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:CPE1661
OrganismClostridium perfringens (strain 13 / Type A) [Complete proteome] [HAMAP]
Taxonomic identifier195102 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length565 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 – 565565Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_0000151551

Regions

Motif120 – 13011"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q8XJU2 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 2626BD869B6ED66E

FASTA56564,626
        10         20         30         40         50         60 
MDYKKLVAER IKEHVDLELE NIEKLIEIPP KPEMGDFAFP CFQLAKVMRK APNMIAAELA 

        70         80         90        100        110        120 
EKINKEGFER VECLGPYLNF FVDKVAFSKN IISKVLEEGD KYGSSKIGEG KNVVVEYSSP 

       130        140        150        160        170        180 
NIAKPFHVGH LFTTAIGHSL YRMLNFEGYN PIRINHLGDW GTQFGKLISA YKRWGNEEAL 

       190        200        210        220        230        240 
EEAPINELLR IYVKFHDEAE NNPELEDEGR MYFKKLEDGD QEAVALWERF KDLSLKEFNK 

       250        260        270        280        290        300 
IYDMLGVDFD SWAGESFYND KMDKVVEELE KANILTESNG AKVVMLDEYN MPPCIVVKSD 

       310        320        330        340        350        360 
GASIYATRDL AAASYRHKTY NFDKCIYVVG KDQILHFNQV FKTLELAGNE WAKNCVHIPF 

       370        380        390        400        410        420 
GLVKFADRKL STRKGNVVLL EDLLNEAIDK TRETIEEKNP QLENKEEVAK KIGIGAILFT 

       430        440        450        460        470        480 
YLKNSRERDI VFDWKEMLSF DGETGPYVQY SYARAKSILR KAEEQKITAE PDFTKLTSKE 

       490        500        510        520        530        540 
EFELAKTLEG LQKAVILGID KLEPSVVTRY SIEVAKAFNK FYNNHTVLNV EDEGLKAARL 

       550        560 
ELIKATAQVI KNALFLIGID VVEKM 

« Hide

References

[1]"Complete genome sequence of Clostridium perfringens, an anaerobic flesh-eater."
Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T., Ogasawara N., Hattori M., Kuhara S., Hayashi H.
Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 13 / Type A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000016 Genomic DNA. Translation: BAB81367.1.
RefSeqNP_562577.1. NC_003366.1.

3D structure databases

ProteinModelPortalQ8XJU2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING195102.CPE1661.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB81367; BAB81367; BAB81367.
GeneID989971.
KEGGcpe:CPE1661.
PATRIC19497271. VBICloPer59675_1731.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247211.
KOK01887.
OMAYVKFHDE.
OrthoDBEOG6JB13C.

Enzyme and pathway databases

BioCycCPER195102:GJFM-1708-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_CLOPE
AccessionPrimary (citable) accession number: Q8XJU2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: March 1, 2002
Last modified: May 14, 2014
This is version 79 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