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Q6MEP4 (SYR_PARUW) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 65. 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:pc0231
OrganismProtochlamydia amoebophila (strain UWE25) [Complete proteome] [HAMAP]
Taxonomic identifier264201 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesParachlamydiaceaeCandidatus Protochlamydia

Protein attributes

Sequence length584 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 – 584584Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_0000242060

Regions

Motif130 – 14011"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q6MEP4 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: D71B63069ED04EED

FASTA58466,381
        10         20         30         40         50         60 
MNTLLSVLAN LFQQATANAF PDLSVLDPNF QPEITPSTQE KFGHYQFNSA MKLAKLLKKN 

        70         80         90        100        110        120 
PRQVAEAIVN QLTDSLPPLS KIEIAGPGFI NMTFSTDFLS KNLDILLRDA HFGIPFPEKP 

       130        140        150        160        170        180 
EKIIIDFSSP NVAKEMHVGH LRSTVIGDSL ARLFEFLGHH VIRLNHLGDW GTAFGMLIAY 

       190        200        210        220        230        240 
MKEEAPNVLS GEQKTDLTHL VSWYRSSKKK FDEEPEFKRR AQLEVVALQQ GEQKAREAWQ 

       250        260        270        280        290        300 
MICEISQKAY QEIYQLLDVK IIDRGESFYN PFLPNIVSDL EKKGLVKISD GAKCIFLEGF 

       310        320        330        340        350        360 
QNREGENLPL MIQKSDGGYN YDTTDMAAIY HRIYHEKGDR LIYITDAGQA THFQMIFKAA 

       370        380        390        400        410        420 
EKAKYLDTTQ IRVDHVPFGL VLGTDGKKFR TRSGETEKLI DLLRTAINCA DKILSEKNPE 

       430        440        450        460        470        480 
MEESERRHLA KSLGIGAIKY ADLSCNRVGD YTFSYDRMLR FEGNTAAFLM YAYVRIAGIK 

       490        500        510        520        530        540 
RRLKANLPAV LENTHINLEH STEIELGLHI LRFHETLNLM ANDLLPNRLT DYLYTLAEKF 

       550        560        570        580 
NAFFRDCRVE GTPQQNTRLL LCEATAKVLK QGLTILGLTT VDKM 

« Hide

References

[1]"Illuminating the evolutionary history of chlamydiae."
Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U., Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D., Rattei T., Mewes H.-W., Wagner M.
Science 304:728-730(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: UWE25.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX908798 Genomic DNA. Translation: CAF22955.1.
RefSeqYP_007230.1. NC_005861.1.

3D structure databases

ProteinModelPortalQ6MEP4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264201.pc0231.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAF22955; CAF22955; pc0231.
GeneID2779797.
KEGGpcu:pc0231.
PATRIC31995746. VBICanPro72727_0233.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247212.
KOK01887.
OMADGTAVYM.
OrthoDBEOG6JB13C.
ProtClustDBPRK01611.

Enzyme and pathway databases

BioCycPAMO264201:GH0M-235-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_PARUW
AccessionPrimary (citable) accession number: Q6MEP4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 65 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