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Q253D1 (SYR_CHLFF) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 52. 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:CF0835
OrganismChlamydophila felis (strain Fe/C-56) [Complete proteome] [HAMAP]
Taxonomic identifier264202 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydophila

Protein attributes

Sequence length562 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 – 562562Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_0000242006

Regions

Motif122 – 13211"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q253D1 [UniParc].

Last modified April 18, 2006. Version 1.
Checksum: CF5A3036A919003C

FASTA56263,380
        10         20         30         40         50         60 
MTLLSYLSSL CREATLSAFP QVENPSPDIT QSTKEHFGHY QCNDAMKLDR TLKMAPRAIA 

        70         80         90        100        110        120 
EAIVNNLPKD NFSSVEVAGA GFINFTFSKE FLKQRLETFS ADLSSGFCVK DPKKIVIDFS 

       130        140        150        160        170        180 
SPNIAKDMHV GHLRSTIIGD CLARVFSFVG NDVLRLNHIG DWGTAFGMLI TYLQEEASED 

       190        200        210        220        230        240 
VGNLEDLTAL YKKAHARFAE DVEFKKRSQA NVVALQSGDP SALNLWKHIC EISERAFQKI 

       250        260        270        280        290        300 
YDILGVAIEK RGESFYNPFL PEIIQDLENK KLITVSDNAK CVFHEGFSIP LMVQKSDGGY 

       310        320        330        340        350        360 
NYATTDLAAM RYRVEKDHAD KIIIVTDMGQ SLHFQLLEAT ALAAGYLRDK ETFSHVGFGL 

       370        380        390        400        410        420 
VLDSEGKKFK TRSGENIKLK ELLNTAVDQA VATLKEHRPE MSEEEISQRA PILGINAIKY 

       430        440        450        460        470        480 
ADLSSHRVSD YVFSFEKMLR FEGNTAMFLL YAYVRIQGIK RRLNIEKLNL EAVVNIQEPA 

       490        500        510        520        530        540 
EEALALALLR FPEAIDVTLK ELCPHFLTDY LYMLTNKFNA FFRDCHIEGS PYQQERLYLC 

       550        560 
ALVEKTLATG MHLLGLQTLD RL 

« Hide

References

[1]"Genome sequence of the cat pathogen, Chlamydophila felis."
Azuma Y., Hirakawa H., Yamashita A., Cai Y., Rahman M.A., Suzuki H., Mitaku S., Toh H., Goto S., Murakami T., Sugi K., Hayashi H., Fukushi H., Hattori M., Kuhara S., Shirai M.
DNA Res. 13:15-23(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Fe/C-56.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006861 Genomic DNA. Translation: BAE81607.1.
RefSeqYP_515752.1. NC_007899.1.

3D structure databases

ProteinModelPortalQ253D1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264202.CF0835.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3958916.
KEGGcfe:CF0835.
PATRIC20205353. VBIChlFel51660_0878.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247212.
KOK01887.
OMAKCFDILG.
OrthoDBEOG6JB13C.

Enzyme and pathway databases

BioCycCFEL264202:GJCG-864-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_CHLFF
AccessionPrimary (citable) accession number: Q253D1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: April 18, 2006
Last modified: May 14, 2014
This is version 52 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