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Q92JH2 (SYR_RICCN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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:RC0095
OrganismRickettsia conorii (strain ATCC VR-613 / Malish 7) [Complete proteome] [HAMAP]
Taxonomic identifier272944 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › spotted fever group ›

Protein attributes

Sequence length576 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.

Subcellular location

Cytoplasm By similarity.

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 – 576576Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_0000151599

Regions

Motif128 – 1369"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q92JH2 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 8486A96C2380337D

FASTA57665,234
        10         20         30         40         50         60 
MNIFNQLKQD IIVASRQLYN NQEIANTATI EIPKDSFNGD LSSNIAMIIA AKESIAPREV 

        70         80         90        100        110        120 
ALKFKEVLIT LPYIASIEIA GPGFINFTIK ADSWQASIKD ILQHEEKFFE IDIDKSRNIN 

       130        140        150        160        170        180 
IEYVSANPTG PMHIGHARGA VYGDVLARIL QKVSYSVTKE YYVNDAGSQI NDLVSTVLLR 

       190        200        210        220        230        240 
YKEALGEQIT IPAGLYPGEY LIPLGQILAK EYGNKLLTMN YAERFKIIKS FAVEKMLDLN 

       250        260        270        280        290        300 
RKDLADLGIK HDIFFSEQSL HDKGEIEETV KLLERMGLIY EGTLPAPKGK IHEEWDNRVQ 

       310        320        330        340        350        360 
KLFKSTKYGD SQDRPIEKAD GSWSYFASDL AYAKDKIERG ANHLIYVLGA DHSGYVKRIE 

       370        380        390        400        410        420 
AIVKALGKEQ VKVDVKICQL VNFVENGVPV KMSKRLGSFA SVQDVNHEVG KDIIRFMMLT 

       430        440        450        460        470        480 
RQNDKPLDFD LVKVKEQSRE NPIFYVQYAH VRTISILSKA KELMPESYNN FESGKYDLSL 

       490        500        510        520        530        540 
LSSEEEIEII KLLASWTKTL EASAKYFEPH RIAFYLINLA SKFHSMWNFG KENSDYRFVI 

       550        560        570 
ESNKELTLAR LALASAIQKV IASGLEVIGV EPMNKM

« Hide

References

[1]"Mechanisms of evolution in Rickettsia conorii and R. prowazekii."
Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V., Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.
Science 293:2093-2098(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC VR-613 / Malish 7.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE006914 Genomic DNA. Translation: AAL02633.1.
PIRG97711.
RefSeqNP_359732.1. NC_003103.1.

3D structure databases

ProteinModelPortalQ92JH2.
ModBaseSearch...

Protein-protein interaction databases

STRING272944.RC0095.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL02633; AAL02633; RC0095.
GeneID928099.
KEGGrco:RC0095.
PATRIC17887298. VBIRicCon45613_0113.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247214.
KOK01887.
OMAHTSANPN.
ProtClustDBPRK01611.

Family and domain databases

Gene3D3.30.1360.70. 1 hit.
3.40.50.620. 1 hit.
HAMAPMF_00123. Arg_tRNA_synth.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR001278. Arg-tRNA-ligase_Ia.
IPR015945. Arg-tRNA-synth_Ia_core.
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]
SUPFAMSSF55190. Arg-tRNA-synth_Ic_N. 1 hit.
SSF47323. tRNAsyn_1a_bind. 1 hit.
TIGRFAMsTIGR00456. argS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYR_RICCN
AccessionPrimary (citable) accession number: Q92JH2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: December 1, 2001
Last modified: May 1, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

Rickettsia conorii

(strain Malish 7): entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents