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Q0I3B0 (SYR_HISS1) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 56. 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:HS_0955
OrganismHistophilus somni (strain 129Pt) (Haemophilus somnus) [Complete proteome] [HAMAP]
Taxonomic identifier205914 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHistophilus

Protein attributes

Sequence length577 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 – 577577Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000018037

Regions

Motif122 – 13211"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q0I3B0 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: D694F23C39762D10

FASTA57765,071
        10         20         30         40         50         60 
MNIQSILSNK IKQAMRQAGA DEQCDALVKP SGKPQFGDYQ ANGIMATAKK LGLNPRDFAQ 

        70         80         90        100        110        120 
KVLDLIDLKN IAEKMEIAGP GFINIFLDKN WLAENIQVTL QDKKLGVTVE EIQTIVVDYS 

       130        140        150        160        170        180 
SPNVAKEMHV GHLRSTIIGD AVVRTLEFLG HNVIRANHVG DWGTQFGMLI AYLEKMENEH 

       190        200        210        220        230        240 
ASAMELADLE AFYRAAKEHY DNDETFAEKA RNYVVKLQNG DAYCRTMWKK LVDITMQQNQ 

       250        260        270        280        290        300 
RNYDRLNVTL TQNDVMGESL YNPMLPEIVA DLKAQGLAVE DEGAQVVYLE EFKNKDGDPM 

       310        320        330        340        350        360 
GVIVQKKDGG FLYTTTDIAA AKYRYHTLKA DRALVFSDTR QSQHMQQAWL ITRKAGYVPD 

       370        380        390        400        410        420 
SFQLEHKNFG MMLGKDGKPF KTRSGGTVKL TDLLDEAIER ADKLISEKST ALSSKEKAAV 

       430        440        450        460        470        480 
IEAVGIGSVK YADLSKNRTT DYVFDWDIML SFEGNTAPYM QYAYTRIRSI FNKTDISEEQ 

       490        500        510        520        530        540 
LHPAKIQLTD EKERLLAIKL LQFEETVQIV GKEGTPHILC AYLYELAGLF SSFYEHCPIL 

       550        560        570 
NNDNENVKLS RLKLALLTEK TLKQGLDLLG IKTVEKM 

« Hide

References

[1]"Complete genome sequence of Haemophilus somnus (Histophilus somni) strain 129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus influenzae Rd."
Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O., Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N., Xie G., Inzana T.J.
J. Bacteriol. 189:1890-1898(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 129Pt.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000436 Genomic DNA. Translation: ABI25230.1.
RefSeqYP_719166.1. NC_008309.1.

3D structure databases

ProteinModelPortalQ0I3B0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING205914.HS_0955.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI25230; ABI25230; HS_0955.
GeneID4240448.
KEGGhso:HS_0955.
PATRIC20281929. VBIHaeSom53361_1001.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycHSOM205914:GJ7V-989-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_HISS1
AccessionPrimary (citable) accession number: Q0I3B0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 3, 2006
Last modified: April 16, 2014
This is version 56 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