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Q4QL12 (SYR_HAEI8) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 58. 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:NTHI1470
OrganismHaemophilus influenzae (strain 86-028NP) [Complete proteome] [HAMAP]
Taxonomic identifier281310 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

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_0000242029

Regions

Motif122 – 13211"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q4QL12 [UniParc].

Last modified July 19, 2005. Version 1.
Checksum: 4FDBEB5083E418E8

FASTA57764,789
        10         20         30         40         50         60 
MNIQSILSDK IKQAMVIAGA DQSCDALVRQ SGKPQFGDYQ ANGIMAAAKK LGLNPREFAQ 

        70         80         90        100        110        120 
KVLDNLQLSD IAEKLEIAGP GFINIFLNPT WLTTEISAAL SHKNLGIQAT NKQTVVIDYS 

       130        140        150        160        170        180 
SPNVAKEMHV GHLRSTIIGD AVARTLEFLG HNVIRANHVG DWGTQFGMLI AYLEKMQNEH 

       190        200        210        220        230        240 
ASEMELQDLE AFYREAKKHY DEDEIFAEKA RNYVVKLQSG DEYCRTMWKR LVDITMQQNQ 

       250        260        270        280        290        300 
HNYNRLNVTL TEKDVMGESL YNPMLPSIVE DLKKQGLAVE NDGALVVYLD EFKNKDGDPM 

       310        320        330        340        350        360 
GVIVQKKDGG FLYTTTDIAA AKYRYETLKA NRALVFSDTR QSQHMQQAWL ITRKAGYVPD 

       370        380        390        400        410        420 
SFSLEHKNFG MMLGKDGKPF KTRTGGTVKL ADLLNEAIER ATVLINEKNT NLSNDEKQAV 

       430        440        450        460        470        480 
IEAIGIGSVK YADLSKNRTT DYVFDWDNML SFEGNTAPYM QYAYTRIRSI FNKTDINSTA 

       490        500        510        520        530        540 
LLAAPLTIKD DKERTLAIKL LQFEEAVQTV GKEGTPHVLC AYLYELAGIF SSFYEHCPIL 

       550        560        570 
NAENESIKLS RLKLALLTEK TLKQGLTLLG IKTVEKM 

« Hide

References

[1]"Genomic sequence of an otitis media isolate of nontypeable Haemophilus influenzae: comparative study with H. influenzae serotype d, strain KW20."
Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B., Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O., Munson R.S. Jr.
J. Bacteriol. 187:4627-4636(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 86-028NP.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000057 Genomic DNA. Translation: AAX88285.1.
RefSeqYP_248945.1. NC_007146.2.

3D structure databases

ProteinModelPortalQ4QL12.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING281310.NTHI1470.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAX88285; AAX88285; NTHI1470.
GeneID3430718.
KEGGhit:NTHI1470.
PATRIC20183037. VBIHaeInf100748_1358.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247212.
KOK01887.
OMANPNGPLH.
OrthoDBEOG6JB13C.
ProtClustDBPRK01611.

Enzyme and pathway databases

BioCycHINF281310:GJ89-1370-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_HAEI8
AccessionPrimary (citable) accession number: Q4QL12
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: July 19, 2005
Last modified: April 16, 2014
This is version 58 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