Skip Header

Contribute Send feedback
Read comments (?) or add your own

A6QHR2 (SYY_STAAE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Tyrosine--tRNA ligase

EC=6.1.1.1
Alternative name(s):
Tyrosyl-tRNA synthetase
Short name=TyrRS
Gene names
Name:tyrS
Ordered Locus Names:NWMN_1622
OrganismStaphylococcus aureus (strain Newman) [Complete proteome] [HAMAP]
Taxonomic identifier426430 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length420 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr) By similarity. HAMAP-Rule MF_02006

Catalytic activity

ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr). HAMAP-Rule MF_02006

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 1 subfamily.

Contains 1 S4 RNA-binding domain.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
RNA-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processtyrosyl-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

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

tyrosine-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 420420Tyrosine--tRNA ligase HAMAP-Rule MF_02006
PRO_1000088630

Regions

Domain353 – 42068S4 RNA-binding
Motif41 – 5010"HIGH" region HAMAP-Rule MF_02006
Motif231 – 2355"KMSKS" region HAMAP-Rule MF_02006

Sites

Binding site361Tyrosine By similarity
Binding site1701Tyrosine By similarity
Binding site1741Tyrosine By similarity
Binding site2341ATP By similarity

Secondary structure

............................................................. 420
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
A6QHR2 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: B6916EA4BE4B21B2

FASTA42047,598
        10         20         30         40         50         60 
MTNVLIEDLK WRGLIYQQTD EQGIEDLLNK EQVTLYCGAD PTADSLHIGH LLPFLTLRRF 

        70         80         90        100        110        120 
QEHGHRPIVL IGGGTGMIGD PSGKSEERVL QTEEQVDKNI EGISKQMHNI FEFGTDHGAV 

       130        140        150        160        170        180 
LVNNRDWLGQ ISLISFLRDY GKHVGVNYML GKDSIQSRLE HGISYTEFTY TILQAIDFGH 

       190        200        210        220        230        240 
LNRELNCKIQ VGGSDQWGNI TSGIELMRRM YGQTDAYGLT IPLVTKSDGK KFGKSESGAV 

       250        260        270        280        290        300 
WLDAEKTSPY EFYQFWINQS DEDVIKFLKY FTFLGKEEID RLEQSKNEAP HLREAQKTLA 

       310        320        330        340        350        360 
EEVTKFIHGE DALNDAIRIS QALFSGDLKS LSAKELKDGF KDVPQVTLSN DTTNIVEVLI 

       370        380        390        400        410        420 
ETGISPSKRQ AREDVNNGAI YINGERQQDV NYALAPEDKI DGEFTIIRRG KKKYFMVNYQ 

« Hide

References

[1]"Genome sequence of Staphylococcus aureus strain Newman and comparative analysis of staphylococcal genomes: polymorphism and evolution of two major pathogenicity islands."
Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.
J. Bacteriol. 190:300-310(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Newman.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009351 Genomic DNA. Translation: BAF67894.1.
RefSeqYP_001332656.1. NC_009641.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JIIX-ray3.20A1-420[»]
1JIJX-ray3.20A1-420[»]
1JIKX-ray2.80A1-420[»]
1JILX-ray2.20A1-420[»]
ProteinModelPortalA6QHR2.
SMRA6QHR2. Positions 2-419.
ModBaseSearch...

Protein-protein interaction databases

STRING426430.NWMN_1622.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAF67894; BAF67894; NWMN_1622.
GeneID5330953.
KEGGsae:NWMN_1622.
PATRIC19586853. VBIStaAur133992_1755.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0162.
HOGENOMHOG000242790.
KOK01866.
OMAGKKKHVL.
ProtClustDBPRK05912.

Enzyme and pathway databases

BioCycSAUR426430:GIXC-1623-MONOMER.

Family and domain databases

Gene3D3.10.290.10. 1 hit.
3.40.50.620. 1 hit.
HAMAPMF_02006. Tyr_tRNA_synth_type1.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002305. aa-tRNA-synth_Ic.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002942. S4_RNA-bd.
IPR002307. Tyr-tRNA-ligase.
IPR024088. Tyr-tRNA-ligase_bac-type.
IPR024107. Tyr-tRNA-ligase_bac_1.
[Graphical view]
PANTHERPTHR11766. PTHR11766. 1 hit.
PfamPF01479. S4. 1 hit.
PF00579. tRNA-synt_1b. 1 hit.
[Graphical view]
PRINTSPR01040. TRNASYNTHTYR.
SMARTSM00363. S4. 1 hit.
[Graphical view]
TIGRFAMsTIGR00234. tyrS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
PS50889. S4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBA6QHR2.
EvolutionaryTraceA6QHR2.

Entry information

Entry nameSYY_STAAE
AccessionPrimary (citable) accession number: A6QHR2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: August 21, 2007
Last modified: May 1, 2013
This is version 51 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families