Skip Header

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

A6U2J5 (SYY_STAA2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 35. 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:
Tyrosine--tRNA ligase

EC=6.1.1.1
Alternative name(s):
Tyrosyl-tRNA synthetase
Short name=TyrRS
Gene names
Name:tyrS
Ordered Locus Names:SaurJH1_1819
OrganismStaphylococcus aureus (strain JH1) [Complete proteome] [HAMAP]
Taxonomic identifier359787 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length420 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 MF_02006

Catalytic activity

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

Subunit structure

Homodimer By similarity. HAMAP MF_02006

Subcellular location

Cytoplasm By similarity HAMAP MF_02006.

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 termComplete proteome
Gene Ontology (GO)
   Biological processtyrosyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

tyrosine-tRNA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 420420Tyrosine--tRNA ligase HAMAP MF_02006
PRO_1000088627

Regions

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

Sites

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

Sequences

Sequence LengthMass (Da)Tools
A6U2J5 [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]"Complete sequence of chromosome of Staphylococcus aureus subsp. aureus JH1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Ivanova N., Tomasz A., Richardson P.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JH1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000736 Genomic DNA. Translation: ABR52663.1.
RefSeqYP_001316950.1. NC_009632.1.

3D structure databases

ProteinModelPortalA6U2J5.
SMRA6U2J5. Positions 2-324.
ModBaseSearch...

Protein-protein interaction databases

STRINGA6U2J5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTAT00000015685; EBSTAP00000015188; EBSTAG00000015684.
GeneID5316809.
GenomeReviewsGene locus SaurJH1_1819 in contig CP000736_GR.
KEGGsah:SaurJH1_1819.
PATRIC19535504. VBIStaAur98826_1862.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0162.
GeneTreeEBGT00050000024462.
HOGENOMHBG288125.
OMATFYIGFD.
ProtClustDBPRK05912.

Enzyme and pathway databases

BioCycSAUR359787:SAURJH1_1819-MONOMER.

Family and domain databases

HAMAPMF_02006. Tyr_tRNA_synth_type1.
[Tree]
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-synth.
IPR024088. Tyr-tRNA-synth_bac-type.
IPR024107. Tyr-tRNA-synth_bac_1.
[Graphical view]
Gene3DG3DSA:3.10.290.10. G3DSA:3.10.290.10. 1 hit.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
KOK01866.
PANTHERPTHR11766. Tyr_tRNA-synt_1b. 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

BindingDBA6U2J5.

Entry information

Entry nameSYY_STAA2
AccessionPrimary (citable) accession number: A6U2J5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: August 21, 2007
Last modified: January 25, 2012
This is version 35 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

SIMILARITY comments

Index of protein domains and families