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O67632 (SYY_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 75. 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:aq_1751
OrganismAquifex aeolicus (strain VF5)
Taxonomic identifier224324 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesAquificaceaeAquifex

Protein attributes

Sequence length392 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_02007

Catalytic activity

ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr). HAMAP MF_02007

Subunit structure

Homodimer By similarity. HAMAP MF_02007

Subcellular location

Cytoplasm By similarity HAMAP MF_02007.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 2 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
Reference 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 – 392392Tyrosine--tRNA ligase HAMAP MF_02007
PRO_0000055640

Regions

Domain330 – 39061S4 RNA-binding
Motif41 – 5010"HIGH" region HAMAP MF_02007
Motif225 – 2295"KMSKS" region HAMAP MF_02007

Sites

Binding site2281ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
O67632 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 7B160BEF801665B2

FASTA39245,200
        10         20         30         40         50         60 
MTPEEQLRII KEGTVEIIEE EELLKKLKEG RPLRVKAGFD PTAPDLHLGH VVLLQKLRQF 

        70         80         90        100        110        120 
QQLGHEVFFI IGDFTAMIGD PTGRSQTRPP LSREQVLENA KTYEHQVFKV LIPEKTTVVF 

       130        140        150        160        170        180 
NSTWLEELGT KGLIELCAKY TVARMLERED FSKRFKEGIP IYIHEFIYPL LQAYDSVAIK 

       190        200        210        220        230        240 
ADVEIGGTDQ KFNLLIGRDI QREYGQEPQV CITLPLLVGT DGVRKMSKSY GNYVGITEDP 

       250        260        270        280        290        300 
KTMFAKIMSI PDEIMWDWFL LLTDYNKEEI EKMRREMHPM EAKKLLAFTI VKRFHSEEEA 

       310        320        330        340        350        360 
RKAKEWWEKT FSQREFPEDA PLVKLNEKKL RAVDFLVKIG AVKSKNEARR VIQGGGLKIN 

       370        380        390 
GEKVTDPNTE IEINGELKVK VGKKKFYRVV SG 

« Hide

References

[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed: 9537320] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000657 Genomic DNA. Translation: AAC07595.1.
PIRF70450.
RefSeqNP_214198.1. NC_000918.1.

3D structure databases

ProteinModelPortalO67632.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1193347.
GenomeReviewsGene locus aq_1751 in contig AE000657_GR.
KEGGaae:aq_1751.
NMPDRfig|224324.1.peg.1213.
PATRIC20960492. VBIAquAeo85532_1350.

Phylogenomic databases

HOGENOMHBG288125.
OMAIPTYFEL.
PhylomeDBO67632.
ProtClustDBPRK05912.

Enzyme and pathway databases

BioCycAAEO224324:AQ_1751-MONOMER.

Family and domain databases

HAMAPMF_02007. Tyr_tRNA_synth_type2.
[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.
IPR024108. Tyr-tRNA-synth_bac_2.
[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...

Entry information

Entry nameSYY_AQUAE
AccessionPrimary (citable) accession number: O67632
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: January 25, 2012
This is version 75 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