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Reviewed, UniProtKB/Swiss-Prot P83453 (SYY_THET2)

Last modified November 24, 2009. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Tyrosyl-tRNA synthetase
    EC=6.1.1.1
Alternative name(s):
    Tyrosine--tRNA ligase
      Short name=TyrRS
Gene names
Name: tyrS
Ordered Locus Names: TT_C1033
OrganismThermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039) [Complete proteome] [HAMAP]
Taxonomic identifier262724 [NCBI]
Taxonomic lineageBacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus

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Protein attributes

Sequence length432 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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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.

Catalytic activity

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

Subunit structure

Homodimer. HAMAP MF_02007

Subcellular location

Cytoplasm By similarity.

Miscellaneous

Although this protein is a class I aminoacyl-tRNA synthetase, it displays a class II mode of tRNA recognition. HAMAP MF_02007

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 2 subfamily.

Contains 1 S4 RNA-binding domain.

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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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 432432Tyrosyl-tRNA synthetase HAMAP MF_02007
PRO_0000055665

Regions

Domain369 – 43062S4 RNA-binding
Motif46 – 5510"HIGH" region HAMAP MF_02007
Motif232 – 2365"KMSKS" region HAMAP MF_02007

Sites

Binding site2351ATP HAMAP MF_02007

Secondary structure

1 ........................................................................... 432
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P83453-1 [UniParc].

Last modified November 15, 2002. Version 1.
Checksum: 71B04B8976B8D91B

FASTA43248,718
        10         20         30         40         50         60 
MAGTGHTPEE ALALLKRGAE EIVPEEELLA KLKEGRPLTV KLGADPTRPD LHLGHAVVLR 

        70         80         90        100        110        120 
KMRQFQELGH KVVLIIGDFT GMIGDPSGRS KTRPPLTLEE TRENAKTYVA QAGKILRQEP 

       130        140        150        160        170        180 
HLFELRYNSE WLEGLTFKEV VRLTSLMTVA QMLEREDFKK RYEAGIPISL HELLYPFAQA 

       190        200        210        220        230        240 
YDSVAIRADV EMGGTDQRFN LLVGREVQRA YGQSPQVCFL MPLLVGLDGR EKMSKSLDNY 

       250        260        270        280        290        300 
IGLTEPPEAM FKKLMRVPDP LLPSYFRLLT DLEEEEIEAL LKAGPVPAHR VLARLLTAAY 

       310        320        330        340        350        360 
ALPQIPPRID RAFYESLGYA WEAFGRDKEA GPEEVRRAEA RYDEVAKGGI PEEIPEVTIP 

       370        380        390        400        410        420 
ASELKEGRIW VARLFTLAGL TPSNAEARRL IQNRGLRLDG EVLTDPMLQV DLSRPRILQR 

       430 
GKDRFVRVRL SD

« Hide

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References

« Hide 'large scale' references
[1]"The genome sequence of the extreme thermophile Thermus thermophilus."
Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H., Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C., Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P., Kramer W., Merkl R., Gottschalk G., Fritz H.-J.
Nat. Biotechnol. 22:547-553(2004) [PubMed: 15064768] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"Class I tyrosyl-tRNA synthetase has a class II mode of cognate tRNA recognition."
Yaremchuk A., Kriklivyi I., Tukalo M., Cusack S.
EMBO J. 21:3829-3840(2002) [PubMed: 12110594] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

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Cross-references

Sequence databases

AE017221 Genomic DNA. Translation: AAS81375.1.
RefSeqYP_005002.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1H3EX-ray2.90A1-432[»]
1H3FX-ray2.00A/B1-432[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGP83453.

Genome annotation databases

GeneID2776306.
GenomeReviewsGene locus TT_C1033 in contig AE017221_GR.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP83453.
OMAYVVQVGK

Enzyme and pathway databases

BioCycTTHE262724:TT_C1033-MON.

Family and domain databases

HAMAPMF_02007.
[Tree]
InterProIPR002305. aa-tRNA-synth_Ib.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002942. S4_RNA_bd.
IPR002307. Tyr-tRNA-synth_Ib_bac/mito.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHERPTHR11766. Tyr_tRNA-synt_1b. 1 hit.
PfamPF00579. tRNA-synt_1b. 1 hit.
[Graphical view]
PRINTSPR01040. TRNASYNTHTYR.
SMARTSM00363. S4. 1 hit.
[Graphical view]
TIGRFAMsTIGR00234. tyrS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. False negative.
PS50889. S4. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameSYY_THET2
AccessionPrimary (citable) accession number: P83453
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: November 15, 2002
Last modified: November 24, 2009
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents