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Reviewed, UniProtKB/Swiss-Prot Q5UPJ7 (SYY_MIMIV)

Last modified November 25, 2008. Version 27. 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

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: YARS
Ordered Locus Names: MIMI_L124
OrganismAcanthamoeba polyphaga mimivirus (APMV) [Complete proteome]
Taxonomic identifier212035 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageMimiviridaeMimivirus
Virus hostAcanthamoeba polyphaga (Amoeba) [TaxID: 5757]

Protein attributes

Sequence length346 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

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

Subunit structure

Homodimer.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family.

Biophysicochemical properties

Kinetic parameters:

KM=0.5 µM for tRNA-Tyr

Ontologies

Keywords

   Biological processProtein biosynthesis
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical term3D-structure
Complete proteome

Gene Ontology (GO)

   Biological processtyrosyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: InterPro

   Molecular functionATP binding

Inferred from electronic annotation. Source: InterPro

tyrosine-tRNA ligase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 346346Tyrosyl-tRNA synthetase
PRO_0000055677

Regions

Motif47 – 5610"HIGH" region
Motif230 – 2345"KMSKS" region

Sites

Binding site2331ATP By similarity

Secondary structure

...................................................... 346
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q5UPJ7-1 [UniParc].

Last modified December 7, 2004. Version 1.
Checksum: 43C8D8C3ECBC87B0

FASTA34639,723
        10         20         30         40         50         60 
MENTDHTNNE HRLTQLLSIA EECETLDRLK QLVDSGRIFT AYNGFEPSGR IHIAQALITV 

        70         80         90        100        110        120 
MNTNNIIECG GQMIIYIADW FAKMNLKMNG DINKIRELGR YFIEVFKACG INLDGTRFIW 

       130        140        150        160        170        180 
ASEFIASNPS YIERMLDIAE FSTISRVKRC CQIMGRNESD CLKASQIFYP CMQAADVFEL 

       190        200        210        220        230        240 
VPEGIDICQL GIDQRKVNML AIEYANDRGL KIPISLSHHM LMSLSGPKKK MSKSDPQGAI 

       250        260        270        280        290        300 
FMDDTEQEVS EKISRAYCTD ETFDNPIFEY IKYLLLRWFG TLNLCGKIYT DIESIQEDFS 

       310        320        330        340 
SMNKRELKTD VANYINTIID LVREHFKKPE LSELLSNVKS YQQPSK 

« Hide

References

« Hide 'large scale' references
[1]"The 1.2-megabase genome sequence of Mimivirus."
Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H., La Scola B., Susan M., Claverie J.-M.
Science 306:1344-1350(2004) [PubMed: 15486256] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], FUNCTION.
Strain: Rowbotham-Bradford.
[2]"Mimivirus TyrRS: preliminary structural and functional characterization of the first amino-acyl tRNA synthetase found in a virus."
Abergel C., Chenivesse S., Byrne D., Suhre K., Arondel V., Claverie J.-M.
Acta Crystallogr. F 61:212-215(2005) [PubMed: 16510997] [Abstract]
Cited for: CRYSTALLIZATION, FUNCTION.
[3]"Virus-encoded aminoacyl-tRNA synthetases: structural and functional characterization of Mimivirus TyrRS and MetRS."
Abergel C., Rudinger-Thirion J., Giege R., Claverie J.-M.
J. Virol. 81:12406-12417(2007) [PubMed: 17855524] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), SUBUNIT, CATALYTIC ACTIVITY, KINETIC PARAMETERS.

Cross-references

Sequence databases

AY653733 Genomic DNA. Translation: AAV50399.1.
RefSeqYP_142478.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2J5BX-ray2.20A/B1-346[»]
ModBaseSearch...

Genome annotation databases

GeneID3162469.

Family and domain databases

InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002305. aa-tRNA-synth_Ib.
IPR014729. Rossmann-like_a/b/a_fold.
IPR015624. Tyr-tRNA-synth_Ib_arc/euk.
IPR016485. TyrRS_arch_euk.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHERPTHR11946:SF8. Tyr-tRNA_synth. 1 hit.
PfamPF00579. tRNA-synt_1b. 1 hit.
[Graphical view]
PIRSFPIRSF006588. TyrRS_arch_euk. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYY_MIMIV
AccessionPrimary (citable) accession number: Q5UPJ7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: December 7, 2004
Last modified: November 25, 2008
This is version 27 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectVirus (Virus annotation project)

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