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B6YWK6 (SYY_THEON) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:TON_0981
OrganismThermococcus onnurineus (strain NA1) [Complete proteome] [HAMAP]
Taxonomic identifier523850 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Thermococcus ›

Protein attributes

Sequence length375 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-Rule MF_02009

Catalytic activity

ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr). HAMAP-Rule MF_02009

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 4 subfamily.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete 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

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 – 375375Tyrosine--tRNA ligase HAMAP-Rule MF_02009
PRO_1000189476

Regions

Motif251 – 2555"KMSKS" region HAMAP-Rule MF_02009

Sites

Binding site371Tyrosine By similarity
Binding site1681Tyrosine By similarity
Binding site1721Tyrosine By similarity
Binding site1751Tyrosine By similarity
Binding site1901Tyrosine By similarity
Binding site2541ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B6YWK6 [UniParc].

Last modified January 20, 2009. Version 1.
Checksum: F3E0B4905B1C4F6E

FASTA37543,133
        10         20         30         40         50         60 
MDIGRKIELI TKRPTEELLT VENLRHLLEI GAPMQHYIGF EISGYIHLGT GLMAGAKIAD 

        70         80         90        100        110        120 
LQKAGIKTRI FLADWHSWIN DKLGGDLEII QKVALTYFKE GMKQSIKVMG GDPDKVEFVL 

       130        140        150        160        170        180 
ASEILEKGDY WQTVIDISKN VTLARMMRSI TIMGRQMGEA IDFAKLIYPA MQVADIFYQG 

       190        200        210        220        230        240 
VTIAHAGMDQ RKAHVIAIEV AQKLKYHAIE HNGEKLKPVA LHHHLLLGLQ EPPVWPIESE 

       250        260        270        280        290        300 
EQYKELKTQM KMSKSKPYSA VFIHDTPEEI KQKLRKAFCP AREVKYNPVL DWAEYIIFRE 

       310        320        330        340        350        360 
EPTEFTIHRP AKFGGDVTYT TFEELKRDFA EGKLHPLDLK NAVAEYLIEL LKPVRDYFEK 

       370 
HPEPLELMRE IKITR

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References

[1]"The complete genome sequence of Thermococcus onnurineus NA1 reveals a mixed heterotrophic and carboxydotrophic metabolism."
Lee H.S., Kang S.G., Bae S.S., Lim J.K., Cho Y., Kim Y.J., Jeon J.H., Cha S.-S., Kwon K.K., Kim H.-T., Park C.-J., Lee H.-W., Kim S.I., Chun J., Colwell R.R., Kim S.-J., Lee J.-H.
J. Bacteriol. 190:7491-7499(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NA1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000855 Genomic DNA. Translation: ACJ16469.1.
RefSeqYP_002307366.1. NC_011529.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING523850.TON_0981.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACJ16469; ACJ16469; TON_0981.
GeneID7017285.
KEGGton:TON_0981.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0162.
HOGENOMHOG000228238.
KOK01866.
OMAYIGFEIS.
ProtClustDBPRK08560.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
HAMAPMF_02009. Tyr_tRNA_synth_type4.
InterProIPR002305. aa-tRNA-synth_Ic.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002307. Tyr-tRNA-ligase.
IPR023678. Tyr-tRNA-ligase_4.
IPR023617. Tyr-tRNA-ligase_arc/euk-type.
[Graphical view]
PfamPF00579. tRNA-synt_1b. 1 hit.
[Graphical view]
PIRSFPIRSF006588. TyrRS_arch_euk. 1 hit.
TIGRFAMsTIGR00234. tyrS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYY_THEON
AccessionPrimary (citable) accession number: B6YWK6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: January 20, 2009
Last modified: May 1, 2013
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

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