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Q979Z1 (SYY_THEVO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 70. 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:TV1019
ORF Names:TVG1042450
OrganismThermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1) [Complete proteome] [HAMAP]
Taxonomic identifier273116 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Thermoplasmata › Thermoplasmatales › Thermoplasmataceae › Thermoplasma ›

Protein attributes

Sequence length331 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 – 331331Tyrosine--tRNA ligase HAMAP-Rule MF_02009
PRO_0000240274

Regions

Motif218 – 2225"KMSKS" region HAMAP-Rule MF_02009

Sites

Binding site311Tyrosine By similarity
Binding site1551Tyrosine By similarity
Binding site1591Tyrosine By similarity
Binding site1621Tyrosine By similarity
Binding site1771Tyrosine By similarity
Binding site2211ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q979Z1 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: 869D3A62B97D622B

FASTA33137,690
        10         20         30         40         50         60 
MLIDKLMKNT REIVTLEDAQ KLDQKAGVKS YIGIEPSGIP HVATAVMWPR KLAELQDDIK 

        70         80         90        100        110        120 
IYVLLADWHA MINNKLHGDL DLIRKGGELL KRSFMAEGLT KAEYLWASQL VSSSNYWEMF 

       130        140        150        160        170        180 
IKTAKRSTLK RLTRALPIMG RTEADAEKDF SMYIYPIMQV TDIFYLDVDI AFGGMDQRHA 

       190        200        210        220        230        240 
HMLARDIADK MKVKKAVSVH GYLLSSLKGN TRMDNFVKMS KSDPNSAILI NDEYKDIERK 

       250        260        270        280        290        300 
VNAAFCPPEK VDGNPLAEIM KYVLIPYYGR DIIIEKPSGN VRIENVDQFQ NDYISGKIAP 

       310        320        330 
TELKKAMIPI LDEMIEPARK VAYDMDLSIF S

« Hide

References

[1]"Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium."
Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y., Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T., Yamamoto Y., Aramaki H., Makino K., Suzuki M.
Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000011 Genomic DNA. Translation: BAB60161.1.
RefSeqNP_111508.1. NC_002689.2.

3D structure databases

ProteinModelPortalQ979Z1.
ModBaseSearch...

Protein-protein interaction databases

STRING273116.TVN0989.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB60161; BAB60161; BAB60161.
GeneID1441129.
KEGGtvo:TVN0989.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0162.
KOK01866.
OMAFEPLWPI.
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.
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.
PROSITEPS00178. AA_TRNA_LIGASE_I. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYY_THEVO
AccessionPrimary (citable) accession number: Q979Z1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: October 1, 2001
Last modified: May 1, 2013
This is version 70 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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