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Q9YA64 (SYY_AERPE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:APE_2074.1
OrganismAeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1) [Complete proteome] [HAMAP]
Taxonomic identifier272557 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiDesulfurococcalesDesulfurococcaceaeAeropyrum

Protein attributes

Sequence length364 AA.
Sequence statusComplete.
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. HAMAP MF_02009

Catalytic activity

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

Subunit structure

Homodimer. Ref.2

Subcellular location

Cytoplasm By similarity HAMAP MF_02009.

Sequence similarities

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

Sequence caution

The sequence BAA81085.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   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: UniProtKB-SubCell

   Molecular functionATP 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 – 364364Tyrosine--tRNA ligase HAMAP MF_02009
PRO_0000240262

Regions

Motif238 – 2425"KMSKS" region HAMAP MF_02009

Sites

Binding site391Tyrosine By similarity
Binding site491ATP Probable
Binding site521ATP Probable
Binding site1651Tyrosine By similarity
Binding site1691Tyrosine By similarity
Binding site1721Tyrosine By similarity
Binding site1871Tyrosine By similarity
Binding site2411ATP Probable

Secondary structure

...................................................... 364
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9YA64 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 3C9ABE0E3BE7EC6B

FASTA36440,765
        10         20         30         40         50         60 
MVRVDVEERF NRIARNTVEI VTEEELKGLL ASGARIKGYI GYEPSGVAHI GWLVWMYKVK 

        70         80         90        100        110        120 
DLVEAGVDFS VLEATWHAYI NDKLGGDMDL IRAAARIVRR VMEAAGVPVE RVRFVDAEEL 

       130        140        150        160        170        180 
ASDKDYWGLV IRVAKRASLA RVRRALTIMG RRAEEAEVDA SKLIYPLMQV SDIFYMDLDI 

       190        200        210        220        230        240 
ALGGMDQRKA HMLARDVAEK LGRKKPVAIH TPIISSLQGP GRMEASQGEI DDVLAEVKMS 

       250        260        270        280        290        300 
KSKPETAVFV VDSDDDIRRK IRKAYCPAKQ VQGNPVLEIA RYILFARDGF TLRVDRPAKY 

       310        320        330        340        350        360 
GGPVEYTSYE ELERDYTDGR LHPLDLKNAV AESLIEVVRP IRGAVLGDPA MKRALEAIEG 


KVTR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000002 Genomic DNA. Translation: BAA81085.2. Different initiation.
PIRE72512.
RefSeqNP_148365.2. NC_000854.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CYAX-ray2.20A1-364[»]
ProteinModelPortalQ9YA64.
SMRQ9YA64. Positions 4-361.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1445173.
GenomeReviewsGene locus APE_2074.1 in contig BA000002_GR.
KEGGape:APE_2074.1.
NMPDRfig|272557.1.peg.1473.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG330667.
OMAGMEQRKI.
PhylomeDBQ9YA64.
ProtClustDBPRK08560.

Enzyme and pathway databases

BioCycAPER272557:APE2074-MONOMER.

Family and domain databases

HAMAPMF_02009. Tyr_tRNA_synth_type4.
[Tree]
InterProIPR002305. aa-tRNA-synth_Ic.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002307. Tyr-tRNA-synth.
IPR023678. Tyr-tRNA-synth_4.
IPR023617. Tyr-tRNA-synth_arc-type.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
KOK01866.
PANTHERPTHR11946:SF8. Tyr-tRNA_synth. 1 hit.
PfamPF00579. tRNA-synt_1b. 1 hit.
[Graphical view]
PIRSFPIRSF006588. TyrRS_arch_euk. 1 hit.
PRINTSPR01040. TRNASYNTHTYR.
TIGRFAMsTIGR00234. TyrS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYY_AERPE
AccessionPrimary (citable) accession number: Q9YA64
Entry history
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: November 1, 1999
Last modified: January 25, 2012
This is version 67 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families