Tyrosine--tRNA ligase

Details

Name
Tyrosine--tRNA ligase
Kind
protein
Synonyms
  • 6.1.1.1
  • Tyrosyl-tRNA synthetase
  • TyrRS
Gene Name
tyrS
UniProtKB Entry
P83453Swiss-Prot
Organism
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
NCBI Taxonomy ID
262724
Amino acid sequence
>lcl|BSEQ0019213|Tyrosine--tRNA ligase
MAGTGHTPEEALALLKRGAEEIVPEEELLAKLKEGRPLTVKLGADPTRPDLHLGHAVVLR
KMRQFQELGHKVVLIIGDFTGMIGDPSGRSKTRPPLTLEETRENAKTYVAQAGKILRQEP
HLFELRYNSEWLEGLTFKEVVRLTSLMTVAQMLEREDFKKRYEAGIPISLHELLYPFAQA
YDSVAIRADVEMGGTDQRFNLLVGREVQRAYGQSPQVCFLMPLLVGLDGREKMSKSLDNY
IGLTEPPEAMFKKLMRVPDPLLPSYFRLLTDLEEEEIEALLKAGPVPAHRVLARLLTAAY
ALPQIPPRIDRAFYESLGYAWEAFGRDKEAGPEEVRRAEARYDEVAKGGIPEEIPEVTIP
ASELKEGRIWVARLFTLAGLTPSNAEARRLIQNRGLRLDGEVLTDPMLQVDLSRPRILQR
GKDRFVRVRLSD
Number of residues
432
Molecular Weight
48717.765
Theoretical pI
6.44
GO Classification
Functions
ATP binding / RNA binding / tyrosine-tRNA ligase activity
Processes
tyrosyl-tRNA aminoacylation
Components
cytoplasm
General 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).
Specific Function
ATP binding
Pfam Domain Function
Signal Regions
Not Available
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0019214|Tyrosine--tRNA ligase (tyrS)
ATGGCGGGCACCGGCCACACCCCGGAAGAGGCCCTGGCCCTCCTCAAGCGGGGGGCCGAG
GAGATCGTCCCCGAGGAAGAGCTTCTCGCCAAGCTCAAGGAGGGGCGGCCCCTCACGGTC
AAGCTCGGGGCCGACCCCACGAGGCCCGACCTGCACCTGGGCCACGCGGTGGTCCTGAGG
AAGATGCGCCAGTTCCAAGAGCTCGGCCACAAGGTGGTCCTCATCATCGGCGACTTCACC
GGGATGATCGGGGACCCTTCGGGCCGTTCCAAGACCCGGCCCCCCCTCACCCTCGAGGAG
ACCCGGGAGAACGCCAAGACCTACGTGGCCCAGGCGGGGAAGATCCTCAGGCAGGAGCCC
CACCTCTTTGAGCTCCGCTACAACTCCGAGTGGCTGGAGGGCCTCACCTTCAAGGAGGTG
GTGCGCCTCACCTCCCTCATGACCGTGGCCCAGATGCTGGAAAGGGAGGACTTTAAAAAG
CGGTACGAGGCGGGGATTCCCATCTCCCTGCACGAGCTTTTGTACCCCTTCGCCCAGGCC
TACGACTCCGTGGCCATAAGGGCCGACGTGGAAATGGGGGGCACGGACCAGCGCTTCAAC
CTCCTGGTGGGCCGGGAGGTGCAACGGGCCTACGGGCAAAGCCCCCAGGTCTGCTTCCTC
ATGCCCCTTCTCGTGGGCCTTGACGGGCGGGAGAAGATGAGCAAGAGCCTGGACAACTAC
ATCGGCCTCACCGAGCCCCCGGAGGCGATGTTCAAGAAGCTCATGCGGGTGCCGGACCCT
CTCCTCCCGAGCTACTTCCGCCTCCTCACGGACCTGGAGGAGGAGGAAATAGAGGCCCTC
CTAAAGGCGGGCCCCGTCCCCGCCCACCGGGTCCTCGCCCGCCTCCTCACCGCGGCCTAC
GCCCTGCCCCAGATCCCCCCCCGGATAGACCGGGCCTTTTACGAAAGCCTCGGCTACGCC
TGGGAGGCCTTCGGGCGGGACAAGGAGGCGGGCCCCGAGGAGGTAAGGAGGGCGGAAGCC
CGCTACGACGAGGTGGCCAAAGGGGGAATCCCCGAGGAGATCCCCGAGGTCACCATCCCC
GCCTCGGAGCTGAAGGAAGGCCGGATCTGGGTGGCGAGGCTTTTTACCTTAGCGGGCCTC
ACCCCCTCCAACGCCGAGGCGAGGAGGCTCATCCAGAACCGGGGCCTGAGGCTGGACGGG
GAGGTCCTCACCGACCCCATGCTCCAGGTGGACCTCTCCCGGCCCCGCATCCTGCAGCGG
GGCAAGGACCGCTTCGTGCGGGTGCGGCTTTCGGACTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP83453
UniProtKB Entry NameSYY_THET2
GenBank Protein ID46196960
GenBank Gene IDAE017221
PDB ID(s)1H3E, 1H3F
KEGG IDtth:TTC1033
General References
  1. Henne A, Bruggemann 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 HP, Kramer W, Merkl R, Gottschalk G, Fritz HJ: The genome sequence of the extreme thermophile Thermus thermophilus. Nat Biotechnol. 2004 May;22(5):547-53. Epub 2004 Apr 4. [Article]
  2. Yaremchuk A, Kriklivyi I, Tukalo M, Cusack S: Class I tyrosyl-tRNA synthetase has a class II mode of cognate tRNA recognition. EMBO J. 2002 Jul 15;21(14):3829-40. [Article]

Associated Data

Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
TyrosinalexperimentalunknowntargetDetails