Isoleucine--tRNA ligase
Details
- Name
- Isoleucine--tRNA ligase
- Kind
- protein
- Synonyms
- 6.1.1.5
- IleRS
- Isoleucyl-tRNA synthetase
- Gene Name
- ileS
- UniProtKB Entry
- P56690Swiss-Prot
- Organism
- Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
- NCBI Taxonomy ID
- 300852
- Amino acid sequence
>lcl|BSEQ0010960|Isoleucine--tRNA ligase MFKEVGEPNFPKLEEEVLAFWKREKIFQKSVENRKGGPRYTVYEGPPTANGLPHVGHAQA RSYKDLFPRYKTMRGYYAPRRAGWDTHGLPVELEVEKKLGLKSKREIEAYGIERFNQACR ESVFTYEKEWEAFTERIAYWVDLENAYATLEPTYIESIWWSLKNLFDRGLLYRDHKVVPY CPRCGTPLSSHEVALGYKEIQDPSVYVRFPLKEPKKLGLEKASLLIWTTTPWTLPGNVAA AVHPEYTYAAFQVGDEALILEEGLGRKLLGEGTPVLKTFPGKALEGLPYTPPYPQALEKG YFVVLADYVSQEDGTGIVHQAPAFGAEDLETARVYGLPLLKTVDEEGKLLVEPFKGLYFR EANRAILRDLRGRGLLFKEESYLHSYPHCWRCSTPLMYYATESWFIKNTLFKDELIRKNQ EIHWVPPHIKEGRYGEWLKNLVDWALSRNRYWGTPLPIWVCQACGKEEAIGSFQELKARA TKPLPEPFDPHRPYVDQVELACACGGTMRRVPYVIDVWYDSGAMPFASLHYPFEHEEVFR ESFPADFIAEGIDQTRGWFNSLHQLGVMLFGSIAFKNVICHGLILDEKGQKMSKSKGNVV DPWDIIREFGADALRWYIYVSAPPEADRRFGPNLVRETVRDYFLTLWNVYSFFVTYANLD RPDLKNPPPPEKRPEMDRWLLARMQDLIQRVTEALEAYDPTTSARALRDFVVEDLSQWYV RRNRRRFWKNEDALDREAAYATLYEALVLVATLAAPFTPFLAEVLWQNLVRSVRPEAKES VHLADWPEADPALADEALVAQMRAVLKVVDLARAARAKSGVKTRTPLPLLLVTAPTALER EGLKRFAHEIAEELNVKEVRVLEPGEEILSYRVLPNLKLLGRKYGKLVPKIREALQRERE RAAALALKGEAIPLEVEGEALTLLPEEVLLEAEAPKGYQALEKDGYVAALKVEVTEALRM EGLARDLIRLLQQARKDMGLKVSDRIRVGYEAEGPYLEALKRHGPWIAEEVLATAFGEGL FGGFEARVEDEEGKAVFHLARAE
- Number of residues
- 1043
- Molecular Weight
- 119245.62
- Theoretical pI
- 6.23
- GO Classification
- Functionsaminoacyl-tRNA editing activity / ATP binding / isoleucine-tRNA ligase activity / zinc ion bindingProcessesisoleucyl-tRNA aminoacylationComponentscytoplasm
- General Function
- Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile) (By similarity).
- Specific Function
- aminoacyl-tRNA editing activity
- Pfam Domain Function
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0010961|Isoleucine--tRNA ligase (ileS) ATGTTCAAGGAGGTCGGCGAGCCCAACTTTCCCAAGCTGGAAGAGGAGGTCTTGGCCTTC TGGAAGCGGGAAAAGATCTTCCAAAAGAGCGTGGAAAACCGCAAAGGCGGTCCCCGCTAC ACCGTCTACGAGGGCCCTCCCACCGCCAACGGCCTCCCCCACGTGGGCCACGCCCAGGCC CGGAGCTACAAGGACCTCTTCCCCCGCTACAAGACCATGCGGGGCTACTACGCGCCCCGG AGGGCAGGCTGGGACACCCACGGGCTTCCCGTGGAGCTGGAGGTGGAGAAGAAGCTCGGC CTCAAGAGCAAGCGGGAGATTGAGGCCTACGGCATTGAGCGCTTCAACCAAGCCTGCCGC GAGTCCGTCTTCACCTACGAGAAGGAGTGGGAGGCCTTTACCGAGCGCATCGCCTACTGG GTGGACCTGGAGAACGCCTACGCCACCTTGGAACCCACCTATATTGAGAGCATCTGGTGG AGCCTGAAGAACCTCTTTGACCGGGGCCTCCTCTACCGGGACCACAAGGTGGTGCCCTAC TGCCCCCGCTGCGGCACCCCCCTCTCCTCCCACGAGGTCGCCCTGGGGTACAAGGAGATC CAAGACCCCTCGGTCTACGTCCGCTTCCCCTTGAAGGAGCCGAAGAAGCTTGGCCTAGAG AAGGCGAGCCTCCTCATCTGGACCACCACCCCCTGGACCCTGCCCGGGAACGTGGCCGCA GCAGTCCACCCGGAGTACACCTACGCCGCCTTCCAGGTGGGAGACGAGGCCCTGATCCTG GAGGAGGGGCTGGGGAGGAAGCTTTTGGGCGAGGGAACCCCGGTCCTCAAAACCTTCCCG GGCAAGGCCCTGGAAGGCCTCCCCTACACCCCCCCCTACCCCCAGGCCTTGGAGAAGGGC TACTTCGTGGTCCTCGCCGACTACGTGAGTCAAGAGGACGGGACGGGCATCGTCCACCAG GCCCCCGCCTTCGGCGCCGAGGACCTGGAGACGGCGAGGGTCTACGGGCTTCCCCTCCTG AAGACCGTGGACGAGGAGGGGAAGCTCCTCGTGGAGCCGTTTAAGGGCCTCTACTTCCGC GAGGCCAACCGGGCGATCCTAAGGGACCTGAGGGGGCGGGGCCTCCTCTTCAAGGAGGAA AGCTACCTCCACAGCTACCCCCACTGCTGGCGGTGCTCCACCCCCCTCATGTACTACGCC ACGGAGAGCTGGTTCATCAAAAACACCCTCTTCAAGGACGAGCTCATCCGCAAGAACCAG GAGATCCACTGGGTGCCCCCCCACATCAAGGAGGGCCGCTACGGGGAGTGGCTCAAGAAC CTCGTGGACTGGGCCTTAAGCCGCAACCGCTACTGGGGGACACCCCTCCCCATCTGGGTC TGCCAGGCGTGCGGCAAGGAGGAGGCCATCGGGAGCTTCCAGGAGCTCAAGGCGAGGGCC ACGAAGCCCCTCCCCGAGCCCTTTGACCCCCACCGCCCCTACGTGGACCAGGTGGAGCTC GCCTGTGCCTGCGGCGGGACCATGCGCCGCGTCCCCTACGTCATTGACGTCTGGTACGAC TCCGGGGCCATGCCCTTCGCCTCCTTGCACTACCCCTTTGAGCACGAAGAGGTGTTCCGG GAGAGCTTCCCCGCGGACTTCATCGCCGAGGGGATTGACCAGACCCGGGGCTGGTTCAAC TCCCTCCACCAGCTCGGGGTGATGCTCTTCGGCTCCATCGCCTTCAAGAACGTGATCTGC CACGGCCTCATCCTGGACGAAAAGGGGCAGAAGATGTCCAAGTCCAAGGGGAACGTGGTG GACCCCTGGGACATCATCCGGGAGTTCGGGGCGGACGCCCTCAGGTGGTACATCTACGTC TCCGCGCCTCCCGAGGCCGACCGGCGCTTCGGGCCCAACCTGGTTCGGGAAACGGTGCGG GACTACTTCCTCACCCTCTGGAACGTCTACAGCTTCTTCGTGACCTACGCCAACCTGGAC CGGCCCGACCTCAAGAACCCCCCTCCCCCCGAGAAGCGGCCCGAGATGGACCGCTGGCTC CTCGCCCGCATGCAGGACCTCATCCAGAGGGTGACGGAGGCCCTCGAGGCCTACGACCCC ACCACGAGCGCCCGCGCCCTGAGGGACTTCGTGGTGGAGGACCTCTCCCAGTGGTACGTC CGCAGGAACCGGCGCCGCTTCTGGAAGAACGAGGACGCCCTGGACCGGGAGGCGGCCTAC GCCACCCTCTACGAGGCCCTCGTCCTGGTGGCCACCCTCGCCGCCCCCTTCACCCCCTTC CTCGCCGAGGTCCTGTGGCAGAACCTGGTGCGGAGCGTCCGGCCCGAGGCCAAGGAGAGC GTCCACCTCGCCGACTGGCCCGAGGCCGACCCGGCCCTGGCCGACGAGGCCCTGGTGGCC CAGATGCGGGCGGTGCTCAAGGTGGTGGACCTGGCCCGGGCGGCCCGGGCGAAAAGCGGG GTCAAGACCCGCACCCCCCTTCCCCTCCTCCTCGTCACCGCCCCCACCGCCTTGGAGCGG GAGGGGTTAAAGCGCTTCGCCCACGAGATCGCCGAGGAGCTCAACGTCAAGGAGGTCCGG GTCCTGGAACCCGGGGAGGAGATCCTCTCCTACAGGGTCCTGCCCAACCTCAAGCTCCTG GGGAGGAAGTACGGCAAGCTCGTCCCCAAAATCCGGGAGGCCCTGCAAAGGGAAAGGGAG CGCGCCGCCGCCTTGGCGCTTAAGGGCGAGGCCATCCCCCTGGAGGTGGAGGGCGAGGCC CTCACCCTCCTCCCGGAGGAGGTCCTCCTCGAGGCCGAGGCCCCCAAGGGCTACCAGGCC CTGGAGAAGGACGGGTACGTGGCCGCCCTCAAGGTGGAGGTCACGGAAGCCCTCCGCATG GAGGGCCTCGCCCGCGACCTCATCCGCCTCCTGCAGCAGGCCCGCAAAGACATGGGCCTC AAGGTCTCGGACCGGATCCGGGTGGGCTACGAGGCGGAGGGCCCCTACCTCGAGGCCCTG AAGCGGCACGGGCCCTGGATCGCCGAGGAGGTGCTGGCCACCGCCTTCGGGGAAGGCCTC TTCGGCGGGTTTGAGGCCCGGGTGGAGGACGAGGAGGGCAAGGCGGTCTTCCACCTGGCC CGGGCGGAGTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P56690 UniProtKB Entry Name SYI_THET8 GenBank Protein ID 55772449 GenBank Gene ID AP008226 PDB ID(s) 1ILE, 1JZQ, 1JZS, 1UDZ, 1UE0, 1WK8, 1WNY, 1WNZ KEGG ID ttj:TTHA1067 NCBI Gene ID 3168241 - General References
- Nureki O, Vassylyev DG, Tateno M, Shimada A, Nakama T, Fukai S, Konno M, Hendrickson TL, Schimmel P, Yokoyama S: Enzyme structure with two catalytic sites for double-sieve selection of substrate. Science. 1998 Apr 24;280(5363):578-82. [Article]
- Nakama T, Nureki O, Yokoyama S: Structural basis for the recognition of isoleucyl-adenylate and an antibiotic, mupirocin, by isoleucyl-tRNA synthetase. J Biol Chem. 2001 Dec 14;276(50):47387-93. Epub 2001 Oct 2. [Article]
- Fukunaga R, Fukai S, Ishitani R, Nureki O, Yokoyama S: Crystal structures of the CP1 domain from Thermus thermophilus isoleucyl-tRNA synthetase and its complex with L-valine. J Biol Chem. 2004 Feb 27;279(9):8396-402. Epub 2003 Dec 12. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details N-[Isoleucinyl]-N'-[adenosyl]-diaminosufone experimental unknown target Details