thrS-cat

Gene

thrS-cat

Protein

Threonine--tRNA ligase catalytic subunit

Organism

Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)

Length

549 amino acids

Function

Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also activates L-serine and transfers it to tRNA(Thr) but cannot deacylate incorrectly charged amino acid; unlike most archaea the editing function is found in a freestanding protein.

Similarity

Belongs to the class-II aminoacyl-tRNA synthetase family.

Mass

64.036 kDa

Sequence

MESYKEVWLKAGLIYALNLLSSGNLKPVEIGLGERYFYVDIDSPDILTLDEAKDFAKYNQYDYQLVEDNRGSITVVYNGHQIKLNGGKPNQNVHPKYFQILSISVHHPSPEKQYVRVLGVGFEKEEQLKDYLNWLEKVSEYDHRIIGDRLDLFSFPEEAPPGVVLFHPNGQIIRKEMMRFMEEINDSMGYKEVYTSHVYRSLLWKISGHYDYYKDKMLLFEIDNDEELGIKPMNCPAHILIYKSKVRSYKDLPIRFSEFGHVYRWEKKGELYGLLRVRGFTQDDGHIFLREDQIKDEIKLLMKKTLDVLAIFGFKGDDVRVNLSTRPDESIGTDEQWNKATDALISALNELNIKYEVKEKEGAFYGPKIDFDIRDSLSRWWQLSTIQVDFNLPERFKLEYVDKDGSKKRPVMVHRAIYGSIDRFMAILLEHFRGKLPTWLSPIQVRVLPITDEIEDYGNSLMAKLRENKIRVDMDSGEETLSKRIKKAYDDGVPYLIIVGRKEKDEGKVTVRARGNIEIRGINVEKFVQALVEEIRNKDLNQSAVSKLK

Protein

Threonine--tRNA ligase catalytic subunit: thrS-cat

Gene

thrS-cat

Protein

Threonine--tRNA ligase catalytic subunit

Organism

Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)

Length

545 amino acids

Function

Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr) (PubMed:15240874). Also activates L-serine and transfers it to tRNA(Thr); unlike most archaea the editing function is found in a freestanding protein (ACQ980D1) (PubMed:15240874). In vitro when both subunits are present, or if the 2 subunits are fused, L-seryl-tRNA(Thr) is no longer produced, the 2 subunits edit incorrectly charged L-seryl-tRNA(Thr) (PubMed:15240874). Has no activity on correctly acylated L-seryl-tRNA(Ser) or L-threonyl-tRNA(Thr).

Similarity

Belongs to the class-II aminoacyl-tRNA synthetase family.

Mass

63.231 kDa

Sequence

MESYKPVWLKGAVILAINLIDKGYKPVAVGLGERDFYIDVKSDTSITLDEVKKAINENVLANVSIENNQIVYKGNKVSIIEDKVSISTNLNPKYFEILNISTHHPNPNEQYVRIRGVAFETEEQLKDYLSWLEKAEETDHRLIGEKLDLFSFHEEAGSGLVLFHPKGQTIRNELIAFMREINDSMGYQEVYTSHVFKTDIWKISGHYTLYRDKLIVFNMEGDEYGVKPMNCPAHILIYKSKPRTYRDLPIRFSEFGHVYRWEKKGELYGLLRVRGFVQDDGHIFLREDQLREEIKMLISKTVEVWHKFGFKDDDIKPYLSTRPDESIGSDELWEKATNALISALQESGLKFGIKEKEGAFYGPKIDFEIRDSLGRWWQLSTIQVDFNLPERFKLEYIDKDGIKKRPVMVHRAIYGSIDRFVAILLEHFKGKLPTWLSSVQVRVLPITDEVNEYAEKVLNDMRKRRIRAEIDYAGETLSKRIKNAYDQGVPYILIVGKKEASEGTVTVRARGNIEVRNVKFEKFLELLITEIAQRDVEQTTVKALK

Protein

Threonine--tRNA ligase catalytic subunit: thrS-cat

Gene

thrS-cat

Protein

Threonine--tRNA ligase catalytic subunit

Organism

Sulfolobus islandicus (strain M.16.27)

Length

545 amino acids

Function

Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also activates L-serine and transfers it to tRNA(Thr) but cannot deacylate incorrectly charged amino acid; unlike most archaea the editing function is found in a freestanding protein.

Similarity

Belongs to the class-II aminoacyl-tRNA synthetase family.

Mass

63.255 kDa

Sequence

MESYKPVWLKGAVILAINLIDKGYKPVAVGLGERDFYIDVKSDTSITLDEVKKAINENVLANVPIENNQIVYKGNKVSIIEDKVSISTNLNPKYFEILNISTHHPNPNEQYVRIRGVAFETEEQLKDYLTWLEKAEETDHRLIGEKLDLFSFHEEAGSGLVLFHPKGQTIRNELIAFMREINDSMGYQEVYTSHVFKTDIWKISGHYTLYRDKLIVFNMEGDEYGVKPMNCPAHILIYKSKPRTYRDLPIRFSEFGHVYRWEKKGELYGLLRVRGFVQDDGHIFLREDQLREEIKMLISKTVEVWHKFGFKDDDIKPYLSTRPDESIGSDELWEKATNALISALQESGLKFGIKEKEGAFYGPKIDFEIRDSLGRWWQLSTIQVDFNLPERFKLEYIDKDGIKKRPVMVHRAIYGSIDRFVAILLEHFKGKLPTWLSSVQVRVLPITDEVNEYAEKVLNDMRKRRIRAEIDYAGETLSKRIKNAYDQGVPYILIVGKKEASEGTVTVRARGNIEVRNVKFEKFLELLITEIAQRDVEQTTVKALK

Protein

Threonine--tRNA ligase catalytic subunit: thrS-cat

Gene

thrS-cat

Protein

Threonine--tRNA ligase catalytic subunit

Organism

Sulfolobus islandicus (strain M.16.4 / Kamchatka #3)

Length

545 amino acids

Function

Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also activates L-serine and transfers it to tRNA(Thr) but cannot deacylate incorrectly charged amino acid; unlike most archaea the editing function is found in a freestanding protein.

Similarity

Belongs to the class-II aminoacyl-tRNA synthetase family.

Mass

63.23 kDa

Sequence

MESYKPVWLKGAVILAINLIDKGYKPVAVGLGERDFYIDVKSDTSITLDEVKKAINENVLANVPIENNQIVYKGNKVSIIEDKVSISTNLNPKYFEILNISTHHPNPNEQYVRIRGVAFETEEQLKDYLTWLEKAEETDHRLIGEKLDLFSFHEEAGSGLVLFHPKGQTIRNELIAFMREINDSMGYQEVYTSHVFKTDIWKISGHYTLYRDKLIVFNMEGDEYGVKPMNCPAHILIYKSKPRTYRDLPIRFSEFGHVYRWEKKGELYGLLRVRGFVQDDGHIFLREDQLMEEIKMLISKTVEVWHKFGFKDDDIKPYLSTRPDESIGSDELWEKATNALISALQESGLKFGIKEKEGAFYGPKIDFEIRDSLGRWWQLSTIQVDFNLPERFKLEYIDKDGIKKRPVMVHRAIYGSIDRFVAILLEHFKGKLPTWLSSVQVRVLPITDEVNEYAEKVLNDMRKRRIRAEIDYAGETLSKRIKNAYDQGVPYILIVGKKEASEGTVTVRARGNIEVRNVKFEKFLELLITEIAQRDVEQTTVKALK

Protein

Threonine--tRNA ligase catalytic subunit: thrS-cat

Gene

thrS-cat

Protein

Threonine--tRNA ligase catalytic subunit

Organism

Sulfolobus islandicus (strain L.S.2.15 / Lassen #1)

Length

545 amino acids

Function

Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also activates L-serine and transfers it to tRNA(Thr) but cannot deacylate incorrectly charged amino acid; unlike most archaea the editing function is found in a freestanding protein.

Similarity

Belongs to the class-II aminoacyl-tRNA synthetase family.

Mass

63.245 kDa

Sequence

MESYKPVWLKGAVILAINLIDKGYKPVAVGLGERDFYIDVKSDTSITLDEVKKAINENVLANVSIENNQIVYKGNKVSIIEDKVSISTNLNPKYFEILNISTHHPNPNEQYVRIRGVAFETEEQLKDYLTWLEKAEETDHRLIGEKLDLFSFHEEAGSGLVLFHPKGQTIRNELIAFMREINDSMGYQEVYTSHVFKTDIWKISGHYTLYRDKLIVFNMEGDEYGVKPMNCPAHILIYKSKPRTYRDLPIRFSEFGHVYRWEKKGELYGLLRVRGFVQDDGHIFLREDQLREEIKMLISKTVEVWHKFGFKDDDIKPYLSTRPDESIGSDELWEKATNALISALQESGLKFGIKEKEGAFYGPKIDFEIRDSLGRWWQLSTIQVDFNLPERFKLEYIDKDGIKKRPVMVHRAIYGSIDRFVAILLEHFKGKLPTWLSSVQVRVLPITDEVNEYAEKVLNDMRKRRIRAEIDYAGETLSKRIKNAYDQGVPYILIVGKKEASEGTVTVRARGNIEVRNVKFEKFLELLITEIAQRDVEQTTVKALK

Protein

Threonine--tRNA ligase catalytic subunit: thrS-cat

Gene

thrS-cat

Protein

Threonine--tRNA ligase catalytic subunit

Organism

Sulfolobus islandicus (strain M.14.25 / Kamchatka #1)

Length

545 amino acids

Function

Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also activates L-serine and transfers it to tRNA(Thr) but cannot deacylate incorrectly charged amino acid; unlike most archaea the editing function is found in a freestanding protein.

Similarity

Belongs to the class-II aminoacyl-tRNA synthetase family.

Mass

63.241 kDa

Sequence

Protein

Threonine--tRNA ligase catalytic subunit: thrS-cat

Gene

thrS-cat

Protein

Threonine--tRNA ligase catalytic subunit

Organism

Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2)

Length

545 amino acids

Function

Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also activates L-serine and transfers it to tRNA(Thr) but cannot deacylate incorrectly charged amino acid; unlike most archaea the editing function is found in a freestanding protein.

Similarity

Belongs to the class-II aminoacyl-tRNA synthetase family.

Mass

63.231 kDa

Sequence

Protein

Threonine--tRNA ligase catalytic subunit: thrS-cat

Gene

thrS-cat

Protein

Threonine--tRNA ligase catalytic subunit

Organism

Sulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1)

Length

545 amino acids

Function

Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also activates L-serine and transfers it to tRNA(Thr) but cannot deacylate incorrectly charged amino acid; unlike most archaea the editing function is found in a freestanding protein.

Similarity

Belongs to the class-II aminoacyl-tRNA synthetase family.

Mass

63.231 kDa

Sequence

Protein

Threonine--tRNA ligase catalytic subunit: thrS-cat

Gene

thrS-cat

Protein

Threonine--tRNA ligase catalytic subunit

Organism

Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)

Length

541 amino acids

Function

Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also activates L-serine and transfers it to tRNA(Thr) but cannot deacylate incorrectly charged amino acid; unlike most archaea the editing function is found in a freestanding protein.

Similarity

Belongs to the class-II aminoacyl-tRNA synthetase family.

Mass

62.755 kDa

Sequence

MESYRGLWLKGAIVMALNMYEAGLTPVEIGLGERDFYIDVQSDSALSLQESEKFAQWKDHKYEIKDGKVTYNGKQILLQGDVTPSGEPRYFKVLNISVHHPSANVQLVRIRGIAFETKEQMDDYLQWLEKASETDHRIIGERMDLFSFHEESGPGLVLFHPKGQLIRNEMINYMREINASMGYQEVYTSHVFRTVLWKISGHYDTYRDKMLIFQKDDDELGIKPMNCPAHILIYKSRVRSYRDLPIRFSEFGNVYRWEKKGELYGLLRTRGFTQDDGHIFLREDQLKDEVKNLVRKTLDVLGKFGFKGEDVRINLSTRPDESIGSDEQWEKATKALLDVLKELNVPYVVKEKEGAFYGPKIDFDIRDSLNRWWQLSTIQVDFNLPERFKLEYVDEDGSKKRPVMVHRAIYGSLDRMIAILLEHFRGKLPTWLSPVQVRVLPISEDNLDYAKRVMDVLVQRGIRTEIDPSGETLSKRIKRGYDDGVPYLVIVGRKEASEEKVTIRARGNVEIKGVPLSRFVDELSLEIGNRDAENTLIKRIG

Protein

Threonine--tRNA ligase catalytic subunit: thrS-cat

Gene

thrS-cat

Protein

Threonine--tRNA ligase catalytic subunit

Organism

Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)

Length

540 amino acids

Function

Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also activates L-serine and transfers it to tRNA(Thr) but cannot deacylate incorrectly charged amino acid; unlike most archaea the editing function is found in a freestanding protein.

Similarity

Belongs to the class-II aminoacyl-tRNA synthetase family.

Mass

63.111 kDa

Sequence

MEEYKGVWLKAGIIYALNLASNGFKPVEVGLGERDFYVDVESDTTLTLDEAKKFATYNQYSYQLKDGYIEFNGNKIKVLGEPSSLEPKYFEILNISVHHPSPNVQYVRIRGVGFEKKEELDQYLKWLEEVSEYDHRIIGERLDLFSFPDETAPGLALFHYKGQIIRKELMKFMEEINESMGYQEVFTAEIYRSILWKTSGHYDYYKDKMVLFKMEDEELGLKPMNCPAHILIYKSKTRSYKDLPIRFSEFGLVFRWEKRGELYGLLRVRGFVQDDGHIFLTEDQIKDEVKMLVKKTIDVLSIFGFKGDDVRINLSTRPDESIGSDELWEKATNALVSALNELGIKYIVKEKEGAFYGPKIDFDIRDSLGRWWQLSTIQVDFNLPERFKLEYIDKDGSRKRPVMIHRAIYGSIERFMAILLEHFRGKLPTWLSPVQVRILPISKDVEDYALNLLSKLKENKIRVELDMSDETLSKRIKKAYDEGVPYMIIVGKKEREEGKVTVRGRNNVEIRGVKFDDFLKALLEEIRNRDLNQSAINKLK

Protein

Threonine--tRNA ligase catalytic subunit: thrS-cat

Gene

thrS-cat

Protein

Threonine--tRNA ligase catalytic subunit

Organism

Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)

Length

471 amino acids

Function

Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr) (Probable). This protein is probably not able to deacylate mischarged L-seryl-tRNA(Thr) as it lacks the appropriate domain (PubMed:19761773).

Similarity

Belongs to the class-II aminoacyl-tRNA synthetase family.

Mass

53.122 kDa

Sequence

MASGQDKTHIDYAYELDITVKPDSRVPVFNREFATFTGAGVPLFSLGGGPIRYALAEVLAKFHARRGYYVVETPIIASTELFKVSGHIEFYRNNMYLFDIEGHEFAVKPMNCPYHILLFLNEVAKHRSKLPLPFKVFEFGRVHRYEPSGSIYGLLRVRGFTQDDAHIIVPGGRVIDVVYDVFEEMKLVLERLFKLGVSSETFKVRLSMSDKSLIGKEFMGSKEEWEGAEEALREAASRINEKYGIDIVELEGEAAFYGPKLDFIMMVEESGVSKEWQMGTIQFDFNLPRRFRLYDVVREEFGIEEVYIIHRALLGSIERFLGVYLEHRRGRMPFTLAPIQFAVIAVKTGGEVDREIEDLASSIAKGLLDKGFRVAVKGSSKTGLSSDVRHIESTAKPAVNVFIGAKEVREKVLDVRVFDLESMKRRRLAIAYGDAADAVENLAAVAEELESPVRSLSGQAPRIPADFSFML

Protein

Threonine--tRNA ligase catalytic subunit: thrS-cat