L-threonylcarbamoyladenylate synthase catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosphate, and is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine
Carbamoyltransferase C-terminus; This domain is found in NodU from Rhizobium, CmcH from ...
5-184
2.58e-96
Carbamoyltransferase C-terminus; This domain is found in NodU from Rhizobium, CmcH from Nocardia lactamdurans and the bifunctional carbamoyltransferase TobZ from Streptoalloteichus tenebrarius. NodU a Rhizobium nodulation protein involved in the synthesis of nodulation factors has 6-O-carbamoyltransferase-like activity. CmcH is involved in cephamycin (antibiotic) biosynthesis and has 3-hydroxymethylcephem carbamoyltransferase activity, EC:2.1.3.7 catalysing the reaction: Carbamoyl phosphate + 3-hydroxymethylceph-3-EM-4-carboxylate <=> phosphate + 3-carbamoyloxymethylcephem. TobZ functions as an ATP carbamoyltransferase and tobramycin carbamoyltransferase. These proteins contain two domains, this is the smaller, C-terminal, domain.
The actual alignment was detected with superfamily member PRK10634:
Pssm-ID: 469714 Cd Length: 190 Bit Score: 277.38 E-value: 2.58e-96
tRNA A37 threonylcarbamoyladenosine synthetase subunit TsaC/SUA5/YrdC [Translation, ribosomal structure and biogenesis]; tRNA A37 threonylcarbamoyladenosine synthetase subunit TsaC/SUA5/YrdC is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 439780 [Multi-domain] Cd Length: 204 Bit Score: 229.98 E-value: 1.48e-77
Telomere recombination; This domain has been shown to bind preferentially to dsRNA. The domain ...
10-184
5.11e-53
Telomere recombination; This domain has been shown to bind preferentially to dsRNA. The domain is found in SUA5 as well as HypF and YrdC. It has also been shown to be required for telomere recombniation in yeast.
Pssm-ID: 460153 [Multi-domain] Cd Length: 176 Bit Score: 166.92 E-value: 5.11e-53
tRNA threonylcarbamoyl adenosine modification protein, Sua5/YciO/YrdC/YwlC family; Has ...
6-176
1.22e-40
tRNA threonylcarbamoyl adenosine modification protein, Sua5/YciO/YrdC/YwlC family; Has paralogs, but YrdC called a tRNA modification protein. Ref 2 authors say probably heteromultimeric complex. Paralogs may mean its does the final binding to the tRNA. [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 272879 [Multi-domain] Cd Length: 201 Bit Score: 136.30 E-value: 1.22e-40
tRNA A37 threonylcarbamoyladenosine synthetase subunit TsaC/SUA5/YrdC [Translation, ribosomal structure and biogenesis]; tRNA A37 threonylcarbamoyladenosine synthetase subunit TsaC/SUA5/YrdC is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 439780 [Multi-domain] Cd Length: 204 Bit Score: 229.98 E-value: 1.48e-77
Telomere recombination; This domain has been shown to bind preferentially to dsRNA. The domain ...
10-184
5.11e-53
Telomere recombination; This domain has been shown to bind preferentially to dsRNA. The domain is found in SUA5 as well as HypF and YrdC. It has also been shown to be required for telomere recombniation in yeast.
Pssm-ID: 460153 [Multi-domain] Cd Length: 176 Bit Score: 166.92 E-value: 5.11e-53
tRNA threonylcarbamoyl adenosine modification protein, Sua5/YciO/YrdC/YwlC family; Has ...
6-176
1.22e-40
tRNA threonylcarbamoyl adenosine modification protein, Sua5/YciO/YrdC/YwlC family; Has paralogs, but YrdC called a tRNA modification protein. Ref 2 authors say probably heteromultimeric complex. Paralogs may mean its does the final binding to the tRNA. [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 272879 [Multi-domain] Cd Length: 201 Bit Score: 136.30 E-value: 1.22e-40
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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