tRNA(Met) cytidine acetyltransferase TmcA family protein may catalyze the formation of N(4)-acetylcytidine (ac4C) at the wobble position of tRNA(Met), by using acetyl-CoA as an acetyl donor and either ATP or GTP
tRNA(Met) C34 N-acetyltransferase TmcA [Translation, ribosomal structure and biogenesis]; tRNA(Met) C34 N-acetyltransferase TmcA is part of the Pathway/BioSystem: tRNA modification
The actual alignment was detected with superfamily member COG1444:
Pssm-ID: 441053 [Multi-domain] Cd Length: 703 Bit Score: 277.10 E-value: 1.36e-80
tRNA(Met) C34 N-acetyltransferase TmcA [Translation, ribosomal structure and biogenesis]; tRNA(Met) C34 N-acetyltransferase TmcA is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 441053 [Multi-domain] Cd Length: 703 Bit Score: 277.10 E-value: 1.36e-80
tRNA(Met) C34 N-acetyltransferase TmcA [Translation, ribosomal structure and biogenesis]; tRNA(Met) C34 N-acetyltransferase TmcA is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 441053 [Multi-domain] Cd Length: 703 Bit Score: 277.10 E-value: 1.36e-80
tRNA(Met) cytidine acetyltransferase TmcA, N-terminal; This domain of unknown function is ...
7-200
9.97e-59
tRNA(Met) cytidine acetyltransferase TmcA, N-terminal; This domain of unknown function is often found at the N-terminus of the bacterial tRNA(Met) cytidine acetyltransferase TmcA. TmcA catalyzes the formation of N(4)-acetylcytidine (ac4C) at the wobble position of tRNA(Met) by using acetyl-CoA as an acetyl donor and either ATP or GTP. This modification is thought to ensure precise recognition of the AUG codon by strengthening C-G base-pair interaction and also prevent misrecognition of the near cognate AUA codon. This domain is also found in mammalian N-acetyltransferase 10 (NAT10) and fungal protein Kre33. Kre33 and NAT10 are RNA cytosine acetyltransferases with specificity toward both 18S rRNA and tRNAs and contain additional putative nuclear and nucleolar localization signals (NLS and NoLS respectively).
Pssm-ID: 462441 [Multi-domain] Cd Length: 178 Bit Score: 199.05 E-value: 9.97e-59
Helicase; This domain contains a P-loop (Walker A) motif, suggesting that it has ATPase ...
280-476
6.54e-52
Helicase; This domain contains a P-loop (Walker A) motif, suggesting that it has ATPase activity, and a Walker B motif. In tRNA(Met) cytidine acetyltransferase (TmcA) it may function as an RNA helicase motor (driven by ATP hydrolysis) which delivers the wobble base to the active centre of the GCN5-related N-acetyltransferase (GNAT) domain. It is found in the bacterial exodeoxyribonuclease V alpha chain (RecD), which has 5'-3' helicase activity. It is structurally similar to the motor domain 1A in other SF1 helicases.
Pssm-ID: 461555 [Multi-domain] Cd Length: 171 Bit Score: 179.65 E-value: 6.54e-52
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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