23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and ...
9-197
1.48e-62
23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and biogenesis]; 23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ is part of the Pathway/BioSystem: 23S rRNA modification
The actual alignment was detected with superfamily member COG0293:
Pssm-ID: 440062 [Multi-domain] Cd Length: 208 Bit Score: 207.62 E-value: 1.48e-62
Spb1 C-terminal domain; This presumed domain is found at the C-terminus of a family of ...
618-716
6.32e-38
Spb1 C-terminal domain; This presumed domain is found at the C-terminus of a family of FtsJ-like methyltransferases. Members of this family are involved in 60S ribosomal biogenesis, for example Swiss:P25582.
The actual alignment was detected with superfamily member pfam07780:
Pssm-ID: 462264 Cd Length: 209 Bit Score: 140.44 E-value: 6.32e-38
Domain of unknown function (DUF3381); This domain is functionally uncharacterized. This domain ...
237-363
2.87e-33
Domain of unknown function (DUF3381); This domain is functionally uncharacterized. This domain is found in eukaryotes. This presumed domain is typically between 156 to 174 amino acids in length. This domain is found associated with pfam07780, pfam01728.
:
Pssm-ID: 463375 [Multi-domain] Cd Length: 150 Bit Score: 124.97 E-value: 2.87e-33
23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and ...
9-197
1.48e-62
23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and biogenesis]; 23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ is part of the Pathway/BioSystem: 23S rRNA modification
Pssm-ID: 440062 [Multi-domain] Cd Length: 208 Bit Score: 207.62 E-value: 1.48e-62
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
24-197
1.42e-59
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping.
Pssm-ID: 426399 Cd Length: 179 Bit Score: 198.58 E-value: 1.42e-59
cell division protein FtsJ; Methylates the 23S rRNA. Previously known as cell division protein ...
13-196
4.44e-47
cell division protein FtsJ; Methylates the 23S rRNA. Previously known as cell division protein ftsJ.// Trusted cutoff too high? [SS 10/1/04] [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 273078 Cd Length: 188 Bit Score: 164.99 E-value: 4.44e-47
Spb1 C-terminal domain; This presumed domain is found at the C-terminus of a family of ...
618-716
6.32e-38
Spb1 C-terminal domain; This presumed domain is found at the C-terminus of a family of FtsJ-like methyltransferases. Members of this family are involved in 60S ribosomal biogenesis, for example Swiss:P25582.
Pssm-ID: 462264 Cd Length: 209 Bit Score: 140.44 E-value: 6.32e-38
Domain of unknown function (DUF3381); This domain is functionally uncharacterized. This domain ...
237-363
2.87e-33
Domain of unknown function (DUF3381); This domain is functionally uncharacterized. This domain is found in eukaryotes. This presumed domain is typically between 156 to 174 amino acids in length. This domain is found associated with pfam07780, pfam01728.
Pssm-ID: 463375 [Multi-domain] Cd Length: 150 Bit Score: 124.97 E-value: 2.87e-33
viral Cap-0 specific (nucleoside-2'-O-)-methyltransferase; Cap-0 specific (nucleoside-2'-O-) ...
31-196
2.50e-07
viral Cap-0 specific (nucleoside-2'-O-)-methyltransferase; Cap-0 specific (nucleoside-2'-O-)-methyltransferase (2'OMTase) catalyzes the methylation of Cap-0 (m7GpppNp) at the 2'-hydroxyl of the ribose of the first nucleotide, using S-adenosyl-L-methionine (AdoMet) as the methyl donor. This reaction is the fourth and last step in mRNA capping, the creation of the stabilizing five-prime cap (5' cap) on mRNA. Some dsDNA and dsRNA viruses, like the bluetongue virus (BTV), a member of the Reoviridae family, and Vaccinia virus, a member of the Poxviridae family, as well as some ss(+)RNA viruses, like Flaviviridae and Nidovirales, cap their mRNAs and encode their own 2'OMTase. In BTV, all four reactions are catalyzed by a single protein, VP4. In Vaccinia, the activity is located in the processing factor of the poly(A) polymerase, VP39.
Pssm-ID: 467730 Cd Length: 179 Bit Score: 51.29 E-value: 2.50e-07
23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and ...
9-197
1.48e-62
23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and biogenesis]; 23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ is part of the Pathway/BioSystem: 23S rRNA modification
Pssm-ID: 440062 [Multi-domain] Cd Length: 208 Bit Score: 207.62 E-value: 1.48e-62
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
24-197
1.42e-59
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping.
Pssm-ID: 426399 Cd Length: 179 Bit Score: 198.58 E-value: 1.42e-59
cell division protein FtsJ; Methylates the 23S rRNA. Previously known as cell division protein ...
13-196
4.44e-47
cell division protein FtsJ; Methylates the 23S rRNA. Previously known as cell division protein ftsJ.// Trusted cutoff too high? [SS 10/1/04] [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 273078 Cd Length: 188 Bit Score: 164.99 E-value: 4.44e-47
Spb1 C-terminal domain; This presumed domain is found at the C-terminus of a family of ...
618-716
6.32e-38
Spb1 C-terminal domain; This presumed domain is found at the C-terminus of a family of FtsJ-like methyltransferases. Members of this family are involved in 60S ribosomal biogenesis, for example Swiss:P25582.
Pssm-ID: 462264 Cd Length: 209 Bit Score: 140.44 E-value: 6.32e-38
Domain of unknown function (DUF3381); This domain is functionally uncharacterized. This domain ...
237-363
2.87e-33
Domain of unknown function (DUF3381); This domain is functionally uncharacterized. This domain is found in eukaryotes. This presumed domain is typically between 156 to 174 amino acids in length. This domain is found associated with pfam07780, pfam01728.
Pssm-ID: 463375 [Multi-domain] Cd Length: 150 Bit Score: 124.97 E-value: 2.87e-33
viral Cap-0 specific (nucleoside-2'-O-)-methyltransferase; Cap-0 specific (nucleoside-2'-O-) ...
31-196
2.50e-07
viral Cap-0 specific (nucleoside-2'-O-)-methyltransferase; Cap-0 specific (nucleoside-2'-O-)-methyltransferase (2'OMTase) catalyzes the methylation of Cap-0 (m7GpppNp) at the 2'-hydroxyl of the ribose of the first nucleotide, using S-adenosyl-L-methionine (AdoMet) as the methyl donor. This reaction is the fourth and last step in mRNA capping, the creation of the stabilizing five-prime cap (5' cap) on mRNA. Some dsDNA and dsRNA viruses, like the bluetongue virus (BTV), a member of the Reoviridae family, and Vaccinia virus, a member of the Poxviridae family, as well as some ss(+)RNA viruses, like Flaviviridae and Nidovirales, cap their mRNAs and encode their own 2'OMTase. In BTV, all four reactions are catalyzed by a single protein, VP4. In Vaccinia, the activity is located in the processing factor of the poly(A) polymerase, VP39.
Pssm-ID: 467730 Cd Length: 179 Bit Score: 51.29 E-value: 2.50e-07
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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The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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