BREX-1 system adenine-specific DNA-methyltransferase PglX is a site-specific DNA methyltransferase associated with BREX (bacteriophage exclusion) type 1 systems
BREX-1 system adenine-specific DNA-methyltransferase PglX; This protein, PglX, is a ...
6-1155
0e+00
BREX-1 system adenine-specific DNA-methyltransferase PglX; This protein, PglX, is a site-specific DNA methyltransferase associated BREX (bacteriophage exclusion) type 1 systems. The phage resistance appears not to be through restriction-modification, as phage DNA appears not to get degraded, but it does manage to inhibit phage replication.
The actual alignment was detected with superfamily member NF033452:
Pssm-ID: 468037 [Multi-domain] Cd Length: 1187 Bit Score: 1622.69 E-value: 0e+00
BREX-1 system adenine-specific DNA-methyltransferase PglX; This protein, PglX, is a ...
6-1155
0e+00
BREX-1 system adenine-specific DNA-methyltransferase PglX; This protein, PglX, is a site-specific DNA methyltransferase associated BREX (bacteriophage exclusion) type 1 systems. The phage resistance appears not to be through restriction-modification, as phage DNA appears not to get degraded, but it does manage to inhibit phage replication.
Pssm-ID: 468037 [Multi-domain] Cd Length: 1187 Bit Score: 1622.69 E-value: 0e+00
MmeI, DNA-methyltransferase domain; Type IIL Restriction-Modification Enzyme MmeI is a large ...
287-368
3.47e-10
MmeI, DNA-methyltransferase domain; Type IIL Restriction-Modification Enzyme MmeI is a large enzyme that integrates DNA recognition and methyltransferase and endonuclease activities within the same polypeptide. MmeI is composed of five domains. An N-terminal endonuclease domain (residues 1-155), connects to a DNA-methyltransferase domain (MTase, residues 301-320) via a multi-helical spacer (residues 156-300). These are followed by the target recognition domain (TRD, residues 621-825), and a final C-terminal helical bundle (residues 826-919). The DNA is embedded between the TRD and the MTase domain. The TRD makes contacts to the DNA bases primarily in the major groove, while the MTase domain makes several contacts to the DNA in the minor groove. This domain corresponds to the DNA-methyltransferase. Structurally, it consists of a twisted beta-sheet flanked by alpha-helices on both sides.
Pssm-ID: 466622 [Multi-domain] Cd Length: 258 Bit Score: 62.10 E-value: 3.47e-10
BREX-1 system adenine-specific DNA-methyltransferase PglX; This protein, PglX, is a ...
6-1155
0e+00
BREX-1 system adenine-specific DNA-methyltransferase PglX; This protein, PglX, is a site-specific DNA methyltransferase associated BREX (bacteriophage exclusion) type 1 systems. The phage resistance appears not to be through restriction-modification, as phage DNA appears not to get degraded, but it does manage to inhibit phage replication.
Pssm-ID: 468037 [Multi-domain] Cd Length: 1187 Bit Score: 1622.69 E-value: 0e+00
MmeI, DNA-methyltransferase domain; Type IIL Restriction-Modification Enzyme MmeI is a large ...
287-368
3.47e-10
MmeI, DNA-methyltransferase domain; Type IIL Restriction-Modification Enzyme MmeI is a large enzyme that integrates DNA recognition and methyltransferase and endonuclease activities within the same polypeptide. MmeI is composed of five domains. An N-terminal endonuclease domain (residues 1-155), connects to a DNA-methyltransferase domain (MTase, residues 301-320) via a multi-helical spacer (residues 156-300). These are followed by the target recognition domain (TRD, residues 621-825), and a final C-terminal helical bundle (residues 826-919). The DNA is embedded between the TRD and the MTase domain. The TRD makes contacts to the DNA bases primarily in the major groove, while the MTase domain makes several contacts to the DNA in the minor groove. This domain corresponds to the DNA-methyltransferase. Structurally, it consists of a twisted beta-sheet flanked by alpha-helices on both sides.
Pssm-ID: 466622 [Multi-domain] Cd Length: 258 Bit Score: 62.10 E-value: 3.47e-10
Eco57I restriction-modification methylase; homologs of the Escherichia coli Eco57I ...
481-571
5.58e-04
Eco57I restriction-modification methylase; homologs of the Escherichia coli Eco57I restriction-modification methylase are found in several phylogenetically diverse bacteria. The structure of TaqI has been solved.
Pssm-ID: 369456 [Multi-domain] Cd Length: 104 Bit Score: 40.36 E-value: 5.58e-04
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440663 [Multi-domain] Cd Length: 172 Bit Score: 39.16 E-value: 5.33e-03
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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