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 ...
6-1153
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.
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Pssm-ID: 468037 [Multi-domain] Cd Length: 1187 Bit Score: 1612.68 E-value: 0e+00
BREX-1 system adenine-specific DNA-methyltransferase PglX; This protein, PglX, is a ...
6-1153
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: 1612.68 E-value: 0e+00
MmeI, DNA-methyltransferase domain; Type IIL Restriction-Modification Enzyme MmeI is a large ...
287-354
1.02e-04
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: 45.54 E-value: 1.02e-04
BREX-1 system adenine-specific DNA-methyltransferase PglX; This protein, PglX, is a ...
6-1153
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: 1612.68 E-value: 0e+00
MmeI, DNA-methyltransferase domain; Type IIL Restriction-Modification Enzyme MmeI is a large ...
287-354
1.02e-04
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: 45.54 E-value: 1.02e-04
Eco57I restriction-modification methylase; homologs of the Escherichia coli Eco57I ...
465-566
3.07e-03
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: 38.44 E-value: 3.07e-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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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
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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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
(labeled illustration) Full Display shows all domain models, in each hit category below, that meet or exceed the RPS-BLAST threshold for statistical significance.
(labeled illustration) Four types of hits can be shown, as available,
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specific hits meet or exceed a domain-specific e-value threshold
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and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
non-specific hits
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the domain superfamily to which the specific and non-specific hits belong
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