class I SAM-dependent DNA methyltransferase catalyzes methylation of specific DNA residues to protect the DNA from cleavage by endonuclease using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor
MmeI, DNA-methyltransferase domain; Type IIL Restriction-Modification Enzyme MmeI is a large ...
325-604
5.62e-170
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: 493.91 E-value: 5.62e-170
BREX-1 system adenine-specific DNA-methyltransferase PglX; This protein, PglX, is a ...
345-407
6.74e-06
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: 50.31 E-value: 6.74e-06
MmeI, DNA-methyltransferase domain; Type IIL Restriction-Modification Enzyme MmeI is a large ...
325-604
5.62e-170
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: 493.91 E-value: 5.62e-170
MmeI, target recognition domain; Type IIL Restriction-Modification Enzyme MmeI is a large ...
621-824
1.44e-112
MmeI, target recognition 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 TRD. It consists of two alpha/beta subdomains.
Pssm-ID: 466615 Cd Length: 206 Bit Score: 343.29 E-value: 1.44e-112
MmeI, helicase spacer domain; Type IIL Restriction-Modification Enzyme MmeI is a large enzyme ...
170-324
8.26e-77
MmeI, helicase spacer 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 endonuclease cuts the two DNA strands at one site simultaneously with enzyme bound at two sites interacting to accomplish the cleavage. This domain corresponds to the multi-helical spacer. It is thought to play a key role in positioning the endonuclease cleavage domain correctly.
Pssm-ID: 466614 Cd Length: 153 Bit Score: 246.62 E-value: 8.26e-77
MmeI, N-terminal domain; Type IIL Restriction-Modification Enzyme MmeI is a large enzyme that ...
1-159
1.82e-28
MmeI, N-terminal 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). This domain corresponds to the N-terminal endonuclease, it cuts the two DNA strands at one site simultaneously with enzyme bound at two sites interacting to accomplish the cleavage.
Pssm-ID: 466613 Cd Length: 138 Bit Score: 111.30 E-value: 1.82e-28
MmeI, C-terminal domain; Type IIL Restriction-Modification Enzyme MmeI is a large enzyme that ...
826-903
4.36e-18
MmeI, C-terminal 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 C-terminal region.
Pssm-ID: 466616 Cd Length: 83 Bit Score: 79.45 E-value: 4.36e-18
BREX-1 system adenine-specific DNA-methyltransferase PglX; This protein, PglX, is a ...
345-407
6.74e-06
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: 50.31 E-value: 6.74e-06
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.
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(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
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