class I SAM-dependent DNA methyltransferase catalyzes the methylation of a specific DNA substrate using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor similar to type I restriction-modification system modification (M) subunit (HsdM), which together with specificity (S) subunit (HsdS), forms a methyltransferase that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence
HsdM N-terminal domain; This domain is found at the N-terminus of the methylase subunit of ...
3-133
6.24e-04
HsdM N-terminal domain; This domain is found at the N-terminus of the methylase subunit of Type I DNA methyltransferases. This domain family is found in bacteria and archaea, and is typically between 123 and 138 amino acids in length. The family is found in association with pfam02384. Mutations in this region of EcoKI methyltransferase abolish the normally strong preference of this system for methylating hemimethylated substrate. The structure of this domain has been shown to be all alpha-helical.
The actual alignment was detected with superfamily member pfam12161:
Pssm-ID: 463478 Cd Length: 123 Bit Score: 39.59 E-value: 6.24e-04
N-6 DNA Methylase; Restriction-modification (R-M) systems protect a bacterial cell against ...
143-441
3.53e-69
N-6 DNA Methylase; Restriction-modification (R-M) systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The R-M system is a complex containing three polypeptides: M (this family), S (pfam01420), and R. This family consists of N-6 adenine-specific DNA methylase EC:2.1.1.72 from Type I and Type IC restriction systems. These methylases have the same sequence specificity as their corresponding restriction enzymes.
Pssm-ID: 426749 [Multi-domain] Cd Length: 310 Bit Score: 223.35 E-value: 3.53e-69
type I restriction system adenine methylase (hsdM); Function: methylation of specific adenine ...
147-440
3.46e-20
type I restriction system adenine methylase (hsdM); Function: methylation of specific adenine residues; required for both restriction and modification activities. The ECOR124/3 I enzyme recognizes 5'GAA(N7)RTCG. for E.coli see (J. Mol. Biol. 257: 960-969 (1996)). [DNA metabolism, Restriction/modification]
Pssm-ID: 211578 [Multi-domain] Cd Length: 501 Bit Score: 93.09 E-value: 3.46e-20
HsdM N-terminal domain; This domain is found at the N-terminus of the methylase subunit of ...
3-133
6.24e-04
HsdM N-terminal domain; This domain is found at the N-terminus of the methylase subunit of Type I DNA methyltransferases. This domain family is found in bacteria and archaea, and is typically between 123 and 138 amino acids in length. The family is found in association with pfam02384. Mutations in this region of EcoKI methyltransferase abolish the normally strong preference of this system for methylating hemimethylated substrate. The structure of this domain has been shown to be all alpha-helical.
Pssm-ID: 463478 Cd Length: 123 Bit Score: 39.59 E-value: 6.24e-04
N-6 DNA Methylase; Restriction-modification (R-M) systems protect a bacterial cell against ...
143-441
3.53e-69
N-6 DNA Methylase; Restriction-modification (R-M) systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The R-M system is a complex containing three polypeptides: M (this family), S (pfam01420), and R. This family consists of N-6 adenine-specific DNA methylase EC:2.1.1.72 from Type I and Type IC restriction systems. These methylases have the same sequence specificity as their corresponding restriction enzymes.
Pssm-ID: 426749 [Multi-domain] Cd Length: 310 Bit Score: 223.35 E-value: 3.53e-69
type I restriction system adenine methylase (hsdM); Function: methylation of specific adenine ...
147-440
3.46e-20
type I restriction system adenine methylase (hsdM); Function: methylation of specific adenine residues; required for both restriction and modification activities. The ECOR124/3 I enzyme recognizes 5'GAA(N7)RTCG. for E.coli see (J. Mol. Biol. 257: 960-969 (1996)). [DNA metabolism, Restriction/modification]
Pssm-ID: 211578 [Multi-domain] Cd Length: 501 Bit Score: 93.09 E-value: 3.46e-20
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 443299 [Multi-domain] Cd Length: 238 Bit Score: 48.22 E-value: 3.28e-06
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
177-288
2.10e-05
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure and biogenesis]; tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 441866 [Multi-domain] Cd Length: 377 Bit Score: 46.71 E-value: 2.10e-05
type II restriction m6 adenine DNA methyltransferase, Alw26I/Eco31I/Esp3I family; Members of ...
165-349
5.34e-04
type II restriction m6 adenine DNA methyltransferase, Alw26I/Eco31I/Esp3I family; Members of this family are the m6-adenine DNA methyltransferase protein, or domain of a fusion protein that also carries m5 cytosine methyltransferase activity, of type II restriction systems of the Alw26I/Eco31I/Esp3I family. A methyltransferase of this family is alway accompanied by a type II restriction endonuclease from the Alw26I/Eco31I/Esp3I family (TIGR02986) and by an adenine-specific modification methyltransferase. Members of this family are unusual in that regions of similarity to homologs outside this family are circularly permuted. [DNA metabolism, Restriction/modification]
Pssm-ID: 274377 [Multi-domain] Cd Length: 524 Bit Score: 42.45 E-value: 5.34e-04
HsdM N-terminal domain; This domain is found at the N-terminus of the methylase subunit of ...
3-133
6.24e-04
HsdM N-terminal domain; This domain is found at the N-terminus of the methylase subunit of Type I DNA methyltransferases. This domain family is found in bacteria and archaea, and is typically between 123 and 138 amino acids in length. The family is found in association with pfam02384. Mutations in this region of EcoKI methyltransferase abolish the normally strong preference of this system for methylating hemimethylated substrate. The structure of this domain has been shown to be all alpha-helical.
Pssm-ID: 463478 Cd Length: 123 Bit Score: 39.59 E-value: 6.24e-04
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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