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Conserved domains on  [gi|2205526725|ref|WP_240700785|]
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type I restriction-modification system subunit M N-terminal domain-containing protein, partial [Propionibacterium freudenreichii]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
hsdM super family cl33272
type I restriction system adenine methylase (hsdM); Function: methylation of specific adenine ...
6-106 6.24e-34

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]


The actual alignment was detected with superfamily member TIGR00497:

Pssm-ID: 211578 [Multi-domain]  Cd Length: 501  Bit Score: 121.98  E-value: 6.24e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205526725   6 ERAALHKAIWQVANDLRGSVDGWDFKAYVLGFLFYRFISENLTEYINRAEHaAGDADFDYRFLS--REDAEFAKAGIVEE 83
Cdd:TIGR00497   1 QRNELEKKIWEIANKLRGSVDGWDFKQYVLGGLFYRFISENLCKYINDSER-RNDPSFSYANLTddYEAIDALKDAAIAS 79
                          90       100
                  ....*....|....*....|...
gi 2205526725  84 KGFFILPEDLFANVRERAPRDEN 106
Cdd:TIGR00497  80 KGFFIKPSQLFQNVVKSIRENED 102
 
Name Accession Description Interval E-value
hsdM TIGR00497
type I restriction system adenine methylase (hsdM); Function: methylation of specific adenine ...
6-106 6.24e-34

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: 121.98  E-value: 6.24e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205526725   6 ERAALHKAIWQVANDLRGSVDGWDFKAYVLGFLFYRFISENLTEYINRAEHaAGDADFDYRFLS--REDAEFAKAGIVEE 83
Cdd:TIGR00497   1 QRNELEKKIWEIANKLRGSVDGWDFKQYVLGGLFYRFISENLCKYINDSER-RNDPSFSYANLTddYEAIDALKDAAIAS 79
                          90       100
                  ....*....|....*....|...
gi 2205526725  84 KGFFILPEDLFANVRERAPRDEN 106
Cdd:TIGR00497  80 KGFFIKPSQLFQNVVKSIRENED 102
HsdM_N pfam12161
HsdM N-terminal domain; This domain is found at the N-terminus of the methylase subunit of ...
10-93 4.62e-12

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: 57.69  E-value: 4.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205526725  10 LHKAIWQVANDLRGSVDGWDFKAYVLGFLFYRFISENLTEYINRAEHAAGDADFDYRFLSREDAEFAKagIVEEKGFFIL 89
Cdd:pfam12161   1 LESFLWNAADILRGDVDASEYKEYILPLLFLKRLDDVLEEREEEVLELIEPLDSGFGFYIPSELRWSK--LANNLDNDEL 78

                  ....
gi 2205526725  90 PEDL 93
Cdd:pfam12161  79 GENL 82
 
Name Accession Description Interval E-value
hsdM TIGR00497
type I restriction system adenine methylase (hsdM); Function: methylation of specific adenine ...
6-106 6.24e-34

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: 121.98  E-value: 6.24e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205526725   6 ERAALHKAIWQVANDLRGSVDGWDFKAYVLGFLFYRFISENLTEYINRAEHaAGDADFDYRFLS--REDAEFAKAGIVEE 83
Cdd:TIGR00497   1 QRNELEKKIWEIANKLRGSVDGWDFKQYVLGGLFYRFISENLCKYINDSER-RNDPSFSYANLTddYEAIDALKDAAIAS 79
                          90       100
                  ....*....|....*....|...
gi 2205526725  84 KGFFILPEDLFANVRERAPRDEN 106
Cdd:TIGR00497  80 KGFFIKPSQLFQNVVKSIRENED 102
HsdM_N pfam12161
HsdM N-terminal domain; This domain is found at the N-terminus of the methylase subunit of ...
10-93 4.62e-12

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: 57.69  E-value: 4.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205526725  10 LHKAIWQVANDLRGSVDGWDFKAYVLGFLFYRFISENLTEYINRAEHAAGDADFDYRFLSREDAEFAKagIVEEKGFFIL 89
Cdd:pfam12161   1 LESFLWNAADILRGDVDASEYKEYILPLLFLKRLDDVLEEREEEVLELIEPLDSGFGFYIPSELRWSK--LANNLDNDEL 78

                  ....
gi 2205526725  90 PEDL 93
Cdd:pfam12161  79 GENL 82
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options: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.
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