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Conserved domains on  [gi|901694064|ref|NP_001297991|]
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nicotinamide N-methyltransferase isoform 2 [Mus musculus]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 106779)

class I SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AdoMet_MTases super family cl17173
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
2-137 2.52e-74

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


The actual alignment was detected with superfamily member pfam01234:

Pssm-ID: 473071  Cd Length: 261  Bit Score: 222.68  E-value: 2.52e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694064    2 ESGFTSKDTYLSHFNPRDYLEKYYSFGSRHCAENEILRHLLKNLFKIFCLGAVKGELLIDIGSGPTIYQLLSACESFTEI 81
Cdd:pfam01234   3 GEGFLAGEEYKKKFNPRAYLNTYYKFASGDAAEMQIVLFFLPNLLQTFGPGGVKGDTLIDIGSGPTIYQLLSACEVFKEI 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 901694064   82 IVSDYTDQNLWELQKWLKKEPGAFDWSPVVTYVCDLEGNRMKGPEKEEKLRRAIKQ 137
Cdd:pfam01234  83 HLSDYLPQNRDELIKWLKKEPGAFDWSPVLKHICELEGDRECWQEKEEKLRALVKR 138
 
Name Accession Description Interval E-value
NNMT_PNMT_TEMT pfam01234
NNMT/PNMT/TEMT family;
2-137 2.52e-74

NNMT/PNMT/TEMT family;


Pssm-ID: 395988  Cd Length: 261  Bit Score: 222.68  E-value: 2.52e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694064    2 ESGFTSKDTYLSHFNPRDYLEKYYSFGSRHCAENEILRHLLKNLFKIFCLGAVKGELLIDIGSGPTIYQLLSACESFTEI 81
Cdd:pfam01234   3 GEGFLAGEEYKKKFNPRAYLNTYYKFASGDAAEMQIVLFFLPNLLQTFGPGGVKGDTLIDIGSGPTIYQLLSACEVFKEI 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 901694064   82 IVSDYTDQNLWELQKWLKKEPGAFDWSPVVTYVCDLEGNRMKGPEKEEKLRRAIKQ 137
Cdd:pfam01234  83 HLSDYLPQNRDELIKWLKKEPGAFDWSPVLKHICELEGDRECWQEKEEKLRALVKR 138
GntF_guanitoxin NF041360
guanitoxin biosynthesis pre-guanitoxin forming N-methyltransferase GntF;
1-118 1.84e-13

guanitoxin biosynthesis pre-guanitoxin forming N-methyltransferase GntF;


Pssm-ID: 469252  Cd Length: 273  Bit Score: 65.81  E-value: 1.84e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694064   1 MESGFTSKDtyLSHFNPRDYLEKYYS-FGSRHCA----ENEILRHLLKNLFKIFCLgavKGELLIDIGSGPTIYQLLSAC 75
Cdd:NF041360   1 MELKFKEND--FQSFEAIPYLNEYFNnYPSDKYGgigfENEKFLQFFAEVAHEHHL---NNSLLLDFGCGPTIYSIISLG 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 901694064  76 ESFTEIIVSDYTDQNLWELQKWLKKEPGAFDWSPVVTYVCDLE 118
Cdd:NF041360  76 QNCREIHMSDYLQQNLEQVKLWQQGKPEAFDWNPYLRRALQIE 118
 
Name Accession Description Interval E-value
NNMT_PNMT_TEMT pfam01234
NNMT/PNMT/TEMT family;
2-137 2.52e-74

NNMT/PNMT/TEMT family;


Pssm-ID: 395988  Cd Length: 261  Bit Score: 222.68  E-value: 2.52e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694064    2 ESGFTSKDTYLSHFNPRDYLEKYYSFGSRHCAENEILRHLLKNLFKIFCLGAVKGELLIDIGSGPTIYQLLSACESFTEI 81
Cdd:pfam01234   3 GEGFLAGEEYKKKFNPRAYLNTYYKFASGDAAEMQIVLFFLPNLLQTFGPGGVKGDTLIDIGSGPTIYQLLSACEVFKEI 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 901694064   82 IVSDYTDQNLWELQKWLKKEPGAFDWSPVVTYVCDLEGNRMKGPEKEEKLRRAIKQ 137
Cdd:pfam01234  83 HLSDYLPQNRDELIKWLKKEPGAFDWSPVLKHICELEGDRECWQEKEEKLRALVKR 138
GntF_guanitoxin NF041360
guanitoxin biosynthesis pre-guanitoxin forming N-methyltransferase GntF;
1-118 1.84e-13

guanitoxin biosynthesis pre-guanitoxin forming N-methyltransferase GntF;


Pssm-ID: 469252  Cd Length: 273  Bit Score: 65.81  E-value: 1.84e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694064   1 MESGFTSKDtyLSHFNPRDYLEKYYS-FGSRHCA----ENEILRHLLKNLFKIFCLgavKGELLIDIGSGPTIYQLLSAC 75
Cdd:NF041360   1 MELKFKEND--FQSFEAIPYLNEYFNnYPSDKYGgigfENEKFLQFFAEVAHEHHL---NNSLLLDFGCGPTIYSIISLG 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 901694064  76 ESFTEIIVSDYTDQNLWELQKWLKKEPGAFDWSPVVTYVCDLE 118
Cdd:NF041360  76 QNCREIHMSDYLQQNLEQVKLWQQGKPEAFDWNPYLRRALQIE 118
 
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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