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Conserved domains on  [gi|392921819|ref|NP_001256582|]
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Methyltransferase FkbM domain-containing protein [Caenorhabditis elegans]

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; ...
 147-275 4.38e-07

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 pfam05050:

Pssm-ID: 473071  Cd Length: 170  Bit Score: 49.10  E-value: 4.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921819  147 QRKMGKLGKTVEFYGADPMTEVNEHLYPQIGK--YFPFAVAKNPGYATASVLI--NRQYFNQSVIHVDmmYFVERLlKLK 222
Cdd:pfam05050  33 PNKLEKLDCTLLNLALGNDVGLYEFYLGGKGGggYLLFAVGDPQGASTSSVLGgeEAKYIEVETVTLD--SFLEEI-KKS 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392921819  223 TIDNLWMDSEGAEYDLFEifekdgsFDRNGIELCQVNL---EVHLSETGPNNLHYE 275
Cdd:pfam05050 110 DIDLLKIDVEGAELEVLE-------GAEKTLKRCQPNIiviEVHFFHYFGGPLFDE 158
 
Name Accession Description Interval E-value
Methyltransf_21 pfam05050
Methyltransferase FkbM domain; This family has members from bacteria to human, and appears to ...
 147-275 4.38e-07

Methyltransferase FkbM domain; This family has members from bacteria to human, and appears to be a methyltransferase.


Pssm-ID: 428282  Cd Length: 170  Bit Score: 49.10  E-value: 4.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921819  147 QRKMGKLGKTVEFYGADPMTEVNEHLYPQIGK--YFPFAVAKNPGYATASVLI--NRQYFNQSVIHVDmmYFVERLlKLK 222
Cdd:pfam05050  33 PNKLEKLDCTLLNLALGNDVGLYEFYLGGKGGggYLLFAVGDPQGASTSSVLGgeEAKYIEVETVTLD--SFLEEI-KKS 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392921819  223 TIDNLWMDSEGAEYDLFEifekdgsFDRNGIELCQVNL---EVHLSETGPNNLHYE 275
Cdd:pfam05050 110 DIDLLKIDVEGAELEVLE-------GAEKTLKRCQPNIiviEVHFFHYFGGPLFDE 158
 
Name Accession Description Interval E-value
Methyltransf_21 pfam05050
Methyltransferase FkbM domain; This family has members from bacteria to human, and appears to ...
 147-275 4.38e-07

Methyltransferase FkbM domain; This family has members from bacteria to human, and appears to be a methyltransferase.


Pssm-ID: 428282  Cd Length: 170  Bit Score: 49.10  E-value: 4.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921819  147 QRKMGKLGKTVEFYGADPMTEVNEHLYPQIGK--YFPFAVAKNPGYATASVLI--NRQYFNQSVIHVDmmYFVERLlKLK 222
Cdd:pfam05050  33 PNKLEKLDCTLLNLALGNDVGLYEFYLGGKGGggYLLFAVGDPQGASTSSVLGgeEAKYIEVETVTLD--SFLEEI-KKS 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392921819  223 TIDNLWMDSEGAEYDLFEifekdgsFDRNGIELCQVNL---EVHLSETGPNNLHYE 275
Cdd:pfam05050 110 DIDLLKIDVEGAELEVLE-------GAEKTLKRCQPNIiviEVHFFHYFGGPLFDE 158
 
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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