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Conserved domains on  [gi|2217341879|ref|XP_047303412|]
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tRNA N(3)-methylcytidine methyltransferase METTL6 isoform X11 [Homo sapiens]

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; ...
76-133 4.95e-03

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 pfam08242:

Pssm-ID: 473071 [Multi-domain]  Cd Length: 98  Bit Score: 35.04  E-value: 4.95e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217341879  76 QNPLYDTERCKVFQCDLTKDDlldhvpPESVDVVMLIFVLSavHPDKMHLVLQNIYKC 133
Cdd:pfam08242  42 ALGLLNAVRVELFQLDLGELD------PGSFDVVVASNVLH--HLADPRAVLRNIRRL 91
 
Name Accession Description Interval E-value
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
76-133 4.95e-03

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 35.04  E-value: 4.95e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217341879  76 QNPLYDTERCKVFQCDLTKDDlldhvpPESVDVVMLIFVLSavHPDKMHLVLQNIYKC 133
Cdd:pfam08242  42 ALGLLNAVRVELFQLDLGELD------PGSFDVVVASNVLH--HLADPRAVLRNIRRL 91
 
Name Accession Description Interval E-value
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
76-133 4.95e-03

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 35.04  E-value: 4.95e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217341879  76 QNPLYDTERCKVFQCDLTKDDlldhvpPESVDVVMLIFVLSavHPDKMHLVLQNIYKC 133
Cdd:pfam08242  42 ALGLLNAVRVELFQLDLGELD------PGSFDVVVASNVLH--HLADPRAVLRNIRRL 91
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
84-133 8.63e-03

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 34.08  E-value: 8.63e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2217341879  84 RCKVFQCDLTKDDLLDhvppESVDVVMLIFVLSAVHPDKMHLVLQNIYKC 133
Cdd:pfam13649  46 NVEFVQGDAEDLPFPD----GSFDLVVSSGVLHHLPDPDLEAALREIARV 91
 
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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