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Conserved domains on  [gi|568975369|ref|XP_006534064|]
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RNA N6-adenosine-methyltransferase METTL16 isoform X3 [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; ...
1-73 1.04e-37

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 pfam05971:

Pssm-ID: 473071 [Multi-domain]  Cd Length: 291  Bit Score: 136.11  E-value: 1.04e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568975369    1 MAEGGELEFVKRIIHDSLQLKKRLRWYSCMLGKKCSLAPLKEELRIQGVPKVTFTEFCQGRTMRWALAWSFYD 73
Cdd:pfam05971 219 WCEGGEAAFIKKMIEESLQFAKQVRWFTTLVSKGCNLPPLKEELRILGAPKVTVTEMAQGQKQSRFIAWSFYD 291
 
Name Accession Description Interval E-value
Methyltransf_10 pfam05971
RNA methyltransferase; This family includes ribosomal RNA large subunit methyltransferase F, ...
1-73 1.04e-37

RNA methyltransferase; This family includes ribosomal RNA large subunit methyltransferase F, and related proteins, including methyltransferase-like protein 16 (METTL16). METTL16 is a conserved RNA methyltransferase which interacts specifically with the MALAT1 triple helix. METTL16 shows nuclear localization. Another functional study indicates that METTL16 regulates expression of human MAT2A, which encodes the SAM synthetase expressed in most cells. Furthermore, results indicate that METTL16 is the long-unknown methyltransferase for the U6 spliceosomal small nuclear RNA (snRNA) and it has evolved an additional function in vertebrates to control SAM homeostasis by post-transcriptionally regulating SAM synthetase gene expression.


Pssm-ID: 399160 [Multi-domain]  Cd Length: 291  Bit Score: 136.11  E-value: 1.04e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568975369    1 MAEGGELEFVKRIIHDSLQLKKRLRWYSCMLGKKCSLAPLKEELRIQGVPKVTFTEFCQGRTMRWALAWSFYD 73
Cdd:pfam05971 219 WCEGGEAAFIKKMIEESLQFAKQVRWFTTLVSKGCNLPPLKEELRILGAPKVTVTEMAQGQKQSRFIAWSFYD 291
PRK11727 PRK11727
23S rRNA (adenine(1618)-N(6))-methyltransferase RlmF;
3-74 1.31e-08

23S rRNA (adenine(1618)-N(6))-methyltransferase RlmF;


Pssm-ID: 236964  Cd Length: 321  Bit Score: 55.26  E-value: 1.31e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568975369   3 EGGELEFVKRIIHDSLQLKKRLRWYSCMLGKKCSLAPLKEELRIQGVPKVTFTEFCQGRTMRWALAWSFYDD 74
Cdd:PRK11727 239 EGGEVAFIKRMIEESKAFAKQVLWFTSLVSKKENLPPLYRALKKVGAVEVKTIEMAQGQKQSRFIAWTFLDD 310
 
Name Accession Description Interval E-value
Methyltransf_10 pfam05971
RNA methyltransferase; This family includes ribosomal RNA large subunit methyltransferase F, ...
1-73 1.04e-37

RNA methyltransferase; This family includes ribosomal RNA large subunit methyltransferase F, and related proteins, including methyltransferase-like protein 16 (METTL16). METTL16 is a conserved RNA methyltransferase which interacts specifically with the MALAT1 triple helix. METTL16 shows nuclear localization. Another functional study indicates that METTL16 regulates expression of human MAT2A, which encodes the SAM synthetase expressed in most cells. Furthermore, results indicate that METTL16 is the long-unknown methyltransferase for the U6 spliceosomal small nuclear RNA (snRNA) and it has evolved an additional function in vertebrates to control SAM homeostasis by post-transcriptionally regulating SAM synthetase gene expression.


Pssm-ID: 399160 [Multi-domain]  Cd Length: 291  Bit Score: 136.11  E-value: 1.04e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568975369    1 MAEGGELEFVKRIIHDSLQLKKRLRWYSCMLGKKCSLAPLKEELRIQGVPKVTFTEFCQGRTMRWALAWSFYD 73
Cdd:pfam05971 219 WCEGGEAAFIKKMIEESLQFAKQVRWFTTLVSKGCNLPPLKEELRILGAPKVTVTEMAQGQKQSRFIAWSFYD 291
PRK11727 PRK11727
23S rRNA (adenine(1618)-N(6))-methyltransferase RlmF;
3-74 1.31e-08

23S rRNA (adenine(1618)-N(6))-methyltransferase RlmF;


Pssm-ID: 236964  Cd Length: 321  Bit Score: 55.26  E-value: 1.31e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568975369   3 EGGELEFVKRIIHDSLQLKKRLRWYSCMLGKKCSLAPLKEELRIQGVPKVTFTEFCQGRTMRWALAWSFYDD 74
Cdd:PRK11727 239 EGGEVAFIKRMIEESKAFAKQVLWFTSLVSKKENLPPLYRALKKVGAVEVKTIEMAQGQKQSRFIAWTFLDD 310
 
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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