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Conserved domains on  [gi|446198385|ref|WP_000276240|]
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MULTISPECIES: class I SAM-dependent methyltransferase [Salmonella]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10116212)

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; similar to Homo sapiens guanidinoacetate N-methyltransferase and Saccharomyces cerevisiae protein arginine N-methyltransferase 2

CATH:  3.40.50.150
EC:  2.1.1.-
Gene Ontology:  GO:1904047|GO:0008168|GO:0032259|GO:0008757
PubMed:  12504684|12826405
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 107-194 2.66e-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.).


:

Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 37.79  E-value: 2.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446198385 107 PENIWAFESDAKIYNEAVISALSSKFPFIKLIKANVGDFFEVSPQKFDLIYLDFCGPlPSKKAGQKTLKAItsilkYHAL 186
Cdd:cd02440   21 GARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEADESFDVIISDPPLH-HLVEDLARFLEEA-----RRLL 94


                 ....*...
gi 446198385 187 SPLGVMIT 194
Cdd:cd02440   95 KPGGVLVL 102
 
Name Accession Description Interval E-value
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 107-194 2.66e-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.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 37.79  E-value: 2.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446198385 107 PENIWAFESDAKIYNEAVISALSSKFPFIKLIKANVGDFFEVSPQKFDLIYLDFCGPlPSKKAGQKTLKAItsilkYHAL 186
Cdd:cd02440   21 GARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEADESFDVIISDPPLH-HLVEDLARFLEEA-----RRLL 94


                 ....*...
gi 446198385 187 SPLGVMIT 194
Cdd:cd02440   95 KPGGVLVL 102
 
Name Accession Description Interval E-value
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 107-194 2.66e-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.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 37.79  E-value: 2.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446198385 107 PENIWAFESDAKIYNEAVISALSSKFPFIKLIKANVGDFFEVSPQKFDLIYLDFCGPlPSKKAGQKTLKAItsilkYHAL 186
Cdd:cd02440   21 GARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEADESFDVIISDPPLH-HLVEDLARFLEEA-----RRLL 94


                 ....*...
gi 446198385 187 SPLGVMIT 194
Cdd:cd02440   95 KPGGVLVL 102
 
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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