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Conserved domains on  [gi|6753944|ref|NP_034385|]
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guanidinoacetate N-methyltransferase isoform 1 [Mus musculus]

Protein Classification

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

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

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:1904047|GO:0008168
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; ...
 63-166 5.87e-13

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: 63.22  E-value: 5.87e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753944   63 RVLEVGFGMAIAASRVQQAPIEEHWIIECNDGVFQRLQD-WALRQPHKVVPLKGLWEEvAPTLPDGHFDGILYDtypLSE 141
Cdd:cd02440   1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKaAAALLADNVEVLKGDAEE-LPPEADESFDVIISD---PPL 76

                        90       100
                ....*....|....*....|....*
gi 6753944  142 EAWHTHQFNFIKNhAFRLLKTGGVL 166
Cdd:cd02440  77 HHLVEDLARFLEE-ARRLLKPGGVL 100
 
Name Accession Description Interval E-value
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 63-166 5.87e-13

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: 63.22  E-value: 5.87e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753944   63 RVLEVGFGMAIAASRVQQAPIEEHWIIECNDGVFQRLQD-WALRQPHKVVPLKGLWEEvAPTLPDGHFDGILYDtypLSE 141
Cdd:cd02440   1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKaAAALLADNVEVLKGDAEE-LPPEADESFDVIISD---PPL 76

                        90       100
                ....*....|....*....|....*
gi 6753944  142 EAWHTHQFNFIKNhAFRLLKTGGVL 166
Cdd:cd02440  77 HHLVEDLARFLEE-ARRLLKPGGVL 100
 
Name Accession Description Interval E-value
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 63-166 5.87e-13

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: 63.22  E-value: 5.87e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753944   63 RVLEVGFGMAIAASRVQQAPIEEHWIIECNDGVFQRLQD-WALRQPHKVVPLKGLWEEvAPTLPDGHFDGILYDtypLSE 141
Cdd:cd02440   1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKaAAALLADNVEVLKGDAEE-LPPEADESFDVIISD---PPL 76

                        90       100
                ....*....|....*....|....*
gi 6753944  142 EAWHTHQFNFIKNhAFRLLKTGGVL 166
Cdd:cd02440  77 HHLVEDLARFLEE-ARRLLKPGGVL 100
 
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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