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Conserved domains on  [gi|1240085863|ref|NP_001341979|]
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leucine carboxyl methyltransferase 1 isoform 2 [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; ...
 10-59 1.47e-10

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 pfam04072:

Pssm-ID: 473071  Cd Length: 188  Bit Score: 57.24  E-value: 1.47e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1240085863  10 IGADLRDlSELEEKLKKCNMNTQLPTLLITECVLVYMTPEQSANLLKWAA 59
Cdd:pfam04072 140 VPVDLRD-DDWPEALRAAGFDPEQPTAWLAEGLLYYLPPEAQDALLDTIA 188
 
Name Accession Description Interval E-value
LCM pfam04072
Leucine carboxyl methyltransferase; Family of leucine carboxyl methyltransferases EC:2.1.1.-. ...
 10-59 1.47e-10

Leucine carboxyl methyltransferase; Family of leucine carboxyl methyltransferases EC:2.1.1.-. This family may need divides a the full alignment contains a significantly shorter mouse sequence.


Pssm-ID: 427692  Cd Length: 188  Bit Score: 57.24  E-value: 1.47e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1240085863  10 IGADLRDlSELEEKLKKCNMNTQLPTLLITECVLVYMTPEQSANLLKWAA 59
Cdd:pfam04072 140 VPVDLRD-DDWPEALRAAGFDPEQPTAWLAEGLLYYLPPEAQDALLDTIA 188
YktD COG3315
O-Methyltransferase involved in polyketide biosynthesis [Secondary metabolites biosynthesis, ...
 4-62 5.22e-04

O-Methyltransferase involved in polyketide biosynthesis [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442544  Cd Length: 246  Bit Score: 39.17  E-value: 5.22e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1240085863   4 SKRYAIIGADLRDLSeLEEKLKKCNMNTQLPTLLITECVLVYMTPEQSANLLKWAASSF 62
Cdd:COG3315   104 PARLRLVAVDLRDPD-WPDALPAAGFDPSRPTLFIAEGVLMYLTEEAVRALLRRIAALF 161
 
Name Accession Description Interval E-value
LCM pfam04072
Leucine carboxyl methyltransferase; Family of leucine carboxyl methyltransferases EC:2.1.1.-. ...
 10-59 1.47e-10

Leucine carboxyl methyltransferase; Family of leucine carboxyl methyltransferases EC:2.1.1.-. This family may need divides a the full alignment contains a significantly shorter mouse sequence.


Pssm-ID: 427692  Cd Length: 188  Bit Score: 57.24  E-value: 1.47e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1240085863  10 IGADLRDlSELEEKLKKCNMNTQLPTLLITECVLVYMTPEQSANLLKWAA 59
Cdd:pfam04072 140 VPVDLRD-DDWPEALRAAGFDPEQPTAWLAEGLLYYLPPEAQDALLDTIA 188
YktD COG3315
O-Methyltransferase involved in polyketide biosynthesis [Secondary metabolites biosynthesis, ...
 4-62 5.22e-04

O-Methyltransferase involved in polyketide biosynthesis [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442544  Cd Length: 246  Bit Score: 39.17  E-value: 5.22e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1240085863   4 SKRYAIIGADLRDLSeLEEKLKKCNMNTQLPTLLITECVLVYMTPEQSANLLKWAASSF 62
Cdd:COG3315   104 PARLRLVAVDLRDPD-WPDALPAAGFDPSRPTLFIAEGVLMYLTEEAVRALLRRIAALF 161
 
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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