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Conserved domains on  [gi|15241038|ref|NP_195791|]
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methyltransferase [Arabidopsis thaliana]

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; ...
 314-472 1.27e-07

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 TIGR01444:

Pssm-ID: 473071  Cd Length: 143  Bit Score: 50.77  E-value: 1.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241038   314 VYVDVGArsygsSIGS---WFKKEYPKQnktfDVFAIEADKAFHEEYKIKKKVN------LLPYAAWVRNETLSFEInHD 384
Cdd:TIGR01444   1 VVIDVGA-----NIGDtslYFARKGAEG----RVIAFEPLPDAYEILEENVKLNnlpnvvLLNAAVGDRDGELEFNV-SD 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241038   385 PGKEVEAKAKGRGMGRIQP--VKKSDSSDLAGEVNLIQgfdfadwlkksvrerdFVVMKMDVEGTEFDLIPRLIKTGAIC 462
Cdd:TIGR01444  71 DDTGNSSLLPTPDADRESEieVEVVTLDDLVEEFGLDK----------------VDLLKIDVEGAELEVLRGAAETLLEK 134

                         170
                  ....*....|
gi 15241038   463 lIDELFLECH 472
Cdd:TIGR01444 135 -RPVIVLEVH 143
Methyltransf_11 super family cl48003
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 147-197 2.06e-05

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


The actual alignment was detected with superfamily member pfam08241:

Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 43.04  E-value: 2.06e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15241038   147 VVRGEGHAIPFEDNAFDFVFSGG-----DRLGKSLKqlefadEITRTLKPEGFAVV 197
Cdd:pfam08241  45 FVVGDAEDLPFPDNSFDLVLSSEvlhhvEDPERALR------EIARVLKPGGILII 94
 
Name Accession Description Interval E-value
fkbM_fam TIGR01444
methyltransferase, FkbM family; Members of this family are characterized by two well-conserved ...
 314-472 1.27e-07

methyltransferase, FkbM family; Members of this family are characterized by two well-conserved short regions separated by a variable in both sequence and length. The first of the two regions is found in a large number of proteins outside this subfamily, a number of which have been characterized as methyltransferases. One member of the present family, FkbM, was shown to be required for a specific methylation in the biosynthesis of the immunosuppressant FK506 in Streptomyces strain MA6548.


Pssm-ID: 273628  Cd Length: 143  Bit Score: 50.77  E-value: 1.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241038   314 VYVDVGArsygsSIGS---WFKKEYPKQnktfDVFAIEADKAFHEEYKIKKKVN------LLPYAAWVRNETLSFEInHD 384
Cdd:TIGR01444   1 VVIDVGA-----NIGDtslYFARKGAEG----RVIAFEPLPDAYEILEENVKLNnlpnvvLLNAAVGDRDGELEFNV-SD 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241038   385 PGKEVEAKAKGRGMGRIQP--VKKSDSSDLAGEVNLIQgfdfadwlkksvrerdFVVMKMDVEGTEFDLIPRLIKTGAIC 462
Cdd:TIGR01444  71 DDTGNSSLLPTPDADRESEieVEVVTLDDLVEEFGLDK----------------VDLLKIDVEGAELEVLRGAAETLLEK 134

                         170
                  ....*....|
gi 15241038   463 lIDELFLECH 472
Cdd:TIGR01444 135 -RPVIVLEVH 143
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 147-197 2.06e-05

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 43.04  E-value: 2.06e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15241038   147 VVRGEGHAIPFEDNAFDFVFSGG-----DRLGKSLKqlefadEITRTLKPEGFAVV 197
Cdd:pfam08241  45 FVVGDAEDLPFPDNSFDLVLSSEvlhhvEDPERALR------EIARVLKPGGILII 94
Methyltransf_21 pfam05050
Methyltransferase FkbM domain; This family has members from bacteria to human, and appears to ...
 317-479 6.44e-05

Methyltransferase FkbM domain; This family has members from bacteria to human, and appears to be a methyltransferase.


Pssm-ID: 428282  Cd Length: 170  Bit Score: 43.71  E-value: 6.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241038   317 DVGARsygssIGSWF---KKEYPKQNKTFDVFAIEADKAFHEEYKIkkkvNLLPYAawvrnetlsfeINHDPGkEVEAKA 393
Cdd:pfam05050   1 DVGAN-----DGVWDsvaLLFEKKCGGGGEVLAIEPNPNKLEKLDC----TLLNLA-----------LGNDVG-LYEFYL 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241038   394 KGRGMGRIQPVKKSDSSDlAGEVNLIQGFDF----------ADWLKKsVRERDFVVMKMDVEGTEFDLIPRLIKTGAICL 463
Cdd:pfam05050  60 GGKGGGGYLLFAVGDPQG-ASTSSVLGGEEAkyievetvtlDSFLEE-IKKSDIDLLKIDVEGAELEVLEGAEKTLKRCQ 137

                         170
                  ....*....|....*.
gi 15241038   464 IDELFLECHYNRWQRC 479
Cdd:pfam05050 138 PNIIVIEVHFFHYFGG 153
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 147-211 1.68e-04

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 41.90  E-value: 1.68e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15241038 147 VVRGEGHAIPFEDNAFDFVFSGG-----DRLGKSLKqlefadEITRTLKPEG-FAVVHVGATDTYSFNSFL 211
Cdd:COG2226  73 FVVGDAEDLPFPDGSFDLVISSFvlhhlPDPERALA------EIARVLKPGGrLVVVDFSPPDLAELEELL 137
 
Name Accession Description Interval E-value
fkbM_fam TIGR01444
methyltransferase, FkbM family; Members of this family are characterized by two well-conserved ...
 314-472 1.27e-07

methyltransferase, FkbM family; Members of this family are characterized by two well-conserved short regions separated by a variable in both sequence and length. The first of the two regions is found in a large number of proteins outside this subfamily, a number of which have been characterized as methyltransferases. One member of the present family, FkbM, was shown to be required for a specific methylation in the biosynthesis of the immunosuppressant FK506 in Streptomyces strain MA6548.


Pssm-ID: 273628  Cd Length: 143  Bit Score: 50.77  E-value: 1.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241038   314 VYVDVGArsygsSIGS---WFKKEYPKQnktfDVFAIEADKAFHEEYKIKKKVN------LLPYAAWVRNETLSFEInHD 384
Cdd:TIGR01444   1 VVIDVGA-----NIGDtslYFARKGAEG----RVIAFEPLPDAYEILEENVKLNnlpnvvLLNAAVGDRDGELEFNV-SD 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241038   385 PGKEVEAKAKGRGMGRIQP--VKKSDSSDLAGEVNLIQgfdfadwlkksvrerdFVVMKMDVEGTEFDLIPRLIKTGAIC 462
Cdd:TIGR01444  71 DDTGNSSLLPTPDADRESEieVEVVTLDDLVEEFGLDK----------------VDLLKIDVEGAELEVLRGAAETLLEK 134

                         170
                  ....*....|
gi 15241038   463 lIDELFLECH 472
Cdd:TIGR01444 135 -RPVIVLEVH 143
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 147-197 2.06e-05

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 43.04  E-value: 2.06e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15241038   147 VVRGEGHAIPFEDNAFDFVFSGG-----DRLGKSLKqlefadEITRTLKPEGFAVV 197
Cdd:pfam08241  45 FVVGDAEDLPFPDNSFDLVLSSEvlhhvEDPERALR------EIARVLKPGGILII 94
Methyltransf_21 pfam05050
Methyltransferase FkbM domain; This family has members from bacteria to human, and appears to ...
 317-479 6.44e-05

Methyltransferase FkbM domain; This family has members from bacteria to human, and appears to be a methyltransferase.


Pssm-ID: 428282  Cd Length: 170  Bit Score: 43.71  E-value: 6.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241038   317 DVGARsygssIGSWF---KKEYPKQNKTFDVFAIEADKAFHEEYKIkkkvNLLPYAawvrnetlsfeINHDPGkEVEAKA 393
Cdd:pfam05050   1 DVGAN-----DGVWDsvaLLFEKKCGGGGEVLAIEPNPNKLEKLDC----TLLNLA-----------LGNDVG-LYEFYL 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241038   394 KGRGMGRIQPVKKSDSSDlAGEVNLIQGFDF----------ADWLKKsVRERDFVVMKMDVEGTEFDLIPRLIKTGAICL 463
Cdd:pfam05050  60 GGKGGGGYLLFAVGDPQG-ASTSSVLGGEEAkyievetvtlDSFLEE-IKKSDIDLLKIDVEGAELEVLEGAEKTLKRCQ 137

                         170
                  ....*....|....*.
gi 15241038   464 IDELFLECHYNRWQRC 479
Cdd:pfam05050 138 PNIIVIEVHFFHYFGG 153
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 147-211 1.68e-04

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 41.90  E-value: 1.68e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15241038 147 VVRGEGHAIPFEDNAFDFVFSGG-----DRLGKSLKqlefadEITRTLKPEG-FAVVHVGATDTYSFNSFL 211
Cdd:COG2226  73 FVVGDAEDLPFPDGSFDLVISSFvlhhlPDPERALA------EIARVLKPGGrLVVVDFSPPDLAELEELL 137
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 147-193 8.87e-03

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 35.62  E-value: 8.87e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15241038   147 VVRGEGHAIPFEDNAFDFVFSGG-------DRLGKSLKqlefadEITRTLKPEG 193
Cdd:pfam13649  49 FVQGDAEDLPFPDGSFDLVVSSGvlhhlpdPDLEAALR------EIARVLKPGG 96
 
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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