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Conserved domains on  [gi|38047397|gb|AAR09601|]
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flavonoid 3'-O-methyltransferase [Mentha x piperita]

Protein Classification

COMT family class I SAM-dependent methyltransferase( domain architecture ID 10547674)

COMT family 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 caffeic acid 3-O-methyltransferase (COMT) that catalyzes the conversion of caffeic acid to ferulic acid and of 5-hydroxyferulic acid to sinapic acid

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Methyltransf_2 pfam00891
O-methyltransferase domain; This family includes a range of O-methyltransferases. These ...
 141-345 1.68e-86

O-methyltransferase domain; This family includes a range of O-methyltransferases. These enzymes utilize S-adenosyl methionine.


:

Pssm-ID: 395719 [Multi-domain]  Cd Length: 208  Bit Score: 260.03  E-value: 1.68e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38047397   141 WYHLKDVIVEGGVAFERAYGVHAFEYHAKDPKFNKIFNQAMHNQSIIFMKRILEIYKgFEGVKSLVDVGGGTGASSKMIV 220
Cdd:pfam00891   1 WRYLADAVREGRNQYNKAFGISLFEAIYRDEEERLLFNRGLQEHWSLIGKDVLTAFD-LSGFRSLVDVGGGTGALAQAIV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38047397   221 SKYPLIKAINFDLPHVIQDASPH------PEVEHVGGDMF-VSVPKADAIFLKWICHDWSDEHCRKLLKNCYDAILGNGK 293
Cdd:pfam00891  80 SLYPGCKGIVFDLPHVVEAAPTHfsageePRVTFHGGDFFkDSLPEADAYILKRVLHDWSDEKCVKLLKRCYKACPAGGK 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 38047397   294 VIIAESTLPEDPNsgpDTIHAIRGDVIMLtVNPGGKERTEKEFRTLALQAGF 345
Cdd:pfam00891 160 VILVESLLGADPS---GPLHTQLYSLNML-AQTEGRERTEAEYSELLTGAGF 207
dimerization pfam08100
dimerization domain; This domain is found at the N-terminus of a variety of plant ...
 37-88 1.95e-08

dimerization domain; This domain is found at the N-terminus of a variety of plant O-methyltransferases. It has been shown to mediate dimerization of these proteins.


:

Pssm-ID: 400439  Cd Length: 50  Bit Score: 49.88  E-value: 1.95e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 38047397    37 MVIKSAIDLNLLELIKRGGeEGASAYELAAQINAENPKAAAeMIDRILQLLA 88
Cdd:pfam08100   1 MVLKCAIELGIPDIIAKHG-KPLSPSELASKLPTKNPEAPV-MLDRLLRLLA 50
 
Name Accession Description Interval E-value
Methyltransf_2 pfam00891
O-methyltransferase domain; This family includes a range of O-methyltransferases. These ...
 141-345 1.68e-86

O-methyltransferase domain; This family includes a range of O-methyltransferases. These enzymes utilize S-adenosyl methionine.


Pssm-ID: 395719 [Multi-domain]  Cd Length: 208  Bit Score: 260.03  E-value: 1.68e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38047397   141 WYHLKDVIVEGGVAFERAYGVHAFEYHAKDPKFNKIFNQAMHNQSIIFMKRILEIYKgFEGVKSLVDVGGGTGASSKMIV 220
Cdd:pfam00891   1 WRYLADAVREGRNQYNKAFGISLFEAIYRDEEERLLFNRGLQEHWSLIGKDVLTAFD-LSGFRSLVDVGGGTGALAQAIV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38047397   221 SKYPLIKAINFDLPHVIQDASPH------PEVEHVGGDMF-VSVPKADAIFLKWICHDWSDEHCRKLLKNCYDAILGNGK 293
Cdd:pfam00891  80 SLYPGCKGIVFDLPHVVEAAPTHfsageePRVTFHGGDFFkDSLPEADAYILKRVLHDWSDEKCVKLLKRCYKACPAGGK 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 38047397   294 VIIAESTLPEDPNsgpDTIHAIRGDVIMLtVNPGGKERTEKEFRTLALQAGF 345
Cdd:pfam00891 160 VILVESLLGADPS---GPLHTQLYSLNML-AQTEGRERTEAEYSELLTGAGF 207
dimerization pfam08100
dimerization domain; This domain is found at the N-terminus of a variety of plant ...
 37-88 1.95e-08

dimerization domain; This domain is found at the N-terminus of a variety of plant O-methyltransferases. It has been shown to mediate dimerization of these proteins.


Pssm-ID: 400439  Cd Length: 50  Bit Score: 49.88  E-value: 1.95e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 38047397    37 MVIKSAIDLNLLELIKRGGeEGASAYELAAQINAENPKAAAeMIDRILQLLA 88
Cdd:pfam08100   1 MVLKCAIELGIPDIIAKHG-KPLSPSELASKLPTKNPEAPV-MLDRLLRLLA 50
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
204-298 6.98e-03

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 35.57  E-value: 6.98e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38047397 204 SLVDVGGGTGASSKMIVSKYPLIKAINFDL-PHVIQDASPH-PEVEHVGGDM--FVSVPKADAIFLKWICHdWSDEHcRK 279
Cdd:COG4106   4 RVLDLGCGTGRLTALLAERFPGARVTGVDLsPEMLARARARlPNVRFVVADLrdLDPPEPFDLVVSNAALH-WLPDH-AA 81

                        90
                ....*....|....*....
gi 38047397 280 LLKNCYDAILGNGKVIIAE 298
Cdd:COG4106  82 LLARLAAALAPGGVLAVQV 100
 
Name Accession Description Interval E-value
Methyltransf_2 pfam00891
O-methyltransferase domain; This family includes a range of O-methyltransferases. These ...
 141-345 1.68e-86

O-methyltransferase domain; This family includes a range of O-methyltransferases. These enzymes utilize S-adenosyl methionine.


Pssm-ID: 395719 [Multi-domain]  Cd Length: 208  Bit Score: 260.03  E-value: 1.68e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38047397   141 WYHLKDVIVEGGVAFERAYGVHAFEYHAKDPKFNKIFNQAMHNQSIIFMKRILEIYKgFEGVKSLVDVGGGTGASSKMIV 220
Cdd:pfam00891   1 WRYLADAVREGRNQYNKAFGISLFEAIYRDEEERLLFNRGLQEHWSLIGKDVLTAFD-LSGFRSLVDVGGGTGALAQAIV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38047397   221 SKYPLIKAINFDLPHVIQDASPH------PEVEHVGGDMF-VSVPKADAIFLKWICHDWSDEHCRKLLKNCYDAILGNGK 293
Cdd:pfam00891  80 SLYPGCKGIVFDLPHVVEAAPTHfsageePRVTFHGGDFFkDSLPEADAYILKRVLHDWSDEKCVKLLKRCYKACPAGGK 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 38047397   294 VIIAESTLPEDPNsgpDTIHAIRGDVIMLtVNPGGKERTEKEFRTLALQAGF 345
Cdd:pfam00891 160 VILVESLLGADPS---GPLHTQLYSLNML-AQTEGRERTEAEYSELLTGAGF 207
dimerization pfam08100
dimerization domain; This domain is found at the N-terminus of a variety of plant ...
 37-88 1.95e-08

dimerization domain; This domain is found at the N-terminus of a variety of plant O-methyltransferases. It has been shown to mediate dimerization of these proteins.


Pssm-ID: 400439  Cd Length: 50  Bit Score: 49.88  E-value: 1.95e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 38047397    37 MVIKSAIDLNLLELIKRGGeEGASAYELAAQINAENPKAAAeMIDRILQLLA 88
Cdd:pfam08100   1 MVLKCAIELGIPDIIAKHG-KPLSPSELASKLPTKNPEAPV-MLDRLLRLLA 50
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
204-298 6.98e-03

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 35.57  E-value: 6.98e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38047397 204 SLVDVGGGTGASSKMIVSKYPLIKAINFDL-PHVIQDASPH-PEVEHVGGDM--FVSVPKADAIFLKWICHdWSDEHcRK 279
Cdd:COG4106   4 RVLDLGCGTGRLTALLAERFPGARVTGVDLsPEMLARARARlPNVRFVVADLrdLDPPEPFDLVVSNAALH-WLPDH-AA 81

                        90
                ....*....|....*....
gi 38047397 280 LLKNCYDAILGNGKVIIAE 298
Cdd:COG4106  82 LLARLAAALAPGGVLAVQV 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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