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Conserved domains on  [gi|30315948|sp|Q9FQY8|]
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RecName: Full=Caffeic acid 3-O-methyltransferase; Short=CAOMT; Short=COMT; AltName: Full=S-adenosysl-L-methionine:caffeic acid 3-O-methyltransferase

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 ...
 136-340 3.35e-101

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: 297.39  E-value: 3.35e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30315948   136 WYHLTDAVLDGGVPFNKAYGMTAFEYHGTDPRFNKVFNRGMSDHSTMTMKKILEDYKgFEGLNSIVDVGGGTGATVNMIV 215
Cdd:pfam00891   1 WRYLADAVREGRNQYNKAFGISLFEAIYRDEEERLLFNRGLQEHWSLIGKDVLTAFD-LSGFRSLVDVGGGTGALAQAIV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30315948   216 SKYPSIKGINFDLSHVIEDAPAY------PGVEHVGRDMF-VSVPKADAIFMKWICHDWSDEHCLKFLKNCYEALPANGK 288
Cdd:pfam00891  80 SLYPGCKGIVFDLPHVVEAAPTHfsageePRVTFHGGDFFkDSLPEADAYILKRVLHDWSDEKCVKLLKRCYKACPAGGK 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 30315948   289 VLVAECILPETPDTSAATKNavhVDIVMLAHnPGGKERTEKEFEALAKGAGF 340
Cdd:pfam00891 160 VILVESLLGADPSGPLHTQL---YSLNMLAQ-TEGRERTEAEYSELLTGAGF 207
dimerization pfam08100
dimerization domain; This domain is found at the N-terminus of a variety of plant ...
 30-81 1.36e-21

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: 86.48  E-value: 1.36e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 30315948    30 MVLKSALELDLLEIMAKAGpgAAISPSELAAQLPTKNPEAPVMLDRMLRLLA 81
Cdd:pfam08100   1 MVLKCAIELGIPDIIAKHG--KPLSPSELASKLPTKNPEAPVMLDRLLRLLA 50
 
Name Accession Description Interval E-value
Methyltransf_2 pfam00891
O-methyltransferase domain; This family includes a range of O-methyltransferases. These ...
 136-340 3.35e-101

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: 297.39  E-value: 3.35e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30315948   136 WYHLTDAVLDGGVPFNKAYGMTAFEYHGTDPRFNKVFNRGMSDHSTMTMKKILEDYKgFEGLNSIVDVGGGTGATVNMIV 215
Cdd:pfam00891   1 WRYLADAVREGRNQYNKAFGISLFEAIYRDEEERLLFNRGLQEHWSLIGKDVLTAFD-LSGFRSLVDVGGGTGALAQAIV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30315948   216 SKYPSIKGINFDLSHVIEDAPAY------PGVEHVGRDMF-VSVPKADAIFMKWICHDWSDEHCLKFLKNCYEALPANGK 288
Cdd:pfam00891  80 SLYPGCKGIVFDLPHVVEAAPTHfsageePRVTFHGGDFFkDSLPEADAYILKRVLHDWSDEKCVKLLKRCYKACPAGGK 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 30315948   289 VLVAECILPETPDTSAATKNavhVDIVMLAHnPGGKERTEKEFEALAKGAGF 340
Cdd:pfam00891 160 VILVESLLGADPSGPLHTQL---YSLNMLAQ-TEGRERTEAEYSELLTGAGF 207
dimerization pfam08100
dimerization domain; This domain is found at the N-terminus of a variety of plant ...
 30-81 1.36e-21

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: 86.48  E-value: 1.36e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 30315948    30 MVLKSALELDLLEIMAKAGpgAAISPSELAAQLPTKNPEAPVMLDRMLRLLA 81
Cdd:pfam08100   1 MVLKCAIELGIPDIIAKHG--KPLSPSELASKLPTKNPEAPVMLDRLLRLLA 50
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
199-293 1.46e-05

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 43.27  E-value: 1.46e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30315948 199 SIVDVGGGTGATVNMIVSKYPSIKGINFDLSHV-IEDAPA-YPGVEHVGRDM--FVSVPKADAIFMKWICHdWSDEHcLK 274
Cdd:COG4106   4 RVLDLGCGTGRLTALLAERFPGARVTGVDLSPEmLARARArLPNVRFVVADLrdLDPPEPFDLVVSNAALH-WLPDH-AA 81

                        90
                ....*....|....*....
gi 30315948 275 FLKNCYEALPANGKVLVAE 293
Cdd:COG4106  82 LLARLAAALAPGGVLAVQV 100
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 200-291 2.75e-04

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: 39.72  E-value: 2.75e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30315948 200 IVDVGGGTGATVNMIVSkYPSIKGINFDLSHV-------IEDAPAYPGVEHVGRDM----FVSVPKADAIFMKWICHdWS 268
Cdd:cd02440   2 VLDLGCGTGALALALAS-GPGARVTGVDISPValelarkAAAALLADNVEVLKGDAeelpPEADESFDVIISDPPLH-HL 79

                        90       100
                ....*....|....*....|...
gi 30315948 269 DEHCLKFLKNCYEALPANGKVLV 291
Cdd:cd02440  80 VEDLARFLEEARRLLKPGGVLVL 102
 
Name Accession Description Interval E-value
Methyltransf_2 pfam00891
O-methyltransferase domain; This family includes a range of O-methyltransferases. These ...
 136-340 3.35e-101

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: 297.39  E-value: 3.35e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30315948   136 WYHLTDAVLDGGVPFNKAYGMTAFEYHGTDPRFNKVFNRGMSDHSTMTMKKILEDYKgFEGLNSIVDVGGGTGATVNMIV 215
Cdd:pfam00891   1 WRYLADAVREGRNQYNKAFGISLFEAIYRDEEERLLFNRGLQEHWSLIGKDVLTAFD-LSGFRSLVDVGGGTGALAQAIV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30315948   216 SKYPSIKGINFDLSHVIEDAPAY------PGVEHVGRDMF-VSVPKADAIFMKWICHDWSDEHCLKFLKNCYEALPANGK 288
Cdd:pfam00891  80 SLYPGCKGIVFDLPHVVEAAPTHfsageePRVTFHGGDFFkDSLPEADAYILKRVLHDWSDEKCVKLLKRCYKACPAGGK 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 30315948   289 VLVAECILPETPDTSAATKNavhVDIVMLAHnPGGKERTEKEFEALAKGAGF 340
Cdd:pfam00891 160 VILVESLLGADPSGPLHTQL---YSLNMLAQ-TEGRERTEAEYSELLTGAGF 207
dimerization pfam08100
dimerization domain; This domain is found at the N-terminus of a variety of plant ...
 30-81 1.36e-21

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: 86.48  E-value: 1.36e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 30315948    30 MVLKSALELDLLEIMAKAGpgAAISPSELAAQLPTKNPEAPVMLDRMLRLLA 81
Cdd:pfam08100   1 MVLKCAIELGIPDIIAKHG--KPLSPSELASKLPTKNPEAPVMLDRLLRLLA 50
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
199-293 1.46e-05

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 43.27  E-value: 1.46e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30315948 199 SIVDVGGGTGATVNMIVSKYPSIKGINFDLSHV-IEDAPA-YPGVEHVGRDM--FVSVPKADAIFMKWICHdWSDEHcLK 274
Cdd:COG4106   4 RVLDLGCGTGRLTALLAERFPGARVTGVDLSPEmLARARArLPNVRFVVADLrdLDPPEPFDLVVSNAALH-WLPDH-AA 81

                        90
                ....*....|....*....
gi 30315948 275 FLKNCYEALPANGKVLVAE 293
Cdd:COG4106  82 LLARLAAALAPGGVLAVQV 100
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 200-291 2.75e-04

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: 39.72  E-value: 2.75e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30315948 200 IVDVGGGTGATVNMIVSkYPSIKGINFDLSHV-------IEDAPAYPGVEHVGRDM----FVSVPKADAIFMKWICHdWS 268
Cdd:cd02440   2 VLDLGCGTGALALALAS-GPGARVTGVDISPValelarkAAAALLADNVEVLKGDAeelpPEADESFDVIISDPPLH-HL 79

                        90       100
                ....*....|....*....|...
gi 30315948 269 DEHCLKFLKNCYEALPANGKVLV 291
Cdd:cd02440  80 VEDLARFLEEARRLLKPGGVLVL 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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