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Conserved domains on  [gi|33641716|gb|AAQ24343|]
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O-methyltransferase, partial [Zea mays]

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 ...
 141-346 7.73e-99

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: 291.23  E-value: 7.73e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33641716   141 WYYLKDAVLDGGIPFNKAYGMTAFEYHGTDSRFNRVFNEGMKNHSVIITKKLLDFYTgFEGVSTLVDVGGGVGATLHAIT 220
Cdd:pfam00891   1 WRYLADAVREGRNQYNKAFGISLFEAIYRDEEERLLFNRGLQEHWSLIGKDVLTAFD-LSGFRSLVDVGGGTGALAQAIV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33641716   221 SRHPHISGVNFDLPHVISEAPPF------PGVRHVGGDMFA-SVPAGDAILMKWILHDWSDAHCATLLKNCYDALPENGK 293
Cdd:pfam00891  80 SLYPGCKGIVFDLPHVVEAAPTHfsageePRVTFHGGDFFKdSLPEADAYILKRVLHDWSDEKCVKLLKRCYKACPAGGK 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 33641716   294 VIVVECVLPVNTEATPKAQGvfhVDMIMLAHnPGGKERYEREFRELAKGAGFS 346
Cdd:pfam00891 160 VILVESLLGADPSGPLHTQL---YSLNMLAQ-TEGRERTEAEYSELLTGAGFS 208
dimerization pfam08100
dimerization domain; This domain is found at the N-terminus of a variety of plant ...
 31-87 3.82e-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: 49.11  E-value: 3.82e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 33641716    31 MTLKNAIELGLLEVLQKEAgggkAALAPEEVVARMpaaPGDPAAAAAMVDRMLRLLA 87
Cdd:pfam08100   1 MVLKCAIELGIPDIIAKHG----KPLSPSELASKL---PTKNPEAPVMLDRLLRLLA 50
 
Name Accession Description Interval E-value
Methyltransf_2 pfam00891
O-methyltransferase domain; This family includes a range of O-methyltransferases. These ...
 141-346 7.73e-99

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: 291.23  E-value: 7.73e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33641716   141 WYYLKDAVLDGGIPFNKAYGMTAFEYHGTDSRFNRVFNEGMKNHSVIITKKLLDFYTgFEGVSTLVDVGGGVGATLHAIT 220
Cdd:pfam00891   1 WRYLADAVREGRNQYNKAFGISLFEAIYRDEEERLLFNRGLQEHWSLIGKDVLTAFD-LSGFRSLVDVGGGTGALAQAIV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33641716   221 SRHPHISGVNFDLPHVISEAPPF------PGVRHVGGDMFA-SVPAGDAILMKWILHDWSDAHCATLLKNCYDALPENGK 293
Cdd:pfam00891  80 SLYPGCKGIVFDLPHVVEAAPTHfsageePRVTFHGGDFFKdSLPEADAYILKRVLHDWSDEKCVKLLKRCYKACPAGGK 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 33641716   294 VIVVECVLPVNTEATPKAQGvfhVDMIMLAHnPGGKERYEREFRELAKGAGFS 346
Cdd:pfam00891 160 VILVESLLGADPSGPLHTQL---YSLNMLAQ-TEGRERTEAEYSELLTGAGFS 208
dimerization pfam08100
dimerization domain; This domain is found at the N-terminus of a variety of plant ...
 31-87 3.82e-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: 49.11  E-value: 3.82e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 33641716    31 MTLKNAIELGLLEVLQKEAgggkAALAPEEVVARMpaaPGDPAAAAAMVDRMLRLLA 87
Cdd:pfam08100   1 MVLKCAIELGIPDIIAKHG----KPLSPSELASKL---PTKNPEAPVMLDRLLRLLA 50
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 203-306 1.05e-03

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: 38.82  E-value: 1.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33641716 203 STLVDVGGGVGATLHAITSRHPHISGVNFDlPHVISEA-----PPFPGVRHVGGDMFA-SVPAG--DAILMKWILHDWSD 274
Cdd:COG2226  24 ARVLDLGCGTGRLALALAERGARVTGVDIS-PEMLELAreraaEAGLNVEFVVGDAEDlPFPDGsfDLVISSFVLHHLPD 102

                        90       100       110
                ....*....|....*....|....*....|..
gi 33641716 275 AhcATLLKNCYDALPENGKVIVVECVLPVNTE 306
Cdd:COG2226 103 P--ERALAEIARVLKPGGRLVVVDFSPPDLAE 132
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 204-297 6.57e-03

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: 35.87  E-value: 6.57e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33641716 204 TLVDVGGGVGATLHAITSRHP-HISGVNFDlPHVISEA------PPFPGVRHVGGDMFASVPAG----DAILMKWILHDW 272
Cdd:cd02440   1 RVLDLGCGTGALALALASGPGaRVTGVDIS-PVALELArkaaaaLLADNVEVLKGDAEELPPEAdesfDVIISDPPLHHL 79

                        90       100
                ....*....|....*....|....*
gi 33641716 273 SDAHcATLLKNCYDALPENGKVIVV 297
Cdd:cd02440  80 VEDL-ARFLEEARRLLKPGGVLVLT 103
 
Name Accession Description Interval E-value
Methyltransf_2 pfam00891
O-methyltransferase domain; This family includes a range of O-methyltransferases. These ...
 141-346 7.73e-99

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: 291.23  E-value: 7.73e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33641716   141 WYYLKDAVLDGGIPFNKAYGMTAFEYHGTDSRFNRVFNEGMKNHSVIITKKLLDFYTgFEGVSTLVDVGGGVGATLHAIT 220
Cdd:pfam00891   1 WRYLADAVREGRNQYNKAFGISLFEAIYRDEEERLLFNRGLQEHWSLIGKDVLTAFD-LSGFRSLVDVGGGTGALAQAIV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33641716   221 SRHPHISGVNFDLPHVISEAPPF------PGVRHVGGDMFA-SVPAGDAILMKWILHDWSDAHCATLLKNCYDALPENGK 293
Cdd:pfam00891  80 SLYPGCKGIVFDLPHVVEAAPTHfsageePRVTFHGGDFFKdSLPEADAYILKRVLHDWSDEKCVKLLKRCYKACPAGGK 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 33641716   294 VIVVECVLPVNTEATPKAQGvfhVDMIMLAHnPGGKERYEREFRELAKGAGFS 346
Cdd:pfam00891 160 VILVESLLGADPSGPLHTQL---YSLNMLAQ-TEGRERTEAEYSELLTGAGFS 208
dimerization pfam08100
dimerization domain; This domain is found at the N-terminus of a variety of plant ...
 31-87 3.82e-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: 49.11  E-value: 3.82e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 33641716    31 MTLKNAIELGLLEVLQKEAgggkAALAPEEVVARMpaaPGDPAAAAAMVDRMLRLLA 87
Cdd:pfam08100   1 MVLKCAIELGIPDIIAKHG----KPLSPSELASKL---PTKNPEAPVMLDRLLRLLA 50
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 203-306 1.05e-03

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: 38.82  E-value: 1.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33641716 203 STLVDVGGGVGATLHAITSRHPHISGVNFDlPHVISEA-----PPFPGVRHVGGDMFA-SVPAG--DAILMKWILHDWSD 274
Cdd:COG2226  24 ARVLDLGCGTGRLALALAERGARVTGVDIS-PEMLELAreraaEAGLNVEFVVGDAEDlPFPDGsfDLVISSFVLHHLPD 102

                        90       100       110
                ....*....|....*....|....*....|..
gi 33641716 275 AhcATLLKNCYDALPENGKVIVVECVLPVNTE 306
Cdd:COG2226 103 P--ERALAEIARVLKPGGRLVVVDFSPPDLAE 132
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 204-297 6.57e-03

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: 35.87  E-value: 6.57e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33641716 204 TLVDVGGGVGATLHAITSRHP-HISGVNFDlPHVISEA------PPFPGVRHVGGDMFASVPAG----DAILMKWILHDW 272
Cdd:cd02440   1 RVLDLGCGTGALALALASGPGaRVTGVDIS-PVALELArkaaaaLLADNVEVLKGDAEELPPEAdesfDVIISDPPLHHL 79

                        90       100
                ....*....|....*....|....*
gi 33641716 273 SDAHcATLLKNCYDALPENGKVIVV 297
Cdd:cd02440  80 VEDL-ARFLEEARRLLKPGGVLVLT 103
 
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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