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Conserved domains on  [gi|15232436|ref|NP_190983|]
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S-adenosyl-L-methionine-dependent methyltransferases superfamily protein [Arabidopsis thaliana]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10789277)

class I SAM-dependent methyltransferase is an enzyme that uses S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyl transfer, creating the product S-adenosyl-L-homocysteine (AdoHcy)

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:0008168|GO:1904047
PubMed:  12826405
SCOP:  3000118

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 6-139 1.22e-12

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: 64.24  E-value: 1.22e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232436   6 EKEAEAYlDARPRypidWFKKIAARTQDHkfAWDVGTGNGQAAIGLVEHYENVVATDINEAQLQRAIKhsRISYHHTPTT 85
Cdd:COG2226   2 DRVAARY-DGREA----LLAALGLRPGAR--VLDLGCGTGRLALALAERGARVTGVDISPEMLELARE--RAAEAGLNVE 72

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15232436  86 ISEDEMVDLLGGENSVDLIVAAQAVHFF-DLNVFYNVAKRVLRKeGGLIAVWVYN 139
Cdd:COG2226  73 FVVGDAEDLPFPDGSFDLVISSFVLHHLpDPERALAEIARVLKP-GGRLVVVDFS 126
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 6-139 1.22e-12

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: 64.24  E-value: 1.22e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232436   6 EKEAEAYlDARPRypidWFKKIAARTQDHkfAWDVGTGNGQAAIGLVEHYENVVATDINEAQLQRAIKhsRISYHHTPTT 85
Cdd:COG2226   2 DRVAARY-DGREA----LLAALGLRPGAR--VLDLGCGTGRLALALAERGARVTGVDISPEMLELARE--RAAEAGLNVE 72

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15232436  86 ISEDEMVDLLGGENSVDLIVAAQAVHFF-DLNVFYNVAKRVLRKeGGLIAVWVYN 139
Cdd:COG2226  73 FVVGDAEDLPFPDGSFDLVISSFVLHHLpDPERALAEIARVLKP-GGRLVVVDFS 126
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 39-130 8.56e-11

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 57.96  E-value: 8.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232436    39 DVGTGNGQAAIGLVEHYE-NVVATDINEAQLQRAikHSRISYHHTPTTISEDEMVDLLGGENSVDLIVAAQAVHFF---D 114
Cdd:pfam13649   3 DLGCGTGRLTLALARRGGaRVTGVDLSPEMLERA--RERAAEAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLpdpD 80

                          90
                  ....*....|....*.
gi 15232436   115 LNVFYNVAKRVLRKEG 130
Cdd:pfam13649  81 LEAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 38-138 7.72e-08

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: 49.74  E-value: 7.72e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232436  38 WDVGTGNGQAAIGLVEHY-ENVVATDINEAQLQRAIKHSRISYHHTPTTISEDEMVDLLGGENSVDLIVAAQAVHFFDLN 116
Cdd:cd02440   3 LDLGCGTGALALALASGPgARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEADESFDVIISDPPLHHLVED 82

                        90       100
                ....*....|....*....|....
gi 15232436 117 V--FYNVAKRVLRKeGGLIAVWVY 138
Cdd:cd02440  83 LarFLEEARRLLKP-GGVLVLTLV 105
PRK14968 PRK14968
putative methyltransferase; Provisional
 28-77 5.62e-03

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 37.19  E-value: 5.62e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 15232436   28 AARTQDHKFAWDVGTGNGQAAIGLVEHYENVVATDINEAQLQRAIKHSRI 77
Cdd:PRK14968  18 NAVDKKGDRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVECAKCNAKL 67
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 6-139 1.22e-12

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: 64.24  E-value: 1.22e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232436   6 EKEAEAYlDARPRypidWFKKIAARTQDHkfAWDVGTGNGQAAIGLVEHYENVVATDINEAQLQRAIKhsRISYHHTPTT 85
Cdd:COG2226   2 DRVAARY-DGREA----LLAALGLRPGAR--VLDLGCGTGRLALALAERGARVTGVDISPEMLELARE--RAAEAGLNVE 72

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15232436  86 ISEDEMVDLLGGENSVDLIVAAQAVHFF-DLNVFYNVAKRVLRKeGGLIAVWVYN 139
Cdd:COG2226  73 FVVGDAEDLPFPDGSFDLVISSFVLHHLpDPERALAEIARVLKP-GGRLVVVDFS 126
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 39-130 8.56e-11

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 57.96  E-value: 8.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232436    39 DVGTGNGQAAIGLVEHYE-NVVATDINEAQLQRAikHSRISYHHTPTTISEDEMVDLLGGENSVDLIVAAQAVHFF---D 114
Cdd:pfam13649   3 DLGCGTGRLTLALARRGGaRVTGVDLSPEMLERA--RERAAEAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLpdpD 80

                          90
                  ....*....|....*.
gi 15232436   115 LNVFYNVAKRVLRKEG 130
Cdd:pfam13649  81 LEAALREIARVLKPGG 96
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 39-135 9.53e-11

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 57.67  E-value: 9.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232436    39 DVGTGNGQAAIGLVEHYENVVATDINEAQLQRAIKHSRISyhhTPTTISED-EMVDLlgGENSVDLIVAAQAVHFF-DLN 116
Cdd:pfam08241   2 DVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPRE---GLTFVVGDaEDLPF--PDNSFDLVLSSEVLHHVeDPE 76

                          90
                  ....*....|....*....
gi 15232436   117 VFYNVAKRVLRKeGGLIAV 135
Cdd:pfam08241  77 RALREIARVLKP-GGILII 94
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 39-139 2.51e-10

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 57.33  E-value: 2.51e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232436  39 DVGTGNGQAAIGLVEHYENVVATDINEAQLQRAIKH---SRISYHHTPttisedeMVDLLGGENSVDLIVAAQAV-HFFD 114
Cdd:COG2227  30 DVGCGTGRLALALARRGADVTGVDISPEALEIARERaaeLNVDFVQGD-------LEDLPLEDGSFDLVICSEVLeHLPD 102

                        90       100
                ....*....|....*....|....*
gi 15232436 115 LNVFYNVAKRVLRKeGGLIAVWVYN 139
Cdd:COG2227 103 PAALLRELARLLKP-GGLLLLSTPN 126
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
10-137 1.32e-08

Predicted methyltransferase, contains TPR repeat [General function prediction only];


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 53.85  E-value: 1.32e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232436  10 EAYLDARPRY--PIDWFKKIAARTQDHKF--AWDVGTGNGQAAIGLVEHYENVVATDINEAQLQRAikHSRISYHHtptt 85
Cdd:COG4976  19 DAALVEDLGYeaPALLAEELLARLPPGPFgrVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKA--REKGVYDR---- 92

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 15232436  86 ISEDEMVDLLGGENSVDLIVAAQAVHFF-DLNVFYNVAKRVLrKEGGLIAVWV 137
Cdd:COG4976  93 LLVADLADLAEPDGRFDLIVAADVLTYLgDLAAVFAGVARAL-KPGGLFIFSV 144
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 38-138 7.72e-08

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: 49.74  E-value: 7.72e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232436  38 WDVGTGNGQAAIGLVEHY-ENVVATDINEAQLQRAIKHSRISYHHTPTTISEDEMVDLLGGENSVDLIVAAQAVHFFDLN 116
Cdd:cd02440   3 LDLGCGTGALALALASGPgARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEADESFDVIISDPPLHHLVED 82

                        90       100
                ....*....|....*....|....
gi 15232436 117 V--FYNVAKRVLRKeGGLIAVWVY 138
Cdd:cd02440  83 LarFLEEARRLLKP-GGVLVLTLV 105
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 39-132 3.20e-07

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 47.75  E-value: 3.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232436    39 DVGTGNGQAAIGLVEHYEN--VVATDINEAQLQRAIKH--SRISYHHTPTTISEDEMVDLLGGenSVDLIVAAQAVHFF- 113
Cdd:pfam08242   2 EIGCGTGTLLRALLEALPGleYTGLDISPAALEAARERlaALGLLNAVRVELFQLDLGELDPG--SFDVVVASNVLHHLa 79

                          90
                  ....*....|....*....
gi 15232436   114 DLNVFYNVAKRVLRKEGGL 132
Cdd:pfam08242  80 DPRAVLRNIRRLLKPGGVL 98
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 10-137 2.42e-06

SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 47.60  E-value: 2.42e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232436  10 EAYLDARPRYPIDWFKKIAARTQDHKFAWDVGTGNGQAAIGLVEHY-ENVVATDINEAQLQRAIKHSRiSYHHTPTTISE 88
Cdd:COG0500   3 DSYYSDELLPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAARFgGRVIGIDLSPEAIALARARAA-KAGLGNVEFLV 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 15232436  89 DEMVDLLG-GENSVDLIVAAQAVHFFD---LNVFYNVAKRVLRKEGGLIAVWV 137
Cdd:COG0500  82 ADLAELDPlPAESFDLVVAFGVLHHLPpeeREALLRELARALKPGGVLLLSAS 134
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 10-135 4.34e-05

Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 42.99  E-value: 4.34e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232436  10 EAYLDARPRYPIDWFKKIA---ARTQDHKFAW--------------DVGTGNGQAAIGLVEHYE-NVVATDINEAQLQRA 71
Cdd:COG2230  11 RLFLDPTMTYSCAYFEDPDdtlEEAQEAKLDLilrklglkpgmrvlDIGCGWGGLALYLARRYGvRVTGVTLSPEQLEYA 90

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232436  72 IKHSRISYHHTPTTISEDEMVDlLGGENSVDLIVAAQAVHFF---DLNVFYNVAKRVLrKEGGLIAV 135
Cdd:COG2230  91 RERAAEAGLADRVEVRLADYRD-LPADGQFDAIVSIGMFEHVgpeNYPAYFAKVARLL-KPGGRLLL 155
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 39-134 8.79e-04

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 39.32  E-value: 8.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232436    39 DVGTGNG---QAAIGLVEHYENVVATDINEAQLQRAIKH------SRISYHhtpttISEDEMVDLLGGENSVDLIVAAQA 109
Cdd:pfam13847   9 DLGCGTGhlsFELAEELGPNAEVVGIDISEEAIEKARENaqklgfDNVEFE-----QGDIEELPELLEDDKFDVVISNCV 83

                          90       100
                  ....*....|....*....|....*.
gi 15232436   110 V-HFFDLNVFYNVAKRVLRKEGGLIA 134
Cdd:pfam13847  84 LnHIPDPDKVLQEILRVLKPGGRLII 109
Methyltransf_18 pfam12847
Methyltransferase domain; Protein in this family function as methyltransferases.
 25-76 2.37e-03

Methyltransferase domain; Protein in this family function as methyltransferases.


Pssm-ID: 463730  Cd Length: 151  Bit Score: 37.80  E-value: 2.37e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15232436    25 KKIAARTQDHKFAWDVGTGNGQAAIGLVEHY--ENVVATDINEAQLQRAIKHSR 76
Cdd:pfam12847   6 QAIASLVPPGSRVADIGTDHAYLPIYLVKNGiaPKAIASDINEGPLEKARENIE 59
PRK14968 PRK14968
putative methyltransferase; Provisional
 28-77 5.62e-03

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 37.19  E-value: 5.62e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 15232436   28 AARTQDHKFAWDVGTGNGQAAIGLVEHYENVVATDINEAQLQRAIKHSRI 77
Cdd:PRK14968  18 NAVDKKGDRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVECAKCNAKL 67
 
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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