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Conserved domains on  [gi|71996911|ref|NP_497790|]
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tRNA N(3)-methylcytidine methyltransferase [Caenorhabditis elegans]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10549439)

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 Homo sapiens tRNA N(3)-methylcytidine methyltransferase METTL6

CATH:  3.40.50.150
EC:  2.1.1.-
Gene Ontology:  GO:1904047|GO:0008168|GO:0032259|GO:0008757
PubMed:  12504684|12826405
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 84-182 2.12e-15

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


:

Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 70.09  E-value: 2.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996911    84 LEAGCGVGNMLFPLVAEIPNLKLFAFDFSDNAVKLLEERAKELELSVATsVVDLSIPSVSSPFEEQVDLATLIFVLSAIh 163
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGLLNAV-RVELFQLDLGELDPGSFDVVVASNVLHHL- 78

                          90
                  ....*....|....*....
gi 71996911   164 PEKHQIsAENVRKMIKIGG 182
Cdd:pfam08242  79 ADPRAV-LRNIRRLLKPGG 96
 
Name Accession Description Interval E-value
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 84-182 2.12e-15

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 70.09  E-value: 2.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996911    84 LEAGCGVGNMLFPLVAEIPNLKLFAFDFSDNAVKLLEERAKELELSVATsVVDLSIPSVSSPFEEQVDLATLIFVLSAIh 163
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGLLNAV-RVELFQLDLGELDPGSFDVVVASNVLHHL- 78

                          90
                  ....*....|....*....
gi 71996911   164 PEKHQIsAENVRKMIKIGG 182
Cdd:pfam08242  79 ADPRAV-LRNIRRLLKPGG 96
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 45-192 4.12e-10

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 58.00  E-value: 4.12e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996911  45 NWDKFYHRNKNNffkdrnwSAEDLKMMCPDIDfeKEISYLEAGCGVGNMLFPLvAEIPNLKLFAFDFSDNAVKLLEERAK 124
Cdd:COG0500   1 PWDSYYSDELLP-------GLAALLALLERLP--KGGRVLDLGCGTGRNLLAL-AARFGGRVIGIDLSPEAIALARARAA 70

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71996911 125 ELELSVATsVVDLSIPSVSSPFEEQVDLATLIFVLSAIHPEKHQISAENVRKMIKIGGSVVVRDYGIN 192
Cdd:COG0500  71 KAGLGNVE-FLVADLAELDPLPAESFDLVVAFGVLHHLPPEEREALLRELARALKPGGVLLLSASDAA 137
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 84-186 3.40e-05

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: 42.03  E-value: 3.40e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996911  84 LEAGCGVGNMLFPLvAEIPNLKLFAFDFSDNAVKLLEERAKELELSVAT-SVVDLSIPSVSSPfeEQVDLATLIFVLSAI 162
Cdd:cd02440   3 LDLGCGTGALALAL-ASGPGARVTGVDISPVALELARKAAAALLADNVEvLKGDAEELPPEAD--ESFDVIISDPPLHHL 79

                        90       100
                ....*....|....*....|....
gi 71996911 163 HPEKHQIsAENVRKMIKIGGSVVV 186
Cdd:cd02440  80 VEDLARF-LEEARRLLKPGGVLVL 102
PRK06922 PRK06922
class I SAM-dependent methyltransferase;
43-188 1.85e-03

class I SAM-dependent methyltransferase;


Pssm-ID: 180751 [Multi-domain]  Cd Length: 677  Bit Score: 39.47  E-value: 1.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996911   43 RKNWDKFYhrNKNNFFKDRNWSAEDLKMMcpdIDFEKEISYLEAGCGVGNMLFPLVAEIPNLKLFAFDFSDNAVKLLEER 122
Cdd:PRK06922 387 KDAYDRFH--NEEVYLEHMNSSADDKRII---LDYIKGDTIVDVGAGGGVMLDMIEEETEDKRIYGIDISENVIDTLKKK 461

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996911  123 aKELElSVATSVVDLSIPSVSSPFE-EQVDlaTLIF------VLSAIHPEKHQISAENVRK-------MIKIGGSVVVRD 188
Cdd:PRK06922 462 -KQNE-GRSWNVIKGDAINLSSSFEkESVD--TIVYssilheLFSYIEYEGKKFNHEVIKKglqsayeVLKPGGRIIIRD 537
 
Name Accession Description Interval E-value
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 84-182 2.12e-15

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 70.09  E-value: 2.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996911    84 LEAGCGVGNMLFPLVAEIPNLKLFAFDFSDNAVKLLEERAKELELSVATsVVDLSIPSVSSPFEEQVDLATLIFVLSAIh 163
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGLLNAV-RVELFQLDLGELDPGSFDVVVASNVLHHL- 78

                          90
                  ....*....|....*....
gi 71996911   164 PEKHQIsAENVRKMIKIGG 182
Cdd:pfam08242  79 ADPRAV-LRNIRRLLKPGG 96
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 84-182 1.69e-10

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 56.42  E-value: 1.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996911    84 LEAGCGVGNMLFPLvAEIPNLKLFAFDFSDNAVKLLEERAKELELSVATSVVDLSipsvSSPFE-EQVDLATLIFVLSAI 162
Cdd:pfam13649   2 LDLGCGTGRLTLAL-ARRGGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAE----DLPFPdGSFDLVVSSGVLHHL 76

                          90       100
                  ....*....|....*....|
gi 71996911   163 HPEKHQISAENVRKMIKIGG 182
Cdd:pfam13649  77 PDPDLEAALREIARVLKPGG 96
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 45-192 4.12e-10

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 58.00  E-value: 4.12e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996911  45 NWDKFYHRNKNNffkdrnwSAEDLKMMCPDIDfeKEISYLEAGCGVGNMLFPLvAEIPNLKLFAFDFSDNAVKLLEERAK 124
Cdd:COG0500   1 PWDSYYSDELLP-------GLAALLALLERLP--KGGRVLDLGCGTGRNLLAL-AARFGGRVIGIDLSPEAIALARARAA 70

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71996911 125 ELELSVATsVVDLSIPSVSSPFEEQVDLATLIFVLSAIHPEKHQISAENVRKMIKIGGSVVVRDYGIN 192
Cdd:COG0500  71 KAGLGNVE-FLVADLAELDPLPAESFDLVVAFGVLHHLPPEEREALLRELARALKPGGVLLLSASDAA 137
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 84-198 3.83e-08

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: 51.15  E-value: 3.83e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996911  84 LEAGCGVGNMLFPLVAEipNLKLFAFDFSDNAVKLLEERAKELELSVATSVVDLSipsvSSPFE-EQVDLATLIFVLSAI 162
Cdd:COG2226  27 LDLGCGTGRLALALAER--GARVTGVDISPEMLELARERAAEAGLNVEFVVGDAE----DLPFPdGSFDLVISSFVLHHL 100

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 71996911 163 hPEKHQISAEnVRKMIKIGGSVVVRDYGINDHAMIR 198
Cdd:COG2226 101 -PDPERALAE-IARVLKPGGRLVVVDFSPPDLAELE 134
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 84-189 6.64e-07

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: 47.32  E-value: 6.64e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996911  84 LEAGCGVGNMLFPLVAEipNLKLFAFDFSDNAVKLLEERAKELELS-VATSVVDLSIPsvsspfEEQVDLATLIFVLSAI 162
Cdd:COG2227  29 LDVGCGTGRLALALARR--GADVTGVDISPEALEIARERAAELNVDfVQGDLEDLPLE------DGSFDLVICSEVLEHL 100

                        90       100
                ....*....|....*....|....*...
gi 71996911 163 -HPEKHqisAENVRKMIKIGGSVVVRDY 189
Cdd:COG2227 101 pDPAAL---LRELARLLKPGGLLLLSTP 125
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 78-238 5.35e-06

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 45.50  E-value: 5.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996911    78 EKEISYLEAGCGVGNMLFPLVAEipNLKLFAFDFSDNAVklleerakelELSVATSVVDLSIPSVSSPFEEQVDLATLIF 157
Cdd:pfam13489  21 PSPGRVLDFGCGTGIFLRLLRAQ--GFSVTGVDPSPIAI----------ERALLNVRFDQFDEQEAAVPAGKFDVIVARE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996911   158 VLSAIHpekHQISA-ENVRKMIKIGGSVVVRDYGiNDHAMIRFGREARisdrfYVRQDGTRAYYFDLNELSEVFEKSGFR 236
Cdd:pfam13489  89 VLEHVP---DPPALlRQIAALLKPGGLLLLSTPL-ASDEADRLLLEWP-----YLRPRNGHISLFSARSLKRLLEEAGFE 159


                  ..
gi 71996911   237 CV 238
Cdd:pfam13489 160 VV 161
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
84-186 3.33e-05

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 41.73  E-value: 3.33e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996911  84 LEAGCGVGNMLFPLVAEIPNLKLFAFDFSDNAVKLLEERAKELELSVAtSVVDLsipsvssPFEEQVDLATLIFVLSaiH 163
Cdd:COG4106   6 LDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARLPNVRFVVA-DLRDL-------DPPEPFDLVVSNAALH--W 75

                        90       100
                ....*....|....*....|...
gi 71996911 164 PEKHQISAENVRKMIKIGGSVVV 186
Cdd:COG4106  76 LPDHAALLARLAAALAPGGVLAV 98
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 84-186 3.40e-05

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: 42.03  E-value: 3.40e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996911  84 LEAGCGVGNMLFPLvAEIPNLKLFAFDFSDNAVKLLEERAKELELSVAT-SVVDLSIPSVSSPfeEQVDLATLIFVLSAI 162
Cdd:cd02440   3 LDLGCGTGALALAL-ASGPGARVTGVDISPVALELARKAAAALLADNVEvLKGDAEELPPEAD--ESFDVIISDPPLHHL 79

                        90       100
                ....*....|....*....|....
gi 71996911 163 HPEKHQIsAENVRKMIKIGGSVVV 186
Cdd:cd02440  80 VEDLARF-LEEARRLLKPGGVLVL 102
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 84-188 1.20e-04

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 41.45  E-value: 1.20e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996911  84 LEAGCGVGNMLFPLvAEIPNLKLFAFDFSDNAVKLLEERAKELELSVATSVVDLSIPSVssPFEEQVDLATLIFVLSAIH 163
Cdd:COG2230  56 LDIGCGWGGLALYL-ARRYGVRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDL--PADGQFDAIVSIGMFEHVG 132

                        90       100
                ....*....|....*....|....*
gi 71996911 164 PEKHQISAENVRKMIKIGGSVVVRD 188
Cdd:COG2230 133 PENYPAYFAKVARLLKPGGRLLLHT 157
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 84-186 1.49e-04

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 39.96  E-value: 1.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996911    84 LEAGCGVGNMLFPLVAEIPNlkLFAFDFSDNAVKLLEERAKELELS-VATSVVDLSIPsvsspfEEQVDLATLIFVLSai 162
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGAR--VTGVDISPEMLELAREKAPREGLTfVVGDAEDLPFP------DNSFDLVLSSEVLH-- 70

                          90       100
                  ....*....|....*....|....
gi 71996911   163 HPEKHQISAENVRKMIKIGGSVVV 186
Cdd:pfam08241  71 HVEDPERALREIARVLKPGGILII 94
PRK06922 PRK06922
class I SAM-dependent methyltransferase;
43-188 1.85e-03

class I SAM-dependent methyltransferase;


Pssm-ID: 180751 [Multi-domain]  Cd Length: 677  Bit Score: 39.47  E-value: 1.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996911   43 RKNWDKFYhrNKNNFFKDRNWSAEDLKMMcpdIDFEKEISYLEAGCGVGNMLFPLVAEIPNLKLFAFDFSDNAVKLLEER 122
Cdd:PRK06922 387 KDAYDRFH--NEEVYLEHMNSSADDKRII---LDYIKGDTIVDVGAGGGVMLDMIEEETEDKRIYGIDISENVIDTLKKK 461

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996911  123 aKELElSVATSVVDLSIPSVSSPFE-EQVDlaTLIF------VLSAIHPEKHQISAENVRK-------MIKIGGSVVVRD 188
Cdd:PRK06922 462 -KQNE-GRSWNVIKGDAINLSSSFEkESVD--TIVYssilheLFSYIEYEGKKFNHEVIKKglqsayeVLKPGGRIIIRD 537
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 78-189 2.51e-03

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 37.40  E-value: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996911    78 EKEISYLEAGCGVGNMLFPLVAEI-PNLKLFAFDFSDNAVKLLEERAKELELSVAT-SVVD-LSIPSVSSpfEEQVDlat 154
Cdd:pfam13847   2 DKGMRVLDLGCGTGHLSFELAEELgPNAEVVGIDISEEAIEKARENAQKLGFDNVEfEQGDiEELPELLE--DDKFD--- 76

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 71996911   155 LIFVLSAIHPEKHQISA-ENVRKMIKIGGSVVVRDY 189
Cdd:pfam13847  77 VVISNCVLNHIPDPDKVlQEILRVLKPGGRLIISDP 112
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
84-163 2.88e-03

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 37.67  E-value: 2.88e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996911  84 LEAGCGVGNMLFPLVAEIpnLKLFAFDFSDNAVKLLEERAKELELSVAtSVVDLSIPsvsspfEEQVDLATLIFVLSAIH 163
Cdd:COG4976  51 LDLGCGTGLLGEALRPRG--YRLTGVDLSEEMLAKAREKGVYDRLLVA-DLADLAEP------DGRFDLIVAADVLTYLG 121
 
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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