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Conserved domains on  [gi|2462587171|ref|XP_054201228|]
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tRNA N(3)-methylcytidine methyltransferase METTL6 isoform X4 [Homo sapiens]

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.
 84-178 1.66e-16

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


:

Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 72.02  E-value: 1.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462587171  84 LEAGCGVGNCLFPLLEEDPNIFAYACDFSPRAI----EYVKQNPLYDTERCKVFQCDLTKDDlldhvpPESVDVVMLIFV 159
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALeaarERLAALGLLNAVRVELFQLDLGELD------PGSFDVVVASNV 74

                          90
                  ....*....|....*....
gi 2462587171 160 LSavHPDKMHLVLQNIYKC 178
Cdd:pfam08242  75 LH--HLADPRAVLRNIRRL 91
 
Name Accession Description Interval E-value
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 84-178 1.66e-16

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 72.02  E-value: 1.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462587171  84 LEAGCGVGNCLFPLLEEDPNIFAYACDFSPRAI----EYVKQNPLYDTERCKVFQCDLTKDDlldhvpPESVDVVMLIFV 159
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALeaarERLAALGLLNAVRVELFQLDLGELD------PGSFDVVVASNV 74

                          90
                  ....*....|....*....
gi 2462587171 160 LSavHPDKMHLVLQNIYKC 178
Cdd:pfam08242  75 LH--HLADPRAVLRNIRRL 91
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 82-177 4.67e-13

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: 63.22  E-value: 4.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462587171  82 TMLEAGCGVGNCLFPLLEeDPNIFAYACDFSPRAIEYVKQNPLYD-TERCKVFQCDLTKddlLDHVPPESVDVVMLIFVL 160
Cdd:cd02440     1 RVLDLGCGTGALALALAS-GPGARVTGVDISPVALELARKAAAALlADNVEVLKGDAEE---LPPEADESFDVIISDPPL 76

                          90
                  ....*....|....*..
gi 2462587171 161 SAVHPDkMHLVLQNIYK 177
Cdd:cd02440    77 HHLVED-LARFLEEARR 92
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 78-177 2.17e-08

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 52.61  E-value: 2.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462587171  78 DQKLTMLEAGCGVGNCLFPLLEEDPNIFaYACDFSPRAIEYVKQN-PLYDTERCKVFQCDLTKddlLDHVPPESVDVVML 156
Cdd:COG0500    25 PKGGRVLDLGCGTGRNLLALAARFGGRV-IGIDLSPEAIALARARaAKAGLGNVEFLVADLAE---LDPLPAESFDLVVA 100

                          90       100
                  ....*....|....*....|.
gi 2462587171 157 IFVLSAVHPDKMHLVLQNIYK 177
Cdd:COG0500   101 FGVLHHLPPEEREALLRELAR 121
 
Name Accession Description Interval E-value
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 84-178 1.66e-16

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 72.02  E-value: 1.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462587171  84 LEAGCGVGNCLFPLLEEDPNIFAYACDFSPRAI----EYVKQNPLYDTERCKVFQCDLTKDDlldhvpPESVDVVMLIFV 159
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALeaarERLAALGLLNAVRVELFQLDLGELD------PGSFDVVVASNV 74

                          90
                  ....*....|....*....
gi 2462587171 160 LSavHPDKMHLVLQNIYKC 178
Cdd:pfam08242  75 LH--HLADPRAVLRNIRRL 91
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 84-178 2.92e-13

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 63.35  E-value: 2.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462587171  84 LEAGCGVGNCLFPLLEEdPNIFAYACDFSPRAIEYVKQNPLYDTERCKVFQCDLTKDDLLDhvppESVDVVMLIFVLSAV 163
Cdd:pfam13649   2 LDLGCGTGRLTLALARR-GGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPD----GSFDLVVSSGVLHHL 76

                          90
                  ....*....|....*
gi 2462587171 164 HPDKMHLVLQNIYKC 178
Cdd:pfam13649  77 PDPDLEAALREIARV 91
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 82-177 4.67e-13

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: 63.22  E-value: 4.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462587171  82 TMLEAGCGVGNCLFPLLEeDPNIFAYACDFSPRAIEYVKQNPLYD-TERCKVFQCDLTKddlLDHVPPESVDVVMLIFVL 160
Cdd:cd02440     1 RVLDLGCGTGALALALAS-GPGARVTGVDISPVALELARKAAAALlADNVEVLKGDAEE---LPPEADESFDVIISDPPL 76

                          90
                  ....*....|....*..
gi 2462587171 161 SAVHPDkMHLVLQNIYK 177
Cdd:cd02440    77 HHLVED-LARFLEEARR 92
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 78-177 2.17e-08

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 52.61  E-value: 2.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462587171  78 DQKLTMLEAGCGVGNCLFPLLEEDPNIFaYACDFSPRAIEYVKQN-PLYDTERCKVFQCDLTKddlLDHVPPESVDVVML 156
Cdd:COG0500    25 PKGGRVLDLGCGTGRNLLALAARFGGRV-IGIDLSPEAIALARARaAKAGLGNVEFLVADLAE---LDPLPAESFDLVVA 100

                          90       100
                  ....*....|....*....|.
gi 2462587171 157 IFVLSAVHPDKMHLVLQNIYK 177
Cdd:COG0500   101 FGVLHHLPPEEREALLRELAR 121
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 54-178 5.85e-08

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: 50.02  E-value: 5.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462587171  54 TNFFKDRHWTTReFEELrsCREFEDQKLTMLEAGCGVGNCLFPLLEEDPNIfaYACDFSPRAIEYVKQNplYDTERCKVF 133
Cdd:COG2227     2 SDPDARDFWDRR-LAAL--LARLLPAGGRVLDVGCGTGRLALALARRGADV--TGVDISPEALEIARER--AAELNVDFV 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2462587171 134 QCDLTKDDLldhvPPESVDVVMLIFVLSavHPDKMHLVLQNIYKC 178
Cdd:COG2227    75 QGDLEDLPL----EDGSFDLVICSEVLE--HLPDPAALLRELARL 113
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 84-176 1.40e-07

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: 49.22  E-value: 1.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462587171  84 LEAGCGVGNCLFPLLEEDPNIfaYACDFSPRAIEYVKQNPLYDTERCKVFQCDLTKDDLldhvPPESVDVVMLIFVLSAV 163
Cdd:COG2226    27 LDLGCGTGRLALALAERGARV--TGVDISPEMLELARERAAEAGLNVEFVVGDAEDLPF----PDGSFDLVISSFVLHHL 100

                          90
                  ....*....|...
gi 2462587171 164 hPDKmHLVLQNIY 176
Cdd:COG2226   101 -PDP-ERALAEIA 111
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 84-178 8.36e-07

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 45.73  E-value: 8.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462587171  84 LEAGCGVGNCLFPLLEEDPNIfaYACDFSPRAIEYVKQNplYDTERCKVFQCDLTKDDLLDhvppESVDVVMLIFVLSav 163
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARV--TGVDISPEMLELAREK--APREGLTFVVGDAEDLPFPD----NSFDLVLSSEVLH-- 70

                          90
                  ....*....|....*
gi 2462587171 164 HPDKMHLVLQNIYKC 178
Cdd:pfam08241  71 HVEDPERALREIARV 85
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 81-177 3.34e-06

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 45.49  E-value: 3.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462587171  81 LTMLEAGCGVGNCLFPLLEED-PNIFAYACDFSPRAIEYVKQN-PLYDTERCKVFQCDLTkdDLLDHVPPESVDVVMLIF 158
Cdd:pfam13847   5 MRVLDLGCGTGHLSFELAEELgPNAEVVGIDISEEAIEKARENaQKLGFDNVEFEQGDIE--ELPELLEDDKFDVVISNC 82

                          90       100
                  ....*....|....*....|
gi 2462587171 159 VLSAV-HPDKmhlVLQNIYK 177
Cdd:pfam13847  83 VLNHIpDPDK---VLQEILR 99
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
74-177 5.84e-06

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 45.37  E-value: 5.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462587171  74 REFEDQKLTMLEAGCGVGNCLFPLLEEDPNIfaYACDFSPRAIEYVKQNPLYDTerckVFQCDLTKDDlldhVPPESVDV 153
Cdd:COG4976    41 RLPPGPFGRVLDLGCGTGLLGEALRPRGYRL--TGVDLSEEMLAKAREKGVYDR----LLVADLADLA----EPDGRFDL 110

                          90       100
                  ....*....|....*....|....
gi 2462587171 154 VMLIFVLSavHPDKMHLVLQNIYK 177
Cdd:COG4976   111 IVAADVLT--YLGDLAAVFAGVAR 132
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
84-178 3.89e-04

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 38.65  E-value: 3.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462587171  84 LEAGCGVGNCLFPLLEEDPNIFAYACDFSPRAIEYVKQN-PlydterckvfQCDLTKDDLLDHVPPESVDVVMLIFVLSa 162
Cdd:COG4106     6 LDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARlP----------NVRFVVADLRDLDPPEPFDLVVSNAALH- 74

                          90
                  ....*....|....*.
gi 2462587171 163 vHPDKMHLVLQNIYKC 178
Cdd:COG4106    75 -WLPDHAALLARLAAA 89
 
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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