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Conserved domains on  [gi|685504982|ref|NP_001288719|]
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tRNA N(3)-methylcytidine methyltransferase METTL6 isoform 2 [Homo sapiens]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10117436)

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 METTL6, which contributes to post-transcriptional methylation of cytidine (formation of 3-methylcytidine) in tRNA; METTL6 interacts with seryl-tRNA synthetase and methylates tRNA(Ser);

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 70-142 1.51e-07

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: 48.20  E-value: 1.51e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 685504982  70 LRSCREQNPLYDTERCKVFQCDLTKddlLDHVPPESVDVVMLIFVLSAVHPDkMHLVLQNIYKVLKPGKSVLF 142
Cdd:cd02440   34 LELARKAAAALLADNVEVLKGDAEE---LPPEADESFDVIISDPPLHHLVED-LARFLEEARRLLKPGGVLVL 102
AdoMet_MTases super family cl17173
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 107-192 8.40e-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.).


The actual alignment was detected with superfamily member pfam13489:

Pssm-ID: 473071 [Multi-domain]  Cd Length: 162  Bit Score: 41.64  E-value: 8.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504982  107 DVVMLIFVLSAVHPdkMHLVLQNIYKVLKPGKSVLFRDYGLYDHAMLRFKassklgENFYVRQDGTRSYFFTDDFLAQLF 186
Cdd:pfam13489  82 DVIVAREVLEHVPD--PPALLRQIAALLKPGGLLLLSTPLASDEADRLLL------EWPYLRPRNGHISLFSARSLKRLL 153


                  ....*.
gi 685504982  187 MDTGYE 192
Cdd:pfam13489 154 EEAGFE 159
 
Name Accession Description Interval E-value
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 70-142 1.51e-07

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: 48.20  E-value: 1.51e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 685504982  70 LRSCREQNPLYDTERCKVFQCDLTKddlLDHVPPESVDVVMLIFVLSAVHPDkMHLVLQNIYKVLKPGKSVLF 142
Cdd:cd02440   34 LELARKAAAALLADNVEVLKGDAEE---LPPEADESFDVIISDPPLHHLVED-LARFLEEARRLLKPGGVLVL 102
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 84-137 2.82e-07

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 47.17  E-value: 2.82e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 685504982   84 RCKVFQCDLTKDDLLDhvppESVDVVMLIFVLSAVHPDKMHLVLQNIYKVLKPG 137
Cdd:pfam13649  46 NVEFVQGDAEDLPFPD----GSFDLVVSSGVLHHLPDPDLEAALREIARVLKPG 95
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 73-137 6.14e-06

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 45.68  E-value: 6.14e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 685504982  73 CREQNPLYDTERCKVFQCDLTKddlLDHVPPESVDVVMLIFVLSAVHPDKMHLVLQNIYKVLKPG 137
Cdd:COG0500   65 ARARAAKAGLGNVEFLVADLAE---LDPLPAESFDLVVAFGVLHHLPPEEREALLRELARALKPG 126
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 107-192 8.40e-05

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 41.64  E-value: 8.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504982  107 DVVMLIFVLSAVHPdkMHLVLQNIYKVLKPGKSVLFRDYGLYDHAMLRFKassklgENFYVRQDGTRSYFFTDDFLAQLF 186
Cdd:pfam13489  82 DVIVAREVLEHVPD--PPALLRQIAALLKPGGLLLLSTPLASDEADRLLL------EWPYLRPRNGHISLFSARSLKRLL 153


                  ....*.
gi 685504982  187 MDTGYE 192
Cdd:pfam13489 154 EEAGFE 159
 
Name Accession Description Interval E-value
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 70-142 1.51e-07

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: 48.20  E-value: 1.51e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 685504982  70 LRSCREQNPLYDTERCKVFQCDLTKddlLDHVPPESVDVVMLIFVLSAVHPDkMHLVLQNIYKVLKPGKSVLF 142
Cdd:cd02440   34 LELARKAAAALLADNVEVLKGDAEE---LPPEADESFDVIISDPPLHHLVED-LARFLEEARRLLKPGGVLVL 102
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 84-137 2.82e-07

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 47.17  E-value: 2.82e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 685504982   84 RCKVFQCDLTKDDLLDhvppESVDVVMLIFVLSAVHPDKMHLVLQNIYKVLKPG 137
Cdd:pfam13649  46 NVEFVQGDAEDLPFPD----GSFDLVVSSGVLHHLPDPDLEAALREIARVLKPG 95
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 76-137 3.06e-06

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 44.67  E-value: 3.06e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 685504982   76 QNPLYDTERCKVFQCDLTKDDlldhvpPESVDVVMLIFVLSavHPDKMHLVLQNIYKVLKPG 137
Cdd:pfam08242  42 ALGLLNAVRVELFQLDLGELD------PGSFDVVVASNVLH--HLADPRAVLRNIRRLLKPG 95
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 73-137 6.14e-06

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 45.68  E-value: 6.14e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 685504982  73 CREQNPLYDTERCKVFQCDLTKddlLDHVPPESVDVVMLIFVLSAVHPDKMHLVLQNIYKVLKPG 137
Cdd:COG0500   65 ARARAAKAGLGNVEFLVADLAE---LDPLPAESFDLVVAFGVLHHLPPEEREALLRELARALKPG 126
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 107-192 8.40e-05

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 41.64  E-value: 8.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504982  107 DVVMLIFVLSAVHPdkMHLVLQNIYKVLKPGKSVLFRDYGLYDHAMLRFKassklgENFYVRQDGTRSYFFTDDFLAQLF 186
Cdd:pfam13489  82 DVIVAREVLEHVPD--PPALLRQIAALLKPGGLLLLSTPLASDEADRLLL------EWPYLRPRNGHISLFSARSLKRLL 153


                  ....*.
gi 685504982  187 MDTGYE 192
Cdd:pfam13489 154 EEAGFE 159
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 68-154 5.02e-04

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: 39.21  E-value: 5.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504982  68 EELRSCREQNPlYDTERCKVFQCDLTKDDLldhvPPESVDVVMLIFVLSAVhPDKmHLVLQNIYKVLKPGKSVLFRDYGL 147
Cdd:COG2226   55 EMLELARERAA-EAGLNVEFVVGDAEDLPF----PDGSFDLVISSFVLHHL-PDP-ERALAEIARVLKPGGRLVVVDFSP 127


                 ....*..
gi 685504982 148 YDHAMLR 154
Cdd:COG2226  128 PDLAELE 134
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 102-142 5.12e-03

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 35.33  E-value: 5.12e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 685504982  102 PPESVDVVMLIFVLSavHPDKMHLVLQNIYKVLKPGKSVLF 142
Cdd:pfam08241  56 PDNSFDLVLSSEVLH--HVEDPERALREIARVLKPGGILII 94
 
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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