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Conserved domains on  [gi|1331036858|ref|NP_001346777|]
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tRNA N(3)-methylcytidine methyltransferase METTL6 isoform 3 [Mus musculus]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10614804)

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 Mus musculus tRNA N(3)-methylcytidine methyltransferase METTL6 isoform 3

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:0032259|GO:0008757|GO:0008168|GO:1904047
PubMed:  12504684|12826405
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 70-137 7.17e-07

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


:

Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 46.02  E-value: 7.17e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331036858  70 LRSCREQHPLYNAeRCKVFQCDLTRDDLLDhvppESVDAVTLIFVLSAVHPEKMRLVLLNVYKVLKPG 137
Cdd:pfam13649  33 LERARERAAEAGL-NVEFVQGDAEDLPFPD----GSFDLVVSSGVLHHLPDPDLEAALREIARVLKPG 95
AdoMet_MTases super family cl17173
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 107-192 4.62e-04

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: 39.72  E-value: 4.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331036858 107 DAVTLIFVLSAVHPekMRLVLLNVYKVLKPGRSVLFRDYGLNDHAmlrfkaGSKLGENFYVRQDGTRSYFFTDEFLAQLF 186
Cdd:pfam13489  82 DVIVAREVLEHVPD--PPALLRQIAALLKPGGLLLLSTPLASDEA------DRLLLEWPYLRPRNGHISLFSARSLKRLL 153


                  ....*.
gi 1331036858 187 VDAGYE 192
Cdd:pfam13489 154 EEAGFE 159
 
Name Accession Description Interval E-value
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 70-137 7.17e-07

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 46.02  E-value: 7.17e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331036858  70 LRSCREQHPLYNAeRCKVFQCDLTRDDLLDhvppESVDAVTLIFVLSAVHPEKMRLVLLNVYKVLKPG 137
Cdd:pfam13649  33 LERARERAAEAGL-NVEFVQGDAEDLPFPD----GSFDLVVSSGVLHHLPDPDLEAALREIARVLKPG 95
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 73-202 9.25e-06

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 44.91  E-value: 9.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331036858  73 CREQHPLYNAERCKVFQCDLTRddlLDHVPPESVDAVTLIFVLSAVHPEKMRLVLLNVYKVLKPGRSVLF--------RD 144
Cdd:COG0500    65 ARARAAKAGLGNVEFLVADLAE---LDPLPAESFDLVVAFGVLHHLPPEEREALLRELARALKPGGVLLLsasdaaaaLS 141

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1331036858 145 YGLNDHAMLRFKAGSKLGENFYVRQDGTRSYFFtDEFLAQLFVDAGYEEVVNEYVFRE 202
Cdd:COG0500   142 LARLLLLATASLLELLLLLRLLALELYLRALLA-AAATEDLRSDALLESANALEYLLS 198
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 70-142 1.59e-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: 42.80  E-value: 1.59e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331036858  70 LRSCREQHPLYNAERCKVFQCDLTRddlLDHVPPESVDAVTLIFVLSAVHPEKMRlVLLNVYKVLKPGRSVLF 142
Cdd:cd02440    34 LELARKAAAALLADNVEVLKGDAEE---LPPEADESFDVIISDPPLHHLVEDLAR-FLEEARRLLKPGGVLVL 102
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 107-192 4.62e-04

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 39.72  E-value: 4.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331036858 107 DAVTLIFVLSAVHPekMRLVLLNVYKVLKPGRSVLFRDYGLNDHAmlrfkaGSKLGENFYVRQDGTRSYFFTDEFLAQLF 186
Cdd:pfam13489  82 DVIVAREVLEHVPD--PPALLRQIAALLKPGGLLLLSTPLASDEA------DRLLLEWPYLRPRNGHISLFSARSLKRLL 153


                  ....*.
gi 1331036858 187 VDAGYE 192
Cdd:pfam13489 154 EEAGFE 159
 
Name Accession Description Interval E-value
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 70-137 7.17e-07

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 46.02  E-value: 7.17e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331036858  70 LRSCREQHPLYNAeRCKVFQCDLTRDDLLDhvppESVDAVTLIFVLSAVHPEKMRLVLLNVYKVLKPG 137
Cdd:pfam13649  33 LERARERAAEAGL-NVEFVQGDAEDLPFPD----GSFDLVVSSGVLHHLPDPDLEAALREIARVLKPG 95
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 76-137 5.68e-06

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 43.90  E-value: 5.68e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331036858  76 QHPLYNAERCKVFQCDLTRDDlldhvpPESVDAVTLIFVLSavHPEKMRLVLLNVYKVLKPG 137
Cdd:pfam08242  42 ALGLLNAVRVELFQLDLGELD------PGSFDVVVASNVLH--HLADPRAVLRNIRRLLKPG 95
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 73-202 9.25e-06

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 44.91  E-value: 9.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331036858  73 CREQHPLYNAERCKVFQCDLTRddlLDHVPPESVDAVTLIFVLSAVHPEKMRLVLLNVYKVLKPGRSVLF--------RD 144
Cdd:COG0500    65 ARARAAKAGLGNVEFLVADLAE---LDPLPAESFDLVVAFGVLHHLPPEEREALLRELARALKPGGVLLLsasdaaaaLS 141

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1331036858 145 YGLNDHAMLRFKAGSKLGENFYVRQDGTRSYFFtDEFLAQLFVDAGYEEVVNEYVFRE 202
Cdd:COG0500   142 LARLLLLATASLLELLLLLRLLALELYLRALLA-AAATEDLRSDALLESANALEYLLS 198
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 70-142 1.59e-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: 42.80  E-value: 1.59e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331036858  70 LRSCREQHPLYNAERCKVFQCDLTRddlLDHVPPESVDAVTLIFVLSAVHPEKMRlVLLNVYKVLKPGRSVLF 142
Cdd:cd02440    34 LELARKAAAALLADNVEVLKGDAEE---LPPEADESFDVIISDPPLHHLVEDLAR-FLEEARRLLKPGGVLVL 102
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 107-192 4.62e-04

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 39.72  E-value: 4.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331036858 107 DAVTLIFVLSAVHPekMRLVLLNVYKVLKPGRSVLFRDYGLNDHAmlrfkaGSKLGENFYVRQDGTRSYFFTDEFLAQLF 186
Cdd:pfam13489  82 DVIVAREVLEHVPD--PPALLRQIAALLKPGGLLLLSTPLASDEA------DRLLLEWPYLRPRNGHISLFSARSLKRLL 153


                  ....*.
gi 1331036858 187 VDAGYE 192
Cdd:pfam13489 154 EEAGFE 159
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 68-154 1.68e-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: 37.67  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331036858  68 EELRSCREQHPlYNAERCKVFQCDLTRDDLldhvPPESVDAVTLIFVLSAV-HPEKmrlVLLNVYKVLKPGRSVLFRDYG 146
Cdd:COG2226    55 EMLELARERAA-EAGLNVEFVVGDAEDLPF----PDGSFDLVISSFVLHHLpDPER---ALAEIARVLKPGGRLVVVDFS 126


                  ....*...
gi 1331036858 147 LNDHAMLR 154
Cdd:COG2226   127 PPDLAELE 134
 
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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