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Conserved domains on  [gi|226693405|ref|NP_001152803|]
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methyltransferase N6AMT1 isoform 2 [Mus musculus]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 106779)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AdoMet_MTases super family cl17173
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 21-133 1.36e-19

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 PRK14968:

Pssm-ID: 473071 [Multi-domain]  Cd Length: 188  Bit Score: 79.94  E-value: 1.36e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693405  21 DVYEPAEDTFLLLDALEAAAAelagvEICLEVGAGSGVVSAFLASMiGPRALymCTDINPEAAACTLETARCNRVHVQPV 100
Cdd:PRK14968   4 EVYEPAEDSFLLAENAVDKKG-----DRVLEVGTGSGIVAIVAAKN-GKKVV--GVDINPYAVECAKCNAKLNNIRNNGV 75

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 226693405 101 I---TDLVHGLLPRlkgKVDLLVFNPPYVVTPPEER 133
Cdd:PRK14968  76 EvirSDLFEPFRGD---KFDVILFNPPYLPTEEEEE 108
 
Name Accession Description Interval E-value
PRK14968 PRK14968
putative methyltransferase; Provisional
 21-133 1.36e-19

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 79.94  E-value: 1.36e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693405  21 DVYEPAEDTFLLLDALEAAAAelagvEICLEVGAGSGVVSAFLASMiGPRALymCTDINPEAAACTLETARCNRVHVQPV 100
Cdd:PRK14968   4 EVYEPAEDSFLLAENAVDKKG-----DRVLEVGTGSGIVAIVAAKN-GKKVV--GVDINPYAVECAKCNAKLNNIRNNGV 75

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 226693405 101 I---TDLVHGLLPRlkgKVDLLVFNPPYVVTPPEER 133
Cdd:PRK14968  76 EvirSDLFEPFRGD---KFDVILFNPPYLPTEEEEE 108
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 22-133 2.07e-17

HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. This model represents an archaeal and eukaryotic protein family that lacks an N-terminal domain found in HemK and its eubacterial homologs. It is found in a single copy in the first six completed archaeal and eukaryotic genomes. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 129628 [Multi-domain]  Cd Length: 179  Bit Score: 74.12  E-value: 2.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693405   22 VYEPAEDTFLLLDALEAAAAelagvEICLEVGAGSGVVSAFLAsmiGPRALYMCTDINPEAAACTLETARCNRVHVQPVI 101
Cdd:TIGR00537   1 VYEPAEDSLLLEANLRELKP-----DDVLEIGAGTGLVAIRLK---GKGKCILTTDINPFAVKELRENAKLNNVGLDVVM 72

                          90       100       110
                  ....*....|....*....|....*....|..
gi 226693405  102 TDLVHGllprLKGKVDLLVFNPPYVVTPPEER 133
Cdd:TIGR00537  73 TDLFKG----VRGKFDVILFNPPYLPLEDDLR 100
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 50-136 9.47e-09

Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 52.07  E-value: 9.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693405  50 LEVGAGSGVVSAFLASMIgPRALYMCTDINPEAAACTLETARCNRVH--VQPVITDLVHGLLPRlkGKVDLLVFNPPYVv 127
Cdd:COG2890  117 LDLGTGSGAIALALAKER-PDARVTAVDISPDALAVARRNAERLGLEdrVRFLQGDLFEPLPGD--GRFDLIVSNPPYI- 192


                 ....*....
gi 226693405 128 tPPEERKSL 136
Cdd:COG2890  193 -PEDEIALL 200
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 50-124 1.58e-07

Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 47.59  E-value: 1.58e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226693405   50 LEVGAGSGVVSAFLASMiGPRALYMCTDINPEAAACTLETARCNRVH-VQPVITDLVHGLLPrlkGKVDLLVFNPP 124
Cdd:pfam05175  36 LDLGCGAGVLGAALAKE-SPDAELTMVDINARALESARENLAANGLEnGEVVASDVYSGVED---GKFDLIISNPP 107
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 50-138 3.13e-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: 40.49  E-value: 3.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693405  50 LEVGAGSGVVSAFLASMIGPRALymCTDINPEAAACTLETARCNRVHVQPVITDLVHGLLPRLKGKVDLLVFNPPYVVTP 129
Cdd:cd02440    3 LDLGCGTGALALALASGPGARVT--GVDISPVALELARKAAAALLADNVEVLKGDAEELPPEADESFDVIISDPPLHHLV 80


                 ....*....
gi 226693405 130 PEERKSLKQ 138
Cdd:cd02440   81 EDLARFLEE 89
 
Name Accession Description Interval E-value
PRK14968 PRK14968
putative methyltransferase; Provisional
 21-133 1.36e-19

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 79.94  E-value: 1.36e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693405  21 DVYEPAEDTFLLLDALEAAAAelagvEICLEVGAGSGVVSAFLASMiGPRALymCTDINPEAAACTLETARCNRVHVQPV 100
Cdd:PRK14968   4 EVYEPAEDSFLLAENAVDKKG-----DRVLEVGTGSGIVAIVAAKN-GKKVV--GVDINPYAVECAKCNAKLNNIRNNGV 75

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 226693405 101 I---TDLVHGLLPRlkgKVDLLVFNPPYVVTPPEER 133
Cdd:PRK14968  76 EvirSDLFEPFRGD---KFDVILFNPPYLPTEEEEE 108
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 22-133 2.07e-17

HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. This model represents an archaeal and eukaryotic protein family that lacks an N-terminal domain found in HemK and its eubacterial homologs. It is found in a single copy in the first six completed archaeal and eukaryotic genomes. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 129628 [Multi-domain]  Cd Length: 179  Bit Score: 74.12  E-value: 2.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693405   22 VYEPAEDTFLLLDALEAAAAelagvEICLEVGAGSGVVSAFLAsmiGPRALYMCTDINPEAAACTLETARCNRVHVQPVI 101
Cdd:TIGR00537   1 VYEPAEDSLLLEANLRELKP-----DDVLEIGAGTGLVAIRLK---GKGKCILTTDINPFAVKELRENAKLNNVGLDVVM 72

                          90       100       110
                  ....*....|....*....|....*....|..
gi 226693405  102 TDLVHGllprLKGKVDLLVFNPPYVVTPPEER 133
Cdd:TIGR00537  73 TDLFKG----VRGKFDVILFNPPYLPLEDDLR 100
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 50-126 3.49e-09

N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 53.24  E-value: 3.49e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226693405  50 LEVGAGSGVVSAFLASMIgPRALYMCTDINPEAaactLETARCNRVHVQPVITDLVHG--LLPRLKGKVDLLVFNPPYV 126
Cdd:PRK09328 113 LDLGTGSGAIALALAKER-PDAEVTAVDISPEA----LAVARRNAKHGLGARVEFLQGdwFEPLPGGRFDLIVSNPPYI 186
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 50-136 9.47e-09

Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 52.07  E-value: 9.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693405  50 LEVGAGSGVVSAFLASMIgPRALYMCTDINPEAAACTLETARCNRVH--VQPVITDLVHGLLPRlkGKVDLLVFNPPYVv 127
Cdd:COG2890  117 LDLGTGSGAIALALAKER-PDARVTAVDISPDALAVARRNAERLGLEdrVRFLQGDLFEPLPGD--GRFDLIVSNPPYI- 192


                 ....*....
gi 226693405 128 tPPEERKSL 136
Cdd:COG2890  193 -PEDEIALL 200
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 50-124 1.58e-07

Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 47.59  E-value: 1.58e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226693405   50 LEVGAGSGVVSAFLASMiGPRALYMCTDINPEAAACTLETARCNRVH-VQPVITDLVHGLLPrlkGKVDLLVFNPP 124
Cdd:pfam05175  36 LDLGCGAGVLGAALAKE-SPDAELTMVDINARALESARENLAANGLEnGEVVASDVYSGVED---GKFDLIISNPP 107
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 49-125 8.50e-07

16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA G1207 methylase RsmC is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 442062 [Multi-domain]  Cd Length: 191  Bit Score: 45.95  E-value: 8.50e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226693405  49 CLEVGAGSGVVSAFLASMIGPRALYMcTDINPEAAACTLETARCNRV-HVQPVITDLVHGLLPrlkGKVDLLVFNPPY 125
Cdd:COG2813   53 VLDLGCGYGVIGLALAKRNPEARVTL-VDVNARAVELARANAAANGLeNVEVLWSDGLSGVPD---GSFDLILSNPPF 126
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 49-125 1.72e-06

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 45.52  E-value: 1.72e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226693405  49 CLEVGAGSGVVSAFLASMIGPRALYMCtDINPEAAACTLETARCNRV--HVQPVITDLVHGLLPRLKGKVDLLVFNPPY 125
Cdd:COG4123   41 VLDLGTGTGVIALMLAQRSPGARITGV-EIQPEAAELARRNVALNGLedRITVIHGDLKEFAAELPPGSFDLVVSNPPY 118
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 50-136 1.47e-05

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 41.01  E-value: 1.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693405   50 LEVGAGSGVVSAFLASMIGprALYMCTDINPEAAACTLETARCNRVHVQPVITDLVHglLPRLKGKVDLLVFNPPYVVTP 129
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGG--ARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAED--LPFPDGSFDLVVSSGVLHHLP 77


                  ....*..
gi 226693405  130 PEERKSL 136
Cdd:pfam13649  78 DPDLEAA 84
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 50-138 3.13e-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: 40.49  E-value: 3.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693405  50 LEVGAGSGVVSAFLASMIGPRALymCTDINPEAAACTLETARCNRVHVQPVITDLVHGLLPRLKGKVDLLVFNPPYVVTP 129
Cdd:cd02440    3 LDLGCGTGALALALASGPGARVT--GVDISPVALELARKAAAALLADNVEVLKGDAEELPPEADESFDVIISDPPLHHLV 80


                 ....*....
gi 226693405 130 PEERKSLKQ 138
Cdd:cd02440   81 EDLARFLEE 89
PRK14967 PRK14967
putative methyltransferase; Provisional
 21-131 1.07e-04

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 40.42  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693405  21 DVYEPAEDTfLLLDALEAAAAELAGVEIcLEVGAGSGVVSAFLASMIGPRAlyMCTDINPEAAACTLETARCNRVHVqpv 100
Cdd:PRK14967  14 GVYRPQEDT-QLLADALAAEGLGPGRRV-LDLCTGSGALAVAAAAAGAGSV--TAVDISRRAVRSARLNALLAGVDV--- 86

                         90       100       110
                 ....*....|....*....|....*....|...
gi 226693405 101 itDLVHGLLPRL--KGKVDLLVFNPPYVVTPPE 131
Cdd:PRK14967  87 --DVRRGDWARAveFRPFDVVVSNPPYVPAPPD 117
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
50-120 1.22e-04

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 40.02  E-value: 1.22e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 226693405  50 LEVGAGSGVVSaFLASMIGPRALYMCtDINPEAAACTLETARCN----RVHvqpVITDLVHGLlpRLKGKVDLLV 120
Cdd:COG4076   40 LDIGTGSGLLS-MLAARAGAKKVYAV-EVNPDIAAVARRIIAANglsdRIT---VINADATDL--DLPEKADVII 107
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 50-136 4.36e-04

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 38.36  E-value: 4.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693405  50 LEVGAGSGVVSAFLASMIGPRalYMCTDINPEA-AACTLETARCNRVHVQPVITDLvHGLLPRLKGKVDLLVFNPPYVVT 128
Cdd:COG0500   31 LDLGCGTGRNLLALAARFGGR--VIGIDLSPEAiALARARAAKAGLGNVEFLVADL-AELDPLPAESFDLVVAFGVLHHL 107


                 ....*...
gi 226693405 129 PPEERKSL 136
Cdd:COG0500  108 PPEEREAL 115
PRK14966 PRK14966
unknown domain/N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase fusion protein; ...
 51-126 1.57e-03

unknown domain/N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase fusion protein; Provisional


Pssm-ID: 184930 [Multi-domain]  Cd Length: 423  Bit Score: 37.37  E-value: 1.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693405  51 EVGAGSGVVSAFLAsMIGPRALYMCTDINPEaaacTLETARCNRVHVQPVItDLVHGL-----LPRlKGKVDLLVFNPPY 125
Cdd:PRK14966 257 DLGTGSGAVAVTVA-LERPDAFVRASDISPP----ALETARKNAADLGARV-EFAHGSwfdtdMPS-EGKWDIIVSNPPY 329


                 .
gi 226693405 126 V 126
Cdd:PRK14966 330 I 330
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 50-93 5.16e-03

tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 N-methylase Trm61 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442009 [Multi-domain]  Cd Length: 249  Bit Score: 35.52  E-value: 5.16e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 226693405  50 LEVGAGSGVVSAFLASMIGPRALYMCTDINPEAAactlETARCN 93
Cdd:COG2519   96 LEAGTGSGALTLALARAVGPEGKVYSYERREDFA----EIARKN 135
 
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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