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Conserved domains on  [gi|1958665191|ref|XP_038944154|]
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methyltransferase N6AMT1 isoform X1 [Rattus norvegicus]

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; ...
 10-148 6.23e-25

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: 94.20  E-value: 6.23e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665191  10 CTDINPKAAACTLETARCNRVHLQPVI---TDLVQGLLPRlkgKVDLLVFNPPYVVTPPEEVGSHGIEAAWAGGRNGREV 86
Cdd:PRK14968   50 GVDINPYAVECAKCNAKLNNIRNNGVEvirSDLFEPFRGD---KFDVILFNPPYLPTEEEEEWDDWLNYALSGGKDGREV 126

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958665191  87 MDRFFPLASQLLSPRGLFYLVTIKENNPEEIFKIMKTRGLQGTTALCRQAGQETLSVLRFSK 148
Cdd:PRK14968  127 IDRFLDEVGRYLKPGGRILLLQSSLTGEDEVLEYLEKLGFEAEVVAEEKFPFEELIVLELVK 188
 
Name Accession Description Interval E-value
PRK14968 PRK14968
putative methyltransferase; Provisional
 10-148 6.23e-25

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 94.20  E-value: 6.23e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665191  10 CTDINPKAAACTLETARCNRVHLQPVI---TDLVQGLLPRlkgKVDLLVFNPPYVVTPPEEVGSHGIEAAWAGGRNGREV 86
Cdd:PRK14968   50 GVDINPYAVECAKCNAKLNNIRNNGVEvirSDLFEPFRGD---KFDVILFNPPYLPTEEEEEWDDWLNYALSGGKDGREV 126

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958665191  87 MDRFFPLASQLLSPRGLFYLVTIKENNPEEIFKIMKTRGLQGTTALCRQAGQETLSVLRFSK 148
Cdd:PRK14968  127 IDRFLDEVGRYLKPGGRILLLQSSLTGEDEVLEYLEKLGFEAEVVAEEKFPFEELIVLELVK 188
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 11-127 6.11e-23

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: 88.76  E-value: 6.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665191  11 TDINPKAAACTLETARCNRVHLQPVITDLVQGLlprlKGKVDLLVFNPPYVVTPPEEVGSHGIEAAWAGGRNGREVMDRF 90
Cdd:TIGR00537  47 TDINPFAVKELRENAKLNNVGLDVVMTDLFKGV----RGKFDVILFNPPYLPLEDDLRRGDWLDVAIDGGKDGRKVIDRF 122

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1958665191  91 FPLASQLLSPRGLFYLVTIKENNPEEIFKIMKTRGLQ 127
Cdd:TIGR00537 123 LDELPEILKEGGRVQLIQSSLNGEPDTFDKLDERGFR 159
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 4-106 2.78e-09

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 54.00  E-value: 2.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665191   4 PQALYMCTDINPKAaactLETARCN--RVHLQPVIT----DLVQGLLPRlkGKVDLLVFNPPYV-----VTPPEEVGSHg 72
Cdd:COG2890   135 PDARVTAVDISPDA----LAVARRNaeRLGLEDRVRflqgDLFEPLPGD--GRFDLIVSNPPYIpedeiALLPPEVRDH- 207

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958665191  73 iEAAWA--GGRNGREVMDRFFPLASQLLSPRGLFYL 106
Cdd:COG2890   208 -EPRLAldGGEDGLDFYRRIIAQAPRLLKPGGWLLL 242
 
Name Accession Description Interval E-value
PRK14968 PRK14968
putative methyltransferase; Provisional
 10-148 6.23e-25

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 94.20  E-value: 6.23e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665191  10 CTDINPKAAACTLETARCNRVHLQPVI---TDLVQGLLPRlkgKVDLLVFNPPYVVTPPEEVGSHGIEAAWAGGRNGREV 86
Cdd:PRK14968   50 GVDINPYAVECAKCNAKLNNIRNNGVEvirSDLFEPFRGD---KFDVILFNPPYLPTEEEEEWDDWLNYALSGGKDGREV 126

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958665191  87 MDRFFPLASQLLSPRGLFYLVTIKENNPEEIFKIMKTRGLQGTTALCRQAGQETLSVLRFSK 148
Cdd:PRK14968  127 IDRFLDEVGRYLKPGGRILLLQSSLTGEDEVLEYLEKLGFEAEVVAEEKFPFEELIVLELVK 188
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 11-127 6.11e-23

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: 88.76  E-value: 6.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665191  11 TDINPKAAACTLETARCNRVHLQPVITDLVQGLlprlKGKVDLLVFNPPYVVTPPEEVGSHGIEAAWAGGRNGREVMDRF 90
Cdd:TIGR00537  47 TDINPFAVKELRENAKLNNVGLDVVMTDLFKGV----RGKFDVILFNPPYLPLEDDLRRGDWLDVAIDGGKDGRKVIDRF 122

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1958665191  91 FPLASQLLSPRGLFYLVTIKENNPEEIFKIMKTRGLQ 127
Cdd:TIGR00537 123 LDELPEILKEGGRVQLIQSSLNGEPDTFDKLDERGFR 159
PRK14967 PRK14967
putative methyltransferase; Provisional
 12-126 5.08e-16

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 71.62  E-value: 5.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665191  12 DINPKAAACTLETARCNRVHLQPVITDLVQGLLPRlkgKVDLLVFNPPYVVTPPEEVGSHGIEAAWAGGRNGREVMDRFF 91
Cdd:PRK14967   66 DISRRAVRSARLNALLAGVDVDVRRGDWARAVEFR---PFDVVVSNPPYVPAPPDAPPSRGPARAWDAGPDGRAVLDRLC 142

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958665191  92 PLASQLLSPRGLFYLVTIKENNPEEIFKIMKTRGL 126
Cdd:PRK14967  143 DAAPALLAPGGSLLLVQSELSGVERTLTRLSEAGL 177
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 4-106 2.78e-09

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 54.00  E-value: 2.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665191   4 PQALYMCTDINPKAaactLETARCN--RVHLQPVIT----DLVQGLLPRlkGKVDLLVFNPPYV-----VTPPEEVGSHg 72
Cdd:COG2890   135 PDARVTAVDISPDA----LAVARRNaeRLGLEDRVRflqgDLFEPLPGD--GRFDLIVSNPPYIpedeiALLPPEVRDH- 207

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958665191  73 iEAAWA--GGRNGREVMDRFFPLASQLLSPRGLFYL 106
Cdd:COG2890   208 -EPRLAldGGEDGLDFYRRIIAQAPRLLKPGGWLLL 242
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 4-110 1.39e-04

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: 40.17  E-value: 1.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665191   4 PQA-LYMcTDINPKAAACTLETARCN-----RVHLqpviTDLVQGLLPrlkGKVDLLVFNPPYvvtppeevgsHgieaaw 77
Cdd:COG2813    72 PEArVTL-VDVNARAVELARANAAANglenvEVLW----SDGLSGVPD---GSFDLILSNPPF----------H------ 127

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958665191  78 AGGRNGREVMDRFFPLASQLLSPRGLFYLVTIK 110
Cdd:COG2813   128 AGRAVDKEVAHALIADAARHLRPGGELWLVANR 160
 
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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