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Conserved domains on  [gi|503241207|ref|WP_013475868|]
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MULTISPECIES: methyltransferase [Micromonospora]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10008106)

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 electron transfer flavoprotein beta subunit lysine methyltransferase

CATH:  3.40.50.150
EC:  2.1.1.-
Gene Ontology:  GO:1904047|GO:0008168|GO:0032259|GO:0008757
PubMed:  12826405|12504684
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 21-224 2.18e-59

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 185.86  E-value: 2.18e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503241207  21 PDRLRLVgTPFVPEVRLYLAEDAILWWARMEAAAGR-SLPPPYWASVWAGGQALARHLLDHPELAaGRRVLDLGAGSGLV 99
Cdd:COG3897    7 RANTRLE-TVLVPEIRLHLAADAHPLWDATEEALGEsGAPPPFWAFLWPSGQALARYLLDHPEVA-GKRVLELGCGLGLV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503241207 100 AIAAALAGADQVIANDIDPYAVAAVTVNARANRVRVTADGADLLDG--VTGADLLVAGDALYDAGLAARVLPYLRRCAAH 177
Cdd:COG3897   85 GIAAAKAGAADVTATDYDPEALAALRLNAALNGVAITTRLGDWRDPpaAGGFDLILGGDVLYERDLAEPLLPFLDRLAAP 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 503241207 178 GVQVLVGDPDRGHLPP--DGLELVASYPVPTTEPSVDSPVRRVQVLRPR 224
Cdd:COG3897  165 GGEVLIGDPGRGYLPAfrERLEALAGYEVVTRELEDTEKVKRGRVLRLR 213
 
Name Accession Description Interval E-value
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 21-224 2.18e-59

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 185.86  E-value: 2.18e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503241207  21 PDRLRLVgTPFVPEVRLYLAEDAILWWARMEAAAGR-SLPPPYWASVWAGGQALARHLLDHPELAaGRRVLDLGAGSGLV 99
Cdd:COG3897    7 RANTRLE-TVLVPEIRLHLAADAHPLWDATEEALGEsGAPPPFWAFLWPSGQALARYLLDHPEVA-GKRVLELGCGLGLV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503241207 100 AIAAALAGADQVIANDIDPYAVAAVTVNARANRVRVTADGADLLDG--VTGADLLVAGDALYDAGLAARVLPYLRRCAAH 177
Cdd:COG3897   85 GIAAAKAGAADVTATDYDPEALAALRLNAALNGVAITTRLGDWRDPpaAGGFDLILGGDVLYERDLAEPLLPFLDRLAAP 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 503241207 178 GVQVLVGDPDRGHLPP--DGLELVASYPVPTTEPSVDSPVRRVQVLRPR 224
Cdd:COG3897  165 GGEVLIGDPGRGYLPAfrERLEALAGYEVVTRELEDTEKVKRGRVLRLR 213
PRK14967 PRK14967
putative methyltransferase; Provisional
 83-154 6.51e-04

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 39.65  E-value: 6.51e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503241207  83 LAAGRRVLDLGAGSGLVAIAAALAGADQVIANDIDPYAVAAVTVNARANRVRVTADGADLLDGVTGA--DLLVA 154
Cdd:PRK14967  34 LGPGRRVLDLCTGSGALAVAAAAAGAGSVTAVDISRRAVRSARLNALLAGVDVDVRRGDWARAVEFRpfDVVVS 107
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 77-148 7.77e-04

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: 39.07  E-value: 7.77e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503241207   77 LLDHPELAAGRRVLDLGAGSGLvAIAAALAGADQVIANDIDPYAVAAVTVNARANRVRVTADGADLLDGVTG 148
Cdd:TIGR00537  11 LEANLRELKPDDVLEIGAGTGL-VAIRLKGKGKCILTTDINPFAVKELRENAKLNNVGLDVVMTDLFKGVRG 81
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 88-183 3.83e-03

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: 35.87  E-value: 3.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503241207  88 RVLDLGAGSGLVAIAAALAGADQVIANDIDPYAVA-AVTVNARANRVRVT---ADGADLL-DGVTGADLLVAGDAL-YDA 161
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVALElARKAAAALLADNVEvlkGDAEELPpEADESFDVIISDPPLhHLV 80

                         90       100
                 ....*....|....*....|..
gi 503241207 162 GLAARVLPYLRRCAAHGVQVLV 183
Cdd:cd02440   81 EDLARFLEEARRLLKPGGVLVL 102
 
Name Accession Description Interval E-value
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 21-224 2.18e-59

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 185.86  E-value: 2.18e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503241207  21 PDRLRLVgTPFVPEVRLYLAEDAILWWARMEAAAGR-SLPPPYWASVWAGGQALARHLLDHPELAaGRRVLDLGAGSGLV 99
Cdd:COG3897    7 RANTRLE-TVLVPEIRLHLAADAHPLWDATEEALGEsGAPPPFWAFLWPSGQALARYLLDHPEVA-GKRVLELGCGLGLV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503241207 100 AIAAALAGADQVIANDIDPYAVAAVTVNARANRVRVTADGADLLDG--VTGADLLVAGDALYDAGLAARVLPYLRRCAAH 177
Cdd:COG3897   85 GIAAAKAGAADVTATDYDPEALAALRLNAALNGVAITTRLGDWRDPpaAGGFDLILGGDVLYERDLAEPLLPFLDRLAAP 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 503241207 178 GVQVLVGDPDRGHLPP--DGLELVASYPVPTTEPSVDSPVRRVQVLRPR 224
Cdd:COG3897  165 GGEVLIGDPGRGYLPAfrERLEALAGYEVVTRELEDTEKVKRGRVLRLR 213
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
71-154 1.67e-05

Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 44.78  E-value: 1.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503241207  71 QALARHLLdhpelaAGRRVLDLGAGSglvaiaaalagADQVIANDIDPYAVAAVTVNARANRV--RVTADGADLLDGVTg 148
Cdd:COG2264  140 EALEKLLK------PGKTVLDVGCGSgilaiaaaklgAKRVLAVDIDPVAVEAARENAELNGVedRIEVVLGDLLEDGP- 212


                 ....*.
gi 503241207 149 ADLLVA 154
Cdd:COG2264  213 YDLVVA 218
PRK14967 PRK14967
putative methyltransferase; Provisional
 83-154 6.51e-04

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 39.65  E-value: 6.51e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503241207  83 LAAGRRVLDLGAGSGLVAIAAALAGADQVIANDIDPYAVAAVTVNARANRVRVTADGADLLDGVTGA--DLLVA 154
Cdd:PRK14967  34 LGPGRRVLDLCTGSGALAVAAAAAGAGSVTAVDISRRAVRSARLNALLAGVDVDVRRGDWARAVEFRpfDVVVS 107
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 77-148 7.77e-04

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: 39.07  E-value: 7.77e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503241207   77 LLDHPELAAGRRVLDLGAGSGLvAIAAALAGADQVIANDIDPYAVAAVTVNARANRVRVTADGADLLDGVTG 148
Cdd:TIGR00537  11 LEANLRELKPDDVLEIGAGTGL-VAIRLKGKGKCILTTDINPFAVKELRENAKLNNVGLDVVMTDLFKGVRG 81
PRK14968 PRK14968
putative methyltransferase; Provisional
 73-148 1.22e-03

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 38.34  E-value: 1.22e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503241207  73 LARHLLDHPelaaGRRVLDLGAGSGLVAIAAALAGADqVIANDIDPYAVAAVTVNARANRVR---VTADGADLLDGVTG 148
Cdd:PRK14968  15 LAENAVDKK----GDRVLEVGTGSGIVAIVAAKNGKK-VVGVDINPYAVECAKCNAKLNNIRnngVEVIRSDLFEPFRG 88
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
71-154 2.15e-03

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 38.21  E-value: 2.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503241207  71 QALARHLLdhpelaAGRRVLDLGAGSGLVAIAAALAGADQVIANDIDPYAVAAVTVNARANRVRvtaDGADLLDGVTGAD 150
Cdd:PRK00517 111 EALEKLVL------PGKTVLDVGCGSGILAIAAAKLGAKKVLAVDIDPQAVEAARENAELNGVE---LNVYLPQGDLKAD 181


                 ....
gi 503241207 151 LLVA 154
Cdd:PRK00517 182 VIVA 185
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 88-183 3.83e-03

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: 35.87  E-value: 3.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503241207  88 RVLDLGAGSGLVAIAAALAGADQVIANDIDPYAVA-AVTVNARANRVRVT---ADGADLL-DGVTGADLLVAGDAL-YDA 161
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVALElARKAAAALLADNVEvlkGDAEELPpEADESFDVIISDPPLhHLV 80

                         90       100
                 ....*....|....*....|..
gi 503241207 162 GLAARVLPYLRRCAAHGVQVLV 183
Cdd:cd02440   81 EDLARFLEEARRLLKPGGVLVL 102
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
85-183 6.00e-03

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 35.18  E-value: 6.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503241207  85 AGRRVLDLGAGS-GLVAIAAALAGADQVIANDIDPYAVAAvtvnARANRVRVTADGADL--LDGVTGADLLVAGDALYDA 161
Cdd:COG4106    1 PPRRVLDLGCGTgRLTALLAERFPGARVTGVDLSPEMLAR----ARARLPNVRFVVADLrdLDPPEPFDLVVSNAALHWL 76

                         90       100
                 ....*....|....*....|..
gi 503241207 162 GLAARVLPYLRRCAAHGVQVLV 183
Cdd:COG4106   77 PDHAALLARLAAALAPGGVLAV 98
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 72-187 9.23e-03

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: 34.99  E-value: 9.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503241207  72 ALARHLLDHpeLAAGRRVLDLGAGSGLVAIAAALAGADqVIANDIDPYAVAAVTVNARANRVR-VTADGADLLDGVTGAD 150
Cdd:COG2227   13 RLAALLARL--LPAGGRVLDVGCGTGRLALALARRGAD-VTGVDISPEALEIARERAAELNVDfVQGDLEDLPLEDGSFD 89

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 503241207 151 LLVAGDALYDAGLAARVLPYLRRCAAHGVQVLVGDPD 187
Cdd:COG2227   90 LVICSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
 
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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