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Conserved domains on  [gi|1020136202|ref|WP_063259512|]
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MULTISPECIES: class I SAM-dependent methyltransferase [Bacillus]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10008163)

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

CATH:  3.40.50.150
EC:  2.1.1.-
PubMed:  12826405|12504684
SCOP:  3000118

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG3963 COG3963
Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];
1-185 7.36e-84

Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];


:

Pssm-ID: 443163  Cd Length: 193  Bit Score: 245.89  E-value: 7.36e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020136202   1 MQLITFLHEFIKHPKHTGAIAPSSKILAKKMVDVIDFNKAKCIVELGPGTGVFTKEIMKRKKKETIFLLIEINEVFYKEL 80
Cdd:COG3963     7 SDELLFLREFLRNPRTVGAIAPSSRALARAMASEVDWSGAGPVVELGPGTGVFTRAILARGVPDARLLAVEINPEFAEHL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020136202  81 KRKFKdeqNVIVVQGSAENIKKYKEEFNIECVDYVLSGLPFTSLPEEVSKLILNNVMEAIHENGEFITFQYSL---VKKG 157
Cdd:COG3963    87 RRRFP---RVTVVNGDAEDLAELLAEHGIGKVDAVVSGLPLLSFPPELRRAILDAAFRVLAPGGVFVQFTYSPrspVPRK 163
                         170       180
                  ....*....|....*....|....*...
gi 1020136202 158 FIQHFFPEITLEKVWLNFPPAYVFSCKK 185
Cdd:COG3963   164 LLRRGFEAVRSGFVWRNLPPARVYVCRK 191
 
Name Accession Description Interval E-value
COG3963 COG3963
Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];
1-185 7.36e-84

Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];


Pssm-ID: 443163  Cd Length: 193  Bit Score: 245.89  E-value: 7.36e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020136202   1 MQLITFLHEFIKHPKHTGAIAPSSKILAKKMVDVIDFNKAKCIVELGPGTGVFTKEIMKRKKKETIFLLIEINEVFYKEL 80
Cdd:COG3963     7 SDELLFLREFLRNPRTVGAIAPSSRALARAMASEVDWSGAGPVVELGPGTGVFTRAILARGVPDARLLAVEINPEFAEHL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020136202  81 KRKFKdeqNVIVVQGSAENIKKYKEEFNIECVDYVLSGLPFTSLPEEVSKLILNNVMEAIHENGEFITFQYSL---VKKG 157
Cdd:COG3963    87 RRRFP---RVTVVNGDAEDLAELLAEHGIGKVDAVVSGLPLLSFPPELRRAILDAAFRVLAPGGVFVQFTYSPrspVPRK 163
                         170       180
                  ....*....|....*....|....*...
gi 1020136202 158 FIQHFFPEITLEKVWLNFPPAYVFSCKK 185
Cdd:COG3963   164 LLRRGFEAVRSGFVWRNLPPARVYVCRK 191
rADc smart00650
Ribosomal RNA adenine dimethylases;
27-121 2.25e-09

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 54.05  E-value: 2.25e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020136202   27 LAKKMVDVIDFNKAKCIVELGPGTGVFTKEIMKRKKKETIfllIEINEVFYKELKRKFKDEQNVIVVQGSAENIKKYKEE 106
Cdd:smart00650   1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTA---IEIDPRLAPRLREKFAAADNLTVIHGDALKFDLPKLQ 77
                           90
                   ....*....|....*
gi 1020136202  107 FniecvDYVLSGLPF 121
Cdd:smart00650  78 P-----YKVVGNLPY 87
RrnaAD pfam00398
Ribosomal RNA adenine dimethylase;
24-121 5.41e-08

Ribosomal RNA adenine dimethylase;


Pssm-ID: 395321 [Multi-domain]  Cd Length: 263  Bit Score: 51.21  E-value: 5.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020136202  24 SKILAKKMVDVIDFNKAKCIVELGPGTGVFTKEIMKRKKKETiflLIEINEVFYKELKRKFKDEQNVIVVQGSAENIKKY 103
Cdd:pfam00398  15 DPKVINEIVDKANLRESDTVLEIGPGKGALTVILAKRAKQVV---AIEIDPRLAKLLQKKLSLDENLTVIHQDFLKFEFP 91
                          90
                  ....*....|....*...
gi 1020136202 104 KEEFNIECVDYVLSGLPF 121
Cdd:pfam00398  92 SLVTHIHQEFLVVGNLPY 109
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
43-132 1.20e-06

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: 45.11  E-value: 1.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020136202  43 IVELGPGTGVFTKEIMKRKKKEtiFLLIEINEVFYKELKRKF--KDEQNVIVVQGSAENIkkykEEFNIECVDYVLSGLP 120
Cdd:cd02440     2 VLDLGCGTGALALALASGPGAR--VTGVDISPVALELARKAAaaLLADNVEVLKGDAEEL----PPEADESFDVIISDPP 75
                          90
                  ....*....|..
gi 1020136202 121 FTSLPEEVSKLI 132
Cdd:cd02440    76 LHHLVEDLARFL 87
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
28-133 5.79e-06

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 45.28  E-value: 5.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020136202  28 AKKMVDVIDFNKAKCIVELGPGTGVFTKEIMKRKKKETIfllIEINEVFYKELKRKFKDEQNVIVVQGSAENIKkyKEEF 107
Cdd:PRK14896   18 VDRIVEYAEDTDGDPVLEIGPGKGALTDELAKRAKKVYA---IELDPRLAEFLRDDEIAAGNVEIIEGDALKVD--LPEF 92
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1020136202 108 NiecvdYVLSGLPF--TS------LPEEVSKLIL 133
Cdd:PRK14896   93 N-----KVVSNLPYqiSSpitfklLKHGFEPAVL 121
 
Name Accession Description Interval E-value
COG3963 COG3963
Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];
1-185 7.36e-84

Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];


Pssm-ID: 443163  Cd Length: 193  Bit Score: 245.89  E-value: 7.36e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020136202   1 MQLITFLHEFIKHPKHTGAIAPSSKILAKKMVDVIDFNKAKCIVELGPGTGVFTKEIMKRKKKETIFLLIEINEVFYKEL 80
Cdd:COG3963     7 SDELLFLREFLRNPRTVGAIAPSSRALARAMASEVDWSGAGPVVELGPGTGVFTRAILARGVPDARLLAVEINPEFAEHL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020136202  81 KRKFKdeqNVIVVQGSAENIKKYKEEFNIECVDYVLSGLPFTSLPEEVSKLILNNVMEAIHENGEFITFQYSL---VKKG 157
Cdd:COG3963    87 RRRFP---RVTVVNGDAEDLAELLAEHGIGKVDAVVSGLPLLSFPPELRRAILDAAFRVLAPGGVFVQFTYSPrspVPRK 163
                         170       180
                  ....*....|....*....|....*...
gi 1020136202 158 FIQHFFPEITLEKVWLNFPPAYVFSCKK 185
Cdd:COG3963   164 LLRRGFEAVRSGFVWRNLPPARVYVCRK 191
rADc smart00650
Ribosomal RNA adenine dimethylases;
27-121 2.25e-09

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 54.05  E-value: 2.25e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020136202   27 LAKKMVDVIDFNKAKCIVELGPGTGVFTKEIMKRKKKETIfllIEINEVFYKELKRKFKDEQNVIVVQGSAENIKKYKEE 106
Cdd:smart00650   1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTA---IEIDPRLAPRLREKFAAADNLTVIHGDALKFDLPKLQ 77
                           90
                   ....*....|....*
gi 1020136202  107 FniecvDYVLSGLPF 121
Cdd:smart00650  78 P-----YKVVGNLPY 87
RsmA COG0030
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ...
27-97 3.17e-08

16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) [Translation, ribosomal structure and biogenesis]; 16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 439801 [Multi-domain]  Cd Length: 270  Bit Score: 52.05  E-value: 3.17e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1020136202  27 LAKKMVDVIDFNKAKCIVELGPGTGVFTKEIMKRKKKetiFLLIEINEVFYKELKRKFKDEQNVIVVQGSA 97
Cdd:COG0030    25 IIRRIVDAAGITPGDTVLEIGPGLGALTRALLERAAR---VTAVEIDRRLAAILRETFAAYPNLTVIEGDA 92
RrnaAD pfam00398
Ribosomal RNA adenine dimethylase;
24-121 5.41e-08

Ribosomal RNA adenine dimethylase;


Pssm-ID: 395321 [Multi-domain]  Cd Length: 263  Bit Score: 51.21  E-value: 5.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020136202  24 SKILAKKMVDVIDFNKAKCIVELGPGTGVFTKEIMKRKKKETiflLIEINEVFYKELKRKFKDEQNVIVVQGSAENIKKY 103
Cdd:pfam00398  15 DPKVINEIVDKANLRESDTVLEIGPGKGALTVILAKRAKQVV---AIEIDPRLAKLLQKKLSLDENLTVIHQDFLKFEFP 91
                          90
                  ....*....|....*...
gi 1020136202 104 KEEFNIECVDYVLSGLPF 121
Cdd:pfam00398  92 SLVTHIHQEFLVVGNLPY 109
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
43-132 1.20e-06

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: 45.11  E-value: 1.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020136202  43 IVELGPGTGVFTKEIMKRKKKEtiFLLIEINEVFYKELKRKF--KDEQNVIVVQGSAENIkkykEEFNIECVDYVLSGLP 120
Cdd:cd02440     2 VLDLGCGTGALALALASGPGAR--VTGVDISPVALELARKAAaaLLADNVEVLKGDAEEL----PPEADESFDVIISDPP 75
                          90
                  ....*....|..
gi 1020136202 121 FTSLPEEVSKLI 132
Cdd:cd02440    76 LHHLVEDLARFL 87
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
28-133 5.79e-06

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 45.28  E-value: 5.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020136202  28 AKKMVDVIDFNKAKCIVELGPGTGVFTKEIMKRKKKETIfllIEINEVFYKELKRKFKDEQNVIVVQGSAENIKkyKEEF 107
Cdd:PRK14896   18 VDRIVEYAEDTDGDPVLEIGPGKGALTDELAKRAKKVYA---IELDPRLAEFLRDDEIAAGNVEIIEGDALKVD--LPEF 92
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1020136202 108 NiecvdYVLSGLPF--TS------LPEEVSKLIL 133
Cdd:PRK14896   93 N-----KVVSNLPYqiSSpitfklLKHGFEPAVL 121
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
43-144 1.49e-05

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 42.17  E-value: 1.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020136202  43 IVELGPGTGVFTKEIMKRKKKEtiFLLIEINEVFYKELKRKFKDEQ-NVIVVQGSAENIkkykeEFNIECVDYVLSGLPF 121
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGAR--VTGVDLSPEMLERARERAAEAGlNVEFVQGDAEDL-----PFPDGSFDLVVSSGVL 73
                          90       100
                  ....*....|....*....|...
gi 1020136202 122 TSLPEEVSKLILNNVMEAIHENG 144
Cdd:pfam13649  74 HHLPDPDLEAALREIARVLKPGG 96
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
27-126 4.44e-05

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: 41.52  E-value: 4.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020136202  27 LAKKMVDVIDFNKAKCIVELGPGTGVFTKEIMKRKKKetiFLLIEINEVFYKELKRKFKDEQ-NVIVVQGSAENIkkyke 105
Cdd:COG2226    10 GREALLAALGLRPGARVLDLGCGTGRLALALAERGAR---VTGVDISPEMLELARERAAEAGlNVEFVVGDAEDL----- 81
                          90       100
                  ....*....|....*....|.
gi 1020136202 106 EFNIECVDYVLSGLPFTSLPE 126
Cdd:COG2226    82 PFPDGSFDLVISSFVLHHLPD 102
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
36-147 8.30e-04

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 38.74  E-value: 8.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020136202  36 DFNKAKCIVELGPGTGVFTKEIMKRKKKEtiFLLIEINEVFYKELKRKFKDE--QNVIVVQGSAENIKKYKEEFniecVD 113
Cdd:COG0500    23 RLPKGGRVLDLGCGTGRNLLALAARFGGR--VIGIDLSPEAIALARARAAKAglGNVEFLVADLAELDPLPAES----FD 96
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1020136202 114 YVLSGLPFTSLPEEVSKLILNNVMEAIHENGEFI 147
Cdd:COG0500    97 LVVAFGVLHHLPPEEREALLRELARALKPGGVLL 130
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
35-121 2.78e-03

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: 37.43  E-value: 2.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020136202  35 IDFNKAKCIVELGPGTGVFTkeIM--KRKKKETIfLLIEINEVFYKELKRKFKD---EQNVIVVQGSaenIKKYKEEFNI 109
Cdd:COG4123    33 APVKKGGRVLDLGTGTGVIA--LMlaQRSPGARI-TGVEIQPEAAELARRNVALnglEDRITVIHGD---LKEFAAELPP 106
                          90
                  ....*....|..
gi 1020136202 110 ECVDYVLSGLPF 121
Cdd:COG4123   107 GSFDLVVSNPPY 118
 
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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