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Conserved domains on  [gi|1184637391|ref|WP_085198636|]
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class I SAM-dependent methyltransferase [Mycobacterium xenopi]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10549394)

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 Saccharomyces cerevisiae tRNA (carboxymethyluridine(34)-5-O)-methyltransferase

CATH:  2.20.25.110
EC:  2.1.1.-
PubMed:  12826405
SCOP:  3000118

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
53-140 1.44e-11

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


:

Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 59.22  E-value: 1.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184637391  53 VDLQTGGGEVLAGAATFPPTMAATESWPPNAALATRRLHPRGVVVVATRDEPpLPFADEAFDLVTSRHpiAVWWT----- 127
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREGLTFVVGDAED-LPFPDNSFDLVLSSE--VLHHVedper 77
                          90
                  ....*....|....*.
gi 1184637391 128 ---EIARVLRPGGTYL 140
Cdd:pfam08241  78 alrEIARVLKPGGILI 93
 
Name Accession Description Interval E-value
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
53-140 1.44e-11

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 59.22  E-value: 1.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184637391  53 VDLQTGGGEVLAGAATFPPTMAATESWPPNAALATRRLHPRGVVVVATRDEPpLPFADEAFDLVTSRHpiAVWWT----- 127
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREGLTFVVGDAED-LPFPDNSFDLVLSSE--VLHHVedper 77
                          90
                  ....*....|....*.
gi 1184637391 128 ---EIARVLRPGGTYL 140
Cdd:pfam08241  78 alrEIARVLKPGGILI 93
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
53-157 1.64e-09

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: 55.00  E-value: 1.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184637391  53 VDLQTGGGEVLAGAATFPPTMAATESWPPNAALATRRLHPRGVVVVATR-DEPPLPFADEAFDLVTSRH------PIAVW 125
Cdd:COG2226    27 LDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGLNVEFVVgDAEDLPFPDGSFDLVISSFvlhhlpDPERA 106
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1184637391 126 WTEIARVLRPGGTYLAQHIGPASVRELVEFFR 157
Cdd:COG2226   107 LAEIARVLKPGGRLVVVDFSPPDLAELEELLA 138
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
106-137 2.42e-03

bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 38.21  E-value: 2.42e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1184637391 106 LPFADEAFDLVT--------SRHPIAVwwTEIARVLRPGG 137
Cdd:PRK00216  115 LPFPDNSFDAVTiafglrnvPDIDKAL--REMYRVLKPGG 152
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
35-137 3.08e-03

ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of methyltransferases involved in the biosynthesis of menaquinone and ubiqinone. Some members such as the UbiE enzyme from E. coli are believed to act in both pathways, while others may act in only the menaquinone pathway. These methyltransferases are members of the UbiE/CoQ family of methyltransferases (pfam01209) which also contains ubiquinone methyltransferases and other methyltransferases. Members of this clade include a wide distribution of bacteria and eukaryotes, but no archaea. An outgroup for this clade is provided by the phosphatidylethanolamine methyltransferase (EC 2.1.1.17) from Rhodobacter sphaeroides. Note that a number of non-orthologous genes which are members of pfam03737 have been erroneously annotated as MenG methyltransferases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273884 [Multi-domain]  Cd Length: 223  Bit Score: 37.63  E-value: 3.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184637391  35 SWGYQRLMSQRLARASAA------VDLQTGGGEVLAGAATFPPTMA-ATESWPPNAALATRR----LHPRGVVVVAtrDE 103
Cdd:TIGR01934  20 SFGLHRLWRRRAVKLIGVfkgqkvLDVACGTGDLAIELAKSAPDRGkVTGVDFSSEMLEVAKkkseLPLNIEFIQA--DA 97
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1184637391 104 PPLPFADEAFDLVT--------SRHPIAVwwTEIARVLRPGG 137
Cdd:TIGR01934  98 EALPFEDNSFDAVTiafglrnvTDIQKAL--REMYRVLKPGG 137
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
53-142 3.36e-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: 36.25  E-value: 3.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184637391  53 VDLQTGGGEVLAGAATFPPTMA-ATESWPPNAALA---TRRLHPRGVVVVATRDEPPLPFADEAFDLVTSRHPIAVWWT- 127
Cdd:cd02440     3 LDLGCGTGALALALASGPGARVtGVDISPVALELArkaAAALLADNVEVLKGDAEELPPEADESFDVIISDPPLHHLVEd 82
                          90       100
                  ....*....|....*....|.
gi 1184637391 128 ------EIARVLRPGGTYLAQ 142
Cdd:cd02440    83 larfleEARRLLKPGGVLVLT 103
 
Name Accession Description Interval E-value
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
53-140 1.44e-11

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 59.22  E-value: 1.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184637391  53 VDLQTGGGEVLAGAATFPPTMAATESWPPNAALATRRLHPRGVVVVATRDEPpLPFADEAFDLVTSRHpiAVWWT----- 127
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREGLTFVVGDAED-LPFPDNSFDLVLSSE--VLHHVedper 77
                          90
                  ....*....|....*.
gi 1184637391 128 ---EIARVLRPGGTYL 140
Cdd:pfam08241  78 alrEIARVLKPGGILI 93
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
53-157 1.64e-09

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: 55.00  E-value: 1.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184637391  53 VDLQTGGGEVLAGAATFPPTMAATESWPPNAALATRRLHPRGVVVVATR-DEPPLPFADEAFDLVTSRH------PIAVW 125
Cdd:COG2226    27 LDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGLNVEFVVgDAEDLPFPDGSFDLVISSFvlhhlpDPERA 106
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1184637391 126 WTEIARVLRPGGTYLAQHIGPASVRELVEFFR 157
Cdd:COG2226   107 LAEIARVLKPGGRLVVVDFSPPDLAELEELLA 138
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
106-137 4.99e-06

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 44.09  E-value: 4.99e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1184637391 106 LPFADEAFDLVTSRHPIAVWWT--------EIARVLRPGG 137
Cdd:pfam13649  57 LPFPDGSFDLVVSSGVLHHLPDpdleaalrEIARVLKPGG 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
38-140 2.86e-05

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: 42.70  E-value: 2.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184637391  38 YQRLMSQRLARASAAVDLQTGGGEVLAGAATFPPTMAATESWPPNAALATRRLHPRGVVVVATrDEPPLPFADEAFDLVT 117
Cdd:COG2227    14 LAALLARLLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELNVDFVQG-DLEDLPLEDGSFDLVI 92
                          90       100
                  ....*....|....*....|....*....
gi 1184637391 118 SRHPI------AVWWTEIARVLRPGGTYL 140
Cdd:COG2227    93 CSEVLehlpdpAALLRELARLLKPGGLLL 121
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
106-137 2.42e-03

bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 38.21  E-value: 2.42e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1184637391 106 LPFADEAFDLVT--------SRHPIAVwwTEIARVLRPGG 137
Cdd:PRK00216  115 LPFPDNSFDAVTiafglrnvPDIDKAL--REMYRVLKPGG 152
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
35-137 3.08e-03

ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of methyltransferases involved in the biosynthesis of menaquinone and ubiqinone. Some members such as the UbiE enzyme from E. coli are believed to act in both pathways, while others may act in only the menaquinone pathway. These methyltransferases are members of the UbiE/CoQ family of methyltransferases (pfam01209) which also contains ubiquinone methyltransferases and other methyltransferases. Members of this clade include a wide distribution of bacteria and eukaryotes, but no archaea. An outgroup for this clade is provided by the phosphatidylethanolamine methyltransferase (EC 2.1.1.17) from Rhodobacter sphaeroides. Note that a number of non-orthologous genes which are members of pfam03737 have been erroneously annotated as MenG methyltransferases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273884 [Multi-domain]  Cd Length: 223  Bit Score: 37.63  E-value: 3.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184637391  35 SWGYQRLMSQRLARASAA------VDLQTGGGEVLAGAATFPPTMA-ATESWPPNAALATRR----LHPRGVVVVAtrDE 103
Cdd:TIGR01934  20 SFGLHRLWRRRAVKLIGVfkgqkvLDVACGTGDLAIELAKSAPDRGkVTGVDFSSEMLEVAKkkseLPLNIEFIQA--DA 97
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1184637391 104 PPLPFADEAFDLVT--------SRHPIAVwwTEIARVLRPGG 137
Cdd:TIGR01934  98 EALPFEDNSFDAVTiafglrnvTDIQKAL--REMYRVLKPGG 137
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
53-142 3.36e-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: 36.25  E-value: 3.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184637391  53 VDLQTGGGEVLAGAATFPPTMA-ATESWPPNAALA---TRRLHPRGVVVVATRDEPPLPFADEAFDLVTSRHPIAVWWT- 127
Cdd:cd02440     3 LDLGCGTGALALALASGPGARVtGVDISPVALELArkaAAALLADNVEVLKGDAEELPPEADESFDVIISDPPLHHLVEd 82
                          90       100
                  ....*....|....*....|.
gi 1184637391 128 ------EIARVLRPGGTYLAQ 142
Cdd:cd02440    83 larfleEARRLLKPGGVLVLT 103
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
94-165 6.00e-03

Predicted SAM-depedendent methyltransferase [General function prediction only];


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 36.38  E-value: 6.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184637391  94 GVVVVATRDEPpLPFADEAFDLVTSRH--------PIAVWWTEIARVLRPGGT----------YLAQHIGPASVRELVEF 155
Cdd:COG4627    29 GVDIVGDLTDP-LPFPDNSVDAIYSSHvlehldyeEAPLALKECYRVLKPGGIlrivvpdlehVARLYLAEYDAALDVAE 107
                          90
                  ....*....|
gi 1184637391 156 FRGPQPAAPR 165
Cdd:COG4627   108 LRLAGPIDPL 117
 
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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