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Conserved domains on  [gi|818871930|gb|KKW08122|]
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Methyltransferase FkbM [Candidatus Kaiserbacteria bacterium GW2011_GWC2_49_12]

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; ...
 61-197 2.44e-31

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 TIGR01444:

Pssm-ID: 473071  Cd Length: 143  Bit Score: 112.79  E-value: 2.44e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818871930   61 TVVDIGAHIGYFTRLAGkRVGLNGHVYAFEPDPNNRLLLEKNVGRYPSVMVSPE--AITSKVGSVSFYHVHGSTGCHSTI 138
Cdd:TIGR01444   1 VVIDVGANIGDTSLYFA-RKGAEGRVIAFEPLPDAYEILEENVKLNNLPNVVLLnaAVGDRDGELEFNVSDDDTGNSSLL 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818871930  139 QQP---NASEFTVPATTLDAFVEARKITHIDVIKMDIEGGEWAAFEGMRNVLKQRSLSIIME 197
Cdd:TIGR01444  80 PTPdadRESEIEVEVVTLDDLVEEFGLDKVDLLKIDVEGAELEVLRGAAETLLEKRPVIVLE 141
 
Name Accession Description Interval E-value
fkbM_fam TIGR01444
methyltransferase, FkbM family; Members of this family are characterized by two well-conserved ...
 61-197 2.44e-31

methyltransferase, FkbM family; Members of this family are characterized by two well-conserved short regions separated by a variable in both sequence and length. The first of the two regions is found in a large number of proteins outside this subfamily, a number of which have been characterized as methyltransferases. One member of the present family, FkbM, was shown to be required for a specific methylation in the biosynthesis of the immunosuppressant FK506 in Streptomyces strain MA6548.


Pssm-ID: 273628  Cd Length: 143  Bit Score: 112.79  E-value: 2.44e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818871930   61 TVVDIGAHIGYFTRLAGkRVGLNGHVYAFEPDPNNRLLLEKNVGRYPSVMVSPE--AITSKVGSVSFYHVHGSTGCHSTI 138
Cdd:TIGR01444   1 VVIDVGANIGDTSLYFA-RKGAEGRVIAFEPLPDAYEILEENVKLNNLPNVVLLnaAVGDRDGELEFNVSDDDTGNSSLL 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818871930  139 QQP---NASEFTVPATTLDAFVEARKITHIDVIKMDIEGGEWAAFEGMRNVLKQRSLSIIME 197
Cdd:TIGR01444  80 PTPdadRESEIEVEVVTLDDLVEEFGLDKVDLLKIDVEGAELEVLRGAAETLLEKRPVIVLE 141
Methyltransf_21 pfam05050
Methyltransferase FkbM domain; This family has members from bacteria to human, and appears to ...
 64-222 4.21e-25

Methyltransferase FkbM domain; This family has members from bacteria to human, and appears to be a methyltransferase.


Pssm-ID: 428282  Cd Length: 170  Bit Score: 97.64  E-value: 4.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818871930   64 DIGAHIG---YFTRLAGKRVGLNGHVYAFEPDPNNrllLEKNVGRYPSVmvspeAITSKVGSVSFYHVHGSTGC------ 134
Cdd:pfam05050   1 DVGANDGvwdSVALLFEKKCGGGGEVLAIEPNPNK---LEKLDCTLLNL-----ALGNDVGLYEFYLGGKGGGGyllfav 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818871930  135 --------HSTIQQPNASEFTVPATTLDAFVEARKITHIDVIKMDIEGGEWAAFEGMRNVLKQRSLSIIMEWKPDALTQG 206
Cdd:pfam05050  73 gdpqgastSSVLGGEEAKYIEVETVTLDSFLEEIKKSDIDLLKIDVEGAELEVLEGAEKTLKRCQPNIIVIEVHFFHYFG 152

                         170
                  ....*....|....*.
gi 818871930  207 AHDPETLLSMLMHEGF 222
Cdd:pfam05050 153 GPLFDEIRQFLRECGY 168
COG4798 COG4798
Predicted methyltransferase [General function prediction only];
56-188 1.45e-05

Predicted methyltransferase [General function prediction only];


Pssm-ID: 443826  Cd Length: 274  Bit Score: 45.29  E-value: 1.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818871930  56 ITPGMTVVDIGAHIGYFTRLAGKRVGLNGHVYAFEPDPNNRL--LLEKNVGRYPSVMVSPEAITSKVGSVSFYHvhgstg 133
Cdd:COG4798   64 VKPGMTVVEIWPGGGWYTEILAPYLGPKGKVYAANFDPDSEPpeYAKRSREAFSAKLAADPALYGNVRVTAFAP------ 137

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 818871930 134 chstiqqpnASEFTVPATTLDAFVEARkITHiDVIKMDIEGgewAAFEGMRNVLK 188
Cdd:COG4798  138 ---------PDDPIAPPGSADLVLTFR-NYH-NWYRAGDAA---AMFAAFFKALK 178
rrmJ PRK11188
23S rRNA (uridine(2552)-2'-O)-methyltransferase RlmE;
46-88 1.08e-03

23S rRNA (uridine(2552)-2'-O)-methyltransferase RlmE;


Pssm-ID: 183025  Cd Length: 209  Bit Score: 39.33  E-value: 1.08e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 818871930  46 RETTRLFKtiitPGMTVVDIGAHIGYFTRLAGKRVGLNGHVYA 88
Cdd:PRK11188  43 QQSDKLFK----PGMTVVDLGAAPGGWSQYAVTQIGDKGRVIA 81
 
Name Accession Description Interval E-value
fkbM_fam TIGR01444
methyltransferase, FkbM family; Members of this family are characterized by two well-conserved ...
 61-197 2.44e-31

methyltransferase, FkbM family; Members of this family are characterized by two well-conserved short regions separated by a variable in both sequence and length. The first of the two regions is found in a large number of proteins outside this subfamily, a number of which have been characterized as methyltransferases. One member of the present family, FkbM, was shown to be required for a specific methylation in the biosynthesis of the immunosuppressant FK506 in Streptomyces strain MA6548.


Pssm-ID: 273628  Cd Length: 143  Bit Score: 112.79  E-value: 2.44e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818871930   61 TVVDIGAHIGYFTRLAGkRVGLNGHVYAFEPDPNNRLLLEKNVGRYPSVMVSPE--AITSKVGSVSFYHVHGSTGCHSTI 138
Cdd:TIGR01444   1 VVIDVGANIGDTSLYFA-RKGAEGRVIAFEPLPDAYEILEENVKLNNLPNVVLLnaAVGDRDGELEFNVSDDDTGNSSLL 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818871930  139 QQP---NASEFTVPATTLDAFVEARKITHIDVIKMDIEGGEWAAFEGMRNVLKQRSLSIIME 197
Cdd:TIGR01444  80 PTPdadRESEIEVEVVTLDDLVEEFGLDKVDLLKIDVEGAELEVLRGAAETLLEKRPVIVLE 141
Methyltransf_21 pfam05050
Methyltransferase FkbM domain; This family has members from bacteria to human, and appears to ...
 64-222 4.21e-25

Methyltransferase FkbM domain; This family has members from bacteria to human, and appears to be a methyltransferase.


Pssm-ID: 428282  Cd Length: 170  Bit Score: 97.64  E-value: 4.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818871930   64 DIGAHIG---YFTRLAGKRVGLNGHVYAFEPDPNNrllLEKNVGRYPSVmvspeAITSKVGSVSFYHVHGSTGC------ 134
Cdd:pfam05050   1 DVGANDGvwdSVALLFEKKCGGGGEVLAIEPNPNK---LEKLDCTLLNL-----ALGNDVGLYEFYLGGKGGGGyllfav 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818871930  135 --------HSTIQQPNASEFTVPATTLDAFVEARKITHIDVIKMDIEGGEWAAFEGMRNVLKQRSLSIIMEWKPDALTQG 206
Cdd:pfam05050  73 gdpqgastSSVLGGEEAKYIEVETVTLDSFLEEIKKSDIDLLKIDVEGAELEVLEGAEKTLKRCQPNIIVIEVHFFHYFG 152

                         170
                  ....*....|....*.
gi 818871930  207 AHDPETLLSMLMHEGF 222
Cdd:pfam05050 153 GPLFDEIRQFLRECGY 168
COG4798 COG4798
Predicted methyltransferase [General function prediction only];
56-188 1.45e-05

Predicted methyltransferase [General function prediction only];


Pssm-ID: 443826  Cd Length: 274  Bit Score: 45.29  E-value: 1.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818871930  56 ITPGMTVVDIGAHIGYFTRLAGKRVGLNGHVYAFEPDPNNRL--LLEKNVGRYPSVMVSPEAITSKVGSVSFYHvhgstg 133
Cdd:COG4798   64 VKPGMTVVEIWPGGGWYTEILAPYLGPKGKVYAANFDPDSEPpeYAKRSREAFSAKLAADPALYGNVRVTAFAP------ 137

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 818871930 134 chstiqqpnASEFTVPATTLDAFVEARkITHiDVIKMDIEGgewAAFEGMRNVLK 188
Cdd:COG4798  138 ---------PDDPIAPPGSADLVLTFR-NYH-NWYRAGDAA---AMFAAFFKALK 178
RlmE COG0293
23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and ...
 55-88 3.03e-04

23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and biogenesis]; 23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 440062 [Multi-domain]  Cd Length: 208  Bit Score: 40.82  E-value: 3.03e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 818871930  55 IITPGMTVVDIGAHIGYFTRLAGKRVGLNGHVYA 88
Cdd:COG0293   47 LIKPGMRVVDLGAAPGGWSQVAAKRVGGKGRVIA 80
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 37-93 4.88e-04

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: 39.21  E-value: 4.88e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 818871930  37 FEMLAGLYERETTRLFKTIITPGMTVVDIGAHIGYFTRLAGKRvglNGHVYAFEPDP 93
Cdd:COG2226    1 FDRVAARYDGREALLAALGLRPGARVLDLGCGTGRLALALAER---GARVTGVDISP 54
rrmJ PRK11188
23S rRNA (uridine(2552)-2'-O)-methyltransferase RlmE;
46-88 1.08e-03

23S rRNA (uridine(2552)-2'-O)-methyltransferase RlmE;


Pssm-ID: 183025  Cd Length: 209  Bit Score: 39.33  E-value: 1.08e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 818871930  46 RETTRLFKtiitPGMTVVDIGAHIGYFTRLAGKRVGLNGHVYA 88
Cdd:PRK11188  43 QQSDKLFK----PGMTVVDLGAAPGGWSQYAVTQIGDKGRVIA 81
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 56-124 1.10e-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: 39.37  E-value: 1.10e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818871930  56 ITPGMTVVDIGAHIGYFT-RLAgKRVGLNGHVYAFEPDPNNRLLLEKNVGRYpsvmVSPEAITSKVGSVS 124
Cdd:COG2519   89 IFPGARVLEAGTGSGALTlALA-RAVGPEGKVYSYERREDFAEIARKNLERF----GLPDNVELKLGDIR 153
 
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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