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Conserved domains on  [gi|446531593|ref|WP_000608939|]
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MULTISPECIES: malonyl-ACP O-methyltransferase BioC [Bacillus]

Protein Classification

malonyl-ACP O-methyltransferase( domain architecture ID 11493568)

malonyl-[acyl-carrier protein] O-methyltransferase BioC is a class I SAM-dependent methyltransferase in the biotin biosynthesis pathway that converts the free carboxyl group of a malonyl-thioester to its methyl ester 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
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 10-265 1.17e-86

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


:

Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 257.99  E-value: 1.17e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593   10 RFNVAAVSYDQYANVQKKMAHSLLSVL-NRRYSETssIRILELGCGTGYVTEKLSNLFPKAHITAIDFAESMIAVAKTRQ 88
Cdd:TIGR02072   1 SFNKAAKTYDRHAKIQREMAKRLLALLkEKGIFIP--ASVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTKL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593   89 NvKNVTFHCEDIERLRLEE-SYDVIISNATFQWLNDLKQVIRNLFHHLSTDGILLFSTFGQETFQELHNSFRRakeekni 167
Cdd:TIGR02072  79 S-ENVQFICGDAEKLPLEDsSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQSFGQ------- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593  168 rneiaIGQRFYSKDQLRHICKIETGDVHVSETCYIESFAEVREFLHSIRKVGATNSNEESycQSPSLFRAMLRIYERDFT 247
Cdd:TIGR02072 151 -----HGLRYLSLDELKALLKNSFELLTLEEELITLSFDDPLDVLRHLKKTGANGLSSGR--TSRKQLKAFLERYEQEFQ 223

                         250
                  ....*....|....*...
gi 446531593  248 gNEGIMATYHALFTYITK 265
Cdd:TIGR02072 224 -PDGLPLTYHVVYGIAKK 240
 
Name Accession Description Interval E-value
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 10-265 1.17e-86

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 257.99  E-value: 1.17e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593   10 RFNVAAVSYDQYANVQKKMAHSLLSVL-NRRYSETssIRILELGCGTGYVTEKLSNLFPKAHITAIDFAESMIAVAKTRQ 88
Cdd:TIGR02072   1 SFNKAAKTYDRHAKIQREMAKRLLALLkEKGIFIP--ASVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTKL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593   89 NvKNVTFHCEDIERLRLEE-SYDVIISNATFQWLNDLKQVIRNLFHHLSTDGILLFSTFGQETFQELHNSFRRakeekni 167
Cdd:TIGR02072  79 S-ENVQFICGDAEKLPLEDsSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQSFGQ------- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593  168 rneiaIGQRFYSKDQLRHICKIETGDVHVSETCYIESFAEVREFLHSIRKVGATNSNEESycQSPSLFRAMLRIYERDFT 247
Cdd:TIGR02072 151 -----HGLRYLSLDELKALLKNSFELLTLEEELITLSFDDPLDVLRHLKKTGANGLSSGR--TSRKQLKAFLERYEQEFQ 223

                         250
                  ....*....|....*...
gi 446531593  248 gNEGIMATYHALFTYITK 265
Cdd:TIGR02072 224 -PDGLPLTYHVVYGIAKK 240
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
47-145 2.57e-38

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 129.94  E-value: 2.57e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593  47 RILELGCGTGYVTEKLSNLFPKAHITAIDFAESMIAVAktRQNVKNVTFHCEDIERLRLEESYDVIISNATFQWLNDLKQ 126
Cdd:COG4106    4 RVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARA--RARLPNVRFVVADLRDLDPPEPFDLVVSNAALHWLPDHAA 81

                         90
                 ....*....|....*....
gi 446531593 127 VIRNLFHHLSTDGILLFST 145
Cdd:COG4106   82 LLARLAAALAPGGVLAVQV 100
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 48-139 9.23e-25

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 94.55  E-value: 9.23e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593   48 ILELGCGTGYVTEKLSNLFpKAHITAIDFAESMIAVAKTR--QNVKNVTFHCEDIERLRLE-ESYDVIISNATFQWLN-- 122
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRG-GARVTGVDLSPEMLERARERaaEAGLNVEFVQGDAEDLPFPdGSFDLVVSSGVLHHLPdp 79

                          90
                  ....*....|....*..
gi 446531593  123 DLKQVIRNLFHHLSTDG 139
Cdd:pfam13649  80 DLEAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 47-146 1.42e-19

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: 81.32  E-value: 1.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593  47 RILELGCGTGYVTEKLSNlFPKAHITAIDFAESMIAVAKTRQ---NVKNVTFHCEDIERLRLE--ESYDVIISNATFQWL 121
Cdd:cd02440    1 RVLDLGCGTGALALALAS-GPGARVTGVDISPVALELARKAAaalLADNVEVLKGDAEELPPEadESFDVIISDPPLHHL 79

                         90       100
                 ....*....|....*....|....*.
gi 446531593 122 -NDLKQVIRNLFHHLSTDGILLFSTF 146
Cdd:cd02440   80 vEDLARFLEEARRLLKPGGVLVLTLV 105
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 2-261 2.72e-18

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 81.73  E-value: 2.72e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593   2 INKTLLQKRFNVAAVSYDQYANVQKKMAHSLLSVLNRRYSETssirILELGCGTG----YVTEKLSnlfpkaHITAIDFA 77
Cdd:PRK10258   4 VNKQAIAAAFGRAAAHYEQHAELQRQSADALLAMLPQRKFTH----VLDAGCGPGwmsrYWRERGS------QVTALDLS 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593  78 ESMIAVAKTRQNVKNvtFHCEDIERLRLEE-SYDVIISNATFQWLNDLKQVIRNLFHHLSTDGILLFSTFGQETFQELHN 156
Cdd:PRK10258  74 PPMLAQARQKDAADH--YLAGDIESLPLATaTFDLAWSNLAVQWCGNLSTALRELYRVVRPGGVVAFTTLVQGSLPELHQ 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593 157 SFrRAKEEKNIRNeiaigqRFYSKDQLRHICK--IETGDVHVSETCYIESFAEVReflhSIRKVGATNSNEESycQSPSL 234
Cdd:PRK10258 152 AW-QAVDERPHAN------RFLPPDAIEQALNgwRYQHHIQPITLWFDDALSAMR----SLKGIGATHLHEGR--DPRIL 218

                        250       260
                 ....*....|....*....|....*...
gi 446531593 235 FRAMLRIYERDFTGNEGIMA-TYHaLFT 261
Cdd:PRK10258 219 TRSQLQRLQLAWPQQQGRYPlTYH-LFL 245
 
Name Accession Description Interval E-value
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 10-265 1.17e-86

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 257.99  E-value: 1.17e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593   10 RFNVAAVSYDQYANVQKKMAHSLLSVL-NRRYSETssIRILELGCGTGYVTEKLSNLFPKAHITAIDFAESMIAVAKTRQ 88
Cdd:TIGR02072   1 SFNKAAKTYDRHAKIQREMAKRLLALLkEKGIFIP--ASVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTKL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593   89 NvKNVTFHCEDIERLRLEE-SYDVIISNATFQWLNDLKQVIRNLFHHLSTDGILLFSTFGQETFQELHNSFRRakeekni 167
Cdd:TIGR02072  79 S-ENVQFICGDAEKLPLEDsSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQSFGQ------- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593  168 rneiaIGQRFYSKDQLRHICKIETGDVHVSETCYIESFAEVREFLHSIRKVGATNSNEESycQSPSLFRAMLRIYERDFT 247
Cdd:TIGR02072 151 -----HGLRYLSLDELKALLKNSFELLTLEEELITLSFDDPLDVLRHLKKTGANGLSSGR--TSRKQLKAFLERYEQEFQ 223

                         250
                  ....*....|....*...
gi 446531593  248 gNEGIMATYHALFTYITK 265
Cdd:TIGR02072 224 -PDGLPLTYHVVYGIAKK 240
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
47-145 2.57e-38

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 129.94  E-value: 2.57e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593  47 RILELGCGTGYVTEKLSNLFPKAHITAIDFAESMIAVAktRQNVKNVTFHCEDIERLRLEESYDVIISNATFQWLNDLKQ 126
Cdd:COG4106    4 RVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARA--RARLPNVRFVVADLRDLDPPEPFDLVVSNAALHWLPDHAA 81

                         90
                 ....*....|....*....
gi 446531593 127 VIRNLFHHLSTDGILLFST 145
Cdd:COG4106   82 LLARLAAALAPGGVLAVQV 100
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 47-145 3.06e-28

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: 104.71  E-value: 3.06e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593  47 RILELGCGTGYVTEKLSNLFpkAHITAIDFAESMIAVAKTRQNVKNVTFHCEDIERLRLE-ESYDVIISNATFQWLNDLK 125
Cdd:COG2227   27 RVLDVGCGTGRLALALARRG--ADVTGVDISPEALEIARERAAELNVDFVQGDLEDLPLEdGSFDLVICSEVLEHLPDPA 104

                         90       100
                 ....*....|....*....|
gi 446531593 126 QVIRNLFHHLSTDGILLFST 145
Cdd:COG2227  105 ALLRELARLLKPGGLLLLST 124
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 11-161 4.19e-28

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: 104.69  E-value: 4.19e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593  11 FNVAAVSYDQYanvqkkmaHSLLSVLNRRysetSSIRILELGCGTGYVTEKLSNLFpkAHITAIDFAESMIAVAKTR--Q 88
Cdd:COG2226    1 FDRVAARYDGR--------EALLAALGLR----PGARVLDLGCGTGRLALALAERG--ARVTGVDISPEMLELARERaaE 66

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446531593  89 NVKNVTFHCEDIERLRLE-ESYDVIISNATFQWLNDLKQVIRNLFHHLSTDGILLFSTFGQETFQELHNSFRRA 161
Cdd:COG2226   67 AGLNVEFVVGDAEDLPFPdGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEELLAEA 140
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
18-145 8.22e-27

Predicted methyltransferase, contains TPR repeat [General function prediction only];


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 102.77  E-value: 8.22e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593  18 YDQYA-------------NVQKKMAHSLLsvlnRRYSETSSIRILELGCGTGYVTEKLSNLFpkAHITAIDFAESMIAVA 84
Cdd:COG4976   11 FDQYAdsydaalvedlgyEAPALLAEELL----ARLPPGPFGRVLDLGCGTGLLGEALRPRG--YRLTGVDLSEEMLAKA 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446531593  85 KTRQNvkNVTFHCEDIERLR-LEESYDVIISNATFQWLNDLKQVIRNLFHHLSTDGILLFST 145
Cdd:COG4976   85 REKGV--YDRLLVADLADLAePDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFIFSV 144
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 48-139 9.23e-25

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 94.55  E-value: 9.23e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593   48 ILELGCGTGYVTEKLSNLFpKAHITAIDFAESMIAVAKTR--QNVKNVTFHCEDIERLRLE-ESYDVIISNATFQWLN-- 122
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRG-GARVTGVDLSPEMLERARERaaEAGLNVEFVQGDAEDLPFPdGSFDLVVSSGVLHHLPdp 79

                          90
                  ....*....|....*..
gi 446531593  123 DLKQVIRNLFHHLSTDG 139
Cdd:pfam13649  80 DLEAALREIARVLKPGG 96
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 49-143 9.54e-23

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 89.26  E-value: 9.54e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593   49 LELGCGTGYVTEKLSNLFPkaHITAIDFAESMIAVAKTRQNVKNVTFHCEDIERLRLE-ESYDVIISNATFQWLNDLKQV 127
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA--RVTGVDISPEMLELAREKAPREGLTFVVGDAEDLPFPdNSFDLVLSSEVLHHVEDPERA 78

                          90
                  ....*....|....*.
gi 446531593  128 IRNLFHHLSTDGILLF 143
Cdd:pfam08241  79 LREIARVLKPGGILII 94
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 45-214 9.98e-22

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 89.59  E-value: 9.98e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593  45 SIRILELGCGTGYVTEKLSNLFpKAHITAIDFAESMIAVAK---TRQNVKNVTFHCEDIERL--RLEESYDVIISNATFQ 119
Cdd:COG0500   27 GGRVLDLGCGTGRNLLALAARF-GGRVIGIDLSPEAIALARaraAKAGLGNVEFLVADLAELdpLPAESFDLVVAFGVLH 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593 120 WLN--DLKQVIRNLFHHLSTDGILLFStfgQETFQELHNSFRRAKEEKNIRNEIAIGQRFYSkDQLRHICKIETGDVHVS 197
Cdd:COG0500  106 HLPpeEREALLRELARALKPGGVLLLS---ASDAAAALSLARLLLLATASLLELLLLLRLLA-LELYLRALLAAAATEDL 181

                        170
                 ....*....|....*..
gi 446531593 198 ETCYIESFAEVREFLHS 214
Cdd:COG0500  182 RSDALLESANALEYLLS 198
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 49-141 2.13e-21

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 85.88  E-value: 2.13e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593   49 LELGCGTGYVTEKLSNLFPKAHITAIDFAESMIAVAKTR------QNVKNVTFHCEDIERLrLEESYDVIISNATFQWLN 122
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERlaalglLNAVRVELFQLDLGEL-DPGSFDVVVASNVLHHLA 79

                          90
                  ....*....|....*....
gi 446531593  123 DLKQVIRNLFHHLSTDGIL 141
Cdd:pfam08242  80 DPRAVLRNIRRLLKPGGVL 98
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 47-146 1.42e-19

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: 81.32  E-value: 1.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593  47 RILELGCGTGYVTEKLSNlFPKAHITAIDFAESMIAVAKTRQ---NVKNVTFHCEDIERLRLE--ESYDVIISNATFQWL 121
Cdd:cd02440    1 RVLDLGCGTGALALALAS-GPGARVTGVDISPVALELARKAAaalLADNVEVLKGDAEELPPEadESFDVIISDPPLHHL 79

                         90       100
                 ....*....|....*....|....*.
gi 446531593 122 -NDLKQVIRNLFHHLSTDGILLFSTF 146
Cdd:cd02440   80 vEDLARFLEEARRLLKPGGVLVLTLV 105
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 2-261 2.72e-18

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 81.73  E-value: 2.72e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593   2 INKTLLQKRFNVAAVSYDQYANVQKKMAHSLLSVLNRRYSETssirILELGCGTG----YVTEKLSnlfpkaHITAIDFA 77
Cdd:PRK10258   4 VNKQAIAAAFGRAAAHYEQHAELQRQSADALLAMLPQRKFTH----VLDAGCGPGwmsrYWRERGS------QVTALDLS 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593  78 ESMIAVAKTRQNVKNvtFHCEDIERLRLEE-SYDVIISNATFQWLNDLKQVIRNLFHHLSTDGILLFSTFGQETFQELHN 156
Cdd:PRK10258  74 PPMLAQARQKDAADH--YLAGDIESLPLATaTFDLAWSNLAVQWCGNLSTALRELYRVVRPGGVVAFTTLVQGSLPELHQ 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593 157 SFrRAKEEKNIRNeiaigqRFYSKDQLRHICK--IETGDVHVSETCYIESFAEVReflhSIRKVGATNSNEESycQSPSL 234
Cdd:PRK10258 152 AW-QAVDERPHAN------RFLPPDAIEQALNgwRYQHHIQPITLWFDDALSAMR----SLKGIGATHLHEGR--DPRIL 218

                        250       260
                 ....*....|....*....|....*...
gi 446531593 235 FRAMLRIYERDFTGNEGIMA-TYHaLFT 261
Cdd:PRK10258 219 TRSQLQRLQLAWPQQQGRYPlTYH-LFL 245
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 42-186 3.19e-18

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 79.00  E-value: 3.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593   42 ETSSIRILELGCGTGYVTEKL-SNLFPKAHITAIDFAESMIAVAKTR---QNVKNVTFHCEDIERLRL---EESYDVIIS 114
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELaEELGPNAEVVGIDISEEAIEKARENaqkLGFDNVEFEQGDIEELPElleDDKFDVVIS 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446531593  115 NATFQWLNDLKQVIRNLFHHLSTDGILLFStfgqeTFQELHNSFRRAKEEKNIRNEIAIGQrfYSKDQLRHI 186
Cdd:pfam13847  81 NCVLNHIPDPDKVLQEILRVLKPGGRLIIS-----DPDSLAELPAHVKEDSTYYAGCVGGA--ILKKKLYEL 145
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 18-141 1.02e-14

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 71.90  E-value: 1.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593  18 YDQYANVQKKMAHSLLSvlnrRYSETSSIRILELGCGTGYVTEKLSNLFPKAHITAIDFAESMIAVAKTRqnVKNVTFHC 97
Cdd:PRK01683   9 YLKFEDERTRPARDLLA----RVPLENPRYVVDLGCGPGNSTELLVERWPAARITGIDSSPAMLAEARSR--LPDCQFVE 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 446531593  98 EDIERLRLEESYDVIISNATFQWLNDLKQVIRNLFHHLSTDGIL 141
Cdd:PRK01683  83 ADIASWQPPQALDLIFANASLQWLPDHLELFPRLVSLLAPGGVL 126
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 47-145 7.62e-14

Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 67.26  E-value: 7.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593  47 RILELGCGTGYVTEKLSNLFpKAHITAIDFAESMIAVAKTR---QNVKN-VTFHCEDIERLRLEESYDVIISNATFQWLN 122
Cdd:COG2230   54 RVLDIGCGWGGLALYLARRY-GVRVTGVTLSPEQLEYARERaaeAGLADrVEVRLADYRDLPADGQFDAIVSIGMFEHVG 132

                         90       100
                 ....*....|....*....|....*
gi 446531593 123 D--LKQVIRNLFHHLSTDGILLFST 145
Cdd:COG2230  133 PenYPAYFAKVARLLKPGGRLLLHT 157
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
 18-120 8.88e-14

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 69.33  E-value: 8.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593  18 YDQYANVQKKMAHSLLSvlnrRYSETSSIRILELGCGTGYVTEKLSNLFPKAHITAIDFAESMIAVAKTRqnvkNVTFHC 97
Cdd:PRK14103   7 YLAFADHRGRPFYDLLA----RVGAERARRVVDLGCGPGNLTRYLARRWPGAVIEALDSSPEMVAAARER----GVDART 78

                         90       100
                 ....*....|....*....|...
gi 446531593  98 EDIERLRLEESYDVIISNATFQW 120
Cdd:PRK14103  79 GDVRDWKPKPDTDVVVSNAALQW 101
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 43-188 3.11e-12

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 63.22  E-value: 3.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593   43 TSSIRILELGCGTGYVTEKLSNLFPkaHITAIDFaeSMIAVAKTRQNVKNVTFHceDIERLRLEESYDVIISNATFQWLN 122
Cdd:pfam13489  21 PSPGRVLDFGCGTGIFLRLLRAQGF--SVTGVDP--SPIAIERALLNVRFDQFD--EQEAAVPAGKFDVIVAREVLEHVP 94

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446531593  123 DLKQVIRNLFHHLSTDGILLFSTFGqetfqelhNSFRRAKEEKNIR--NEIAIGQRFYSKDQLRHICK 188
Cdd:pfam13489  95 DPPALLRQIAALLKPGGLLLLSTPL--------ASDEADRLLLEWPylRPRNGHISLFSARSLKRLLE 154
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 47-143 4.38e-12

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: 63.29  E-value: 4.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593  47 RILELGCGTGYVTEKLSNLFPKAHITAIDfaESMIAVAKTRQNVK-----NVTFHCEDIERLRLEESYDVIISNATF-QW 120
Cdd:COG2813   52 RVLDLGCGYGVIGLALAKRNPEARVTLVD--VNARAVELARANAAangleNVEVLWSDGLSGVPDGSFDLILSNPPFhAG 129

                         90       100
                 ....*....|....*....|....*..
gi 446531593 121 LNDLKQVIRNLFH----HLSTDGILLF 143
Cdd:COG2813  130 RAVDKEVAHALIAdaarHLRPGGELWL 156
PRK08317 PRK08317
hypothetical protein; Provisional
 47-132 7.76e-12

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 63.42  E-value: 7.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593  47 RILELGCGTGYVTEKLSNLF-PKAHITAIDFAESMIAVAKTR--QNVKNVTFHCEDIERLRLE-ESYDVIISNATFQWLN 122
Cdd:PRK08317  22 RVLDVGCGPGNDARELARRVgPEGRVVGIDRSEAMLALAKERaaGLGPNVEFVRGDADGLPFPdGSFDAVRSDRVLQHLE 101

                         90
                 ....*....|
gi 446531593 123 DLKQVIRNLF 132
Cdd:PRK08317 102 DPARALAEIA 111
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 47-115 1.21e-10

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: 59.77  E-value: 1.21e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446531593  47 RILELGCGTGYVTEKLSNLFPKAHITAIDFAESMIAVAktRQNVKN------VTFHCEDIERLRLE---ESYDVIISN 115
Cdd:COG4123   40 RVLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELA--RRNVALngledrITVIHGDLKEFAAElppGSFDLVVSN 115
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 32-143 2.30e-09

Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 55.29  E-value: 2.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593   32 LLSVLNRRYSEtssiRILELGCGTGYVTEKLSNLFPKAHITAIDfaESMIAVAKTRQN-----VKNVTFHCEDIERLRLE 106
Cdd:pfam05175  23 LLEHLPKDLSG----KVLDLGCGAGVLGAALAKESPDAELTMVD--INARALESARENlaangLENGEVVASDVYSGVED 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 446531593  107 ESYDVIISNATF-QWLNDLKQVIRNLFH----HLSTDGILLF 143
Cdd:pfam05175  97 GKFDLIISNPPFhAGLATTYNVAQRFIAdakrHLRPGGELWI 138
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 39-143 2.63e-09

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 56.70  E-value: 2.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593  39 RYSETSSIRILELGCGTGYVTEKLSNLFPKAHITAIDFAESMIAVAktRQNVKN------VTFHCEDI-ERLRLEESYDV 111
Cdd:COG2890  107 LLPAGAPPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVA--RRNAERlgledrVRFLQGDLfEPLPGDGRFDL 184

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446531593 112 IISN----ATFQW----------------------LNDLKQVIRNLFHHLSTDGILLF 143
Cdd:COG2890  185 IVSNppyiPEDEIallppevrdheprlaldggedgLDFYRRIIAQAPRLLKPGGWLLL 242
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 1-112 1.13e-08

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 54.39  E-value: 1.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593   1 MINKTLLQKRFNVAAVSYDQyAN---------VQKKMAHSLLSVLNRrysetssIRILELGCGTGYVTEKLSN-LFPKAH 70
Cdd:PRK00216   7 EEKQEKVAEMFDSIAPKYDL-MNdllsfglhrVWRRKTIKWLGVRPG-------DKVLDLACGTGDLAIALAKaVGKTGE 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 446531593  71 ITAIDFAESMIAVAKTR----QNVKNVTFHCEDIERLRLE-ESYDVI 112
Cdd:PRK00216  79 VVGLDFSEGMLAVGREKlrdlGLSGNVEFVQGDAEALPFPdNSFDAV 125
COG3963 COG3963
Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];
47-169 7.58e-08

Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];


Pssm-ID: 443163  Cd Length: 193  Bit Score: 51.36  E-value: 7.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593  47 RILELGCGTGYVTEK-LSNLFPKAHITAIDFAESMiaVAKTRQNVKNVTFHCEDIERL------RLEESYDVIISN---A 116
Cdd:COG3963   48 PVVELGPGTGVFTRAiLARGVPDARLLAVEINPEF--AEHLRRRFPRVTVVNGDAEDLaellaeHGIGKVDAVVSGlplL 125

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446531593 117 TFQwLNDLKQVIRNLFHHLSTDGILL---FSTFGQETFQELHNSFRRAKEEKNIRN 169
Cdd:COG3963  126 SFP-PELRRAILDAAFRVLAPGGVFVqftYSPRSPVPRKLLRRGFEAVRSGFVWRN 180
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 44-143 1.15e-07

N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 51.70  E-value: 1.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593  44 SSIRILELGCGTGYVTEKLSNLFPKAHITAIDFAESMIAVAktRQNVK-----NVTFHCEDI-ERLRlEESYDVIISN-- 115
Cdd:PRK09328 108 EPLRVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVA--RRNAKhglgaRVEFLQGDWfEPLP-GGRFDLIVSNpp 184

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446531593 116 --ATFQW----------------------LNDLKQVIRNLFHHLSTDGILLF 143
Cdd:PRK09328 185 yiPEADIhllqpevrdhephlalfggedgLDFYRRIIEQAPRYLKPGGWLLL 236
YtxK COG0827
Adenine-specific DNA N6-methylase [Replication, recombination and repair];
43-156 1.68e-07

Adenine-specific DNA N6-methylase [Replication, recombination and repair];


Pssm-ID: 440589 [Multi-domain]  Cd Length: 327  Bit Score: 51.49  E-value: 1.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593  43 TSSIRILELGCGTGY-VTEKLSNLFPKAHITAIDFAESMIAVAKTRQNV--KNVTFHCEDIERLRLEESYDVIISN---- 115
Cdd:COG0827  114 KEGLRILDPAVGTGNlLTTVLNQLKKKVNAYGVEVDDLLIRLAAVLANLqgHPVELFHQDALQPLLIDPVDVVISDlpvg 193

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446531593 116 --------ATFQWLNDLKQV-IRNLF-----HHLSTDGILLF----STFGQETFQELHN 156
Cdd:COG0827  194 yypnderaKRFKLKADEGHSyAHHLFieqslNYLKPGGYLFFlvpsNLFESDQAAQLRE 252
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 47-143 4.23e-07

tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443298  Cd Length: 173  Bit Score: 48.64  E-value: 4.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593  47 RILELGCGTGYVT----EKLSnlfPKAHITAIDFAESMIAVAktRQNVK------NVTFHCED----IERLrLEESYDVI 112
Cdd:COG4122   19 RILEIGTGTGYSTlwlaRALP---DDGRLTTIEIDPERAAIA--RENFAragladRIRLILGDalevLPRL-ADGPFDLV 92

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446531593 113 isnatF------QWLNDLKQVIRnlfhHLSTDGILLF 143
Cdd:COG4122   93 -----FidadksNYPDYLELALP----LLRPGGLIVA 120
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 47-144 4.54e-07

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 49.45  E-value: 4.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593  47 RILELGCGTGYVTEKLSNLfpKAHITAIDFAESMIAVAKTRQN----VKNVTFHCEDIERLRleESYDVIISnatfqwLN 122
Cdd:PRK07580  66 RILDAGCGVGSLSIPLARR--GAKVVASDISPQMVEEARERAPeaglAGNITFEVGDLESLL--GRFDTVVC------LD 135

                         90       100
                 ....*....|....*....|....*...
gi 446531593 123 DL----KQVIRNLFHHLS--TDGILLFS 144
Cdd:PRK07580 136 VLihypQEDAARMLAHLAslTRGSLIFT 163
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
28-161 1.95e-06

Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 47.13  E-value: 1.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593  28 MAHSLLSVL-NRRysetssiRILELGCGTGYVTEKLSNLFPKAHITAIDFAESMIAVAKT-------RQNVKNVTFHCED 99
Cdd:COG0421   27 MAHVPLLFHpNPK-------RVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREyfpllapAFDDPRLRVVIGD 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593 100 ----IERLrlEESYDVIISNAT-------------FqwlndlkqvIRNLFHHLSTDGILLF----STFGQETFQELHNSF 158
Cdd:COG0421  100 grafLREA--EESYDVIIVDLTdpvgpaeglftreF---------YEDCRRALKPGGVLVVnlgsPFYGLDLLRRVLATL 168


                 ...
gi 446531593 159 RRA 161
Cdd:COG0421  169 REV 171
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
47-115 2.16e-06

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 47.21  E-value: 2.16e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446531593  47 RILELGCGTGYVTEKLSNLFPKaHITAIDFAESMIAVAktRQNVK----NVTFHCEDIERLRLEESYDVIISN 115
Cdd:COG2263   48 TVLDLGCGTGMLAIGAALLGAK-KVVGVDIDPEALEIA--RENAErlgvRVDFIRADVTRIPLGGSVDTVVMN 117
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 48-148 4.89e-06

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 47.44  E-value: 4.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593  48 ILELGCGTGYVTEKLSNlfPKAHITAIDFAESMIavaKTRQNV----KNVTFHCEDIERLRL---EESYDVIISNATFQW 120
Cdd:PLN02336  41 VLELGAGIGRFTGELAK--KAGQVIALDFIESVI---KKNESInghyKNVKFMCADVTSPDLnisDGSVDLIFSNWLLMY 115

                         90       100       110
                 ....*....|....*....|....*....|..
gi 446531593 121 LND--LKQVIRNLFHHLSTDGILLF--STFGQ 148
Cdd:PLN02336 116 LSDkeVENLAERMVKWLKVGGYIFFreSCFHQ 147
arsM PRK11873
arsenite methyltransferase;
47-132 1.51e-05

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 45.32  E-value: 1.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593  47 RILELGCGTGYvteklsNLF-------PKAHITAIDFAESMIAVAKTRQ---NVKNVTFHCEDIERLRLE-ESYDVIISN 115
Cdd:PRK11873  80 TVLDLGSGGGF------DCFlaarrvgPTGKVIGVDMTPEMLAKARANArkaGYTNVEFRLGEIEALPVAdNSVDVIISN 153

                         90
                 ....*....|....*..
gi 446531593 116 ATFQWLNDLKQVIRNLF 132
Cdd:PRK11873 154 CVINLSPDKERVFKEAF 170
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
46-141 1.62e-05

tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;


Pssm-ID: 182918  Cd Length: 255  Bit Score: 44.95  E-value: 1.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593  46 IRILELGCGTGYVTEKLSNLfpKAHITAIDFAESMIAVAK----TRQNVKNVTF-HC--EDIERlRLEESYDVIISNATF 118
Cdd:PRK11036  46 LRVLDAGGGEGQTAIKLAEL--GHQVILCDLSAEMIQRAKqaaeAKGVSDNMQFiHCaaQDIAQ-HLETPVDLILFHAVL 122

                         90       100
                 ....*....|....*....|...
gi 446531593 119 QWLNDLKQVIRNLFHHLSTDGIL 141
Cdd:PRK11036 123 EWVADPKSVLQTLWSVLRPGGAL 145
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
47-114 1.77e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 44.64  E-value: 1.77e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446531593  47 RILELGCGTGYVTEKLSNLFPKaHITAIDFAESMIAVAktRQNVK------NVTFHCEDIERLRLEESYDVIIS 114
Cdd:COG4076   38 VVLDIGTGSGLLSMLAARAGAK-KVYAVEVNPDIAAVA--RRIIAanglsdRITVINADATDLDLPEKADVIIS 108
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 47-116 2.55e-05

Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 43.92  E-value: 2.55e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446531593  47 RILELGCGTGYVTEKLSNLFpkAHITAIDFAESMIAVAKTR---QNVKNVTFHCEDIER-LRLEESYDVIISNA 116
Cdd:COG2518   69 RVLEIGTGSGYQAAVLARLA--GRVYSVERDPELAERARERlaaLGYDNVTVRVGDGALgWPEHAPFDRIIVTA 140
RsmG COG0357
16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ...
 65-143 4.16e-05

16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ribosomal structure and biogenesis]; 16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 440126  Cd Length: 211  Bit Score: 43.60  E-value: 4.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593  65 LFPKAHITAID-------FAESMIAVAktrqNVKNVTFHCEDIERLRLEESYDVIISNAtfqwLNDLKQVIRNLFHHLST 137
Cdd:COG0357   88 ARPDLQVTLVDslgkkiaFLREVVREL----GLKNVTVVHGRAEELAPREKFDVVTARA----VAPLPDLLELALPLLKP 159


                 ....*.
gi 446531593 138 DGILLF 143
Cdd:COG0357  160 GGRLLA 165
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
 47-159 6.58e-05

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 43.42  E-value: 6.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593  47 RILELGCGTG----YVTEKLSnlfpkAHITAIDFAESMIAVAKTRQNVKN-VTFHCEDIERLRLEES-YDVIISNATFQW 120
Cdd:PTZ00098  55 KVLDIGSGLGggckYINEKYG-----AHVHGVDICEKMVNIAKLRNSDKNkIEFEANDILKKDFPENtFDMIYSRDAILH 129

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446531593 121 LN--DLKQVIRNLFHHLSTDGILLFSTFGQETFQELHNSFR 159
Cdd:PTZ00098 130 LSyaDKKKLFEKCYKWLKPNGILLITDYCADKIENWDEEFK 170
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 36-129 9.29e-05

HemK family putative methylases; 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. Both E. coli and H. influenzae have two members rather than one. The members from the Mycoplasmas have an additional C-terminal domain. [Protein fate, Protein modification and repair]


Pssm-ID: 273125 [Multi-domain]  Cd Length: 284  Bit Score: 43.11  E-value: 9.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593   36 LNRRYSETSSIRILELGCGTGYVTEKLSNLFPKAHITAIDFAESMIAVAKtrQNVK------NVTFHCEDIERLRLEESY 109
Cdd:TIGR00536 106 LASLISQPPILHILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAVAE--ENAEknqlehRVEFIQSNLFEPLAGQKI 183

                          90       100
                  ....*....|....*....|...
gi 446531593  110 DVIISNATF---QWLNDLKQVIR 129
Cdd:TIGR00536 184 DIIVSNPPYideEDLADLPNVVR 206
pcm PRK00312
protein-L-isoaspartate(D-aspartate) O-methyltransferase;
47-142 1.36e-04

protein-L-isoaspartate(D-aspartate) O-methyltransferase;


Pssm-ID: 178974 [Multi-domain]  Cd Length: 212  Bit Score: 42.11  E-value: 1.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593  47 RILELGCGTGYVTEKLSNLFpkAHITAIDFAESMIAVAKTR---QNVKNVTFHCEDIER-LRLEESYDVIISNATFqwln 122
Cdd:PRK00312  81 RVLEIGTGSGYQAAVLAHLV--RRVFSVERIKTLQWEAKRRlkqLGLHNVSVRHGDGWKgWPAYAPFDRILVTAAA---- 154

                         90       100
                 ....*....|....*....|
gi 446531593 123 dlKQVIRNLFHHLSTDGILL 142
Cdd:PRK00312 155 --PEIPRALLEQLKEGGILV 172
PRK06202 PRK06202
hypothetical protein; Provisional
 39-138 2.25e-04

hypothetical protein; Provisional


Pssm-ID: 180466 [Multi-domain]  Cd Length: 232  Bit Score: 41.52  E-value: 2.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593  39 RYSETSSIRILELGCGTGYVTEKLSNLfpkAH-------ITAIDFAESMIAVAKTRQNVKNVTF---HCEDIERLRleES 108
Cdd:PRK06202  55 ALSADRPLTLLDIGCGGGDLAIDLARW---ARrdglrleVTAIDPDPRAVAFARANPRRPGVTFrqaVSDELVAEG--ER 129

                         90       100       110
                 ....*....|....*....|....*....|
gi 446531593 109 YDVIISNatfqwlndlkqvirNLFHHLSTD 138
Cdd:PRK06202 130 FDVVTSN--------------HFLHHLDDA 145
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 47-113 4.74e-04

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: 40.53  E-value: 4.74e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446531593  47 RILELGCGTGYVTEKLSN-LFPKAHITAIDFAESMIAVAktRQNVK------NVTFHCEDIERLRLEESYDVII 113
Cdd:COG2519   94 RVLEAGTGSGALTLALARaVGPEGKVYSYERREDFAEIA--RKNLErfglpdNVELKLGDIREGIDEGDVDAVF 165
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
47-154 5.35e-04

Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 40.04  E-value: 5.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593   47 RILELGCGTGYVTEKLSNLF-PKAHITAIDFAESMiaVAKTRQNVK-----NVTFHCEDiERLRLEES--YDVIISNATf 118
Cdd:pfam01135  76 RVLEIGSGSGYLTACFARMVgEVGRVVSIEHIPEL--VEIARRNLEklgleNVIVVVGD-GRQGWPEFapYDAIHVGAA- 151

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 446531593  119 qwlndLKQVIRNLFHHLSTDGILLFSTfGQETFQEL 154
Cdd:pfam01135 152 -----APEIPEALIDQLKEGGRLVIPV-GPNGNQVL 181
Methyltransf_32 pfam13679
Methyltransferase domain; This family appears to be a methyltransferase domain.
 27-87 2.34e-03

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


Pssm-ID: 379330 [Multi-domain]  Cd Length: 138  Bit Score: 37.55  E-value: 2.34e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446531593   27 KMAHSLLSVLNRRYSETSSIRILELGCGTGYVTEKLSNLFPKAHITAIDFAESMIAVAKTR 87
Cdd:pfam13679   8 HLAEFIAPLLKELLDENGPITIVDHGAGKGYLGFILYYLKYGVRVYGIDTRAELVEKANAL 68
PRK01544 PRK01544
bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) ...
 31-115 3.18e-03

bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) methyltransferase; Reviewed


Pssm-ID: 234958 [Multi-domain]  Cd Length: 506  Bit Score: 38.69  E-value: 3.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531593  31 SLLSVLNRRYSetssiRILELGCGTGYVTEKLSNLFPKAHITAIDFAESMIAVAKTRQNVKNVT-----FHCEDIERLRl 105
Cdd:PRK01544 130 DISSNCNDKFL-----NILELGTGSGCIAISLLCELPNANVIATDISLDAIEVAKSNAIKYEVTdriqiIHSNWFENIE- 203

                         90
                 ....*....|
gi 446531593 106 EESYDVIISN 115
Cdd:PRK01544 204 KQKFDFIVSN 213
 
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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