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Conserved domains on  [gi|446531580|ref|WP_000608926|]
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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 6.71e-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: 256.06  E-value: 6.71e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580   10 RFNVAAVSYDQYANVQKKMAHSLLSTLNRRYSANSsIRILELGCGTGYVTEKLSNLFPKAHITAIDFAESMIAVAKTRpN 89
Cdd:TIGR02072   1 SFNKAAKTYDRHAKIQREMAKRLLALLKEKGIFIP-ASVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTK-L 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580   90 VKNVTFHCEDIERLRLEE-SYDVIISNATFQWLNDLKQVIRNLFHHLSTDGILLFSTFGQETFQELHNSFRRakeeknir 168
Cdd:TIGR02072  79 SENVQFICGDAEKLPLEDsSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQSFGQ-------- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580  169 neiaIGQRFYSKDQLRHICKIETGDVHVSETCYIESFAEVREFLHSIRKVGATNSNEESycQSPSLFRAMLRIYERDFTg 248
Cdd:TIGR02072 151 ----HGLRYLSLDELKALLKNSFELLTLEEELITLSFDDPLDVLRHLKKTGANGLSSGR--TSRKQLKAFLERYEQEFQ- 223

                         250
                  ....*....|....*..
gi 446531580  249 NEGIMATYHALFTYITK 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 6.71e-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: 256.06  E-value: 6.71e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580   10 RFNVAAVSYDQYANVQKKMAHSLLSTLNRRYSANSsIRILELGCGTGYVTEKLSNLFPKAHITAIDFAESMIAVAKTRpN 89
Cdd:TIGR02072   1 SFNKAAKTYDRHAKIQREMAKRLLALLKEKGIFIP-ASVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTK-L 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580   90 VKNVTFHCEDIERLRLEE-SYDVIISNATFQWLNDLKQVIRNLFHHLSTDGILLFSTFGQETFQELHNSFRRakeeknir 168
Cdd:TIGR02072  79 SENVQFICGDAEKLPLEDsSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQSFGQ-------- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580  169 neiaIGQRFYSKDQLRHICKIETGDVHVSETCYIESFAEVREFLHSIRKVGATNSNEESycQSPSLFRAMLRIYERDFTg 248
Cdd:TIGR02072 151 ----HGLRYLSLDELKALLKNSFELLTLEEELITLSFDDPLDVLRHLKKTGANGLSSGR--TSRKQLKAFLERYEQEFQ- 223

                         250
                  ....*....|....*..
gi 446531580  249 NEGIMATYHALFTYITK 265
Cdd:TIGR02072 224 PDGLPLTYHVVYGIAKK 240
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
47-145 1.25e-37

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 128.02  E-value: 1.25e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580  47 RILELGCGTGYVTEKLSNLFPKAHITAIDFAESMIAVAKTRpnVKNVTFHCEDIERLRLEESYDVIISNATFQWLNDLKQ 126
Cdd:COG4106    4 RVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARAR--LPNVRFVVADLRDLDPPEPFDLVVSNAALHWLPDHAA 81

                         90
                 ....*....|....*....
gi 446531580 127 VIRNLFHHLSTDGILLFST 145
Cdd:COG4106   82 LLARLAAALAPGGVLAVQV 100
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 48-139 1.78e-24

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 93.78  E-value: 1.78e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580   48 ILELGCGTGYVTEKLSNLFpKAHITAIDFAESMIAVAKTR--PNVKNVTFHCEDIERLRLE-ESYDVIISNATFQWLN-- 122
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRG-GARVTGVDLSPEMLERARERaaEAGLNVEFVQGDAEDLPFPdGSFDLVVSSGVLHHLPdp 79

                          90
                  ....*....|....*..
gi 446531580  123 DLKQVIRNLFHHLSTDG 139
Cdd:pfam13649  80 DLEAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 47-146 1.26e-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: 1.26e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580  47 RILELGCGTGYVTEKLSNlFPKAHITAIDFAESMIAVAKT---RPNVKNVTFHCEDIERLRLE--ESYDVIISNATFQWL 121
Cdd:cd02440    1 RVLDLGCGTGALALALAS-GPGARVTGVDISPVALELARKaaaALLADNVEVLKGDAEELPPEadESFDVIISDPPLHHL 79

                         90       100
                 ....*....|....*....|....*.
gi 446531580 122 -NDLKQVIRNLFHHLSTDGILLFSTF 146
Cdd:cd02440   80 vEDLARFLEEARRLLKPGGVLVLTLV 105
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 2-261 4.74e-17

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 78.26  E-value: 4.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580   2 INKTLLQKRFNVAAVSYDQYANVQKKMAHSLLSTLNRRYSANssirILELGCGTG----YVTEKLSnlfpkaHITAIDFA 77
Cdd:PRK10258   4 VNKQAIAAAFGRAAAHYEQHAELQRQSADALLAMLPQRKFTH----VLDAGCGPGwmsrYWRERGS------QVTALDLS 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580  78 ESMIAVAKTRPNVKNvtFHCEDIERLRLEE-SYDVIISNATFQWLNDLKQVIRNLFHHLSTDGILLFSTFGQETFQELHN 156
Cdd:PRK10258  74 PPMLAQARQKDAADH--YLAGDIESLPLATaTFDLAWSNLAVQWCGNLSTALRELYRVVRPGGVVAFTTLVQGSLPELHQ 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580 157 SFrRAKEEKNIRNeiaigqRFYSKDQLRHICK--IETGDVHVSETCYIESFAEVReflhSIRKVGATNSNEESycQSPSL 234
Cdd:PRK10258 152 AW-QAVDERPHAN------RFLPPDAIEQALNgwRYQHHIQPITLWFDDALSAMR----SLKGIGATHLHEGR--DPRIL 218

                        250       260
                 ....*....|....*....|....*...
gi 446531580 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 6.71e-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: 256.06  E-value: 6.71e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580   10 RFNVAAVSYDQYANVQKKMAHSLLSTLNRRYSANSsIRILELGCGTGYVTEKLSNLFPKAHITAIDFAESMIAVAKTRpN 89
Cdd:TIGR02072   1 SFNKAAKTYDRHAKIQREMAKRLLALLKEKGIFIP-ASVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTK-L 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580   90 VKNVTFHCEDIERLRLEE-SYDVIISNATFQWLNDLKQVIRNLFHHLSTDGILLFSTFGQETFQELHNSFRRakeeknir 168
Cdd:TIGR02072  79 SENVQFICGDAEKLPLEDsSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQSFGQ-------- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580  169 neiaIGQRFYSKDQLRHICKIETGDVHVSETCYIESFAEVREFLHSIRKVGATNSNEESycQSPSLFRAMLRIYERDFTg 248
Cdd:TIGR02072 151 ----HGLRYLSLDELKALLKNSFELLTLEEELITLSFDDPLDVLRHLKKTGANGLSSGR--TSRKQLKAFLERYEQEFQ- 223

                         250
                  ....*....|....*..
gi 446531580  249 NEGIMATYHALFTYITK 265
Cdd:TIGR02072 224 PDGLPLTYHVVYGIAKK 240
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
47-145 1.25e-37

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 128.02  E-value: 1.25e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580  47 RILELGCGTGYVTEKLSNLFPKAHITAIDFAESMIAVAKTRpnVKNVTFHCEDIERLRLEESYDVIISNATFQWLNDLKQ 126
Cdd:COG4106    4 RVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARAR--LPNVRFVVADLRDLDPPEPFDLVVSNAALHWLPDHAA 81

                         90
                 ....*....|....*....
gi 446531580 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 ...
 33-145 3.19e-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: 3.19e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580  33 LSTLNRRYsANSSIRILELGCGTGYVTEKLSNLFpkAHITAIDFAESMIAVAKTRPNVKNVTFHCEDIERLRLE-ESYDV 111
Cdd:COG2227   14 LAALLARL-LPAGGRVLDVGCGTGRLALALARRG--ADVTGVDISPEALEIARERAAELNVDFVQGDLEDLPLEdGSFDL 90

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446531580 112 IISNATFQWLNDLKQVIRNLFHHLSTDGILLFST 145
Cdd:COG2227   91 VICSEVLEHLPDPAALLRELARLLKPGGLLLLST 124
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 11-161 4.37e-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: 4.37e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580  11 FNVAAVSYDQYanvqkkmaHSLLSTLNRRysanSSIRILELGCGTGYVTEKLSNLFpkAHITAIDFAESMIAVAKTR--P 88
Cdd:COG2226    1 FDRVAARYDGR--------EALLAALGLR----PGARVLDLGCGTGRLALALAERG--ARVTGVDISPEMLELARERaaE 66

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446531580  89 NVKNVTFHCEDIERLRLE-ESYDVIISNATFQWLNDLKQVIRNLFHHLSTDGILLFSTFGQETFQELHNSFRRA 161
Cdd:COG2226   67 AGLNVEFVVGDAEDLPFPdGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEELLAEA 140
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
18-145 1.74e-27

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 104.31  E-value: 1.74e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580  18 YDQYA-------------NVQKKMAHSLLstlnRRYSANSSIRILELGCGTGYVTEKLSNLFpkAHITAIDFAESMIAVA 84
Cdd:COG4976   11 FDQYAdsydaalvedlgyEAPALLAEELL----ARLPPGPFGRVLDLGCGTGLLGEALRPRG--YRLTGVDLSEEMLAKA 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446531580  85 KTRPNvkNVTFHCEDIERLR-LEESYDVIISNATFQWLNDLKQVIRNLFHHLSTDGILLFST 145
Cdd:COG4976   85 REKGV--YDRLLVADLADLAePDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFIFSV 144
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 48-139 1.78e-24

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 93.78  E-value: 1.78e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580   48 ILELGCGTGYVTEKLSNLFpKAHITAIDFAESMIAVAKTR--PNVKNVTFHCEDIERLRLE-ESYDVIISNATFQWLN-- 122
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRG-GARVTGVDLSPEMLERARERaaEAGLNVEFVQGDAEDLPFPdGSFDLVVSSGVLHHLPdp 79

                          90
                  ....*....|....*..
gi 446531580  123 DLKQVIRNLFHHLSTDG 139
Cdd:pfam13649  80 DLEAALREIARVLKPGG 96
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 49-143 3.42e-22

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 87.72  E-value: 3.42e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580   49 LELGCGTGYVTEKLSNLFPkaHITAIDFAESMIAVAKTRPNVKNVTFHCEDIERLRLE-ESYDVIISNATFQWLNDLKQV 127
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA--RVTGVDISPEMLELAREKAPREGLTFVVGDAEDLPFPdNSFDLVLSSEVLHHVEDPERA 78

                          90
                  ....*....|....*.
gi 446531580  128 IRNLFHHLSTDGILLF 143
Cdd:pfam08241  79 LREIARVLKPGGILII 94
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 43-214 3.13e-21

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 88.43  E-value: 3.13e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580  43 NSSIRILELGCGTGYVTEKLSNLFpKAHITAIDFAESMIAVAK---TRPNVKNVTFHCEDIERL--RLEESYDVIISNAT 117
Cdd:COG0500   25 PKGGRVLDLGCGTGRNLLALAARF-GGRVIGIDLSPEAIALARaraAKAGLGNVEFLVADLAELdpLPAESFDLVVAFGV 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580 118 FQWLN--DLKQVIRNLFHHLSTDGILLFStfgQETFQELHNSFRRAKEEKNIRNEIAIGQRFYSkDQLRHICKIETGDVH 195
Cdd:COG0500  104 LHHLPpeEREALLRELARALKPGGVLLLS---ASDAAAALSLARLLLLATASLLELLLLLRLLA-LELYLRALLAAAATE 179

                        170
                 ....*....|....*....
gi 446531580 196 VSETCYIESFAEVREFLHS 214
Cdd:COG0500  180 DLRSDALLESANALEYLLS 198
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 49-141 9.80e-21

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 83.96  E-value: 9.80e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580   49 LELGCGTGYVTEKLSNLFPKAHITAIDFAESMIAVAKTR------PNVKNVTFHCEDIERLrLEESYDVIISNATFQWLN 122
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERlaalglLNAVRVELFQLDLGEL-DPGSFDVVVASNVLHHLA 79

                          90
                  ....*....|....*....
gi 446531580  123 DLKQVIRNLFHHLSTDGIL 141
Cdd:pfam08242  80 DPRAVLRNIRRLLKPGGVL 98
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 47-146 1.26e-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: 1.26e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580  47 RILELGCGTGYVTEKLSNlFPKAHITAIDFAESMIAVAKT---RPNVKNVTFHCEDIERLRLE--ESYDVIISNATFQWL 121
Cdd:cd02440    1 RVLDLGCGTGALALALAS-GPGARVTGVDISPVALELARKaaaALLADNVEVLKGDAEELPPEadESFDVIISDPPLHHL 79

                         90       100
                 ....*....|....*....|....*.
gi 446531580 122 -NDLKQVIRNLFHHLSTDGILLFSTF 146
Cdd:cd02440   80 vEDLARFLEEARRLLKPGGVLVLTLV 105
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 43-186 7.70e-18

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 77.84  E-value: 7.70e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580   43 NSSIRILELGCGTGYVTEKL-SNLFPKAHITAIDFAESMIAVAKTRP---NVKNVTFHCEDIERLRL---EESYDVIISN 115
Cdd:pfam13847   2 DKGMRVLDLGCGTGHLSFELaEELGPNAEVVGIDISEEAIEKARENAqklGFDNVEFEQGDIEELPElleDDKFDVVISN 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446531580  116 ATFQWLNDLKQVIRNLFHHLSTDGILLFStfgqeTFQELHNSFRRAKEEKNIRNEIAIGQrfYSKDQLRHI 186
Cdd:pfam13847  82 CVLNHIPDPDKVLQEILRVLKPGGRLIIS-----DPDSLAELPAHVKEDSTYYAGCVGGA--ILKKKLYEL 145
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 2-261 4.74e-17

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 78.26  E-value: 4.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580   2 INKTLLQKRFNVAAVSYDQYANVQKKMAHSLLSTLNRRYSANssirILELGCGTG----YVTEKLSnlfpkaHITAIDFA 77
Cdd:PRK10258   4 VNKQAIAAAFGRAAAHYEQHAELQRQSADALLAMLPQRKFTH----VLDAGCGPGwmsrYWRERGS------QVTALDLS 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580  78 ESMIAVAKTRPNVKNvtFHCEDIERLRLEE-SYDVIISNATFQWLNDLKQVIRNLFHHLSTDGILLFSTFGQETFQELHN 156
Cdd:PRK10258  74 PPMLAQARQKDAADH--YLAGDIESLPLATaTFDLAWSNLAVQWCGNLSTALRELYRVVRPGGVVAFTTLVQGSLPELHQ 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580 157 SFrRAKEEKNIRNeiaigqRFYSKDQLRHICK--IETGDVHVSETCYIESFAEVReflhSIRKVGATNSNEESycQSPSL 234
Cdd:PRK10258 152 AW-QAVDERPHAN------RFLPPDAIEQALNgwRYQHHIQPITLWFDDALSAMR----SLKGIGATHLHEGR--DPRIL 218

                        250       260
                 ....*....|....*....|....*...
gi 446531580 235 FRAMLRIYERDFTGNEGIMA-TYHaLFT 261
Cdd:PRK10258 219 TRSQLQRLQLAWPQQQGRYPlTYH-LFL 245
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
 18-120 1.98e-14

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 70.87  E-value: 1.98e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580  18 YDQYANVQKKMAHSLLStlnrRYSANSSIRILELGCGTGYVTEKLSNLFPKAHITAIDFAESMIAVAKTRpnvkNVTFHC 97
Cdd:PRK14103   7 YLAFADHRGRPFYDLLA----RVGAERARRVVDLGCGPGNLTRYLARRWPGAVIEALDSSPEMVAAARER----GVDART 78

                         90       100
                 ....*....|....*....|...
gi 446531580  98 EDIERLRLEESYDVIISNATFQW 120
Cdd:PRK14103  79 GDVRDWKPKPDTDVVVSNAALQW 101
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 47-141 3.00e-14

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 70.36  E-value: 3.00e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580  47 RILELGCGTGYVTEKLSNLFPKAHITAIDFAESMIAVAKTRpnVKNVTFHCEDIERLRLEESYDVIISNATFQWLNDLKQ 126
Cdd:PRK01683  34 YVVDLGCGPGNSTELLVERWPAARITGIDSSPAMLAEARSR--LPDCQFVEADIASWQPPQALDLIFANASLQWLPDHLE 111

                         90
                 ....*....|....*
gi 446531580 127 VIRNLFHHLSTDGIL 141
Cdd:PRK01683 112 LFPRLVSLLAPGGVL 126
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 47-145 1.37e-13

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 66.49  E-value: 1.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580  47 RILELGCGTGYVTEKLSNLFpKAHITAIDFAESMIAVAKTRPNVK----NVTFHCEDIERLRLEESYDVIISNATFQWLN 122
Cdd:COG2230   54 RVLDIGCGWGGLALYLARRY-GVRVTGVTLSPEQLEYARERAAEAgladRVEVRLADYRDLPADGQFDAIVSIGMFEHVG 132

                         90       100
                 ....*....|....*....|....*
gi 446531580 123 D--LKQVIRNLFHHLSTDGILLFST 145
Cdd:COG2230  133 PenYPAYFAKVARLLKPGGRLLLHT 157
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 44-188 2.45e-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: 2.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580   44 SSIRILELGCGTGYVTEKLSNLFPkaHITAIDFaeSMIAVAKTRPNVKNVTFHceDIERLRLEESYDVIISNATFQWLND 123
Cdd:pfam13489  22 SPGRVLDFGCGTGIFLRLLRAQGF--SVTGVDP--SPIAIERALLNVRFDQFD--EQEAAVPAGKFDVIVAREVLEHVPD 95

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446531580  124 LKQVIRNLFHHLSTDGILLFSTFGqetfqelhNSFRRAKEEKNIR--NEIAIGQRFYSKDQLRHICK 188
Cdd:pfam13489  96 PPALLRQIAALLKPGGLLLLSTPL--------ASDEADRLLLEWPylRPRNGHISLFSARSLKRLLE 154
PRK08317 PRK08317
hypothetical protein; Provisional
 47-132 1.30e-11

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 62.65  E-value: 1.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580  47 RILELGCGTGYVTEKLSNLF-PKAHITAIDFAESMIAVAKTRP--NVKNVTFHCEDIERLRLE-ESYDVIISNATFQWLN 122
Cdd:PRK08317  22 RVLDVGCGPGNDARELARRVgPEGRVVGIDRSEAMLALAKERAagLGPNVEFVRGDADGLPFPdGSFDAVRSDRVLQHLE 101

                         90
                 ....*....|
gi 446531580 123 DLKQVIRNLF 132
Cdd:PRK08317 102 DPARALAEIA 111
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 32-143 5.31e-11

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: 60.20  E-value: 5.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580  32 LLSTLNrrysANSSIRILELGCGTGYVTEKLSNLFPKAHITAIDfaESMIAVAKTR-----PNVKNVTFHCEDIERLRLE 106
Cdd:COG2813   41 LLEHLP----EPLGGRVLDLGCGYGVIGLALAKRNPEARVTLVD--VNARAVELARanaaaNGLENVEVLWSDGLSGVPD 114

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446531580 107 ESYDVIISNATF-QWLNDLKQVIRNLFH----HLSTDGILLF 143
Cdd:COG2813  115 GSFDLILSNPPFhAGRAVDKEVAHALIAdaarHLRPGGELWL 156
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 32-143 1.97e-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: 1.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580   32 LLSTLNrrysANSSIRILELGCGTGYVTEKLSNLFPKAHITAIDfaESMIAVAKTR-----PNVKNVTFHCEDIERLRLE 106
Cdd:pfam05175  23 LLEHLP----KDLSGKVLDLGCGAGVLGAALAKESPDAELTMVD--INARALESARenlaaNGLENGEVVASDVYSGVED 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 446531580  107 ESYDVIISNATF-QWLNDLKQVIRNLFH----HLSTDGILLF 143
Cdd:pfam05175  97 GKFDLIISNPPFhAGLATTYNVAQRFIAdakrHLRPGGELWI 138
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 47-115 2.10e-09

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: 56.31  E-value: 2.10e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446531580  47 RILELGCGTGYVTEKLSNLFPKAHITAIDFAESMIAVAKTrpNVKN------VTFHCEDIERLRLE---ESYDVIISN 115
Cdd:COG4123   40 RVLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARR--NVALngledrITVIHGDLKEFAAElppGSFDLVVSN 115
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 39-143 1.93e-08

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 54.00  E-value: 1.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580  39 RYSANSSIRILELGCGTGYVTEKLSNLFPKAHITAIDFAESMIAVAKTrpNVKN------VTFHCEDI-ERLRLEESYDV 111
Cdd:COG2890  107 LLPAGAPPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARR--NAERlgledrVRFLQGDLfEPLPGDGRFDL 184

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446531580 112 IISN----ATFQW----------------------LNDLKQVIRNLFHHLSTDGILLF 143
Cdd:COG2890  185 IVSNppyiPEDEIallppevrdheprlaldggedgLDFYRRIIAQAPRLLKPGGWLLL 242
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 46-112 4.17e-08

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 52.46  E-value: 4.17e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446531580  46 IRILELGCGTGYVTEKLSN-LFPKAHITAIDFAESMIAVAKTR----PNVKNVTFHCEDIERLRLE-ESYDVI 112
Cdd:PRK00216  53 DKVLDLACGTGDLAIALAKaVGKTGEVVGLDFSEGMLAVGREKlrdlGLSGNVEFVQGDAEALPFPdNSFDAV 125
YtxK COG0827
Adenine-specific DNA N6-methylase [Replication, recombination and repair];
43-156 1.13e-07

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


Pssm-ID: 440589 [Multi-domain]  Cd Length: 327  Bit Score: 51.87  E-value: 1.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580  43 NSSIRILELGCGTGY-VTEKLSNLFPKAHITAIDFAESMIAVAKTRPNV--KNVTFHCEDIERLRLEESYDVIISN---- 115
Cdd:COG0827  114 KEGLRILDPAVGTGNlLTTVLNQLKKKVNAYGVEVDDLLIRLAAVLANLqgHPVELFHQDALQPLLIDPVDVVISDlpvg 193

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446531580 116 --------ATFQWLNDLKQV-IRNLF-----HHLSTDGILLF----STFGQETFQELHN 156
Cdd:COG0827  194 yypnderaKRFKLKADEGHSyAHHLFieqslNYLKPGGYLFFlvpsNLFESDQAAQLRE 252
COG3963 COG3963
Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];
47-169 1.60e-07

Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];


Pssm-ID: 443163  Cd Length: 193  Bit Score: 50.21  E-value: 1.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580  47 RILELGCGTGYVTEK-LSNLFPKAHITAIDFAESMIAVAKTR-PnvkNVTFHCEDIERL------RLEESYDVIISN--- 115
Cdd:COG3963   48 PVVELGPGTGVFTRAiLARGVPDARLLAVEINPEFAEHLRRRfP---RVTVVNGDAEDLaellaeHGIGKVDAVVSGlpl 124

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446531580 116 ATFQwLNDLKQVIRNLFHHLSTDGILL---FSTFGQETFQELHNSFRRAKEEKNIRN 169
Cdd:COG3963  125 LSFP-PELRRAILDAAFRVLAPGGVFVqftYSPRSPVPRKLLRRGFEAVRSGFVWRN 180
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 38-143 1.74e-07

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 50.93  E-value: 1.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580  38 RRYSANSSIRILELGCGTGYVTEKLSNLFPKAHITAIDFAESMIAVAKTrpNVK-----NVTFHCEDI-ERLRlEESYDV 111
Cdd:PRK09328 102 EALLLKEPLRVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARR--NAKhglgaRVEFLQGDWfEPLP-GGRFDL 178

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446531580 112 IISN----ATFQW----------------------LNDLKQVIRNLFHHLSTDGILLF 143
Cdd:PRK09328 179 IVSNppyiPEADIhllqpevrdhephlalfggedgLDFYRRIIEQAPRYLKPGGWLLL 236
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
28-161 4.86e-07

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


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 49.06  E-value: 4.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580  28 MAHSLLSTL-NRRysanssiRILELGCGTGYVTEKLSNLFPKAHITAIDFAESMIAVAK-----TRPNVKN--VTFHCED 99
Cdd:COG0421   27 MAHVPLLFHpNPK-------RVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAReyfplLAPAFDDprLRVVIGD 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580 100 ----IERLrlEESYDVIISNAT-------------FqwlndlkqvIRNLFHHLSTDGILLF----STFGQETFQELHNSF 158
Cdd:COG0421  100 grafLREA--EESYDVIIVDLTdpvgpaeglftreF---------YEDCRRALKPGGVLVVnlgsPFYGLDLLRRVLATL 168


                 ...
gi 446531580 159 RRA 161
Cdd:COG0421  169 REV 171
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 47-143 8.06e-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: 47.87  E-value: 8.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580  47 RILELGCGTGYVT----EKLSnlfPKAHITAIDFAESMIAVAK---TRPNV-KNVTFHCED----IERLrLEESYDVIis 114
Cdd:COG4122   19 RILEIGTGTGYSTlwlaRALP---DDGRLTTIEIDPERAAIARenfARAGLaDRIRLILGDalevLPRL-ADGPFDLV-- 92

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446531580 115 natF------QWLNDLKQVIRnlfhHLSTDGILLF 143
Cdd:COG4122   93 ---FidadksNYPDYLELALP----LLRPGGLIVA 120
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 47-144 9.80e-07

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 48.29  E-value: 9.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580  47 RILELGCGTGYVTEKLSNLfpKAHITAIDFAESMIAVAKTR----PNVKNVTFHCEDIERLRleESYDVIISnatfqwLN 122
Cdd:PRK07580  66 RILDAGCGVGSLSIPLARR--GAKVVASDISPQMVEEARERapeaGLAGNITFEVGDLESLL--GRFDTVVC------LD 135

                         90       100
                 ....*....|....*....|....*...
gi 446531580 123 DL----KQVIRNLFHHLS--TDGILLFS 144
Cdd:PRK07580 136 VLihypQEDAARMLAHLAslTRGSLIFT 163
PRK06202 PRK06202
hypothetical protein; Provisional
 39-138 6.49e-06

hypothetical protein; Provisional


Pssm-ID: 180466 [Multi-domain]  Cd Length: 232  Bit Score: 46.15  E-value: 6.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580  39 RYSANSSIRILELGCGTGYVTEKLSNLfpkAH-------ITAIDFAESMIAVAKTRPNVKNVTF---HCEDIERLRleES 108
Cdd:PRK06202  55 ALSADRPLTLLDIGCGGGDLAIDLARW---ARrdglrleVTAIDPDPRAVAFARANPRRPGVTFrqaVSDELVAEG--ER 129

                         90       100       110
                 ....*....|....*....|....*....|
gi 446531580 109 YDVIISNatfqwlndlkqvirNLFHHLSTD 138
Cdd:PRK06202 130 FDVVTSN--------------HFLHHLDDA 145
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
47-115 1.08e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 44.89  E-value: 1.08e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446531580  47 RILELGCGTGYVTEKLSNLFPKaHITAIDFAESMIAVAKTrpNVK----NVTFHCEDIERLRLEESYDVIISN 115
Cdd:COG2263   48 TVLDLGCGTGMLAIGAALLGAK-KVVGVDIDPEALEIARE--NAErlgvRVDFIRADVTRIPLGGSVDTVVMN 117
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
32-141 1.28e-05

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


Pssm-ID: 182918  Cd Length: 255  Bit Score: 45.34  E-value: 1.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580  32 LLSTLNRRysansSIRILELGCGTGYVTEKLSNLfpKAHITAIDFAESMIAVAK----TRPNVKNVTF-HC--EDIERlR 104
Cdd:PRK11036  37 LLAELPPR-----PLRVLDAGGGEGQTAIKLAEL--GHQVILCDLSAEMIQRAKqaaeAKGVSDNMQFiHCaaQDIAQ-H 108

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446531580 105 LEESYDVIISNATFQWLNDLKQVIRNLFHHLSTDGIL 141
Cdd:PRK11036 109 LETPVDLILFHAVLEWVADPKSVLQTLWSVLRPGGAL 145
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 48-148 1.30e-05

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 45.90  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580  48 ILELGCGTGYVTEKLSNlfPKAHITAIDFAESMIavaKTRPNV----KNVTFHCEDIERLRL---EESYDVIISNATFQW 120
Cdd:PLN02336  41 VLELGAGIGRFTGELAK--KAGQVIALDFIESVI---KKNESInghyKNVKFMCADVTSPDLnisDGSVDLIFSNWLLMY 115

                         90       100       110
                 ....*....|....*....|....*....|..
gi 446531580 121 LND--LKQVIRNLFHHLSTDGILLF--STFGQ 148
Cdd:PLN02336 116 LSDkeVENLAERMVKWLKVGGYIFFreSCFHQ 147
arsM PRK11873
arsenite methyltransferase;
47-132 2.93e-05

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 44.55  E-value: 2.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580  47 RILELGCGTGYvteklsNLF-------PKAHITAIDFAESMIAVAK---TRPNVKNVTFHCEDIERLRLE-ESYDVIISN 115
Cdd:PRK11873  80 TVLDLGSGGGF------DCFlaarrvgPTGKVIGVDMTPEMLAKARanaRKAGYTNVEFRLGEIEALPVAdNSVDVIISN 153

                         90
                 ....*....|....*..
gi 446531580 116 ATFQWLNDLKQVIRNLF 132
Cdd:PRK11873 154 CVINLSPDKERVFKEAF 170
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 446531580  65 LFPKAHITAID-------FAESMIAVAktrpNVKNVTFHCEDIERLRLEESYDVIISNAtfqwLNDLKQVIRNLFHHLST 137
Cdd:COG0357   88 ARPDLQVTLVDslgkkiaFLREVVREL----GLKNVTVVHGRAEELAPREKFDVVTARA----VAPLPDLLELALPLLKP 159


                 ....*.
gi 446531580 138 DGILLF 143
Cdd:COG0357  160 GGRLLA 165
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
47-114 5.59e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 43.10  E-value: 5.59e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446531580  47 RILELGCGTGYVTEKLSNLFPKaHITAIDFAESMIAVAK----TRPNVKNVTFHCEDIERLRLEESYDVIIS 114
Cdd:COG4076   38 VVLDIGTGSGLLSMLAARAGAK-KVYAVEVNPDIAAVARriiaANGLSDRITVINADATDLDLPEKADVIIS 108
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
 43-159 5.90e-05

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 43.42  E-value: 5.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580  43 NSSIRILELGCGTG----YVTEKLSnlfpkAHITAIDFAESMIAVAKTRPNVKN-VTFHCEDIERLRLEES-YDVIISNA 116
Cdd:PTZ00098  51 NENSKVLDIGSGLGggckYINEKYG-----AHVHGVDICEKMVNIAKLRNSDKNkIEFEANDILKKDFPENtFDMIYSRD 125

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 446531580 117 TFQWLN--DLKQVIRNLFHHLSTDGILLFSTFGQETFQELHNSFR 159
Cdd:PTZ00098 126 AILHLSyaDKKKLFEKCYKWLKPNGILLITDYCADKIENWDEEFK 170
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 47-116 8.74e-05

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 42.38  E-value: 8.74e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446531580  47 RILELGCGTGYVTEKLSNLFpkAHITAIDFAESMIAVAKTR---PNVKNVTFHCEDIER-LRLEESYDVIISNA 116
Cdd:COG2518   69 RVLEIGTGSGYQAAVLARLA--GRVYSVERDPELAERARERlaaLGYDNVTVRVGDGALgWPEHAPFDRIIVTA 140
pcm PRK00312
protein-L-isoaspartate(D-aspartate) O-methyltransferase;
47-142 1.59e-04

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


Pssm-ID: 178974 [Multi-domain]  Cd Length: 212  Bit Score: 41.73  E-value: 1.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580  47 RILELGCGTGYVTEKLSNLFpkAHITAIDFAESMIAVAKTR---PNVKNVTFHCEDIER-LRLEESYDVIISNATFqwln 122
Cdd:PRK00312  81 RVLEIGTGSGYQAAVLAHLV--RRVFSVERIKTLQWEAKRRlkqLGLHNVSVRHGDGWKgWPAYAPFDRILVTAAA---- 154

                         90       100
                 ....*....|....*....|
gi 446531580 123 dlKQVIRNLFHHLSTDGILL 142
Cdd:PRK00312 155 --PEIPRALLEQLKEGGILV 172
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 36-129 2.21e-04

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: 41.96  E-value: 2.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580   36 LNRRYSANSSIRILELGCGTGYVTEKLSNLFPKAHITAIDFAESMIAVAKTrpNVK------NVTFHCEDIERLRLEESY 109
Cdd:TIGR00536 106 LASLISQPPILHILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAVAEE--NAEknqlehRVEFIQSNLFEPLAGQKI 183

                          90       100
                  ....*....|....*....|...
gi 446531580  110 DVIISNATF---QWLNDLKQVIR 129
Cdd:TIGR00536 184 DIIVSNPPYideEDLADLPNVVR 206
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
47-154 1.15e-03

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


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 39.27  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580   47 RILELGCGTGYVTEKLSNLF-PKAHITAIDFAESMiaVAKTRPNVK-----NVTFHCEDiERLRLEES--YDVIISNATf 118
Cdd:pfam01135  76 RVLEIGSGSGYLTACFARMVgEVGRVVSIEHIPEL--VEIARRNLEklgleNVIVVVGD-GRQGWPEFapYDAIHVGAA- 151

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 446531580  119 qwlndLKQVIRNLFHHLSTDGILLFSTfGQETFQEL 154
Cdd:pfam01135 152 -----APEIPEALIDQLKEGGRLVIPV-GPNGNQVL 181
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 47-113 1.18e-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: 1.18e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446531580  47 RILELGCGTGYVTEKLSN-LFPKAHITAIDFAESMIAVAKTrpNVK------NVTFHCEDIERLRLEESYDVII 113
Cdd:COG2519   94 RVLEAGTGSGALTLALARaVGPEGKVYSYERREDFAEIARK--NLErfglpdNVELKLGDIREGIDEGDVDAVF 165
methyltran_NanM TIGR04371
putative sugar O-methyltransferase; Members of this family appear to be SAM-dependent ...
 32-113 4.31e-03

putative sugar O-methyltransferase; Members of this family appear to be SAM-dependent O-methyltransferases acting on sugars, based on iterated sequence searches and gene context. Members occur in Leptospira O-antigen regions, as well NanM from the biosynthesis cluster for nanchangmycin, which produces 4-O-methyl-L-rhodinose as an intermediate. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 275164  Cd Length: 273  Bit Score: 37.78  E-value: 4.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580   32 LLSTLNRRYSANSSIRILELGCGTGYVTEKLSNLFPKAHITAIDFAEsMIAVA-----KTRPNVKNVTF-HCEDIERLRL 105
Cdd:TIGR04371 137 RLNFLKKFFGDLSVFRVLEIGGGYGRLGEILLKLFPNAIYYIVDLPP-QLALSeaylsEVFPEEKVVLYaQTRKQENIDL 215


                  ....*...
gi 446531580  106 EESYDVII 113
Cdd:TIGR04371 216 PDDGRIYF 223
rsmC PRK09489
16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC;
32-118 4.48e-03

16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC;


Pssm-ID: 181902 [Multi-domain]  Cd Length: 342  Bit Score: 38.00  E-value: 4.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531580  32 LLSTLNRRYSANssirILELGCGTGYVTEKLSNLFPKAHIT-------AIDFAESMIAVAKTRPNV--KNVTFHcedier 102
Cdd:PRK09489 188 LLSTLTPHTKGK----VLDVGCGAGVLSAVLARHSPKIRLTlsdvsaaALESSRATLAANGLEGEVfaSNVFSD------ 257

                         90
                 ....*....|....*.
gi 446531580 103 lrLEESYDVIISNATF 118
Cdd:PRK09489 258 --IKGRFDMIISNPPF 271
Methyltransf_32 pfam13679
Methyltransferase domain; This family appears to be a methyltransferase domain.
 27-87 6.10e-03

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


Pssm-ID: 379330 [Multi-domain]  Cd Length: 138  Bit Score: 36.01  E-value: 6.10e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446531580   27 KMAHSLLSTLNRRYSANSSIRILELGCGTGYVTEKLSNLFPKAHITAIDFAESMIAVAKTR 87
Cdd:pfam13679   8 HLAEFIAPLLKELLDENGPITIVDHGAGKGYLGFILYYLKYGVRVYGIDTRAELVEKANAL 68
PRK01544 PRK01544
bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) ...
 45-115 7.41e-03

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


Pssm-ID: 234958 [Multi-domain]  Cd Length: 506  Bit Score: 37.54  E-value: 7.41e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446531580  45 SIRILELGCGTGYVTEKLSNLFPKAHITAIDFAESMIAVAKTRPNVKNVT-----FHCEDIERLRlEESYDVIISN 115
Cdd:PRK01544 139 FLNILELGTGSGCIAISLLCELPNANVIATDISLDAIEVAKSNAIKYEVTdriqiIHSNWFENIE-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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