NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|507034405|ref|WP_016106102|]
View 

malonyl-ACP O-methyltransferase BioC [Bacillus cereus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 4.37e-83

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: 249.13  E-value: 4.37e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405   10 RFNGAAVSYDQYANVQKKMAHSLLSILKRRyNETSSIRILELGCGTGYVTEQLSKLFPKAQITAVDFAESMITIAKTRQN 89
Cdd:TIGR02072   1 SFNKAAKTYDRHAKIQREMAKRLLALLKEK-GIFIPASVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTKLS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405   90 tENVTFHCEDIERLRLEE-SYDVIISNATFQWLNNVKQVIRNLFHHLSTDGIVLFSTFGQETFQELHASFQRakeekniq 168
Cdd:TIGR02072  80 -ENVQFICGDAEKLPLEDsSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQSFGQ-------- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405  169 netlIGQRFYSKDQLLHICKIETGDVHVSETCYIERFAEVREFLHSIRKVGATNSNEESycQSPSLFRTMLRIYERDFtE 248
Cdd:TIGR02072 151 ----HGLRYLSLDELKALLKNSFELLTLEEELITLSFDDPLDVLRHLKKTGANGLSSGR--TSRKQLKAFLERYEQEF-Q 223

                         250
                  ....*....|....*..
gi 507034405  249 KEGIVATYHALFTYITK 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 4.37e-83

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: 249.13  E-value: 4.37e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405   10 RFNGAAVSYDQYANVQKKMAHSLLSILKRRyNETSSIRILELGCGTGYVTEQLSKLFPKAQITAVDFAESMITIAKTRQN 89
Cdd:TIGR02072   1 SFNKAAKTYDRHAKIQREMAKRLLALLKEK-GIFIPASVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTKLS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405   90 tENVTFHCEDIERLRLEE-SYDVIISNATFQWLNNVKQVIRNLFHHLSTDGIVLFSTFGQETFQELHASFQRakeekniq 168
Cdd:TIGR02072  80 -ENVQFICGDAEKLPLEDsSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQSFGQ-------- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405  169 netlIGQRFYSKDQLLHICKIETGDVHVSETCYIERFAEVREFLHSIRKVGATNSNEESycQSPSLFRTMLRIYERDFtE 248
Cdd:TIGR02072 151 ----HGLRYLSLDELKALLKNSFELLTLEEELITLSFDDPLDVLRHLKKTGANGLSSGR--TSRKQLKAFLERYEQEF-Q 223

                         250
                  ....*....|....*..
gi 507034405  249 KEGIVATYHALFTYITK 265
Cdd:TIGR02072 224 PDGLPLTYHVVYGIAKK 240
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
47-145 1.21e-35

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 123.01  E-value: 1.21e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405  47 RILELGCGTGYVTEQLSKLFPKAQITAVDFAESMITIAktRQNTENVTFHCEDIERLRLEESYDVIISNATFQWLNNVKQ 126
Cdd:COG4106    4 RVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARA--RARLPNVRFVVADLRDLDPPEPFDLVVSNAALHWLPDHAA 81

                         90
                 ....*....|....*....
gi 507034405 127 VIRNLFHHLSTDGIVLFST 145
Cdd:COG4106   82 LLARLAAALAPGGVLAVQV 100
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 48-139 8.46e-24

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 92.24  E-value: 8.46e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405   48 ILELGCGTGYVTEQLSKLFpKAQITAVDFAESMITIAKTR--QNTENVTFHCEDIERLRLE-ESYDVIISNATFQWLN-- 122
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRG-GARVTGVDLSPEMLERARERaaEAGLNVEFVQGDAEDLPFPdGSFDLVVSSGVLHHLPdp 79

                          90
                  ....*....|....*..
gi 507034405  123 NVKQVIRNLFHHLSTDG 139
Cdd:pfam13649  80 DLEAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 47-146 3.02e-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: 80.55  E-value: 3.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405  47 RILELGCGTGYVTEQLSKlFPKAQITAVDFAESMITIAKTRQNT---ENVTFHCEDIERLRLE--ESYDVIISNATFQWL 121
Cdd:cd02440    1 RVLDLGCGTGALALALAS-GPGARVTGVDISPVALELARKAAAAllaDNVEVLKGDAEELPPEadESFDVIISDPPLHHL 79

                         90       100
                 ....*....|....*....|....*.
gi 507034405 122 -NNVKQVIRNLFHHLSTDGIVLFSTF 146
Cdd:cd02440   80 vEDLARFLEEARRLLKPGGVLVLTLV 105
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 2-261 5.45e-17

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 77.88  E-value: 5.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405   2 INKTLLQKRFNGAAVSYDQYANVQKKMAHSLLSILKRRYNETssirILELGCGTG----YVTEQLSklfpkaQITAVDFA 77
Cdd:PRK10258   4 VNKQAIAAAFGRAAAHYEQHAELQRQSADALLAMLPQRKFTH----VLDAGCGPGwmsrYWRERGS------QVTALDLS 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405  78 ESMITIAKTRQNTENvtFHCEDIERLRLEE-SYDVIISNATFQWLNNVKQVIRNLFHHLSTDGIVLFSTFGQETFQELHA 156
Cdd:PRK10258  74 PPMLAQARQKDAADH--YLAGDIESLPLATaTFDLAWSNLAVQWCGNLSTALRELYRVVRPGGVVAFTTLVQGSLPELHQ 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405 157 SFQrAKEEKNIQNetligqRFYSKDQLLHICK--IETGDVHVSETCYIERFAEVReflhSIRKVGATNSNEESycQSPSL 234
Cdd:PRK10258 152 AWQ-AVDERPHAN------RFLPPDAIEQALNgwRYQHHIQPITLWFDDALSAMR----SLKGIGATHLHEGR--DPRIL 218

                        250       260
                 ....*....|....*....|....*...
gi 507034405 235 FRTMLRIYERDFTEKEGIVA-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 4.37e-83

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: 249.13  E-value: 4.37e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405   10 RFNGAAVSYDQYANVQKKMAHSLLSILKRRyNETSSIRILELGCGTGYVTEQLSKLFPKAQITAVDFAESMITIAKTRQN 89
Cdd:TIGR02072   1 SFNKAAKTYDRHAKIQREMAKRLLALLKEK-GIFIPASVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTKLS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405   90 tENVTFHCEDIERLRLEE-SYDVIISNATFQWLNNVKQVIRNLFHHLSTDGIVLFSTFGQETFQELHASFQRakeekniq 168
Cdd:TIGR02072  80 -ENVQFICGDAEKLPLEDsSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQSFGQ-------- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405  169 netlIGQRFYSKDQLLHICKIETGDVHVSETCYIERFAEVREFLHSIRKVGATNSNEESycQSPSLFRTMLRIYERDFtE 248
Cdd:TIGR02072 151 ----HGLRYLSLDELKALLKNSFELLTLEEELITLSFDDPLDVLRHLKKTGANGLSSGR--TSRKQLKAFLERYEQEF-Q 223

                         250
                  ....*....|....*..
gi 507034405  249 KEGIVATYHALFTYITK 265
Cdd:TIGR02072 224 PDGLPLTYHVVYGIAKK 240
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
47-145 1.21e-35

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 123.01  E-value: 1.21e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405  47 RILELGCGTGYVTEQLSKLFPKAQITAVDFAESMITIAktRQNTENVTFHCEDIERLRLEESYDVIISNATFQWLNNVKQ 126
Cdd:COG4106    4 RVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARA--RARLPNVRFVVADLRDLDPPEPFDLVVSNAALHWLPDHAA 81

                         90
                 ....*....|....*....
gi 507034405 127 VIRNLFHHLSTDGIVLFST 145
Cdd:COG4106   82 LLARLAAALAPGGVLAVQV 100
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 32-145 1.87e-27

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: 102.79  E-value: 1.87e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405  32 LLSILKRRYNETSsiRILELGCGTGYVTEQLSKLFpkAQITAVDFAESMITIAKTRQNTENVTFHCEDIERLRLE-ESYD 110
Cdd:COG2227   14 LAALLARLLPAGG--RVLDVGCGTGRLALALARRG--ADVTGVDISPEALEIARERAAELNVDFVQGDLEDLPLEdGSFD 89

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 507034405 111 VIISNATFQWLNNVKQVIRNLFHHLSTDGIVLFST 145
Cdd:COG2227   90 LVICSEVLEHLPDPAALLRELARLLKPGGLLLLST 124
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 11-161 3.09e-27

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: 102.76  E-value: 3.09e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405  11 FNGAAVSYDQYanvqkkmaHSLLSILKRRYNEtssiRILELGCGTGYVTEQLSKLFpkAQITAVDFAESMITIAKTR--Q 88
Cdd:COG2226    1 FDRVAARYDGR--------EALLAALGLRPGA----RVLDLGCGTGRLALALAERG--ARVTGVDISPEMLELARERaaE 66

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507034405  89 NTENVTFHCEDIERLRLE-ESYDVIISNATFQWLNNVKQVIRNLFHHLSTDGIVLFSTFGQETFQELHASFQRA 161
Cdd:COG2226   67 AGLNVEFVVGDAEDLPFPdGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEELLAEA 140
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
1-145 1.58e-25

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 99.30  E-value: 1.58e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405   1 MINKTLLQKRFNGAAVSYDQ--YANVQKKMAHSLLSILKRRYNETSSIRILELGCGTGYVTEQLSKLFpkAQITAVDFAE 78
Cdd:COG4976    1 MALDAYVEALFDQYADSYDAalVEDLGYEAPALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRG--YRLTGVDLSE 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507034405  79 SMITIAKTRQNteNVTFHCEDIERLR-LEESYDVIISNATFQWLNNVKQVIRNLFHHLSTDGIVLFST 145
Cdd:COG4976   79 EMLAKAREKGV--YDRLLVADLADLAePDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFIFSV 144
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 48-139 8.46e-24

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 92.24  E-value: 8.46e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405   48 ILELGCGTGYVTEQLSKLFpKAQITAVDFAESMITIAKTR--QNTENVTFHCEDIERLRLE-ESYDVIISNATFQWLN-- 122
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRG-GARVTGVDLSPEMLERARERaaEAGLNVEFVQGDAEDLPFPdGSFDLVVSSGVLHHLPdp 79

                          90
                  ....*....|....*..
gi 507034405  123 NVKQVIRNLFHHLSTDG 139
Cdd:pfam13649  80 DLEAALREIARVLKPGG 96
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 49-143 1.31e-22

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 88.88  E-value: 1.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405   49 LELGCGTGYVTEQLSKLFPkaQITAVDFAESMITIAKTRQNTENVTFHCEDIERLRLE-ESYDVIISNATFQWLNNVKQV 127
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA--RVTGVDISPEMLELAREKAPREGLTFVVGDAEDLPFPdNSFDLVLSSEVLHHVEDPERA 78

                          90
                  ....*....|....*.
gi 507034405  128 IRNLFHHLSTDGIVLF 143
Cdd:pfam08241  79 LREIARVLKPGGILII 94
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 45-214 9.83e-20

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 84.58  E-value: 9.83e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405  45 SIRILELGCGTGYVTEQLSKLFpKAQITAVDFAESMITIAK---TRQNTENVTFHCEDIERL--RLEESYDVIISNATFQ 119
Cdd:COG0500   27 GGRVLDLGCGTGRNLLALAARF-GGRVIGIDLSPEAIALARaraAKAGLGNVEFLVADLAELdpLPAESFDLVVAFGVLH 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405 120 WLN--NVKQVIRNLFHHLSTDGIVLFStfgQETFQELHASFQRAKEEKNIQNETLIGQRFYSkDQLLHICKIETGDVHVS 197
Cdd:COG0500  106 HLPpeEREALLRELARALKPGGVLLLS---ASDAAAALSLARLLLLATASLLELLLLLRLLA-LELYLRALLAAAATEDL 181

                        170
                 ....*....|....*..
gi 507034405 198 ETCYIERFAEVREFLHS 214
Cdd:COG0500  182 RSDALLESANALEYLLS 198
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 49-141 1.14e-19

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 81.26  E-value: 1.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405   49 LELGCGTGYVTEQLSKLFPKAQITAVDFAESMITIAKTR------QNTENVTFHCEDIERLrLEESYDVIISNATFQWLN 122
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERlaalglLNAVRVELFQLDLGEL-DPGSFDVVVASNVLHHLA 79

                          90
                  ....*....|....*....
gi 507034405  123 NVKQVIRNLFHHLSTDGIV 141
Cdd:pfam08242  80 DPRAVLRNIRRLLKPGGVL 98
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 47-146 3.02e-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: 80.55  E-value: 3.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405  47 RILELGCGTGYVTEQLSKlFPKAQITAVDFAESMITIAKTRQNT---ENVTFHCEDIERLRLE--ESYDVIISNATFQWL 121
Cdd:cd02440    1 RVLDLGCGTGALALALAS-GPGARVTGVDISPVALELARKAAAAllaDNVEVLKGDAEELPPEadESFDVIISDPPLHHL 79

                         90       100
                 ....*....|....*....|....*.
gi 507034405 122 -NNVKQVIRNLFHHLSTDGIVLFSTF 146
Cdd:cd02440   80 vEDLARFLEEARRLLKPGGVLVLTLV 105
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 2-261 5.45e-17

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 77.88  E-value: 5.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405   2 INKTLLQKRFNGAAVSYDQYANVQKKMAHSLLSILKRRYNETssirILELGCGTG----YVTEQLSklfpkaQITAVDFA 77
Cdd:PRK10258   4 VNKQAIAAAFGRAAAHYEQHAELQRQSADALLAMLPQRKFTH----VLDAGCGPGwmsrYWRERGS------QVTALDLS 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405  78 ESMITIAKTRQNTENvtFHCEDIERLRLEE-SYDVIISNATFQWLNNVKQVIRNLFHHLSTDGIVLFSTFGQETFQELHA 156
Cdd:PRK10258  74 PPMLAQARQKDAADH--YLAGDIESLPLATaTFDLAWSNLAVQWCGNLSTALRELYRVVRPGGVVAFTTLVQGSLPELHQ 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405 157 SFQrAKEEKNIQNetligqRFYSKDQLLHICK--IETGDVHVSETCYIERFAEVReflhSIRKVGATNSNEESycQSPSL 234
Cdd:PRK10258 152 AWQ-AVDERPHAN------RFLPPDAIEQALNgwRYQHHIQPITLWFDDALSAMR----SLKGIGATHLHEGR--DPRIL 218

                        250       260
                 ....*....|....*....|....*...
gi 507034405 235 FRTMLRIYERDFTEKEGIVA-TYHaLFT 261
Cdd:PRK10258 219 TRSQLQRLQLAWPQQQGRYPlTYH-LFL 245
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 42-186 7.02e-16

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 72.83  E-value: 7.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405   42 ETSSIRILELGCGTGYVTEQL-SKLFPKAQITAVDFAESMITIAKTR---QNTENVTFHCEDIERLRL---EESYDVIIS 114
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELaEELGPNAEVVGIDISEEAIEKARENaqkLGFDNVEFEQGDIEELPElleDDKFDVVIS 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507034405  115 NATFQWLNNVKQVIRNLFHHLSTDGIVLFStfgqeTFQELHASFQRAKEEKNIQNETLIGQrfYSKDQLLHI 186
Cdd:pfam13847  81 NCVLNHIPDPDKVLQEILRVLKPGGRLIIS-----DPDSLAELPAHVKEDSTYYAGCVGGA--ILKKKLYEL 145
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 47-145 1.24e-14

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 69.57  E-value: 1.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405  47 RILELGCGTGYVTEQLSKLFpKAQITAVDFAESMITIAKTRQN----TENVTFHCEDIERLRLEESYDVIISNATFQWLN 122
Cdd:COG2230   54 RVLDIGCGWGGLALYLARRY-GVRVTGVTLSPEQLEYARERAAeaglADRVEVRLADYRDLPADGQFDAIVSIGMFEHVG 132

                         90       100
                 ....*....|....*....|....*
gi 507034405 123 --NVKQVIRNLFHHLSTDGIVLFST 145
Cdd:COG2230  133 peNYPAYFAKVARLLKPGGRLLLHT 157
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
 18-120 3.79e-13

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 67.41  E-value: 3.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405  18 YDQYANVQKKMAHSLLSilkrRYNETSSIRILELGCGTGYVTEQLSKLFPKAQITAVDFAESMITIAKTRqnteNVTFHC 97
Cdd:PRK14103   7 YLAFADHRGRPFYDLLA----RVGAERARRVVDLGCGPGNLTRYLARRWPGAVIEALDSSPEMVAAARER----GVDART 78

                         90       100
                 ....*....|....*....|...
gi 507034405  98 EDIERLRLEESYDVIISNATFQW 120
Cdd:PRK14103  79 GDVRDWKPKPDTDVVVSNAALQW 101
PRK08317 PRK08317
hypothetical protein; Provisional
 47-145 9.30e-13

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 66.11  E-value: 9.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405  47 RILELGCGTGYVTEQLSKLF-PKAQITAVDFAESMITIAKTR--QNTENVTFHCEDIERLRLE-ESYDVIISNATFQWLN 122
Cdd:PRK08317  22 RVLDVGCGPGNDARELARRVgPEGRVVGIDRSEAMLALAKERaaGLGPNVEFVRGDADGLPFPdGSFDAVRSDRVLQHLE 101

                         90       100
                 ....*....|....*....|....
gi 507034405 123 NVKQVIRNLFHHLSTDG-IVLFST 145
Cdd:PRK08317 102 DPARALAEIARVLRPGGrVVVLDT 125
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 22-188 3.69e-12

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 62.83  E-value: 3.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405   22 ANVQKKMAHSLLSILKRRyneTSSIRILELGCGTGYVTEQLSKLFPkaQITAVDFAESMITIAKtrqntENVTFHCED-I 100
Cdd:pfam13489   3 HQRERLLADLLLRLLPKL---PSPGRVLDFGCGTGIFLRLLRAQGF--SVTGVDPSPIAIERAL-----LNVRFDQFDeQ 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405  101 ERLRLEESYDVIISNATFQWLNNVKQVIRNLFHHLSTDGIVLFSTFGqetfqelhASFQRAKEEKNIQNETLIGQR--FY 178
Cdd:pfam13489  73 EAAVPAGKFDVIVAREVLEHVPDPPALLRQIAALLKPGGLLLLSTPL--------ASDEADRLLLEWPYLRPRNGHisLF 144

                         170
                  ....*....|
gi 507034405  179 SKDQLLHICK 188
Cdd:pfam13489 145 SARSLKRLLE 154
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 18-140 1.14e-11

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 63.04  E-value: 1.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405  18 YDQYANVQKKMAHSLLSilkrRYNETSSIRILELGCGTGYVTEQLSKLFPKAQITAVDFAESMITIAKTRqnTENVTFHC 97
Cdd:PRK01683   9 YLKFEDERTRPARDLLA----RVPLENPRYVVDLGCGPGNSTELLVERWPAARITGIDSSPAMLAEARSR--LPDCQFVE 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 507034405  98 EDIERLRLEESYDVIISNATFQWLNNVKQVIRNLFHHLSTDGI 140
Cdd:PRK01683  83 ADIASWQPPQALDLIFANASLQWLPDHLELFPRLVSLLAPGGV 125
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 47-115 5.07e-11

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: 60.93  E-value: 5.07e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507034405  47 RILELGCGTGYVTEQLSKLFPKAQITAVDFAESMITIAktRQNTEN------VTFHCEDIERLRLE---ESYDVIISN 115
Cdd:COG4123   40 RVLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELA--RRNVALngledrITVIHGDLKEFAAElppGSFDLVVSN 115
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 47-139 5.83e-10

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: 57.12  E-value: 5.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405  47 RILELGCGTGYVTEQLSKLFPKAQITAVDfaESMITIAKTRQN-----TENVTFHCEDIERLRLEESYDVIISNATF-QW 120
Cdd:COG2813   52 RVLDLGCGYGVIGLALAKRNPEARVTLVD--VNARAVELARANaaangLENVEVLWSDGLSGVPDGSFDLILSNPPFhAG 129

                         90       100
                 ....*....|....*....|...
gi 507034405 121 LNNVKQVIRNLFH----HLSTDG 139
Cdd:COG2813  130 RAVDKEVAHALIAdaarHLRPGG 152
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 4-113 9.77e-10

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 57.15  E-value: 9.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405   4 KTLLQKRFNGAAV-------SYDQYANVQK-------KMAHSLLSILKRrYNETSSIRILELGCGTGYVTEQLSKLfpKA 69
Cdd:PRK07580  10 KSEVRTYFNRTGFdrwariySDAPVSKVRAtvraghqRMRDTVLSWLPA-DGDLTGLRILDAGCGVGSLSIPLARR--GA 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 507034405  70 QITAVDFAESMITIAKTRQNTE----NVTFHCEDIERLRleESYDVII 113
Cdd:PRK07580  87 KVVASDISPQMVEEARERAPEAglagNITFEVGDLESLL--GRFDTVV 132
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 1-112 7.79e-09

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 54.77  E-value: 7.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405   1 MINKTLLQKRFNGAAVSYDQyAN---------VQKKMAHSLLsilkrryNETSSIRILELGCGTGYVTEQLSK-LFPKAQ 70
Cdd:PRK00216   7 EEKQEKVAEMFDSIAPKYDL-MNdllsfglhrVWRRKTIKWL-------GVRPGDKVLDLACGTGDLAIALAKaVGKTGE 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 507034405  71 ITAVDFAESMITIAKTR----QNTENVTFHCEDIERLRLE-ESYDVI 112
Cdd:PRK00216  79 VVGLDFSEGMLAVGREKlrdlGLSGNVEFVQGDAEALPFPdNSFDAV 125
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 39-115 5.44e-08

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 52.46  E-value: 5.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405  39 RYNETSSIRILELGCGTGYVTEQLSKLFPKAQITAVDFAESMITIAktRQN------TENVTFHCEDI-ERLRLEESYDV 111
Cdd:COG2890  107 LLPAGAPPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVA--RRNaerlglEDRVRFLQGDLfEPLPGDGRFDL 184


                 ....
gi 507034405 112 IISN 115
Cdd:COG2890  185 IVSN 188
COG3963 COG3963
Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];
47-146 7.73e-08

Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];


Pssm-ID: 443163  Cd Length: 193  Bit Score: 51.36  E-value: 7.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405  47 RILELGCGTGYVTEQ-LSKLFPKAQITAVDFAESMitIAKTRQNTENVTFHCEDIERL------RLEESYDVIISN---A 116
Cdd:COG3963   48 PVVELGPGTGVFTRAiLARGVPDARLLAVEINPEF--AEHLRRRFPRVTVVNGDAEDLaellaeHGIGKVDAVVSGlplL 125

                         90       100       110
                 ....*....|....*....|....*....|
gi 507034405 117 TFQwLNNVKQVIRNLFHHLSTDGIvlFSTF 146
Cdd:COG3963  126 SFP-PELRRAILDAAFRVLAPGGV--FVQF 152
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 47-139 8.15e-08

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: 50.67  E-value: 8.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405   47 RILELGCGTGYVTEQLSKLFPKAQITAVDfaESMITIAKTRQN-----TENVTFHCEDIERLRLEESYDVIISNATF-QW 120
Cdd:pfam05175  34 KVLDLGCGAGVLGAALAKESPDAELTMVD--INARALESARENlaangLENGEVVASDVYSGVEDGKFDLIISNPPFhAG 111

                          90       100
                  ....*....|....*....|...
gi 507034405  121 LNNVKQVIRNLFH----HLSTDG 139
Cdd:pfam05175 112 LATTYNVAQRFIAdakrHLRPGG 134
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
10-161 1.22e-07

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


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 50.60  E-value: 1.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405  10 RFNGA---AVSYDQYANVQKkMAHSLLSILKRRynetssIRILELGCGTGYVTEQLSKLFPKAQITAVDFAESMITIAKT 86
Cdd:COG0421    7 VLDGVvqsTMELDEFEYHEM-MAHVPLLFHPNP------KRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELARE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405  87 -------RQNTENVTFHCED----IERLrlEESYDVIISNAT-------------FqwlnnvkqvIRNLFHHLSTDGIVL 142
Cdd:COG0421   80 yfpllapAFDDPRLRVVIGDgrafLREA--EESYDVIIVDLTdpvgpaeglftreF---------YEDCRRALKPGGVLV 148

                        170       180
                 ....*....|....*....|...
gi 507034405 143 F----STFGQETFQELHASFQRA 161
Cdd:COG0421  149 VnlgsPFYGLDLLRRVLATLREV 171
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 38-115 2.72e-07

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 50.55  E-value: 2.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405  38 RRYNETSSIRILELGCGTGYVTEQLSKLFPKAQITAVDFAESMITIAKT---RQNTENVTFHCEDI-ERLRlEESYDVII 113
Cdd:PRK09328 102 EALLLKEPLRVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRnakHGLGARVEFLQGDWfEPLP-GGRFDLIV 180


                 ..
gi 507034405 114 SN 115
Cdd:PRK09328 181 SN 182
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
47-115 3.80e-07

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 49.52  E-value: 3.80e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 507034405  47 RILELGCGTGYVTEqLSKLFPKAQITAVDFAESMITIAKT--RQNTENVTFHCEDIERLRLEESYDVIISN 115
Cdd:COG2263   48 TVLDLGCGTGMLAI-GAALLGAKKVVGVDIDPEALEIAREnaERLGVRVDFIRADVTRIPLGGSVDTVVMN 117
YtxK COG0827
Adenine-specific DNA N6-methylase [Replication, recombination and repair];
39-115 7.23e-07

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


Pssm-ID: 440589 [Multi-domain]  Cd Length: 327  Bit Score: 49.56  E-value: 7.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405  39 RYNETSSIRILELGCGTGY----VTEQLSKlfpKAQITAVDFAESMITIAKTRQNTEN--VTFHCEDIERLRLEESYDVI 112
Cdd:COG0827  110 KFTKKEGLRILDPAVGTGNllttVLNQLKK---KVNAYGVEVDDLLIRLAAVLANLQGhpVELFHQDALQPLLIDPVDVV 186


                 ...
gi 507034405 113 ISN 115
Cdd:COG0827  187 ISD 189
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 48-180 1.39e-05

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 45.90  E-value: 1.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405  48 ILELGCGTGYVTEQLSKlfPKAQITAVDFAESMItiaKTRQNT----ENVTFHCEDIERLRL---EESYDVIISNATFQW 120
Cdd:PLN02336  41 VLELGAGIGRFTGELAK--KAGQVIALDFIESVI---KKNESInghyKNVKFMCADVTSPDLnisDGSVDLIFSNWLLMY 115

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507034405 121 LNN--VKQVIRNLFHHLSTDGIVLFStfgqetfqelHASFQRAKEEKNIQNETLIGQ-RFYSK 180
Cdd:PLN02336 116 LSDkeVENLAERMVKWLKVGGYIFFR----------ESCFHQSGDSKRKNNPTHYREpRFYTK 168
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
46-141 1.73e-05

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


Pssm-ID: 182918  Cd Length: 255  Bit Score: 44.95  E-value: 1.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405  46 IRILELGCGTGYVTEQLSKLfpKAQITAVDFAESMITIAK----TRQNTENVTF-HC--EDIERlRLEESYDVIISNATF 118
Cdd:PRK11036  46 LRVLDAGGGEGQTAIKLAEL--GHQVILCDLSAEMIQRAKqaaeAKGVSDNMQFiHCaaQDIAQ-HLETPVDLILFHAVL 122

                         90       100
                 ....*....|....*....|...
gi 507034405 119 QWLNNVKQVIRNLFHHLSTDGIV 141
Cdd:PRK11036 123 EWVADPKSVLQTLWSVLRPGGAL 145
arsM PRK11873
arsenite methyltransferase;
47-115 2.01e-05

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 44.94  E-value: 2.01e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507034405  47 RILELGCGTG---YVTEQlsKLFPKAQITAVDFAESMITIAktRQNTE-----NVTFHCEDIERLRLE-ESYDVIISN 115
Cdd:PRK11873  80 TVLDLGSGGGfdcFLAAR--RVGPTGKVIGVDMTPEMLAKA--RANARkagytNVEFRLGEIEALPVAdNSVDVIISN 153
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 47-143 4.01e-05

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: 42.86  E-value: 4.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405  47 RILELGCGTGYVTEQLSKLFPK-AQITAVDFAESMITIAktRQN------TENVTFHCED----IERLrLEESYDVIISN 115
Cdd:COG4122   19 RILEIGTGTGYSTLWLARALPDdGRLTTIEIDPERAAIA--RENfaraglADRIRLILGDalevLPRL-ADGPFDLVFID 95

                         90       100
                 ....*....|....*....|....*...
gi 507034405 116 AtfqWLNNVKQVIRNLFHHLSTDGIVLF 143
Cdd:COG4122   96 A---DKSNYPDYLELALPLLRPGGLIVA 120
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
47-154 5.16e-05

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


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 43.13  E-value: 5.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405   47 RILELGCGTGYVTEQLSKLF-PKAQITAVDFAESMITIAKTRQNT---ENVTFHCEDiERLRLEES--YDVIISNATfqw 120
Cdd:pfam01135  76 RVLEIGSGSGYLTACFARMVgEVGRVVSIEHIPELVEIARRNLEKlglENVIVVVGD-GRQGWPEFapYDAIHVGAA--- 151

                          90       100       110
                  ....*....|....*....|....*....|....
gi 507034405  121 lnnVKQVIRNLFHHLSTDGIVLFSTfGQETFQEL 154
Cdd:pfam01135 152 ---APEIPEALIDQLKEGGRLVIPV-GPNGNQVL 181
PRK06202 PRK06202
hypothetical protein; Provisional
 34-141 7.31e-05

hypothetical protein; Provisional


Pssm-ID: 180466 [Multi-domain]  Cd Length: 232  Bit Score: 43.07  E-value: 7.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405  34 SILKRRYNETSSIRILELGCGTGYVTEQLSKLFP----KAQITAVDFAESMITIAKTRQNTENVTF---HCEDIERLRle 106
Cdd:PRK06202  50 RLLRPALSADRPLTLLDIGCGGGDLAIDLARWARrdglRLEVTAIDPDPRAVAFARANPRRPGVTFrqaVSDELVAEG-- 127

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 507034405 107 ESYDVIISNatfqwlnnvkqvirNLFHHLSTDGIV 141
Cdd:PRK06202 128 ERFDVVTSN--------------HFLHHLDDAEVV 148
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
47-114 9.91e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 42.72  E-value: 9.91e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507034405  47 RILELGCGTGYvteqLSKLFPKA---QITAVDFAESMITIAK----TRQNTENVTFHCEDIERLRLEESYDVIIS 114
Cdd:COG4076   38 VVLDIGTGSGL----LSMLAARAgakKVYAVEVNPDIAAVARriiaANGLSDRITVINADATDLDLPEKADVIIS 108
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 47-116 1.26e-04

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 42.00  E-value: 1.26e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507034405  47 RILELGCGTGYVTEQLSKLFpkAQITAVDFAESMITIAKTR---QNTENVTFHCEDIER-LRLEESYDVIISNA 116
Cdd:COG2518   69 RVLEIGTGSGYQAAVLARLA--GRVYSVERDPELAERARERlaaLGYDNVTVRVGDGALgWPEHAPFDRIIVTA 140
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 47-115 1.66e-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: 42.34  E-value: 1.66e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507034405   47 RILELGCGTGYVTEQLSKLFPKAQITAVDFAESMITIAKtrQNTE------NVTFHCEDIERLRLEESYDVIISN 115
Cdd:TIGR00536 117 HILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAVAE--ENAEknqlehRVEFIQSNLFEPLAGQKIDIIVSN 189
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
7-159 2.11e-04

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 41.66  E-value: 2.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405    7 LQKRFNGAAVSYDQYANVQKKMAHSLL-SILKRRYNETSSIRILELGCGTGYVTEQLSKLF-PKAQITAVDFAESMITIA 84
Cdd:pfam01209   4 VGDVFSSVASKYDLMNDVISFGIHRLWkDFTMKCMGVKRGNKFLDVAGGTGDWTFGLSDSAgSSGKVVGLDINENMLKEG 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507034405   85 KTRQNTE---NVTFHCEDIERLRLEE-SYDVIISNATFQWLNNVKQVIRNLFHHLSTDGIVLFSTFGQETFQELHASFQ 159
Cdd:pfam01209  84 EKKAKEEgkyNIEFLQGNAEELPFEDdSFDIVTISFGLRNFPDYLKVLKEAFRVLKPGGRVVCLEFSKPENPLLSQAYE 162
methyltran_NanM TIGR04371
putative sugar O-methyltransferase; Members of this family appear to be SAM-dependent ...
 32-76 2.27e-04

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: 41.63  E-value: 2.27e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 507034405   32 LLSILKRRYNETSSIRILELGCGTGYVTEQLSKLFPKAQITAVDF 76
Cdd:TIGR04371 137 RLNFLKKFFGDLSVFRVLEIGGGYGRLGEILLKLFPNAIYYIVDL 181
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 29-160 4.08e-04

FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping.


Pssm-ID: 426399  Cd Length: 179  Bit Score: 40.26  E-value: 4.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405   29 AHSLLSILKRRYNETSSIRILELGCGTGYVTEQLSKLfPKAQITAVDFAEsmITIAKTRQNtENVTFHCEDIERL----- 103
Cdd:pfam01728   6 AYKLLEIDEKFGLLKPGKTVLDLGAAPGGWSQVALQR-GAGKVVGVDLGP--MQLWKPRND-PGVTFIQGDIRDPetldl 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507034405  104 ---RLEESYDVIIS----NATfqwLNNVKQVIRNL----------FHHLSTDGIVLFSTFGQETFQELHASFQR 160
Cdd:pfam01728  82 leeLLGRKVDLVLSdgspFIS---GNKVLDHLRSLdlvkaalevaLELLRKGGNFVCKVFQGEDFSELLYLLKL 152
PRK12335 PRK12335
tellurite resistance protein TehB; Provisional
 47-142 6.03e-04

tellurite resistance protein TehB; Provisional


Pssm-ID: 183450 [Multi-domain]  Cd Length: 287  Bit Score: 40.31  E-value: 6.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405  47 RILELGCGTGYVTEQLSKL-FpkaQITAVDF-AESMITIAKTRQNTE-NVTFHCEDIERLRLEESYDVIISNATFQWLN- 122
Cdd:PRK12335 123 KALDLGCGQGRNSLYLALLgF---DVTAVDInQQSLENLQEIAEKENlNIRTGLYDINSASIQEEYDFILSTVVLMFLNr 199

                         90       100
                 ....*....|....*....|.
gi 507034405 123 -NVKQVIRNLFHHLSTDGIVL 142
Cdd:PRK12335 200 eRIPAIIKNMQEHTNPGGYNL 220
PRK01544 PRK01544
bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) ...
 23-115 1.03e-03

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


Pssm-ID: 234958 [Multi-domain]  Cd Length: 506  Bit Score: 40.23  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405  23 NVQKKMAH--SLLSILKRRYNETSSiRILELGCGTGYVTEQLSKLFPKAQITAVDFAESMITIAKTRQNTENVT-----F 95
Cdd:PRK01544 116 NPEKKQLNpcFRGNDISSNCNDKFL-NILELGTGSGCIAISLLCELPNANVIATDISLDAIEVAKSNAIKYEVTdriqiI 194

                         90       100
                 ....*....|....*....|
gi 507034405  96 HCEDIERLRlEESYDVIISN 115
Cdd:PRK01544 195 HSNWFENIE-KQKFDFIVSN 213
Methyltransf_24 pfam13578
Methyltransferase domain; This family appears to be a methyltransferase domain.
 49-143 1.58e-03

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


Pssm-ID: 433324 [Multi-domain]  Cd Length: 106  Bit Score: 37.29  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405   49 LELGCGTGYVTEQLSKLFPKA---QITAVD----FAESMITIAKTRqNTENVTFHCEDIERLR---LEESYDVII--SNA 116
Cdd:pfam13578   1 VEIGTYSGVSTLWLAAALRDNglgRLTAVDpdpgAEEAGALLRKAG-LDDRVRLIVGDSREALpslADGPIDLLFidGDH 79

                          90       100
                  ....*....|....*....|....*..
gi 507034405  117 TFQWlnnVKQVIRNLFHHLSTDGIVLF 143
Cdd:pfam13578  80 TYEA---VLNDLELWLPRLAPGGVILF 103
pcm PRK00312
protein-L-isoaspartate(D-aspartate) O-methyltransferase;
47-177 1.88e-03

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


Pssm-ID: 178974 [Multi-domain]  Cd Length: 212  Bit Score: 38.65  E-value: 1.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405  47 RILELGCGTGYVTEQLSKLFpkAQITAVDFAESMITIAKTRQNT---ENVTFHCEDIER-LRLEESYDVIISNATFqwln 122
Cdd:PRK00312  81 RVLEIGTGSGYQAAVLAHLV--RRVFSVERIKTLQWEAKRRLKQlglHNVSVRHGDGWKgWPAYAPFDRILVTAAA---- 154

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 507034405 123 nvKQVIRNLFHHLSTDGIvLFSTFGQETFQELhasfQRAKEEKN-IQNETLIGQRF 177
Cdd:PRK00312 155 --PEIPRALLEQLKEGGI-LVAPVGGEEQQLL----TRVRKRGGrFEREVLEEVRF 203
Methyltransf_2 pfam00891
O-methyltransferase domain; This family includes a range of O-methyltransferases. These ...
 47-142 4.00e-03

O-methyltransferase domain; This family includes a range of O-methyltransferases. These enzymes utilize S-adenosyl methionine.


Pssm-ID: 395719 [Multi-domain]  Cd Length: 208  Bit Score: 37.38  E-value: 4.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405   47 RILELGCGTGYVTEQLSKLFPKAQITAVDFAEsMITIAKTR---QNTENVTFHCEDIERLRLEESYDVIISNATFQWLN- 122
Cdd:pfam00891  63 SLVDVGGGTGALAQAIVSLYPGCKGIVFDLPH-VVEAAPTHfsaGEEPRVTFHGGDFFKDSLPEADAYILKRVLHDWSDe 141

                          90       100
                  ....*....|....*....|
gi 507034405  123 NVKQVIRNLFHHLSTDGIVL 142
Cdd:pfam00891 142 KCVKLLKRCYKACPAGGKVI 161
COG4262 COG4262
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction ...
 47-141 4.32e-03

Predicted spermidine synthase with an N-terminal membrane domain [General function prediction only];


Pssm-ID: 443404 [Multi-domain]  Cd Length: 426  Bit Score: 37.92  E-value: 4.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405  47 RILELGCGTGYVTEQLSKLFPKAQITAVDFAESMITIAKTRQ----------NTENVTFHCEDIeRLRLEES---YDVII 113
Cdd:COG4262  289 RVLVLGGGDGLAAREVLKYPDVESVTLVDLDPEVTDLAKTNPflrelnggalNDPRVTVVNADA-FQFLRETdekYDVII 367

                         90       100       110
                 ....*....|....*....|....*....|....
gi 507034405 114 SNA----TFQwLNNV--KQVIRNLFHHLSTDGIV 141
Cdd:COG4262  368 VDLpdpsNFS-LGKLysVEFYRLVRRHLAPGGVL 400
RsmG COG0357
16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ...
 65-143 4.42e-03

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: 37.44  E-value: 4.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405  65 LFPKAQITAVD-------FAESMITIAktrqNTENVTFHCEDIERLRLEESYDVIISNAtfqwLNNVKQVIRNLFHHLST 137
Cdd:COG0357   88 ARPDLQVTLVDslgkkiaFLREVVREL----GLKNVTVVHGRAEELAPREKFDVVTARA----VAPLPDLLELALPLLKP 159


                 ....*.
gi 507034405 138 DGIVLF 143
Cdd:COG0357  160 GGRLLA 165
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
 47-190 8.90e-03

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 36.87  E-value: 8.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034405  47 RILELGCGTG----YVTEQLSklfpkAQITAVDFAESMITIAKTR-QNTENVTFHCEDIERLRLEES-YDVIISNATFQW 120
Cdd:PTZ00098  55 KVLDIGSGLGggckYINEKYG-----AHVHGVDICEKMVNIAKLRnSDKNKIEFEANDILKKDFPENtFDMIYSRDAILH 129

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507034405 121 LN--NVKQVIRNLFHHLSTDGIVLFSTFGQETFQELHASFqraKEEKNIQNETLIGQRFYSkdQLLHICKIE 190
Cdd:PTZ00098 130 LSyaDKKKLFEKCYKWLKPNGILLITDYCADKIENWDEEF---KAYIKKRKYTLIPIQEYG--DLIKSCNFQ 196
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH