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Conserved domains on  [gi|501218648|ref|WP_012261666|]
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MULTISPECIES: malonyl-ACP O-methyltransferase BioC [Bacillus]

Protein Classification

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

malonyl-[acyl-carrier protein] O-methyltransferase BioC is a class I SAM-dependent methyltransferase in the biotin biosynthesis pathway that converts the free carboxyl group of a malonyl-thioester to its methyl ester using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 10-265 1.06e-79

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: 240.27  E-value: 1.06e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648   10 RFNGAAVSYDQYANVQKKMAHSLLSTLKERYSETSsIRILELGCGTGYVTEQLSNLFPKAHITAVDFADEMIAVAKTRKS 89
Cdd:TIGR02072   1 SFNKAAKTYDRHAKIQREMAKRLLALLKEKGIFIP-ASVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTKLS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648   90 lGNVMFRCEDIEQLKL-ENPYDVIISNATFQWLNDLKETVKNLFNYLSEEGILLFSTFGNTTFQELHTSFQRakkekgih 168
Cdd:TIGR02072  80 -ENVQFICGDAEKLPLeDSSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQSFGQ-------- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648  169 nctsIGQRFVSKEQLVNICKNPLGNVHVSETCYIESFTEVREFLHSIRKVGATNSNEESycQSPSLFRTMLRIYERDFTG 248
Cdd:TIGR02072 151 ----HGLRYLSLDELKALLKNSFELLTLEEELITLSFDDPLDVLRHLKKTGANGLSSGR--TSRKQLKAFLERYEQEFQP 224

                         250
                  ....*....|....*..
gi 501218648  249 kEGIMATYHALFTYITK 265
Cdd:TIGR02072 225 -DGLPLTYHVVYGIAKK 240
 
Name Accession Description Interval E-value
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 10-265 1.06e-79

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: 240.27  E-value: 1.06e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648   10 RFNGAAVSYDQYANVQKKMAHSLLSTLKERYSETSsIRILELGCGTGYVTEQLSNLFPKAHITAVDFADEMIAVAKTRKS 89
Cdd:TIGR02072   1 SFNKAAKTYDRHAKIQREMAKRLLALLKEKGIFIP-ASVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTKLS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648   90 lGNVMFRCEDIEQLKL-ENPYDVIISNATFQWLNDLKETVKNLFNYLSEEGILLFSTFGNTTFQELHTSFQRakkekgih 168
Cdd:TIGR02072  80 -ENVQFICGDAEKLPLeDSSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQSFGQ-------- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648  169 nctsIGQRFVSKEQLVNICKNPLGNVHVSETCYIESFTEVREFLHSIRKVGATNSNEESycQSPSLFRTMLRIYERDFTG 248
Cdd:TIGR02072 151 ----HGLRYLSLDELKALLKNSFELLTLEEELITLSFDDPLDVLRHLKKTGANGLSSGR--TSRKQLKAFLERYEQEFQP 224

                         250
                  ....*....|....*..
gi 501218648  249 kEGIMATYHALFTYITK 265
Cdd:TIGR02072 225 -DGLPLTYHVVYGIAKK 240
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
47-145 1.67e-35

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 122.62  E-value: 1.67e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648  47 RILELGCGTGYVTEQLSNLFPKAHITAVDFADEMIAVAktRKSLGNVMFRCEDIEQLKLENPYDVIISNATFQWLNDLKE 126
Cdd:COG4106    4 RVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARA--RARLPNVRFVVADLRDLDPPEPFDLVVSNAALHWLPDHAA 81

                         90
                 ....*....|....*....
gi 501218648 127 TVKNLFNYLSEEGILLFST 145
Cdd:COG4106   82 LLARLAAALAPGGVLAVQV 100
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 49-143 2.85e-21

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 85.41  E-value: 2.85e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648   49 LELGCGTGYVTEQLSNLFPkaHITAVDFADEMIAVAKTRKSLGNVMFRCEDIEQLKLE-NPYDVIISNATFQWLNDLKET 127
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA--RVTGVDISPEMLELAREKAPREGLTFVVGDAEDLPFPdNSFDLVLSSEVLHHVEDPERA 78

                          90
                  ....*....|....*.
gi 501218648  128 VKNLFNYLSEEGILLF 143
Cdd:pfam08241  79 LREIARVLKPGGILII 94
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 47-146 1.40e-16

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: 73.23  E-value: 1.40e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648  47 RILELGCGTGYVTEQLSNlFPKAHITAVDFADEMIAVAKTRKSLG---NVMFRCEDIEQLKLE--NPYDVIISNATFQWL 121
Cdd:cd02440    1 RVLDLGCGTGALALALAS-GPGARVTGVDISPVALELARKAAAALladNVEVLKGDAEELPPEadESFDVIISDPPLHHL 79

                         90       100
                 ....*....|....*....|....*.
gi 501218648 122 -NDLKETVKNLFNYLSEEGILLFSTF 146
Cdd:cd02440   80 vEDLARFLEEARRLLKPGGVLVLTLV 105
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
 18-120 2.90e-15

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 73.18  E-value: 2.90e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648  18 YDQYANVQKKMAHSLLStlkeRYSETSSIRILELGCGTGYVTEQLSNLFPKAHITAVDFADEMIAVAKTRkslgNVMFRC 97
Cdd:PRK14103   7 YLAFADHRGRPFYDLLA----RVGAERARRVVDLGCGPGNLTRYLARRWPGAVIEALDSSPEMVAAARER----GVDART 78

                         90       100
                 ....*....|....*....|...
gi 501218648  98 EDIEQLKLENPYDVIISNATFQW 120
Cdd:PRK14103  79 GDVRDWKPKPDTDVVVSNAALQW 101
 
Name Accession Description Interval E-value
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 10-265 1.06e-79

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: 240.27  E-value: 1.06e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648   10 RFNGAAVSYDQYANVQKKMAHSLLSTLKERYSETSsIRILELGCGTGYVTEQLSNLFPKAHITAVDFADEMIAVAKTRKS 89
Cdd:TIGR02072   1 SFNKAAKTYDRHAKIQREMAKRLLALLKEKGIFIP-ASVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTKLS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648   90 lGNVMFRCEDIEQLKL-ENPYDVIISNATFQWLNDLKETVKNLFNYLSEEGILLFSTFGNTTFQELHTSFQRakkekgih 168
Cdd:TIGR02072  80 -ENVQFICGDAEKLPLeDSSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQSFGQ-------- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648  169 nctsIGQRFVSKEQLVNICKNPLGNVHVSETCYIESFTEVREFLHSIRKVGATNSNEESycQSPSLFRTMLRIYERDFTG 248
Cdd:TIGR02072 151 ----HGLRYLSLDELKALLKNSFELLTLEEELITLSFDDPLDVLRHLKKTGANGLSSGR--TSRKQLKAFLERYEQEFQP 224

                         250
                  ....*....|....*..
gi 501218648  249 kEGIMATYHALFTYITK 265
Cdd:TIGR02072 225 -DGLPLTYHVVYGIAKK 240
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
47-145 1.67e-35

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 122.62  E-value: 1.67e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648  47 RILELGCGTGYVTEQLSNLFPKAHITAVDFADEMIAVAktRKSLGNVMFRCEDIEQLKLENPYDVIISNATFQWLNDLKE 126
Cdd:COG4106    4 RVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARA--RARLPNVRFVVADLRDLDPPEPFDLVVSNAALHWLPDHAA 81

                         90
                 ....*....|....*....
gi 501218648 127 TVKNLFNYLSEEGILLFST 145
Cdd:COG4106   82 LLARLAAALAPGGVLAVQV 100
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 47-145 1.15e-25

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: 97.78  E-value: 1.15e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648  47 RILELGCGTGYVTEQLSNLFpkAHITAVDFADEMIAVAKTRKSLGNVMFRCEDIEQLKLE-NPYDVIISNATFQWLNDLK 125
Cdd:COG2227   27 RVLDVGCGTGRLALALARRG--ADVTGVDISPEALEIARERAAELNVDFVQGDLEDLPLEdGSFDLVICSEVLEHLPDPA 104

                         90       100
                 ....*....|....*....|
gi 501218648 126 ETVKNLFNYLSEEGILLFST 145
Cdd:COG2227  105 ALLRELARLLKPGGLLLLST 124
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 11-161 2.65e-25

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: 97.37  E-value: 2.65e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648  11 FNGAAVSYDQYanvqkkmaHSLLSTLKERysetSSIRILELGCGTGYVTEQLSNLFpkAHITAVDFADEMIAVAKTR--K 88
Cdd:COG2226    1 FDRVAARYDGR--------EALLAALGLR----PGARVLDLGCGTGRLALALAERG--ARVTGVDISPEMLELARERaaE 66

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501218648  89 SLGNVMFRCEDIEQLKLE-NPYDVIISNATFQWLNDLKETVKNLFNYLSEEGILLFSTFGNTTFQELHTSFQRA 161
Cdd:COG2226   67 AGLNVEFVVGDAEDLPFPdGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEELLAEA 140
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
1-145 9.45e-25

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 97.38  E-value: 9.45e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648   1 MINKTLLQKRFNGAAVSYDQ--YANVQKKMAHSLLSTLKERYSETSSIRILELGCGTGYVTEQLSNLFpkAHITAVDFAD 78
Cdd:COG4976    1 MALDAYVEALFDQYADSYDAalVEDLGYEAPALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRG--YRLTGVDLSE 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501218648  79 EMIAVAKTRKslGNVMFRCEDIEQLK-LENPYDVIISNATFQWLNDLKETVKNLFNYLSEEGILLFST 145
Cdd:COG4976   79 EMLAKAREKG--VYDRLLVADLADLAePDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFIFSV 144
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 49-143 2.85e-21

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 85.41  E-value: 2.85e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648   49 LELGCGTGYVTEQLSNLFPkaHITAVDFADEMIAVAKTRKSLGNVMFRCEDIEQLKLE-NPYDVIISNATFQWLNDLKET 127
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA--RVTGVDISPEMLELAREKAPREGLTFVVGDAEDLPFPdNSFDLVLSSEVLHHVEDPERA 78

                          90
                  ....*....|....*.
gi 501218648  128 VKNLFNYLSEEGILLF 143
Cdd:pfam08241  79 LREIARVLKPGGILII 94
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 48-139 1.29e-20

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 83.77  E-value: 1.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648   48 ILELGCGTGYVTEQLSNLFpKAHITAVDFADEMIAVAKTR--KSLGNVMFRCEDIEQLKLE-NPYDVIISNATFQWLN-- 122
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRG-GARVTGVDLSPEMLERARERaaEAGLNVEFVQGDAEDLPFPdGSFDLVVSSGVLHHLPdp 79

                          90
                  ....*....|....*..
gi 501218648  123 DLKETVKNLFNYLSEEG 139
Cdd:pfam13649  80 DLEAALREIARVLKPGG 96
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 45-144 1.99e-18

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 80.73  E-value: 1.99e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648  45 SIRILELGCGTGYVTEQLSNLFpKAHITAVDFADEMIAVAKTRKS---LGNVMFRCEDIEQLK--LENPYDVIISNATFQ 119
Cdd:COG0500   27 GGRVLDLGCGTGRNLLALAARF-GGRVIGIDLSPEAIALARARAAkagLGNVEFLVADLAELDplPAESFDLVVAFGVLH 105

                         90       100
                 ....*....|....*....|....*..
gi 501218648 120 WLN--DLKETVKNLFNYLSEEGILLFS 144
Cdd:COG0500  106 HLPpeEREALLRELARALKPGGVLLLS 132
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 42-146 6.39e-18

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 78.23  E-value: 6.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648   42 ETSSIRILELGCGTGYVTEQL-SNLFPKAHITAVDFADEMIAVAKTRKS---LGNVMFRCEDIEQLKL---ENPYDVIIS 114
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELaEELGPNAEVVGIDISEEAIEKARENAQklgFDNVEFEQGDIEELPElleDDKFDVVIS 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 501218648  115 NATFQWLNDLKETVKNLFNYLSEEGILLFSTF 146
Cdd:pfam13847  81 NCVLNHIPDPDKVLQEILRVLKPGGRLIISDP 112
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 49-141 1.98e-17

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 75.48  E-value: 1.98e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648   49 LELGCGTGYVTEQLSNLFPKAHITAVDFADEMIAVAKTR-KSLGNVMFRCEDIEQLKLEN----PYDVIISNATFQWLND 123
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERlAALGLLNAVRVELFQLDLGEldpgSFDVVVASNVLHHLAD 80

                          90
                  ....*....|....*...
gi 501218648  124 LKETVKNLFNYLSEEGIL 141
Cdd:pfam08242  81 PRAVLRNIRRLLKPGGVL 98
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 47-146 1.40e-16

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: 73.23  E-value: 1.40e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648  47 RILELGCGTGYVTEQLSNlFPKAHITAVDFADEMIAVAKTRKSLG---NVMFRCEDIEQLKLE--NPYDVIISNATFQWL 121
Cdd:cd02440    1 RVLDLGCGTGALALALAS-GPGARVTGVDISPVALELARKAAAALladNVEVLKGDAEELPPEadESFDVIISDPPLHHL 79

                         90       100
                 ....*....|....*....|....*.
gi 501218648 122 -NDLKETVKNLFNYLSEEGILLFSTF 146
Cdd:cd02440   80 vEDLARFLEEARRLLKPGGVLVLTLV 105
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
 18-120 2.90e-15

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 73.18  E-value: 2.90e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648  18 YDQYANVQKKMAHSLLStlkeRYSETSSIRILELGCGTGYVTEQLSNLFPKAHITAVDFADEMIAVAKTRkslgNVMFRC 97
Cdd:PRK14103   7 YLAFADHRGRPFYDLLA----RVGAERARRVVDLGCGPGNLTRYLARRWPGAVIEALDSSPEMVAAARER----GVDART 78

                         90       100
                 ....*....|....*....|...
gi 501218648  98 EDIEQLKLENPYDVIISNATFQW 120
Cdd:PRK14103  79 GDVRDWKPKPDTDVVVSNAALQW 101
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 2-261 5.74e-15

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 72.48  E-value: 5.74e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648   2 INKTLLQKRFNGAAVSYDQYANVQKKMAHSLLSTLKERYSETssirILELGCGTG----YVTEQLSnlfpkaHITAVDFA 77
Cdd:PRK10258   4 VNKQAIAAAFGRAAAHYEQHAELQRQSADALLAMLPQRKFTH----VLDAGCGPGwmsrYWRERGS------QVTALDLS 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648  78 DEMIAVAKTRKSLGNvmFRCEDIEQLKL-ENPYDVIISNATFQWLNDLKETVKNLFNYLSEEGILLFSTFGNTTFQELHT 156
Cdd:PRK10258  74 PPMLAQARQKDAADH--YLAGDIESLPLaTATFDLAWSNLAVQWCGNLSTALRELYRVVRPGGVVAFTTLVQGSLPELHQ 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648 157 SFQrAKKEKGIHNctsigqRFVSKEQLVNICK--NPLGNVHVSETCYIESFTEVReflhSIRKVGATNSNEESycQSPSL 234
Cdd:PRK10258 152 AWQ-AVDERPHAN------RFLPPDAIEQALNgwRYQHHIQPITLWFDDALSAMR----SLKGIGATHLHEGR--DPRIL 218

                        250       260
                 ....*....|....*....|....*...
gi 501218648 235 FRTMLRIYERDFTGKEGIMA-TYHaLFT 261
Cdd:PRK10258 219 TRSQLQRLQLAWPQQQGRYPlTYH-LFL 245
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 18-141 9.73e-15

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 71.90  E-value: 9.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648  18 YDQYANVQKKMAHSLLStlkeRYSETSSIRILELGCGTGYVTEQLSNLFPKAHITAVDFADEMIAVAKTRksLGNVMFRC 97
Cdd:PRK01683   9 YLKFEDERTRPARDLLA----RVPLENPRYVVDLGCGPGNSTELLVERWPAARITGIDSSPAMLAEARSR--LPDCQFVE 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 501218648  98 EDIEQLKLENPYDVIISNATFQWLNDLKETVKNLFNYLSEEGIL 141
Cdd:PRK01683  83 ADIASWQPPQALDLIFANASLQWLPDHLELFPRLVSLLAPGGVL 126
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 47-145 7.56e-13

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 64.57  E-value: 7.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648  47 RILELGCGTGYVTEQLSNLFpKAHITAVDFADEMIAVAKTRKSL----GNVMFRCEDIEQLKLENPYDVIISNATFQWLN 122
Cdd:COG2230   54 RVLDIGCGWGGLALYLARRY-GVRVTGVTLSPEQLEYARERAAEaglaDRVEVRLADYRDLPADGQFDAIVSIGMFEHVG 132

                         90       100
                 ....*....|....*....|....*
gi 501218648 123 D--LKETVKNLFNYLSEEGILLFST 145
Cdd:COG2230  133 PenYPAYFAKVARLLKPGGRLLLHT 157
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 22-149 4.69e-12

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 62.45  E-value: 4.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648   22 ANVQKKMAHSLLSTLKERyseTSSIRILELGCGTGYVTEQLSNLFPkaHITAVDFADEMIAVAKtrksLGNVMFRCEDIE 101
Cdd:pfam13489   3 HQRERLLADLLLRLLPKL---PSPGRVLDFGCGTGIFLRLLRAQGF--SVTGVDPSPIAIERAL----LNVRFDQFDEQE 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 501218648  102 QLKLENPYDVIISNATFQWLNDLKETVKNLFNYLSEEGILLFSTFGNT 149
Cdd:pfam13489  74 AAVPAGKFDVIVAREVLEHVPDPPALLRQIAALLKPGGLLLLSTPLAS 121
YtxK COG0827
Adenine-specific DNA N6-methylase [Replication, recombination and repair];
32-159 2.31e-09

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


Pssm-ID: 440589 [Multi-domain]  Cd Length: 327  Bit Score: 56.88  E-value: 2.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648  32 LLSTLKERYSETSSIRILELGCGTGY-VTEQLSNLFPKAHITAVDFADEMIAVAKTRKSLGN--VMFRCEDIEQLKLENP 108
Cdd:COG0827  103 LIGYLVEKFTKKEGLRILDPAVGTGNlLTTVLNQLKKKVNAYGVEVDDLLIRLAAVLANLQGhpVELFHQDALQPLLIDP 182

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501218648 109 YDVIISN------------ATFQWLNDLKET-VKNLF-----NYLSEEGILLF----STFGNTTFQELHTSFQ 159
Cdd:COG0827  183 VDVVISDlpvgyypnderaKRFKLKADEGHSyAHHLFieqslNYLKPGGYLFFlvpsNLFESDQAAQLREFLK 255
PRK08317 PRK08317
hypothetical protein; Provisional
 47-123 2.48e-09

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 56.10  E-value: 2.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648  47 RILELGCGTGYVTEQLSNLF-PKAHITAVDFADEMIAVAKTRK--SLGNVMFRCEDIEQLKLENPY-DVIISNATFQWLN 122
Cdd:PRK08317  22 RVLDVGCGPGNDARELARRVgPEGRVVGIDRSEAMLALAKERAagLGPNVEFVRGDADGLPFPDGSfDAVRSDRVLQHLE 101


                 .
gi 501218648 123 D 123
Cdd:PRK08317 102 D 102
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 32-115 7.99e-09

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: 54.04  E-value: 7.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648  32 LLSTLKERYSEtssiRILELGCGTGYVTEQLSNLFPKAHITAVDfADEMiAVAKTRKS-----LGNVMFRCEDI-EQLKl 105
Cdd:COG2813   41 LLEHLPEPLGG----RVLDLGCGYGVIGLALAKRNPEARVTLVD-VNAR-AVELARANaaangLENVEVLWSDGlSGVP- 113

                         90
                 ....*....|
gi 501218648 106 ENPYDVIISN 115
Cdd:COG2813  114 DGSFDLILSN 123
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 47-115 2.93e-08

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: 53.22  E-value: 2.93e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501218648  47 RILELGCGTGYVTEQLSNLFPKAHITAVDFADEMIAVAktRKSL------GNVMFRCEDIEQLKLE---NPYDVIISN 115
Cdd:COG4123   40 RVLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELA--RRNValngleDRITVIHGDLKEFAAElppGSFDLVVSN 115
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 1-107 4.81e-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: 4.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648   1 MINKTLLQKRFNGAAVSYDQyAN---------VQKKMAhslLSTLKERYSEtssiRILELGCGTGYVTEQLSN-LFPKAH 70
Cdd:PRK00216   7 EEKQEKVAEMFDSIAPKYDL-MNdllsfglhrVWRRKT---IKWLGVRPGD----KVLDLACGTGDLAIALAKaVGKTGE 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 501218648  71 ITAVDFADEMIAVAKTR----KSLGNVMFRCEDIEQLKLEN 107
Cdd:PRK00216  79 VVGLDFSEGMLAVGREKlrdlGLSGNVEFVQGDAEALPFPD 119
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 38-115 1.51e-07

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 51.30  E-value: 1.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648  38 ERYSETSSIRILELGCGTGYVTEQLSNLFPKAHITAVDFADEMIAVAKT-RKSLG---NVMFRCEDI-EQLKLENPYDVI 112
Cdd:COG2890  106 ALLPAGAPPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRnAERLGledRVRFLQGDLfEPLPGDGRFDLI 185


                 ...
gi 501218648 113 ISN 115
Cdd:COG2890  186 VSN 188
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 32-118 1.56e-07

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: 49.90  E-value: 1.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648   32 LLSTLKERYSEtssiRILELGCGTGYVTEQLSNLFPKAHITAVDfADEMiAVAKTRKSL-----GNVMFRCEDIEQLKLE 106
Cdd:pfam05175  23 LLEHLPKDLSG----KVLDLGCGAGVLGAALAKESPDAELTMVD-INAR-ALESARENLaanglENGEVVASDVYSGVED 96

                          90
                  ....*....|..
gi 501218648  107 NPYDVIISNATF 118
Cdd:pfam05175  97 GKFDLIISNPPF 108
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
32-141 2.72e-07

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


Pssm-ID: 182918  Cd Length: 255  Bit Score: 50.35  E-value: 2.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648  32 LLSTLKERysetsSIRILELGCGTGYVTEQLSNLfpKAHITAVDFADEMIAVAKTRKS----LGNVMFRC---EDIEQlK 104
Cdd:PRK11036  37 LLAELPPR-----PLRVLDAGGGEGQTAIKLAEL--GHQVILCDLSAEMIQRAKQAAEakgvSDNMQFIHcaaQDIAQ-H 108

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 501218648 105 LENPYDVIISNATFQWLNDLKETVKNLFNYLSEEGIL 141
Cdd:PRK11036 109 LETPVDLILFHAVLEWVADPKSVLQTLWSVLRPGGAL 145
arsM PRK11873
arsenite methyltransferase;
47-115 4.19e-07

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 49.95  E-value: 4.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648  47 RILELGCGTGYvteqlsNLF-------PKAHITAVDFADEMIAVAK--TRKS-LGNVMFRCEDIEQLKLE-NPYDVIISN 115
Cdd:PRK11873  80 TVLDLGSGGGF------DCFlaarrvgPTGKVIGVDMTPEMLAKARanARKAgYTNVEFRLGEIEALPVAdNSVDVIISN 153
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 4-113 1.11e-06

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 48.29  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648   4 KTLLQKRFNGAAV-------SYDQYANVQK-------KMAHSLLSTLKErYSETSSIRILELGCGTGYVTEQLSNLfpKA 69
Cdd:PRK07580  10 KSEVRTYFNRTGFdrwariySDAPVSKVRAtvraghqRMRDTVLSWLPA-DGDLTGLRILDAGCGVGSLSIPLARR--GA 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 501218648  70 HITAVDFADEMIAVAKTR----KSLGNVMFRCEDIEQLKleNPYDVII 113
Cdd:PRK07580  87 KVVASDISPQMVEEARERapeaGLAGNITFEVGDLESLL--GRFDTVV 132
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 47-116 1.11e-06

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 47.78  E-value: 1.11e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501218648  47 RILELGCGTGYVTEQLSNLFpkAHITAVDFADEMIAVAKTR-KSLG--NVMFRCEDIEQ-LKLENPYDVIISNA 116
Cdd:COG2518   69 RVLEIGTGSGYQAAVLARLA--GRVYSVERDPELAERARERlAALGydNVTVRVGDGALgWPEHAPFDRIIVTA 140
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 38-115 1.25e-06

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 48.62  E-value: 1.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648  38 ERYSETSSIRILELGCGTGYVTEQLSNLFPKAHITAVDFADEMIAVAKT---RKSLGNVMFRCEDI-EQLKLEnPYDVII 113
Cdd:PRK09328 102 EALLLKEPLRVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRnakHGLGARVEFLQGDWfEPLPGG-RFDLIV 180


                 ..
gi 501218648 114 SN 115
Cdd:PRK09328 181 SN 182
pcm PRK00312
protein-L-isoaspartate(D-aspartate) O-methyltransferase;
47-142 1.86e-06

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


Pssm-ID: 178974 [Multi-domain]  Cd Length: 212  Bit Score: 47.51  E-value: 1.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648  47 RILELGCGTGYVTEQLSNLFpkAHITAVDFADEMIAVAKTR-KSLG--NVMFRCEDIEQ-LKLENPYDVIISNATFqwln 122
Cdd:PRK00312  81 RVLEIGTGSGYQAAVLAHLV--RRVFSVERIKTLQWEAKRRlKQLGlhNVSVRHGDGWKgWPAYAPFDRILVTAAA---- 154

                         90       100
                 ....*....|....*....|
gi 501218648 123 dlKETVKNLFNYLSEEGILL 142
Cdd:PRK00312 155 --PEIPRALLEQLKEGGILV 172
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
47-115 6.59e-06

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 45.67  E-value: 6.59e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501218648  47 RILELGCGTGYVTEQLSNLFPKaHITAVDFADEMIAVAKT--RKSLGNVMFRCEDIEQLKLENPYDVIISN 115
Cdd:COG2263   48 TVLDLGCGTGMLAIGAALLGAK-KVVGVDIDPEALEIAREnaERLGVRVDFIRADVTRIPLGGSVDTVVMN 117
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
47-142 6.87e-06

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


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 45.82  E-value: 6.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648   47 RILELGCGTGYVTEQLSNLF-PKAHITAVDFADEMIAVAKTR-KSLG--NVMFRCEDIEQLKLEN-PYDVIISNATfqwl 121
Cdd:pfam01135  76 RVLEIGSGSGYLTACFARMVgEVGRVVSIEHIPELVEIARRNlEKLGleNVIVVVGDGRQGWPEFaPYDAIHVGAA---- 151

                          90       100
                  ....*....|....*....|.
gi 501218648  122 ndLKETVKNLFNYLSEEGILL 142
Cdd:pfam01135 152 --APEIPEALIDQLKEGGRLV 170
COG3963 COG3963
Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];
47-114 1.49e-05

Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];


Pssm-ID: 443163  Cd Length: 193  Bit Score: 44.43  E-value: 1.49e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501218648  47 RILELGCGTGYVTEQ-LSNLFPKAHITAVDFADEMiaVAKTRKSLGNVMFRCEDIEQLK------LENPYDVIIS 114
Cdd:COG3963   48 PVVELGPGTGVFTRAiLARGVPDARLLAVEINPEF--AEHLRRRFPRVTVVNGDAEDLAellaehGIGKVDAVVS 120
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
10-161 1.56e-05

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


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 44.43  E-value: 1.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648  10 RFNGA---AVSYDQYANVQKkMAHSLLSTLKERysetssIRILELGCGTGYVTEQLSNLFPKAHITAVDFADEMIAVAK- 85
Cdd:COG0421    7 VLDGVvqsTMELDEFEYHEM-MAHVPLLFHPNP------KRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELARe 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648  86 ----TRKSLGN--VMFRCED-IEQLK-LENPYDVIISNAT---------FQwlndlKETVKNLFNYLSEEGILLFSTFGN 148
Cdd:COG0421   80 yfplLAPAFDDprLRVVIGDgRAFLReAEESYDVIIVDLTdpvgpaeglFT-----REFYEDCRRALKPGGVLVVNLGSP 154

                        170
                 ....*....|...
gi 501218648 149 TTFQELHTSFQRA 161
Cdd:COG0421  155 FYGLDLLRRVLAT 167
methyltran_NanM TIGR04371
putative sugar O-methyltransferase; Members of this family appear to be SAM-dependent ...
 5-133 2.56e-05

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: 44.72  E-value: 2.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648    5 TLLQKRFNG--AAVSYDQYANVqkkmahslLSTLKERYSETSSIRILELGCGTGYVTEQLSNLFPKAHITAVDFAdEMIA 82
Cdd:TIGR04371 116 PIEVFSFDGrsFSRSYLNYVLR--------LNFLKKFFGDLSVFRVLEIGGGYGRLGEILLKLFPNAIYYIVDLP-PQLA 186

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501218648   83 VA-----------------KTRK-------SLGNVMFRC-EDIEQLKlENPYDVIISNATFQWLNdlKETVKNLFN 133
Cdd:TIGR04371 187 LSeaylsevfpeekvvlyaQTRKqenidlpDDGRIYFLPpWQLPLLG-NGKIDLFVNFISFQEME--PDVVDNYLS 259
PRK01544 PRK01544
bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) ...
 23-144 1.04e-04

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


Pssm-ID: 234958 [Multi-domain]  Cd Length: 506  Bit Score: 43.32  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648  23 NVQKKMAH--SLLSTLKERYSETSSiRILELGCGTGYVTEQLSNLFPKAHITAVDFADEMIAVAKTRKSLGNVMFRCEDI 100
Cdd:PRK01544 116 NPEKKQLNpcFRGNDISSNCNDKFL-NILELGTGSGCIAISLLCELPNANVIATDISLDAIEVAKSNAIKYEVTDRIQII 194

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 501218648 101 EQLKLEN----PYDVIISNATFQWLNDLKETVKNLFNYlsEEGILLFS 144
Cdd:PRK01544 195 HSNWFENiekqKFDFIVSNPPYISHSEKSEMAIETINY--EPSIALFA 240
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 47-129 2.37e-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: 41.57  E-value: 2.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648   47 RILELGCGTGYVTEQLSNLFPKAHITAVDFADEMIAVAKtrkslgnvmfrcEDIEQLKLENP----------------YD 110
Cdd:TIGR00536 117 HILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAVAE------------ENAEKNQLEHRvefiqsnlfeplagqkID 184

                          90       100
                  ....*....|....*....|..
gi 501218648  111 VIISNATF---QWLNDLKETVK 129
Cdd:TIGR00536 185 IIVSNPPYideEDLADLPNVVR 206
PRK13943 PRK13943
protein-L-isoaspartate O-methyltransferase; Provisional
 16-126 3.27e-04

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 237568 [Multi-domain]  Cd Length: 322  Bit Score: 41.37  E-value: 3.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648  16 VSYDQYANVQKKMAHSLLSTLKERYSETSSIRILELGCGTGYVTEQLSNLF-PKAHITAVDFADEMIAVA-KTRKSLG-- 91
Cdd:PRK13943  52 VSYDDGEEYSTSSQPSLMALFMEWVGLDKGMRVLEIGGGTGYNAAVMSRVVgEKGLVVSVEYSRKICEIAkRNVRRLGie 131

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 501218648  92 NVMFRCED----IEQLKlenPYDVII-----SNATFQWLNDLKE 126
Cdd:PRK13943 132 NVIFVCGDgyygVPEFA---PYDVIFvtvgvDEVPETWFTQLKE 172
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
 47-165 7.67e-04

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 39.95  E-value: 7.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648  47 RILELGCGTG----YVTEQLSnlfpkAHITAVDFADEMIAVAKTRKSLGN-VMFRCEDIEQLKL-ENPYDVIISNATFQW 120
Cdd:PTZ00098  55 KVLDIGSGLGggckYINEKYG-----AHVHGVDICEKMVNIAKLRNSDKNkIEFEANDILKKDFpENTFDMIYSRDAILH 129

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 501218648 121 LN--DLKETVKNLFNYLSEEGILLFSTFGNTTFQELHTSFQRAKKEK 165
Cdd:PTZ00098 130 LSyaDKKKLFEKCYKWLKPNGILLITDYCADKIENWDEEFKAYIKKR 176
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 47-112 1.34e-03

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: 38.63  E-value: 1.34e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501218648  47 RILELGCGTGYVTEQL-SNLFPKAHITAVDFADEMIAVAK---TRKSLGN-VMFRCED-IEQLK--LENPYDVI 112
Cdd:COG4122   19 RILEIGTGTGYSTLWLaRALPDDGRLTTIEIDPERAAIARenfARAGLADrIRLILGDaLEVLPrlADGPFDLV 92
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 48-131 3.50e-03

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 38.58  E-value: 3.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648  48 ILELGCGTGYVTEQLSNlfPKAHITAVDFADEMIavaKTRKSLG----NVMFRCEDI--EQLKLE-NPYDVIISNATFQW 120
Cdd:PLN02336  41 VLELGAGIGRFTGELAK--KAGQVIALDFIESVI---KKNESINghykNVKFMCADVtsPDLNISdGSVDLIFSNWLLMY 115

                         90
                 ....*....|.
gi 501218648 121 LNDlkETVKNL 131
Cdd:PLN02336 116 LSD--KEVENL 124
PRK06202 PRK06202
hypothetical protein; Provisional
 36-115 4.29e-03

hypothetical protein; Provisional


Pssm-ID: 180466 [Multi-domain]  Cd Length: 232  Bit Score: 37.67  E-value: 4.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501218648  36 LKERYSETSSIRILELGCGTGYVTEQLSNLfpkAH-------ITAVDFADEMIAVAKTRKSLGNVMFRCEDIEQLKLENP 108
Cdd:PRK06202  52 LRPALSADRPLTLLDIGCGGGDLAIDLARW---ARrdglrleVTAIDPDPRAVAFARANPRRPGVTFRQAVSDELVAEGE 128


                 ....*...
gi 501218648 109 -YDVIISN 115
Cdd:PRK06202 129 rFDVVTSN 136
 
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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