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Conserved domains on  [gi|388432524|gb|EIL89525|]
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biotin synthesis protein [Rhodanobacter fulvus Jip2]

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 ...
 15-263 1.39e-73

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: 225.63  E-value: 1.39e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524   15 FGRAAGTYEKHDVLQREVQSLLLDRL-DFYLQTPQRVVDIGAGTGRGSALLKQRYPKAEVIAIDLALPMLRAAKKHSSwr 93
Cdd:TIGR02072   2 FNKAAKTYDRHAKIQREMAKRLLALLkEKGIFIPASVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTKLS-- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524   94 KPFLRVCAEATALPLADHSVDVLHSNLCFQWVDALPPLFAECVRVLKPGGMLVFSSFGPDTLKELRAAWaeadqQAHVSR 173
Cdd:TIGR02072  80 ENVQFICGDAEKLPLEDSSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQSF-----GQHGLR 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524  174 FLDMHDVGDAvLAAGLRDPVLDVCRYTLTYSEPRKLLQDLQGLGATNADhareRNLTGKARYRRMLEAYESMRLDGHIPA 253
Cdd:TIGR02072 155 YLSLDELKAL-LKNSFELLTLEEELITLSFDDPLDVLRHLKKTGANGLS----SGRTSRKQLKAFLERYEQEFQPDGLPL 229

                         250
                  ....*....|
gi 388432524  254 TWEVVTAHAW 263
Cdd:TIGR02072 230 TYHVVYGIAK 239
 
Name Accession Description Interval E-value
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 15-263 1.39e-73

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: 225.63  E-value: 1.39e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524   15 FGRAAGTYEKHDVLQREVQSLLLDRL-DFYLQTPQRVVDIGAGTGRGSALLKQRYPKAEVIAIDLALPMLRAAKKHSSwr 93
Cdd:TIGR02072   2 FNKAAKTYDRHAKIQREMAKRLLALLkEKGIFIPASVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTKLS-- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524   94 KPFLRVCAEATALPLADHSVDVLHSNLCFQWVDALPPLFAECVRVLKPGGMLVFSSFGPDTLKELRAAWaeadqQAHVSR 173
Cdd:TIGR02072  80 ENVQFICGDAEKLPLEDSSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQSF-----GQHGLR 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524  174 FLDMHDVGDAvLAAGLRDPVLDVCRYTLTYSEPRKLLQDLQGLGATNADhareRNLTGKARYRRMLEAYESMRLDGHIPA 253
Cdd:TIGR02072 155 YLSLDELKAL-LKNSFELLTLEEELITLSFDDPLDVLRHLKKTGANGLS----SGRTSRKQLKAFLERYEQEFQPDGLPL 229

                         250
                  ....*....|
gi 388432524  254 TWEVVTAHAW 263
Cdd:TIGR02072 230 TYHVVYGIAK 239
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 5-259 4.38e-39

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 137.58  E-value: 4.38e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524   5 QLDQSRIAHQFGRAAGTYEKHDVLQREVQSLLLDRLdfylqtPQR----VVDIGAGTGRGSALLKQRypKAEVIAIDLAL 80
Cdd:PRK10258   3 TVNKQAIAAAFGRAAAHYEQHAELQRQSADALLAML------PQRkfthVLDAGCGPGWMSRYWRER--GSQVTALDLSP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524  81 PMLRAAKKHSSWRKpflRVCAEATALPLADHSVDVLHSNLCFQWVDALPPLFAECVRVLKPGGMLVFSSFGPDTLKELRA 160
Cdd:PRK10258  75 PMLAQARQKDAADH---YLAGDIESLPLATATFDLAWSNLAVQWCGNLSTALRELYRVVRPGGVVAFTTLVQGSLPELHQ 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524 161 AWAEADQQAHVSRFLDMHDVGDAVLAAGLRDPVLDVcryTLTYSEPRKLLQDLQGLGATNADHARERNLTGKARYRRMLE 240
Cdd:PRK10258 152 AWQAVDERPHANRFLPPDAIEQALNGWRYQHHIQPI---TLWFDDALSAMRSLKGIGATHLHEGRDPRILTRSQLQRLQL 228

                        250
                 ....*....|....*....
gi 388432524 241 AYEsmRLDGHIPATWEVVT 259
Cdd:PRK10258 229 AWP--QQQGRYPLTYHLFL 245
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 15-165 8.75e-31

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: 112.39  E-value: 8.75e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524  15 FGRAAGTYEKHDvlqrevqsLLLDRLDfyLQTPQRVVDIGAGTGRGSALLKQRypKAEVIAIDLALPMLRAAKKHSSWRK 94
Cdd:COG2226    1 FDRVAARYDGRE--------ALLAALG--LRPGARVLDLGCGTGRLALALAER--GARVTGVDISPEMLELARERAAEAG 68

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 388432524  95 PFLR-VCAEATALPLADHSVDVLHSNLCFQWVDALPPLFAECVRVLKPGGMLVFSSFGPDTLKELRAAWAEA 165
Cdd:COG2226   69 LNVEfVVGDAEDLPFPDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEELLAEA 140
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 51-147 2.43e-25

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 96.58  E-value: 2.43e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524   51 VDIGAGTGRGSALLKQRYPkaEVIAIDLALPMLRAAKKHSSwRKPFLRVCAEATALPLADHSVDVLHSNLCFQWVDALPP 130
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA--RVTGVDISPEMLELAREKAP-REGLTFVVGDAEDLPFPDNSFDLVLSSEVLHHVEDPER 77

                          90
                  ....*....|....*..
gi 388432524  131 LFAECVRVLKPGGMLVF 147
Cdd:pfam08241  78 ALREIARVLKPGGILII 94
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 49-150 1.52e-12

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: 62.83  E-value: 1.52e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524  49 RVVDIGAGTGrGSALLKQRYPKAEVIAIDLALPMLRAAKKHSSWRKP----FLRVCAEaTALPLADHSVDVLHSNLCFQW 124
Cdd:cd02440    1 RVLDLGCGTG-ALALALASGPGARVTGVDISPVALELARKAAAALLAdnveVLKGDAE-ELPPEADESFDVIISDPPLHH 78

                         90       100
                 ....*....|....*....|....*..
gi 388432524 125 -VDALPPLFAECVRVLKPGGMLVFSSF 150
Cdd:cd02440   79 lVEDLARFLEEARRLLKPGGVLVLTLV 105
 
Name Accession Description Interval E-value
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 15-263 1.39e-73

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: 225.63  E-value: 1.39e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524   15 FGRAAGTYEKHDVLQREVQSLLLDRL-DFYLQTPQRVVDIGAGTGRGSALLKQRYPKAEVIAIDLALPMLRAAKKHSSwr 93
Cdd:TIGR02072   2 FNKAAKTYDRHAKIQREMAKRLLALLkEKGIFIPASVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTKLS-- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524   94 KPFLRVCAEATALPLADHSVDVLHSNLCFQWVDALPPLFAECVRVLKPGGMLVFSSFGPDTLKELRAAWaeadqQAHVSR 173
Cdd:TIGR02072  80 ENVQFICGDAEKLPLEDSSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQSF-----GQHGLR 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524  174 FLDMHDVGDAvLAAGLRDPVLDVCRYTLTYSEPRKLLQDLQGLGATNADhareRNLTGKARYRRMLEAYESMRLDGHIPA 253
Cdd:TIGR02072 155 YLSLDELKAL-LKNSFELLTLEEELITLSFDDPLDVLRHLKKTGANGLS----SGRTSRKQLKAFLERYEQEFQPDGLPL 229

                         250
                  ....*....|
gi 388432524  254 TWEVVTAHAW 263
Cdd:TIGR02072 230 TYHVVYGIAK 239
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 5-259 4.38e-39

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 137.58  E-value: 4.38e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524   5 QLDQSRIAHQFGRAAGTYEKHDVLQREVQSLLLDRLdfylqtPQR----VVDIGAGTGRGSALLKQRypKAEVIAIDLAL 80
Cdd:PRK10258   3 TVNKQAIAAAFGRAAAHYEQHAELQRQSADALLAML------PQRkfthVLDAGCGPGWMSRYWRER--GSQVTALDLSP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524  81 PMLRAAKKHSSWRKpflRVCAEATALPLADHSVDVLHSNLCFQWVDALPPLFAECVRVLKPGGMLVFSSFGPDTLKELRA 160
Cdd:PRK10258  75 PMLAQARQKDAADH---YLAGDIESLPLATATFDLAWSNLAVQWCGNLSTALRELYRVVRPGGVVAFTTLVQGSLPELHQ 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524 161 AWAEADQQAHVSRFLDMHDVGDAVLAAGLRDPVLDVcryTLTYSEPRKLLQDLQGLGATNADHARERNLTGKARYRRMLE 240
Cdd:PRK10258 152 AWQAVDERPHANRFLPPDAIEQALNGWRYQHHIQPI---TLWFDDALSAMRSLKGIGATHLHEGRDPRILTRSQLQRLQL 228

                        250
                 ....*....|....*....
gi 388432524 241 AYEsmRLDGHIPATWEVVT 259
Cdd:PRK10258 229 AWP--QQQGRYPLTYHLFL 245
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 15-165 8.75e-31

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: 112.39  E-value: 8.75e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524  15 FGRAAGTYEKHDvlqrevqsLLLDRLDfyLQTPQRVVDIGAGTGRGSALLKQRypKAEVIAIDLALPMLRAAKKHSSWRK 94
Cdd:COG2226    1 FDRVAARYDGRE--------ALLAALG--LRPGARVLDLGCGTGRLALALAER--GARVTGVDISPEMLELARERAAEAG 68

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 388432524  95 PFLR-VCAEATALPLADHSVDVLHSNLCFQWVDALPPLFAECVRVLKPGGMLVFSSFGPDTLKELRAAWAEA 165
Cdd:COG2226   69 LNVEfVVGDAEDLPFPDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEELLAEA 140
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 51-147 2.43e-25

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 96.58  E-value: 2.43e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524   51 VDIGAGTGRGSALLKQRYPkaEVIAIDLALPMLRAAKKHSSwRKPFLRVCAEATALPLADHSVDVLHSNLCFQWVDALPP 130
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA--RVTGVDISPEMLELAREKAP-REGLTFVVGDAEDLPFPDNSFDLVLSSEVLHHVEDPER 77

                          90
                  ....*....|....*..
gi 388432524  131 LFAECVRVLKPGGMLVF 147
Cdd:pfam08241  78 ALREIARVLKPGGILII 94
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 50-143 2.61e-23

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 91.47  E-value: 2.61e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524   50 VVDIGAGTGRGSALLKQRYpKAEVIAIDLALPMLRAAKKHSSWRKPFLR-VCAEATALPLADHSVDVLHSNLCFQWV--D 126
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRG-GARVTGVDLSPEMLERARERAAEAGLNVEfVQGDAEDLPFPDGSFDLVVSSGVLHHLpdP 79

                          90
                  ....*....|....*..
gi 388432524  127 ALPPLFAECVRVLKPGG 143
Cdd:pfam13649  80 DLEAALREIARVLKPGG 96
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
47-148 3.55e-22

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 88.34  E-value: 3.55e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524  47 PQRVVDIGAGTGRGSALLKQRYPKAEVIAIDLALPMLRAAKKhsswRKPFLR-VCAEATALPLaDHSVDVLHSNLCFQWV 125
Cdd:COG4106    2 PRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARA----RLPNVRfVVADLRDLDP-PEPFDLVVSNAALHWL 76

                         90       100
                 ....*....|....*....|...
gi 388432524 126 DALPPLFAECVRVLKPGGMLVFS 148
Cdd:COG4106   77 PDHAALLARLAAALAPGGVLAVQ 99
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 36-148 1.92e-19

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: 81.99  E-value: 1.92e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524  36 LLDRLDFYLQTPQRVVDIGAGTGRGSALLKQRypKAEVIAIDLALPMLRAAKKHSSWRKPFLRvCAEATALPLADHSVDV 115
Cdd:COG2227   14 LAALLARLLPAGGRVLDVGCGTGRLALALARR--GADVTGVDISPEALEIARERAAELNVDFV-QGDLEDLPLEDGSFDL 90

                         90       100       110
                 ....*....|....*....|....*....|...
gi 388432524 116 LHSNLCFQWVDALPPLFAECVRVLKPGGMLVFS 148
Cdd:COG2227   91 VICSEVLEHLPDPAALLRELARLLKPGGLLLLS 123
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 11-146 4.11e-17

ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of methyltransferases involved in the biosynthesis of menaquinone and ubiqinone. Some members such as the UbiE enzyme from E. coli are believed to act in both pathways, while others may act in only the menaquinone pathway. These methyltransferases are members of the UbiE/CoQ family of methyltransferases (pfam01209) which also contains ubiquinone methyltransferases and other methyltransferases. Members of this clade include a wide distribution of bacteria and eukaryotes, but no archaea. An outgroup for this clade is provided by the phosphatidylethanolamine methyltransferase (EC 2.1.1.17) from Rhodobacter sphaeroides. Note that a number of non-orthologous genes which are members of pfam03737 have been erroneously annotated as MenG methyltransferases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273884 [Multi-domain]  Cd Length: 223  Bit Score: 78.07  E-value: 4.11e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524   11 IAHQFGRAAGTYekhDVLQReVQSLLLDRL-------DFYLQTPQRVVDIGAGTGRGSALLKQRYPK-AEVIAIDLALPM 82
Cdd:TIGR01934   1 VQEMFDRIAPKY---DLLND-LLSFGLHRLwrrravkLIGVFKGQKVLDVACGTGDLAIELAKSAPDrGKVTGVDFSSEM 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 388432524   83 LRAAKKHSSWRKPFLRVCAEATALPLADHSVDVLHSNLCFQWVDALPPLFAECVRVLKPGGMLV 146
Cdd:TIGR01934  77 LEVAKKKSELPLNIEFIQADAEALPFEDNSFDAVTIAFGLRNVTDIQKALREMYRVLKPGGRLV 140
PRK08317 PRK08317
hypothetical protein; Provisional
 30-191 4.08e-16

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 75.74  E-value: 4.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524  30 REVQSLLLDRLDfyLQTPQRVVDIGAGTGRGSALLKQRY-PKAEVIAIDLALPMLRAAKKHSSWRKPFLR-VCAEATALP 107
Cdd:PRK08317   5 RRYRARTFELLA--VQPGDRVLDVGCGPGNDARELARRVgPEGRVVGIDRSEAMLALAKERAAGLGPNVEfVRGDADGLP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524 108 LADHSVDVLHSNLCFQWVDALPPLFAECVRVLKPGG----------MLVFSSFGPDTLKELRAAWAEADQQAHVSRFLdm 177
Cdd:PRK08317  83 FPDGSFDAVRSDRVLQHLEDPARALAEIARVLRPGGrvvvldtdwdTLVWHSGDRALMRKILNFWSDHFADPWLGRRL-- 160

                        170
                 ....*....|....
gi 388432524 178 hdvGDAVLAAGLRD 191
Cdd:PRK08317 161 ---PGLFREAGLTD 171
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
11-165 4.23e-16

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 74.65  E-value: 4.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524  11 IAHQFGRAAGTYEKH--DVLQREVQSLLLDRL--DFYLQTPQRVVDIGAGTGRGSALLKQRYpkAEVIAIDLALPMLRAA 86
Cdd:COG4976    7 VEALFDQYADSYDAAlvEDLGYEAPALLAEELlaRLPPGPFGRVLDLGCGTGLLGEALRPRG--YRLTGVDLSEEMLAKA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524  87 KKHSSWRKpFLrvCAEATALPLADHSVDVLHSNLCFQWVDALPPLFAECVRVLKPGGMLVFSS-------FGPDTLKELR 159
Cdd:COG4976   85 REKGVYDR-LL--VADLADLAEPDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFIFSVedadgsgRYAHSLDYVR 161


                 ....*.
gi 388432524 160 AAWAEA 165
Cdd:COG4976  162 DLLAAA 167
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 7-148 5.23e-15

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 72.49  E-value: 5.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524   7 DQSRIAHQFGRAAGTYekhDVLQReVQSLLLDRL--DF-----YLQTPQRVVDIGAGTGRGSALLKQRYPK-AEVIAIDL 78
Cdd:PRK00216   9 KQEKVAEMFDSIAPKY---DLMND-LLSFGLHRVwrRKtikwlGVRPGDKVLDLACGTGDLAIALAKAVGKtGEVVGLDF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524  79 ALPMLRAAKKHSSWRKPFLR---VCAEATALPLADHSVD----------VLHSNLCFQwvdalpplfaECVRVLKPGGML 145
Cdd:PRK00216  85 SEGMLAVGREKLRDLGLSGNvefVQGDAEALPFPDNSFDavtiafglrnVPDIDKALR----------EMYRVLKPGGRL 154


                 ....*.
gi 388432524 146 V---FS 148
Cdd:PRK00216 155 VileFS 160
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 49-150 1.52e-12

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: 62.83  E-value: 1.52e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524  49 RVVDIGAGTGrGSALLKQRYPKAEVIAIDLALPMLRAAKKHSSWRKP----FLRVCAEaTALPLADHSVDVLHSNLCFQW 124
Cdd:cd02440    1 RVLDLGCGTG-ALALALASGPGARVTGVDISPVALELARKAAAALLAdnveVLKGDAE-ELPPEADESFDVIISDPPLHH 78

                         90       100
                 ....*....|....*....|....*..
gi 388432524 125 -VDALPPLFAECVRVLKPGGMLVFSSF 150
Cdd:cd02440   79 lVEDLARFLEEARRLLKPGGVLVLTLV 105
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 44-199 1.93e-12

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 65.74  E-value: 1.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524  44 LQTPQRVVDIGAGTGRGSALLKQRYPKAEVIAIDLALPMLRAAKKhsswRKPFLRVCAEATALPLADHSVDVLHSNLCFQ 123
Cdd:PRK01683  29 LENPRYVVDLGCGPGNSTELLVERWPAARITGIDSSPAMLAEARS----RLPDCQFVEADIASWQPPQALDLIFANASLQ 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524 124 WVDALPPLFAECVRVLKPGGMLVFSSfgPDTLkelraawaeaDQQAHVSrfldMHDVGDAVL-------AAGLRDPVLDV 196
Cdd:PRK01683 105 WLPDHLELFPRLVSLLAPGGVLAVQM--PDNL----------DEPSHVL----MREVAENGPweqnlpdRGARRAPLPPP 168


                 ...
gi 388432524 197 CRY 199
Cdd:PRK01683 169 HAY 171
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 51-145 8.69e-12

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 60.46  E-value: 8.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524   51 VDIGAGTGRGSALLKQRYPKAEVIAIDLALPMLRAAKKHSSWRKPFLRVCAEATALPLADH---SVDVLHSNLCFQWVDA 127
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGLLNAVRVELFQLDLGELdpgSFDVVVASNVLHHLAD 80

                          90
                  ....*....|....*...
gi 388432524  128 LPPLFAECVRVLKPGGML 145
Cdd:pfam08242  81 PRAVLRNIRRLLKPGGVL 98
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 44-175 1.55e-10

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 59.54  E-value: 1.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524  44 LQTPQRVVDIGAGTGRGSALLKQRYpKAEVIAIDLALPMLRAAKKHSSWRKP---FLRVCAEATALPLADHSVDVLHSNL 120
Cdd:COG0500   24 LPKGGRVLDLGCGTGRNLLALAARF-GGRVIGIDLSPEAIALARARAAKAGLgnvEFLVADLAELDPLPAESFDLVVAFG 102

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 388432524 121 CFQWVDA--LPPLFAECVRVLKPGGMLVFSSFGP----DTLKELRAAWAEADQQAHVSRFL 175
Cdd:COG0500  103 VLHHLPPeeREALLRELARALKPGGVLLLSASDAaaalSLARLLLLATASLLELLLLLRLL 163
arsM PRK11873
arsenite methyltransferase;
44-163 1.88e-10

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 59.96  E-value: 1.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524  44 LQTPQRVVDIGAGTGRGSALLKQRY-PKAEVIAIDLALPMLRAAKKHSswRK------PFLRvcAEATALPLADHSVDVL 116
Cdd:PRK11873  75 LKPGETVLDLGSGGGFDCFLAARRVgPTGKVIGVDMTPEMLAKARANA--RKagytnvEFRL--GEIEALPVADNSVDVI 150

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 388432524 117 HSNlCfqwVDALPP----LFAECVRVLKPGGMLVFSSFG-----PDTLKELRAAWA 163
Cdd:PRK11873 151 ISN-C---VINLSPdkerVFKEAFRVLKPGGRFAISDVVlrgelPEEIRNDAELYA 202
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 49-164 2.60e-09

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 54.73  E-value: 2.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524   49 RVVDIGAGTGR-GSALLKQRYPKAEVIAIDLALPMLRAAKKHSSwRKPFLRV---CAEATALP--LADHSVDVLHSNLCF 122
Cdd:pfam13847   6 RVLDLGCGTGHlSFELAEELGPNAEVVGIDISEEAIEKARENAQ-KLGFDNVefeQGDIEELPelLEDDKFDVVISNCVL 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 388432524  123 QWVDALPPLFAECVRVLKPGGMLVFSSfgPDTLKELRAAWAE 164
Cdd:pfam13847  85 NHIPDPDKVLQEILRVLKPGGRLIISD--PDSLAELPAHVKE 124
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 37-193 2.60e-09

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 57.45  E-value: 2.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524  37 LDRLDfyLQTPQRVVDIGAGTGRGSALLKQRYpKAEVIAIDLALPMLRAAKKHSSWRKPFLRV-CAEATALPLADHSVDV 115
Cdd:PLN02336 259 VDKLD--LKPGQKVLDVGCGIGGGDFYMAENF-DVHVVGIDLSVNMISFALERAIGRKCSVEFeVADCTKKTYPDNSFDV 335

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524 116 LHSNLCFQWVDALPPLFAECVRVLKPGGMLVFSSF--GPDTLKELRAAWAEadqqahvSRFLDMHDV---GDAVLAAGLR 190
Cdd:PLN02336 336 IYSRDTILHIQDKPALFRSFFKWLKPGGKVLISDYcrSPGTPSPEFAEYIK-------QRGYDLHDVqayGQMLKDAGFD 408


                 ...
gi 388432524 191 DPV 193
Cdd:PLN02336 409 DVI 411
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 29-149 3.64e-09

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 54.55  E-value: 3.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524  29 QREVQSLLLDRLDfyLQTPQRVVDIGAGTGRGSALLKQRYpKAEVIAIDLALPMLRAAKKHSSWRKPFLRV---CAEATA 105
Cdd:COG2230   36 QEAKLDLILRKLG--LKPGMRVLDIGCGWGGLALYLARRY-GVRVTGVTLSPEQLEYARERAAEAGLADRVevrLADYRD 112

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 388432524 106 LPlADHSVDVLHSNLCFQWV--DALPPLFAECVRVLKPGGMLVFSS 149
Cdd:COG2230  113 LP-ADGQFDAIVSIGMFEHVgpENYPAYFAKVARLLKPGGRLLLHT 157
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 36-190 3.95e-08

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 51.66  E-value: 3.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524   36 LLDRLDFYLQTPQRVVDIGAGTGRGSALLKQRYPkaEVIAIDLALPMLRAAKKHSSwRKPFLRVCAEATALPLadhsvDV 115
Cdd:pfam13489  12 LLLRLLPKLPSPGRVLDFGCGTGIFLRLLRAQGF--SVTGVDPSPIAIERALLNVR-FDQFDEQEAAVPAGKF-----DV 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 388432524  116 LHSNLCFQWVDALPPLFAECVRVLKPGGMLVFSSFGPDT--LKELRAAWAEADQQAHVSrFLDMHDVGDAVLAAGLR 190
Cdd:pfam13489  84 IVAREVLEHVPDPPALLRQIAALLKPGGLLLLSTPLASDeaDRLLLEWPYLRPRNGHIS-LFSARSLKRLLEEAGFE 159
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
 36-147 1.72e-07

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 51.23  E-value: 1.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524  36 LLDRLDfyLQTPQRVVDIGAGTGRGSALLKQRYPKAEVIAIDLALPMLRAAKKhsswRKPFLRVCAEATALPLADhsVDV 115
Cdd:PRK14103  21 LLARVG--AERARRVVDLGCGPGNLTRYLARRWPGAVIEALDSSPEMVAAARE----RGVDARTGDVRDWKPKPD--TDV 92

                         90       100       110
                 ....*....|....*....|....*....|..
gi 388432524 116 LHSNLCFQWVDALPPLFAECVRVLKPGGMLVF 147
Cdd:PRK14103  93 VVSNAALQWVPEHADLLVRWVDELAPGSWIAV 124
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
8-162 2.67e-06

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 47.43  E-value: 2.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524    8 QSRIAHQFGRAAGTYEK---------HDVLQREVQSLLLDRldfylqTPQRVVDIGAGTGRGS-ALLKQRYPKAEVIAID 77
Cdd:pfam01209   1 EQRVGDVFSSVASKYDLmndvisfgiHRLWKDFTMKCMGVK------RGNKFLDVAGGTGDWTfGLSDSAGSSGKVVGLD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524   78 LALPMLRAAKKHSSwRKPFLRV---CAEATALPLADHSVDVLHSNLCFQWVDALPPLFAECVRVLKPGGMLVFSSFGPDT 154
Cdd:pfam01209  75 INENMLKEGEKKAK-EEGKYNIeflQGNAEELPFEDDSFDIVTISFGLRNFPDYLKVLKEAFRVLKPGGRVVCLEFSKPE 153


                  ....*...
gi 388432524  155 LKELRAAW 162
Cdd:pfam01209 154 NPLLSQAY 161
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 35-147 1.22e-05

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: 45.18  E-value: 1.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524  35 LLLDRLDfyLQTPQRVVDIGAGTGRGSALLKQRYPKAEVIAIDLALPMLRAAKKhsSWRKPFL---RVCAEATALPLADH 111
Cdd:COG2813   40 LLLEHLP--EPLGGRVLDLGCGYGVIGLALAKRNPEARVTLVDVNARAVELARA--NAAANGLenvEVLWSDGLSGVPDG 115

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 388432524 112 SVDVLHSNlcfqwvdalPP--------------LFAECVRVLKPGGMLVF 147
Cdd:COG2813  116 SFDLILSN---------PPfhagravdkevahaLIADAARHLRPGGELWL 156
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
106-177 1.91e-05

Predicted SAM-depedendent methyltransferase [General function prediction only];


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 44.09  E-value: 1.91e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 388432524 106 LPLADHSVDVLHSNLCFQ--WVDALPPLFAECVRVLKPGGMLVFSSfgPDTLKELRAAWAEADQQAHVSRFLDM 177
Cdd:COG4627   40 LPFPDNSVDAIYSSHVLEhlDYEEAPLALKECYRVLKPGGILRIVV--PDLEHVARLYLAEYDAALDVAELRLA 111
rrmA PRK11088
23S rRNA methyltransferase A; Provisional
 19-160 2.75e-05

23S rRNA methyltransferase A; Provisional


Pssm-ID: 236841 [Multi-domain]  Cd Length: 272  Bit Score: 44.52  E-value: 2.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524  19 AGTYekhDVLQREVQSLLLDRLDfylQTPQRVVDIGAGTGRGSALLKQRYPKAEVIAI---DLALPMLRAAKKhsswRKP 95
Cdd:PRK11088  64 AGHY---QPLRDAVANLLAERLD---EKATALLDIGCGEGYYTHALADALPEITTMQLfglDISKVAIKYAAK----RYP 133

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 388432524  96 FLRVC-AEATALPLADHSVD-VLHsnlcfqwVDAlPPLFAECVRVLKPGGMLVFSSFGPDTLKELRA 160
Cdd:PRK11088 134 QVTFCvASSHRLPFADQSLDaIIR-------IYA-PCKAEELARVVKPGGIVITVTPGPRHLFELKG 192
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 44-78 5.93e-05

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: 43.59  E-value: 5.93e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 388432524  44 LQTPQRVVDIGAGTGRGSALLKQRYPKAEVIAIDL 78
Cdd:COG4123   35 VKKGGRVLDLGTGTGVIALMLAQRSPGARITGVEI 69
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 47-147 2.83e-04

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: 40.55  E-value: 2.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524  47 PQRVVDIGAGTGRGSALLKQRYPK-AEVIAIDLALPMLRAAKKHssWRKPFLR-----VCAEAT-ALP-LADHSVDvlhs 118
Cdd:COG4122   17 AKRILEIGTGTGYSTLWLARALPDdGRLTTIEIDPERAAIAREN--FARAGLAdrirlILGDALeVLPrLADGPFD---- 90

                         90       100       110
                 ....*....|....*....|....*....|...
gi 388432524 119 nLCFqwVDA----LPPLFAECVRVLKPGGMLVF 147
Cdd:COG4122   91 -LVF--IDAdksnYPDYLELALPLLRPGGLIVA 120
PRK08287 PRK08287
decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;
31-77 3.00e-04

decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;


Pssm-ID: 181354  Cd Length: 187  Bit Score: 40.76  E-value: 3.00e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 388432524  31 EVQSLLLDRLDfyLQTPQRVVDIGAGTGRGSALLKQRYPKAEVIAID 77
Cdd:PRK08287  18 EVRALALSKLE--LHRAKHLIDVGAGTGSVSIEAALQFPSLQVTAIE 62
PRK05785 PRK05785
hypothetical protein; Provisional
 47-138 5.73e-04

hypothetical protein; Provisional


Pssm-ID: 235607 [Multi-domain]  Cd Length: 226  Bit Score: 40.44  E-value: 5.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524  47 PQRVVDIGAGTGRGSALLKQRYpKAEVIAIDLALPMLRAAKKHSSwrkpflRVCAEATALPLADHSVDVLHSNLCFQWVD 126
Cdd:PRK05785  52 PKKVLDVAAGKGELSYHFKKVF-KYYVVALDYAENMLKMNLVADD------KVVGSFEALPFRDKSFDVVMSSFALHASD 124

                         90
                 ....*....|..
gi 388432524 127 ALPPLFAECVRV 138
Cdd:PRK05785 125 NIEKVIAEFTRV 136
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
 41-153 7.90e-04

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 40.34  E-value: 7.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524  41 DFYLQTPQRVVDIGAGTGRGSALLKQRYpKAEVIAIDLALPMLRAAKKHSSWRKPFLRVCAEATALPLADHSVDVLHSN- 119
Cdd:PTZ00098  47 DIELNENSKVLDIGSGLGGGCKYINEKY-GAHVHGVDICEKMVNIAKLRNSDKNKIEFEANDILKKDFPENTFDMIYSRd 125

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 388432524 120 --LCFQWVDAlPPLFAECVRVLKPGGMLVFSSFGPD 153
Cdd:PTZ00098 126 aiLHLSYADK-KKLFEKCYKWLKPNGILLITDYCAD 160
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 35-158 1.71e-03

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: 38.34  E-value: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524   35 LLLDRLDfyLQTPQRVVDIGAGTGRGSALLKQRYPKAEVIAIDLALPMLRAAKKhsswrkpflrvcaeatalPLADHSVD 114
Cdd:pfam05175  22 LLLEHLP--KDLSGKVLDLGCGAGVLGAALAKESPDAELTMVDINARALESARE------------------NLAANGLE 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 388432524  115 VLHsnlcFQWVDAL--------------PP--------------LFAECVRVLKPGGML--VFSSF--GPDTLKEL 158
Cdd:pfam05175  82 NGE----VVASDVYsgvedgkfdliisnPPfhaglattynvaqrFIADAKRHLRPGGELwiVANRFlgYPPLLEEL 153
PRK06922 PRK06922
class I SAM-dependent methyltransferase;
49-146 2.95e-03

class I SAM-dependent methyltransferase;


Pssm-ID: 180751 [Multi-domain]  Cd Length: 677  Bit Score: 39.08  E-value: 2.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524  49 RVVDIGAGTGRGSALLKQRYPKAEVIAIDLALPMLRAAKK-----HSSWRkpflrvCAEATALPLADH----SVD----- 114
Cdd:PRK06922 421 TIVDVGAGGGVMLDMIEEETEDKRIYGIDISENVIDTLKKkkqneGRSWN------VIKGDAINLSSSfekeSVDtivys 494

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 388432524 115 -VLHSnlCFQWVDALPPLFAECV---------RVLKPGGMLV 146
Cdd:PRK06922 495 sILHE--LFSYIEYEGKKFNHEVikkglqsayEVLKPGGRII 534
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
40-163 3.44e-03

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


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 37.89  E-value: 3.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524  40 LDFYLQTPQRVVDIGAGTGRGSALLKQRYPKAEVIAIDLALPMLRAAKKH-----SSWRKPFLRVCAE--ATALPLADHS 112
Cdd:COG0421   31 PLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYfpllaPAFDDPRLRVVIGdgRAFLREAEES 110

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 388432524 113 VDVLHsnlcfqwVDALPPL-----------FAECVRVLKPGGMLVFSSFGPDT-LKELRAAWA 163
Cdd:COG0421  111 YDVII-------VDLTDPVgpaeglftrefYEDCRRALKPGGVLVVNLGSPFYgLDLLRRVLA 166
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 50-150 8.32e-03

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 37.42  E-value: 8.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388432524  50 VVDIGAGTGRGSALLKQRypKAEVIAIDLalpMLRAAKKHSSWRKPFLRV---CAEATA--LPLADHSVDVLHSNLCFQW 124
Cdd:PLN02336  41 VLELGAGIGRFTGELAKK--AGQVIALDF---IESVIKKNESINGHYKNVkfmCADVTSpdLNISDGSVDLIFSNWLLMY 115

                         90       100       110
                 ....*....|....*....|....*....|
gi 388432524 125 V--DALPPLFAECVRVLKPGGMLVF--SSF 150
Cdd:PLN02336 116 LsdKEVENLAERMVKWLKVGGYIFFreSCF 145
 
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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