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Conserved domains on  [gi|491530464|ref|WP_005388087|]
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MULTISPECIES: malonyl-ACP O-methyltransferase BioC [Vibrio]

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 ...
 27-271 2.67e-70

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: 216.77  E-value: 2.67e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464   27 SFGKAAETYDKHAAFQRDVGHQLLDKLPEN--LTGKRVLDLGCGTGYFSQLLQQRG--AEVVCGDISQAMLDKAEQRCGA 102
Cdd:TIGR02072   1 SFNKAAKTYDRHAKIQREMAKRLLALLKEKgiFIPASVLDIGCGTGYLTRALLKRFpqAEFIALDISAGMLAQAKTKLSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464  103 vRMHYQVADAENLPFDDDSFDYVFSSLALQWCTDLSYPLKEVRRVLKNGGKAWFSTLVDGSLYELRASWEkidayQHVNN 182
Cdd:TIGR02072  81 -NVQFICGDAEKLPLEDSSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQSFG-----QHGLR 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464  183 FLTLNQVKIALAQSrCDSHQLDLTTITVWYDSAFSVMRDLKGIGANHVSGRShglTSRETLLKVEHAYQAFKNDQGlLPA 262
Cdd:TIGR02072 155 YLSLDELKALLKNS-FELLTLEEELITLSFDDPLDVLRHLKKTGANGLSSGR---TSRKQLKAFLERYEQEFQPDG-LPL 229


                  ....*....
gi 491530464  263 SYQVCFGVI 271
Cdd:TIGR02072 230 TYHVVYGIA 238
 
Name Accession Description Interval E-value
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 27-271 2.67e-70

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: 216.77  E-value: 2.67e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464   27 SFGKAAETYDKHAAFQRDVGHQLLDKLPEN--LTGKRVLDLGCGTGYFSQLLQQRG--AEVVCGDISQAMLDKAEQRCGA 102
Cdd:TIGR02072   1 SFNKAAKTYDRHAKIQREMAKRLLALLKEKgiFIPASVLDIGCGTGYLTRALLKRFpqAEFIALDISAGMLAQAKTKLSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464  103 vRMHYQVADAENLPFDDDSFDYVFSSLALQWCTDLSYPLKEVRRVLKNGGKAWFSTLVDGSLYELRASWEkidayQHVNN 182
Cdd:TIGR02072  81 -NVQFICGDAEKLPLEDSSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQSFG-----QHGLR 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464  183 FLTLNQVKIALAQSrCDSHQLDLTTITVWYDSAFSVMRDLKGIGANHVSGRShglTSRETLLKVEHAYQAFKNDQGlLPA 262
Cdd:TIGR02072 155 YLSLDELKALLKNS-FELLTLEEELITLSFDDPLDVLRHLKKTGANGLSSGR---TSRKQLKAFLERYEQEFQPDG-LPL 229


                  ....*....
gi 491530464  263 SYQVCFGVI 271
Cdd:TIGR02072 230 TYHVVYGIA 238
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 20-271 1.13e-67

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 210.38  E-value: 1.13e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464  20 DKDAIASSFGKAAETYDKHAAFQRdvghQLLDKLPENLTGKR---VLDLGCGTGYFSQLLQQRGAEVVCGDISQAMLDKA 96
Cdd:PRK10258   5 NKQAIAAAFGRAAAHYEQHAELQR----QSADALLAMLPQRKfthVLDAGCGPGWMSRYWRERGSQVTALDLSPPMLAQA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464  97 EQRCGAvrMHYQVADAENLPFDDDSFDYVFSSLALQWCTDLSYPLKEVRRVLKNGGKAWFSTLVDGSLYELRASWEKIDA 176
Cdd:PRK10258  81 RQKDAA--DHYLAGDIESLPLATATFDLAWSNLAVQWCGNLSTALRELYRVVRPGGVVAFTTLVQGSLPELHQAWQAVDE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464 177 YQHVNNFLTLNQVKIALAQSRCDSHQLdltTITVWYDSAFSVMRDLKGIGANHV-SGRSHGLTSRETLLKVEHAYqafKN 255
Cdd:PRK10258 159 RPHANRFLPPDAIEQALNGWRYQHHIQ---PITLWFDDALSAMRSLKGIGATHLhEGRDPRILTRSQLQRLQLAW---PQ 232

                        250
                 ....*....|....*.
gi 491530464 256 DQGLLPASYQVCFGVI 271
Cdd:PRK10258 233 QQGRYPLTYHLFLGVI 248
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 35-173 1.76e-40

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: 137.05  E-value: 1.76e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464  35 YDKHAAFqRDVGHQLLDKLPENlTGKRVLDLGCGTGYFSQLLQQRGAEVVCGDISQAMLDKAEQRCGA--VRMHYQVADA 112
Cdd:COG2226    1 FDRVAAR-YDGREALLAALGLR-PGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEagLNVEFVVGDA 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491530464 113 ENLPFDDDSFDYVFSSLALQWCTDLSYPLKEVRRVLKNGGKAWFSTLVDGSLYELRASWEK 173
Cdd:COG2226   79 EDLPFPDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEELLAE 139
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 62-152 3.33e-32

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 114.20  E-value: 3.33e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464   62 VLDLGCGTGYFSQLLQQR-GAEVVCGDISQAMLDKAEQRCGA--VRMHYQVADAENLPFDDDSFDYVFSSLALQWCTDLS 138
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRgGARVTGVDLSPEMLERARERAAEagLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPDPD 80

                          90
                  ....*....|....*.
gi 491530464  139 YP--LKEVRRVLKNGG 152
Cdd:pfam13649  81 LEaaLREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 61-160 5.02e-18

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: 77.47  E-value: 5.02e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464  61 RVLDLGCGTGYFSQLLQQRGAEVVCG-DISQAMLDKAEQ---RCGAVRMHYQVADAENLPFD-DDSFDYVFSSLALQWCT 135
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGvDISPVALELARKaaaALLADNVEVLKGDAEELPPEaDESFDVIISDPPLHHLV 80

                         90       100
                 ....*....|....*....|....*.
gi 491530464 136 DLSYP-LKEVRRVLKNGGKAWFSTLV 160
Cdd:cd02440   81 EDLARfLEEARRLLKPGGVLVLTLVL 106
 
Name Accession Description Interval E-value
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 27-271 2.67e-70

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: 216.77  E-value: 2.67e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464   27 SFGKAAETYDKHAAFQRDVGHQLLDKLPEN--LTGKRVLDLGCGTGYFSQLLQQRG--AEVVCGDISQAMLDKAEQRCGA 102
Cdd:TIGR02072   1 SFNKAAKTYDRHAKIQREMAKRLLALLKEKgiFIPASVLDIGCGTGYLTRALLKRFpqAEFIALDISAGMLAQAKTKLSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464  103 vRMHYQVADAENLPFDDDSFDYVFSSLALQWCTDLSYPLKEVRRVLKNGGKAWFSTLVDGSLYELRASWEkidayQHVNN 182
Cdd:TIGR02072  81 -NVQFICGDAEKLPLEDSSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQSFG-----QHGLR 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464  183 FLTLNQVKIALAQSrCDSHQLDLTTITVWYDSAFSVMRDLKGIGANHVSGRShglTSRETLLKVEHAYQAFKNDQGlLPA 262
Cdd:TIGR02072 155 YLSLDELKALLKNS-FELLTLEEELITLSFDDPLDVLRHLKKTGANGLSSGR---TSRKQLKAFLERYEQEFQPDG-LPL 229


                  ....*....
gi 491530464  263 SYQVCFGVI 271
Cdd:TIGR02072 230 TYHVVYGIA 238
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 20-271 1.13e-67

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 210.38  E-value: 1.13e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464  20 DKDAIASSFGKAAETYDKHAAFQRdvghQLLDKLPENLTGKR---VLDLGCGTGYFSQLLQQRGAEVVCGDISQAMLDKA 96
Cdd:PRK10258   5 NKQAIAAAFGRAAAHYEQHAELQR----QSADALLAMLPQRKfthVLDAGCGPGWMSRYWRERGSQVTALDLSPPMLAQA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464  97 EQRCGAvrMHYQVADAENLPFDDDSFDYVFSSLALQWCTDLSYPLKEVRRVLKNGGKAWFSTLVDGSLYELRASWEKIDA 176
Cdd:PRK10258  81 RQKDAA--DHYLAGDIESLPLATATFDLAWSNLAVQWCGNLSTALRELYRVVRPGGVVAFTTLVQGSLPELHQAWQAVDE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464 177 YQHVNNFLTLNQVKIALAQSRCDSHQLdltTITVWYDSAFSVMRDLKGIGANHV-SGRSHGLTSRETLLKVEHAYqafKN 255
Cdd:PRK10258 159 RPHANRFLPPDAIEQALNGWRYQHHIQ---PITLWFDDALSAMRSLKGIGATHLhEGRDPRILTRSQLQRLQLAW---PQ 232

                        250
                 ....*....|....*.
gi 491530464 256 DQGLLPASYQVCFGVI 271
Cdd:PRK10258 233 QQGRYPLTYHLFLGVI 248
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 35-173 1.76e-40

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: 137.05  E-value: 1.76e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464  35 YDKHAAFqRDVGHQLLDKLPENlTGKRVLDLGCGTGYFSQLLQQRGAEVVCGDISQAMLDKAEQRCGA--VRMHYQVADA 112
Cdd:COG2226    1 FDRVAAR-YDGREALLAALGLR-PGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEagLNVEFVVGDA 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491530464 113 ENLPFDDDSFDYVFSSLALQWCTDLSYPLKEVRRVLKNGGKAWFSTLVDGSLYELRASWEK 173
Cdd:COG2226   79 EDLPFPDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEELLAE 139
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 62-152 3.33e-32

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 114.20  E-value: 3.33e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464   62 VLDLGCGTGYFSQLLQQR-GAEVVCGDISQAMLDKAEQRCGA--VRMHYQVADAENLPFDDDSFDYVFSSLALQWCTDLS 138
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRgGARVTGVDLSPEMLERARERAAEagLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPDPD 80

                          90
                  ....*....|....*.
gi 491530464  139 YP--LKEVRRVLKNGG 152
Cdd:pfam13649  81 LEaaLREIARVLKPGG 96
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 63-156 3.79e-32

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 113.91  E-value: 3.79e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464   63 LDLGCGTGYFSQLLQQRGAEVVCGDISQAMLDKAEQRCGAVRMHYQVADAENLPFDDDSFDYVFSSLALQWCTDLSYPLK 142
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREGLTFVVGDAEDLPFPDNSFDLVLSSEVLHHVEDPERALR 80

                          90
                  ....*....|....
gi 491530464  143 EVRRVLKNGGKAWF 156
Cdd:pfam08241  81 EIARVLKPGGILII 94
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 47-158 5.35e-31

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: 112.03  E-value: 5.35e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464  47 HQLLDKLPenLTGKRVLDLGCGTGYFSQLLQQRGAEVVCGDISQAMLDKAEQRCGAVRMHYQVADAENLPFDDDSFDYVF 126
Cdd:COG2227   15 AALLARLL--PAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELNVDFVQGDLEDLPLEDGSFDLVI 92

                         90       100       110
                 ....*....|....*....|....*....|..
gi 491530464 127 SSLALQWCTDLSYPLKEVRRVLKNGGKAWFST 158
Cdd:COG2227   93 CSEVLEHLPDPAALLRELARLLKPGGLLLLST 124
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
21-158 3.53e-24

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 95.84  E-value: 3.53e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464  21 KDAIASSFGKAAETYDKHA------AFQRDVGHQLLDKLPENlTGKRVLDLGCGTGYFSQLLQQRGAEVVCGDISQAMLD 94
Cdd:COG4976    4 DAYVEALFDQYADSYDAALvedlgyEAPALLAEELLARLPPG-PFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLA 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491530464  95 KAEQRCGAVRMHyqVADAENLPFDDDSFDYVFSSLALQWCTDLSYPLKEVRRVLKNGGKAWFST 158
Cdd:COG4976   83 KAREKGVYDRLL--VADLADLAEPDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFIFSV 144
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
59-152 2.18e-23

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 91.04  E-value: 2.18e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464  59 GKRVLDLGCGTGYFSQLLQQR--GAEVVCGDISQAMLDKAEQRCGAVRmhYQVADAENLPFdDDSFDYVFSSLALQWCTD 136
Cdd:COG4106    2 PRRVLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLARARARLPNVR--FVVADLRDLDP-PEPFDLVVSNAALHWLPD 78

                         90
                 ....*....|....*.
gi 491530464 137 LSYPLKEVRRVLKNGG 152
Cdd:COG4106   79 HAALLARLAAALAPGG 94
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 19-154 9.21e-23

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 93.29  E-value: 9.21e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464  19 QDKDAIASSFGKAAETYDK---------HAAFqRDVGHQLLDKLPenltGKRVLDLGCGTGYFSQLLQQRG---AEVVCG 86
Cdd:PRK00216   8 EKQEKVAEMFDSIAPKYDLmndllsfglHRVW-RRKTIKWLGVRP----GDKVLDLACGTGDLAIALAKAVgktGEVVGL 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491530464  87 DISQAMLDKAEQRC----GAVRMHYQVADAENLPFDDDSFDYVFSSLALQWCTDLSYPLKEVRRVLKNGGKA 154
Cdd:PRK00216  83 DFSEGMLAVGREKLrdlgLSGNVEFVQGDAEALPFPDNSFDAVTIAFGLRNVPDIDKALREMYRVLKPGGRL 154
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 28-153 1.36e-21

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: 90.01  E-value: 1.36e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464   28 FGKAAETYDK---------HAAFQRDVGHQLLDKLPEnltgkRVLDLGCGTGYFSQLLQQRG---AEVVCGDISQAMLDK 95
Cdd:TIGR01934   5 FDRIAPKYDLlndllsfglHRLWRRRAVKLIGVFKGQ-----KVLDVACGTGDLAIELAKSApdrGKVTGVDFSSEMLEV 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 491530464   96 AEQRCGA-VRMHYQVADAENLPFDDDSFDYVFSSLALQWCTDLSYPLKEVRRVLKNGGK 153
Cdd:TIGR01934  80 AKKKSELpLNIEFIQADAEALPFEDNSFDAVTIAFGLRNVTDIQKALREMYRVLKPGGR 138
PRK08317 PRK08317
hypothetical protein; Provisional
 42-154 4.00e-20

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 86.53  E-value: 4.00e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464  42 QRDVGHQLLDKLPenltGKRVLDLGCGTGYFSQLLQQR---GAEVVCGDISQAMLDKAEQR----CGAVRMHYqvADAEN 114
Cdd:PRK08317   7 YRARTFELLAVQP----GDRVLDVGCGPGNDARELARRvgpEGRVVGIDRSEAMLALAKERaaglGPNVEFVR--GDADG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 491530464 115 LPFDDDSFDYVFSSLALQWCTDLSYPLKEVRRVLKNGGKA 154
Cdd:PRK08317  81 LPFPDGSFDAVRSDRVLQHLEDPARALAEIARVLRPGGRV 120
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 61-160 5.02e-18

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: 77.47  E-value: 5.02e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464  61 RVLDLGCGTGYFSQLLQQRGAEVVCG-DISQAMLDKAEQ---RCGAVRMHYQVADAENLPFD-DDSFDYVFSSLALQWCT 135
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGvDISPVALELARKaaaALLADNVEVLKGDAEELPPEaDESFDVIISDPPLHHLV 80

                         90       100
                 ....*....|....*....|....*.
gi 491530464 136 DLSYP-LKEVRRVLKNGGKAWFSTLV 160
Cdd:cd02440   81 EDLARfLEEARRLLKPGGVLVLTLVL 106
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 59-152 7.98e-18

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 78.23  E-value: 7.98e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464   59 GKRVLDLGCGTGYFSQLLQQR---GAEVVCGDISQAMLDKAEQRC---GAVRMHYQVADAENLP--FDDDSFDYVFSSLA 130
Cdd:pfam13847   4 GMRVLDLGCGTGHLSFELAEElgpNAEVVGIDISEEAIEKARENAqklGFDNVEFEQGDIEELPelLEDDKFDVVISNCV 83

                          90       100
                  ....*....|....*....|..
gi 491530464  131 LQWCTDLSYPLKEVRRVLKNGG 152
Cdd:pfam13847  84 LNHIPDPDKVLQEILRVLKPGG 105
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
28-153 1.08e-17

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 79.79  E-value: 1.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464   28 FGKAAETYDKHAAF----QRDVGHQLLDKLPENLTGKRVLDLGCGTG----YFSQLLQQRGAEVVCgDISQAMLDKAEQR 99
Cdd:pfam01209   8 FSSVASKYDLMNDVisfgIHRLWKDFTMKCMGVKRGNKFLDVAGGTGdwtfGLSDSAGSSGKVVGL-DINENMLKEGEKK 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 491530464  100 C---GAVRMHYQVADAENLPFDDDSFDYVFSSLALQWCTDLSYPLKEVRRVLKNGGK 153
Cdd:pfam01209  87 AkeeGKYNIEFLQGNAEELPFEDDSFDIVTISFGLRNFPDYLKVLKEAFRVLKPGGR 143
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 48-152 1.14e-16

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 76.11  E-value: 1.14e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464  48 QLLDKLPENLtgkRVLDLGCGTGYFSQLLQQRGAEVVCG-DISQAMLDKAEQRC---GAVRMHYQVAD-AENLPFDDDSF 122
Cdd:COG0500   19 ALLERLPKGG---RVLDLGCGTGRNLLALAARFGGRVIGiDLSPEAIALARARAakaGLGNVEFLVADlAELDPLPAESF 95

                         90       100       110
                 ....*....|....*....|....*....|...
gi 491530464 123 DYVFSSLALQWCtDLSYP---LKEVRRVLKNGG 152
Cdd:COG0500   96 DLVVAFGVLHHL-PPEERealLRELARALKPGG 127
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 59-158 1.76e-16

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 74.58  E-value: 1.76e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464  59 GKRVLDLGCGTGYFS-QLLQQRGAEVVCGDISQAMLDKAEQRCGAVRMHYQV----ADAENLPFdDDSFDYVFSSLALQW 133
Cdd:COG2230   52 GMRVLDIGCGWGGLAlYLARRYGVRVTGVTLSPEQLEYARERAAEAGLADRVevrlADYRDLPA-DGQFDAIVSIGMFEH 130

                         90       100
                 ....*....|....*....|....*..
gi 491530464 134 CTDLSYP--LKEVRRVLKNGGKAWFST 158
Cdd:COG2230  131 VGPENYPayFAKVARLLKPGGRLLLHT 157
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 42-164 2.09e-16

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 76.03  E-value: 2.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464  42 QRDV--GHQ-----LLDKLPE--NLTGKRVLDLGCGTGYFSQLLQQRGAEVVCGDISQAMLDKAEQRC----GAVRMHYQ 108
Cdd:PRK07580  38 RATVraGHQrmrdtVLSWLPAdgDLTGLRILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEARERApeagLAGNITFE 117

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 491530464 109 VADAENLpfdDDSFDYV--FSSLalqwctdLSYPLKEVRRVLKNggkawFSTLVDGSL 164
Cdd:PRK07580 118 VGDLESL---LGRFDTVvcLDVL-------IHYPQEDAARMLAH-----LASLTRGSL 160
BchM-ChlM TIGR02021
magnesium protoporphyrin O-methyltransferase; This model represents the ...
 20-150 2.51e-14

magnesium protoporphyrin O-methyltransferase; This model represents the S-adenosylmethionine-dependent O-methyltransferase responsible for methylation of magnesium protoporphyrin IX. This step is essentiasl for the biosynthesis of both chlorophyll and bacteriochlorophyll. This model encompasses two closely related clades, from cyanobacteria (and plants) where it is called ChlM and other photosynthetic bacteria where it is known as BchM. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 273930 [Multi-domain]  Cd Length: 219  Bit Score: 70.21  E-value: 2.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464   20 DKDAIASSF-GKAAETY-------DKHAAFQRDV--GHQ-----LLDKLPEN-LTGKRVLDLGCGTGYFSQLLQQRGAEV 83
Cdd:TIGR02021   1 QKEQVRHYFdGTAFQRWariygsgDPVSRVRQTVreGRAamrrkLLDWLPKDpLKGKRVLDAGCGTGLLSIELAKRGAIV 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491530464   84 VCGDISQAMLDKAEQRCGAV----RMHYQVADAENLpfdDDSFDYVFsslalqwCTD--LSYPLKEVRRVLKN 150
Cdd:TIGR02021  81 KAVDISEQMVQMARNRAQGRdvagNVEFEVNDLLSL---CGEFDIVV-------CMDvlIHYPASDMAKALGH 143
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 63-153 7.74e-13

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 63.16  E-value: 7.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464   63 LDLGCGTGYFSQLL--QQRGAEVVCGDISQAMLDKAEQR------CGAVRMHYQVADAENLpfDDDSFDYVFSSLALQWC 134
Cdd:pfam08242   1 LEIGCGTGTLLRALleALPGLEYTGLDISPAALEAARERlaalglLNAVRVELFQLDLGEL--DPGSFDVVVASNVLHHL 78

                          90
                  ....*....|....*....
gi 491530464  135 TDLSYPLKEVRRVLKNGGK 153
Cdd:pfam08242  79 ADPRAVLRNIRRLLKPGGV 97
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 41-183 1.31e-12

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 63.99  E-value: 1.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464   41 FQRDVGHQLLDKL----PENLTGKRVLDLGCGTGYFSQLLQQRGAEVVCGDISQAMLDKAeqrcgAVRMHYQVADAENLP 116
Cdd:pfam13489   1 YAHQRERLLADLLlrllPKLPSPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERA-----LLNVRFDQFDEQEAA 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491530464  117 FDDDSFDYVFSSLALQWCTDLSYPLKEVRRVLKNGGKAWFST-LVDGSLYELRASWEKID-AYQHVNNF 183
Cdd:pfam13489  76 VPAGKFDVIVAREVLEHVPDPPALLRQIAALLKPGGLLLLSTpLASDEADRLLLEWPYLRpRNGHISLF 144
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 56-185 1.10e-11

tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440663 [Multi-domain]  Cd Length: 172  Bit Score: 61.89  E-value: 1.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464  56 NLT----GKRVLDLGCGTG---YFSQLLqqrGAEVVCGDISQAMLDKAEQRC---GAVRMHYQVADAENLPFDDDSFDYV 125
Cdd:COG1041   20 NLAgakeGDTVLDPFCGTGtilIEAGLL---GRRVIGSDIDPKMVEGARENLehyGYEDADVIRGDARDLPLADESVDAI 96

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464 126 --------FSSLALQWCTDLSYP-LKEVRRVLKNGGKAWFSTLVDGSLYELRASWEKIDAY-QHVNNFLT 185
Cdd:COG1041   97 vtdppygrSSKISGEELLELYEKaLEEAARVLKPGGRVVIVTPRDIDELLEEAGFKVLERHeQRVHKSLT 166
rrmA PRK11088
23S rRNA methyltransferase A; Provisional
 43-169 6.74e-10

23S rRNA methyltransferase A; Provisional


Pssm-ID: 236841 [Multi-domain]  Cd Length: 272  Bit Score: 58.38  E-value: 6.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464  43 RDVGHQLLDK-LPENltGKRVLDLGCGTGYFS----QLLQQRGAEVVCG-DISQAMLDKAEQRCGAVrmHYQVADAENLP 116
Cdd:PRK11088  71 RDAVANLLAErLDEK--ATALLDIGCGEGYYThalaDALPEITTMQLFGlDISKVAIKYAAKRYPQV--TFCVASSHRLP 146

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 491530464 117 FDDDSFDYVFSSLAlqwctdlsyPLK--EVRRVLKNGGkaWFSTLVDGS--LYELRA 169
Cdd:PRK11088 147 FADQSLDAIIRIYA---------PCKaeELARVVKPGG--IVITVTPGPrhLFELKG 192
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
56-127 2.91e-09

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 55.30  E-value: 2.91e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491530464  56 NLTGKRVLDLGCGTGYFSQLLQQRGAE-VVCGDISQAMLDKAEQ--RCGAVRMHYQVADAENLPfDDDSFDYVFS 127
Cdd:COG2263   43 DIEGKTVLDLGCGTGMLAIGAALLGAKkVVGVDIDPEALEIAREnaERLGVRVDFIRADVTRIP-LGGSVDTVVM 116
PLN02585 PLN02585
magnesium protoporphyrin IX methyltransferase
 4-102 8.02e-09

magnesium protoporphyrin IX methyltransferase


Pssm-ID: 215319 [Multi-domain]  Cd Length: 315  Bit Score: 55.25  E-value: 8.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464   4 ATTALAQTLALESFHQDKDAIASSFG----KAAETYDKHAAFQR---------DV---------GH-QLLDKL------P 54
Cdd:PLN02585  61 AVAALAAALSLTDPERRRQLQAEEVGgddkEVVREYFNTTGFERwrkiygetdEVnkvqldirlGHaQTVEKVllwlaeD 140

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 491530464  55 ENLTGKRVLDLGCGTGYFSQLLQQRGAEVVCGDISQAMLDKAEQRCGA 102
Cdd:PLN02585 141 GSLAGVTVCDAGCGTGSLAIPLALEGAIVSASDISAAMVAEAERRAKE 188
PLN02244 PLN02244
tocopherol O-methyltransferase
 60-153 9.58e-08

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 52.44  E-value: 9.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464  60 KRVLDLGCGTGYFSQLLQQR-GAEVVCGDIS--QAM----LDKAEQRCGAVRmhYQVADAENLPFDDDSFDYVFSSLALQ 132
Cdd:PLN02244 120 KRIVDVGCGIGGSSRYLARKyGANVKGITLSpvQAAranaLAAAQGLSDKVS--FQVADALNQPFEDGQFDLVWSMESGE 197

                         90       100
                 ....*....|....*....|.
gi 491530464 133 WCTDLSYPLKEVRRVLKNGGK 153
Cdd:PLN02244 198 HMPDKRKFVQELARVAAPGGR 218
PLN02233 PLN02233
ubiquinone biosynthesis methyltransferase
 58-154 1.06e-07

ubiquinone biosynthesis methyltransferase


Pssm-ID: 177877 [Multi-domain]  Cd Length: 261  Bit Score: 51.82  E-value: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464  58 TGKRVLDLGCGTGYFSQLLQQR---GAEVVCGDISQAMLDKA--EQRCGAVRMHYQV----ADAENLPFDDDSFDYVFSS 128
Cdd:PLN02233  73 MGDRVLDLCCGSGDLAFLLSEKvgsDGKVMGLDFSSEQLAVAasRQELKAKSCYKNIewieGDATDLPFDDCYFDAITMG 152

                         90       100
                 ....*....|....*....|....*.
gi 491530464 129 LALQWCTDLSYPLKEVRRVLKNGGKA 154
Cdd:PLN02233 153 YGLRNVVDRLKAMQEMYRVLKPGSRV 178
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 49-156 1.09e-07

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: 50.96  E-value: 1.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464  49 LLDKLPENLTGkRVLDLGCGTGYFSQLLQQR--GAEVVCGDISQAMLDKAE---QRCGAVRMHYQVADAENlPFDDDSFD 123
Cdd:COG2813   41 LLEHLPEPLGG-RVLDLGCGYGVIGLALAKRnpEARVTLVDVNARAVELARanaAANGLENVEVLWSDGLS-GVPDGSFD 118

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 491530464 124 YVFS------------SLALQWctdlsypLKEVRRVLKNGGKAWF 156
Cdd:COG2813  119 LILSnppfhagravdkEVAHAL-------IADAARHLRPGGELWL 156
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
 47-133 1.20e-07

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 51.61  E-value: 1.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464  47 HQLLDKLPEnLTGKRVLDLGCGTGYFSQLLQQR--GAEVVCGDISQAMLDKAEQRcgavRMHYQVADAENLPFDDDSfDY 124
Cdd:PRK14103  19 YDLLARVGA-ERARRVVDLGCGPGNLTRYLARRwpGAVIEALDSSPEMVAAARER----GVDARTGDVRDWKPKPDT-DV 92


                 ....*....
gi 491530464 125 VFSSLALQW 133
Cdd:PRK14103  93 VVSNAALQW 101
PRK14968 PRK14968
putative methyltransferase; Provisional
 53-161 1.52e-07

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 50.28  E-value: 1.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464  53 LPENLT---GKRVLDLGCGTGYFSQLLQQRGAEVVCGDISQAMLDKAeqRCGAVRMHYQVADAE----NL--PFDDDSFD 123
Cdd:PRK14968  15 LAENAVdkkGDRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVECA--KCNAKLNNIRNNGVEvirsDLfePFRGDKFD 92

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491530464 124 -------YVFSSLALQWCTDLSYP--------------LKEVRRVLKNGGKAWF--STLVD 161
Cdd:PRK14968  93 vilfnppYLPTEEEEEWDDWLNYAlsggkdgrevidrfLDEVGRYLKPGGRILLlqSSLTG 153
PLN02490 PLN02490
MPBQ/MSBQ methyltransferase
 61-154 4.14e-07

MPBQ/MSBQ methyltransferase


Pssm-ID: 215270 [Multi-domain]  Cd Length: 340  Bit Score: 50.28  E-value: 4.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464  61 RVLDLGCGTGyFSQL--LQQRGAE-VVCGDISQAMLDKAEQRCGAVRMHYQVADAENLPFDDDSFDYVFSSLALQWCTDL 137
Cdd:PLN02490 116 KVVDVGGGTG-FTTLgiVKHVDAKnVTILDQSPHQLAKAKQKEPLKECKIIEGDAEDLPFPTDYADRYVSAGSIEYWPDP 194

                         90
                 ....*....|....*..
gi 491530464 138 SYPLKEVRRVLKNGGKA 154
Cdd:PLN02490 195 QRGIKEAYRVLKIGGKA 211
MetW pfam07021
Methionine biosynthesis protein MetW; This family consists of several bacterial and one ...
 59-147 1.13e-06

Methionine biosynthesis protein MetW; This family consists of several bacterial and one archaeal methionine biosynthesis MetW proteins. Biosynthesis of methionine from homoserine in Pseudomonas putida takes place in three steps. The first step is the acylation of homoserine to yield an acyl-L-homoserine. This reaction is catalyzed by the products of the metXW genes and is equivalent to the first step in enterobacteria, gram-positive bacteria and fungi, except that in these microorganizms the reaction is catalyzed by a single polypeptide (the product of the metA gene in Escherichia coli and the met5 gene product in Neurospora crassa). In Pseudomonas putida, as in gram-positive bacteria and certain fungi, the second and third steps are a direct sulfhydrylation that converts the O-acyl-L-homoserine into homocysteine and further methylation to yield methionine. The latter reaction can be mediated by either of the two methionine synthetases present in the cells.


Pssm-ID: 399779  Cd Length: 193  Bit Score: 47.84  E-value: 1.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464   59 GKRVLDLGCGTGYFSQLLQQ------RGAEvvcgdISQAMLDKAEQRcgAVRMHYQVADAENLPFDDDSFDYVFSSLALQ 132
Cdd:pfam07021  14 GSRVLDLGCGDGTLLYLLKEekgvdgYGIE-----LDAAGVAECVAK--GLYVIQGDLDEGLEHFPDKSFDYVILSQTLQ 86

                          90
                  ....*....|....*
gi 491530464  133 WCTDLSYPLKEVRRV 147
Cdd:pfam07021  87 ATRNPREVLDEMLRI 101
metW TIGR02081
methionine biosynthesis protein MetW; This protein is found alongside MetX, of the enzyme that ...
 59-147 1.66e-06

methionine biosynthesis protein MetW; This protein is found alongside MetX, of the enzyme that acylates homoserine as a first step toward methionine biosynthesis, in many species. It appears to act in methionine biosynthesis but is not fully characterized. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 273958  Cd Length: 194  Bit Score: 47.36  E-value: 1.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464   59 GKRVLDLGCGTGYFSQLLQQR------GAEvvcgdISQAMLDKAEQRcgAVRMHYQVADaENLP-FDDDSFDYVFSSLAL 131
Cdd:TIGR02081  14 GSRVLDLGCGDGELLALLRDEkqvrgyGIE-----IDQDGVLACVAR--GVNVIQGDLD-EGLEaFPDKSFDYVILSQTL 85

                          90
                  ....*....|....*.
gi 491530464  132 QWCTDLSYPLKEVRRV 147
Cdd:TIGR02081  86 QATRNPEEILDEMLRV 101
arsM PRK11873
arsenite methyltransferase;
59-160 2.61e-06

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 47.64  E-value: 2.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464  59 GKRVLDLGCGTGyFSQLL--QQRGAE--VVCGDISQAMLDKAE---QRCGAVRMHYQVADAENLPFDDDSFDYVFSSLAL 131
Cdd:PRK11873  78 GETVLDLGSGGG-FDCFLaaRRVGPTgkVIGVDMTPEMLAKARanaRKAGYTNVEFRLGEIEALPVADNSVDVIISNCVI 156

                         90       100
                 ....*....|....*....|....*....
gi 491530464 132 QWCTDLSYPLKEVRRVLKNGGKAWFSTLV 160
Cdd:PRK11873 157 NLSPDKERVFKEAFRVLKPGGRFAISDVV 185
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
109-153 2.63e-06

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


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 46.40  E-value: 2.63e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 491530464 109 VADAEN-LPFDDDSFDYVFSSLALQwctDLSYP-----LKEVRRVLKNGGK 153
Cdd:COG4627   33 VGDLTDpLPFPDNSVDAIYSSHVLE---HLDYEeaplaLKECYRVLKPGGI 80
COG3963 COG3963
Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];
60-153 2.77e-06

Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];


Pssm-ID: 443163  Cd Length: 193  Bit Score: 46.74  E-value: 2.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464  60 KRVLDLGCGTGYFSQLLQQRG---AEVVCGDISQAMLDKAEQRCGAVRMHYqvADAENLP-----FDDDSFDYVFSSLAL 131
Cdd:COG3963   47 GPVVELGPGTGVFTRAILARGvpdARLLAVEINPEFAEHLRRRFPRVTVVN--GDAEDLAellaeHGIGKVDAVVSGLPL 124

                         90       100
                 ....*....|....*....|....*....
gi 491530464 132 qwctdLSYP-------LKEVRRVLKNGGK 153
Cdd:COG3963  125 -----LSFPpelrraiLDAAFRVLAPGGV 148
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 61-136 3.22e-06

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 47.25  E-value: 3.22e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491530464  61 RVLDLGCGTGYFSQLLQQR--GAEVVCGDISQAMLDKAEQRCGAVRmhYQVAD-AENLPfdDDSFDYVFSSLALQWCTD 136
Cdd:PRK01683  34 YVVDLGCGPGNSTELLVERwpAARITGIDSSPAMLAEARSRLPDCQ--FVEADiASWQP--PQALDLIFANASLQWLPD 108
PRK05785 PRK05785
hypothetical protein; Provisional
 60-150 3.90e-06

hypothetical protein; Provisional


Pssm-ID: 235607 [Multi-domain]  Cd Length: 226  Bit Score: 46.60  E-value: 3.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464  60 KRVLDLGCGTGYFSQLLQQ-RGAEVVCGDISQAMLdkaeqRCGAVRMHYQVADAENLPFDDDSFDYVFSSLALQWCTDLS 138
Cdd:PRK05785  53 KKVLDVAAGKGELSYHFKKvFKYYVVALDYAENML-----KMNLVADDKVVGSFEALPFRDKSFDVVMSSFALHASDNIE 127

                         90
                 ....*....|..
gi 491530464 139 YPLKEVRRVLKN 150
Cdd:PRK05785 128 KVIAEFTRVSRK 139
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 44-156 1.59e-05

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: 44.12  E-value: 1.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464   44 DVGHQ-LLDKLPENLTGKrVLDLGCGTGYFSQLLQQRG--AEVVCGDISQAMLDKAE---QRCGAVRMHYQVADAENlPF 117
Cdd:pfam05175  17 DIGSRlLLEHLPKDLSGK-VLDLGCGAGVLGAALAKESpdAELTMVDINARALESARenlAANGLENGEVVASDVYS-GV 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 491530464  118 DDDSFDYVFSS----LALQWCTDLSYPL-KEVRRVLKNGGKAWF 156
Cdd:pfam05175  95 EDGKFDLIISNppfhAGLATTYNVAQRFiADAKRHLRPGGELWI 138
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 47-95 3.30e-05

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


Pssm-ID: 426399  Cd Length: 179  Bit Score: 43.35  E-value: 3.30e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 491530464   47 HQLLDKLPENLTGKRVLDLGCGTGYFSQLLQQRGAEVVCG-DISQAMLDK 95
Cdd:pfam01728  10 LEIDEKFGLLKPGKTVLDLGAAPGGWSQVALQRGAGKVVGvDLGPMQLWK 59
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 48-156 3.40e-05

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 44.74  E-value: 3.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464  48 QLLDKLPEnLTGKRVLDLGCGTGYFSQLLQQRGAEVVCGDISQAMLDKAEQRCGAVR-MHYQVAD--AENLPFDDDSFDY 124
Cdd:PLN02336  28 EILSLLPP-YEGKSVLELGAGIGRFTGELAKKAGQVIALDFIESVIKKNESINGHYKnVKFMCADvtSPDLNISDGSVDL 106

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 491530464 125 VFSSLALQWCTDlsyplKEVRRV-------LKNGGKAWF 156
Cdd:PLN02336 107 IFSNWLLMYLSD-----KEVENLaermvkwLKVGGYIFF 140
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
48-98 3.90e-05

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


Pssm-ID: 182918  Cd Length: 255  Bit Score: 43.80  E-value: 3.90e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 491530464  48 QLLDKLPENLTgkRVLDLGCGTGYFSQLLQQRGAEVVCGDISQAMLDKAEQ 98
Cdd:PRK11036  36 RLLAELPPRPL--RVLDAGGGEGQTAIKLAELGHQVILCDLSAEMIQRAKQ 84
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 48-118 1.21e-04

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 42.00  E-value: 1.21e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491530464  48 QLLDKLPenltGKRVLDLGCGTGYFSQLLQQRGAEVVCGDISQAMLDKAEQR---CGAVRMHYQVAD-----AENLPFD 118
Cdd:COG2518   60 EALDLKP----GDRVLEIGTGSGYQAAVLARLAGRVYSVERDPELAERARERlaaLGYDNVTVRVGDgalgwPEHAPFD 134
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 59-126 1.42e-04

tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure and biogenesis]; tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 42.47  E-value: 1.42e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491530464  59 GKRVLDLGCGTGYFSQLLQQRGAEVVCGDISQAMLDKAEQ---RCGAVRMHYQVADAEN-LP--FDDDSFDYVF 126
Cdd:COG2265  234 GERVLDLYCGVGTFALPLARRAKKVIGVEIVPEAVEDAREnarLNGLKNVEFVAGDLEEvLPelLWGGRPDVVV 307
PRK12335 PRK12335
tellurite resistance protein TehB; Provisional
 61-134 6.50e-04

tellurite resistance protein TehB; Provisional


Pssm-ID: 183450 [Multi-domain]  Cd Length: 287  Bit Score: 40.31  E-value: 6.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464  61 RVLDLGCGTGYFSQLLQQRGAEVVCGDISQAMLDKAEqrcgavrmhyQVADAENLPFD-----------DDSFDYVFSSL 129
Cdd:PRK12335 123 KALDLGCGQGRNSLYLALLGFDVTAVDINQQSLENLQ----------EIAEKENLNIRtglydinsasiQEEYDFILSTV 192


                 ....*
gi 491530464 130 ALQWC 134
Cdd:PRK12335 193 VLMFL 197
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 59-157 1.16e-03

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 40.12  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464  59 GKRVLDLGCGTG----YFSqllQQRGAEVVCGDISQAMLDKAEQRCGAVR--MHYQVADAENLPFDDDSFDYVFSSLALQ 132
Cdd:PLN02336 267 GQKVLDVGCGIGggdfYMA---ENFDVHVVGIDLSVNMISFALERAIGRKcsVEFEVADCTKKTYPDNSFDVIYSRDTIL 343

                         90       100
                 ....*....|....*....|....*
gi 491530464 133 WCTDLSYPLKEVRRVLKNGGKAWFS 157
Cdd:PLN02336 344 HIQDKPALFRSFFKWLKPGGKVLIS 368
PRK06922 PRK06922
class I SAM-dependent methyltransferase;
28-174 1.24e-03

class I SAM-dependent methyltransferase;


Pssm-ID: 180751 [Multi-domain]  Cd Length: 677  Bit Score: 40.24  E-value: 1.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464  28 FGKAAETYDK---HAAFQRDVGHQLLDK--LPENLTGKRVLDLGCGTGYFSQLLQQR--GAEVVCGDISQAMLDKAEQRc 100
Cdd:PRK06922 383 FGLRKDAYDRfhnEEVYLEHMNSSADDKriILDYIKGDTIVDVGAGGGVMLDMIEEEteDKRIYGIDISENVIDTLKKK- 461

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464 101 gAVRMH--YQV--ADAENLP--FDDDSFD-YVFSSLALQWCTDLSYP------------LKEVRRVLKNGGKAwfsTLVD 161
Cdd:PRK06922 462 -KQNEGrsWNVikGDAINLSssFEKESVDtIVYSSILHELFSYIEYEgkkfnhevikkgLQSAYEVLKPGGRI---IIRD 537

                        170
                 ....*....|...
gi 491530464 162 GSLYELRASWEKI 174
Cdd:PRK06922 538 GIMTEDKRLMRVI 550
PRK11207 PRK11207
tellurite resistance methyltransferase TehB;
59-131 1.35e-03

tellurite resistance methyltransferase TehB;


Pssm-ID: 183040  Cd Length: 197  Bit Score: 38.95  E-value: 1.35e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491530464  59 GKRVLDLGCGTGYFSQLLQQRGAEVVCGDISQAMLDKAEQRCGAVRM---HYQVADAENLPFDDDsFDYVFSSLAL 131
Cdd:PRK11207  31 PGKTLDLGCGNGRNSLYLAANGFDVTAWDKNPMSIANLERIKAAENLdnlHTAVVDLNNLTFDGE-YDFILSTVVL 105
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 45-126 1.83e-03

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 38.84  E-value: 1.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464  45 VGHQLLDKLPENLTGKRVLDLGCGT-GYF-SQLLQQRGAEVVCGDISQAMLDKAEQRCGAVRMHYQVAD--AENLPFDDD 120
Cdd:cd05188  121 TAYHALRRAGVLKPGDTVLVLGAGGvGLLaAQLAKAAGARVIVTDRSDEKLELAKELGADHVIDYKEEDleEELRLTGGG 200


                 ....*.
gi 491530464 121 SFDYVF 126
Cdd:cd05188  201 GADVVI 206
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 49-157 2.47e-03

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 38.33  E-value: 2.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464  49 LLDkLPEnLTGKRVLDLGCGTGYFSQLLQQRGA-EVVCGDISQAMLDKAEQRCGA--VRMHYQVADAENLPfDDDSFDYV 125
Cdd:COG3897   63 LLD-HPE-VAGKRVLELGCGLGLVGIAAAKAGAaDVTATDYDPEALAALRLNAALngVAITTRLGDWRDPP-AAGGFDLI 139

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 491530464 126 fsslalqWCTDLSY------PLKEV-RRVLKNGGKAWFS 157
Cdd:COG3897  140 -------LGGDVLYerdlaePLLPFlDRLAAPGGEVLIG 171
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 59-156 2.69e-03

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: 38.20  E-value: 2.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464  59 GKRVLDLGCGTGYFSQLLQQR--GAEVVCGDISQAMLDKAE---QRCG-AVRMHYQVADAENLP--FDDDSFDYVFS--- 127
Cdd:COG4123   38 GGRVLDLGTGTGVIALMLAQRspGARITGVEIQPEAAELARrnvALNGlEDRITVIHGDLKEFAaeLPPGSFDLVVSnpp 117

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 491530464 128 ---------------SLALQwCTDLSYP--LKEVRRVLKNGGKAWF 156
Cdd:COG4123  118 yfkagsgrkspdearAIARH-EDALTLEdlIRAAARLLKPGGRFAL 162
Methyltransf_9 pfam08003
Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It ...
 57-160 2.95e-03

Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It also includes two putative methyltransferase proteins, Swiss:Q8EEE6 and Swiss:Q88MX8.


Pssm-ID: 429781 [Multi-domain]  Cd Length: 315  Bit Score: 38.54  E-value: 2.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464   57 LTGKRVLDLGCGTGYFSQLLQQRGAEVVCG-DISQAMLDKAEqrcgAVR--------MHYQVADAENLPfDDDSFDYVFS 127
Cdd:pfam08003 114 LKGRTILDVGCGNGYHMWRMLGEGAAMVVGiDPSELFLCQFE----AVRkllgndqrAHLLPLGIEQLP-ALAAFDTVFS 188

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 491530464  128 SLALQwctDLSYPLKEVRRV---LKNGGKAWFSTLV 160
Cdd:pfam08003 189 MGVLY---HRRSPLDHLLQLkdqLVKGGELVLETLV 221
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
59-127 4.53e-03

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 37.91  E-value: 4.53e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464  59 GKRVLDLGCGTGYFSQLLQQR-GAEVVCGDISQAMLDKAEQRCGAVRMHYQVADAENLpfdDDSFDYVFS 127
Cdd:PRK11705 168 GMRVLDIGCGWGGLARYAAEHyGVSVVGVTISAEQQKLAQERCAGLPVEIRLQDYRDL---NGQFDRIVS 234
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
48-70 5.25e-03

Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 37.46  E-value: 5.25e-03
                         10        20
                 ....*....|....*....|...
gi 491530464  48 QLLDKLPenLTGKRVLDLGCGTG 70
Cdd:COG2264  140 EALEKLL--KPGKTVLDVGCGSG 160
COG2521 COG2521
Predicted archaeal methyltransferase [General function prediction only];
59-153 5.40e-03

Predicted archaeal methyltransferase [General function prediction only];


Pssm-ID: 442011 [Multi-domain]  Cd Length: 285  Bit Score: 37.58  E-value: 5.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464  59 GKRVLDLGCGTGYFSQLLQQRGA-EVVCGDISQAMLDKAEQ-------RCGAVRMHyqVADAENL--PFDDDSFDYV--- 125
Cdd:COG2521  133 GDRVLDTCTGLGYTAIEALKRGArEVITVEKDPNVLELAELnpwsrelANERIKII--LGDASEVikTFPDESFDAIihd 210

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 491530464 126 ---FS------SLALqwctdlsYplKEVRRVLKNGGK 153
Cdd:COG2521  211 pprFSlagelySLEF-------Y--RELYRVLKPGGR 238
rsmC PRK09489
16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC;
44-83 6.03e-03

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


Pssm-ID: 181902 [Multi-domain]  Cd Length: 342  Bit Score: 37.61  E-value: 6.03e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 491530464  44 DVGHQLL-DKLPENLTGKrVLDLGCGTGYFSQLLQQRGAEV 83
Cdd:PRK09489 182 DVGSQLLlSTLTPHTKGK-VLDVGCGAGVLSAVLARHSPKI 221
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
59-98 6.71e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 36.94  E-value: 6.71e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 491530464  59 GKRVLDLGCGTGYFSQLLQQRGAE-VVCGDISQAMLDKAEQ 98
Cdd:COG4076   36 GDVVLDIGTGSGLLSMLAARAGAKkVYAVEVNPDIAAVARR 76
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
48-123 8.00e-03

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 37.05  E-value: 8.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530464  48 QLLDKLPenLTGKRVLDLGCGTGYFSQLLQQRGAEVVCG-DI-SQAML---DKAEQRcgavrmhyQVADAENLPFDDDSF 122
Cdd:PRK00517 111 EALEKLV--LPGKTVLDVGCGSGILAIAAAKLGAKKVLAvDIdPQAVEaarENAELN--------GVELNVYLPQGDLKA 180


                 .
gi 491530464 123 D 123
Cdd:PRK00517 181 D 181
 
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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